|
Name |
Accession |
Description |
Interval |
E-value |
| dmsA_ynfE |
TIGR02166 |
anaerobic dimethyl sulfoxide reductase, A subunit, DmsA/YnfE family; Members of this family ... |
11-809 |
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: 1454.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 11 ISRRTLVK-STAIGSLALAAGGISLPFglkSAAAAVKHAVQPPEDTVVWGACSVNCGSRCALRLHVRDNEVYWVETDNTG 89
Cdd:TIGR02166 1 ISRRHFLKtSAALGGLAAASGALSLPF---SVNAAAEATPTGPDEKVVWSACTVNCGSRCPLRVHVKDGEITRIETDNTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 90 EDVYGDHQVRACLRGRSIRRRINHPDRLNYPMKRVGKRGEGKFERITWDEALDTIAASLKDVVANYGNEAVYINYSSGIV 169
Cdd:TIGR02166 78 DDEYGNHQVRACLRGRSMRRRVYNPDRLKYPMKRVGKRGEGKFERISWDEATDTIADNLKRIIEKYGNEAIYVNYGTGTT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 170 GGNITRSSPyASLVARLMNCYGGFLSHYGTYSTAQIACAMPYTYG-SNDGNSTSDIENTKLVVMFGNNPAETRMSGGGIT 248
Cdd:TIGR02166 158 GGTMSRSWP-PTAVARLLNLCGGYLNQYGSYSTAQINEAMPYTYGiSADGSSLDDIENSKLVVMFGNNPAETRMSGGGQT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 249 YYLEQARERSNARMIVIDPRYTDTAAGREDEWIPIRPGTDAALVAGIAWVLIDENLVDQPFLDKYCVGYDEKTLPEGAPA 328
Cdd:TIGR02166 237 YYFLQALEKSNARVIVIDPRYTDTVAGREDEWIPIRPGTDAALVAAIAYVMISENLHDQAFLDRYCVGFDEKTLPASAPK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 329 NGHYKAYILGQGDDHTAKTPEWASRITGIPADRIVKLAREIGSAKPAYICQGWGPQRQANGELTSRAIAMLPILTGNVG- 407
Cdd:TIGR02166 317 NGSYKDYILGEGADGTPKTPEWASKITGIPADTIIKLAREIGNAKPAFISQGWGPQRHANGEQAARAIMMLALLTGNVGi 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 408 ---NSGARESTYTITIERMPLPDNPVKTQISCFSWTDAIARGPEMTALRDGVRGKDKLDVPIKFIWNYAGNTLINQHSDI 484
Cdd:TIGR02166 397 kggNNGAREGNYSLPFARMPELPNPVKTSISCFLWTDAIDRGTEMTAIKDGVRGKDKLDSNIKFLWNYAGNCLINQHSDI 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 485 NKTHDILQDESKCEMIVVIDNFMTSSAKYADIVLPDLMTVEQEDIIPNDYAGNMGYLIFLQPVTAPKFERKPIYWIMSEV 564
Cdd:TIGR02166 477 NRTHKILQDESKCEMIVVIDNHMTSSAKYADILLPDTTTLEQNDFIEDSYASNMSYLIFMQKAIEPLFECKPIYDMLSEV 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 565 AKRLGpdIHQKFTEGRTQEQWLQYLYAKMLEKDPKLPSYDELKKRGIYKRKDPNGHFVAYKKFRENPEANPLKTPSGKIE 644
Cdd:TIGR02166 557 AKRLG--VEAEFTEGRTQEEWLEHLYAQTRAADPALPSFAELRKQGIYKAKSAPGPFVAFEDFRRDPEANPLKTPSGKIE 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 645 IYSSKLAEIAATWELEKDETISPLPVYASTFDGWDAPERARFPLQLFGFHFKARTHSSYGNVDVLKAACRQEVWLNPVDA 724
Cdd:TIGR02166 635 IYSERLAQIAHTWELPEGDVITPLPEYVPTFEGPDDPLRKDFPLQLTGFHYKGRTHSTYGNVDWLREAAPQELWINPIDA 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 725 EKRGIKNGDTVRVFNDRGEVRIEAKVTPRIMPGVSAMGQGAWHDANmsGDRVDHGSCINTLTTHRPSPLAKGNPQHTNLV 804
Cdd:TIGR02166 715 QKRGITNGDMVRIFNSRGEVEIPAKVTPRIMPGVVALGQGAWYQPD--KNGIDVGGCINTLTTQRPSPLAKGNPQHTNLV 792
|
....*
gi 2278930946 805 QIEKV 809
Cdd:TIGR02166 793 EVEKA 797
|
|
| PRK14990 |
PRK14990 |
anaerobic dimethyl sulfoxide reductase subunit A; Provisional |
11-809 |
0e+00 |
|
anaerobic dimethyl sulfoxide reductase subunit A; Provisional
Pssm-ID: 184952 [Multi-domain] Cd Length: 814 Bit Score: 1311.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 11 ISRRTLVKSTAIGSLALAAGGISLPFGLKSAAAAVKHAVQPPEDtVVWGACSVNCGSRCALRLHVRDNEVYWVETDNTGE 90
Cdd:PRK14990 14 VSRRGLVKTTAIGGLAMASSALTLPFSRIAHAVDSAIPTKSDEK-VIWSACTVNCGSRCPLRMHVVDGEIKYVETDNTGD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 91 DVY-GDHQVRACLRGRSIRRRINHPDRLNYPMKRVGKRGEGKFERITWDEALDTIAASLKDVVANYGNEAVYINYSSGIV 169
Cdd:PRK14990 93 DNYdGLHQVRACLRGRSMRRRVYNPDRLKYPMKRVGARGEGKFERISWEEAYDIIATNMQRLIKEYGNESIYLNYGTGTL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 170 GGNITRS-SPYASLVARLMNCYGGFLSHYGTYSTAQIACAMPYTYGS-NDGNSTSDIENTKLVVMFGNNPAETRMSGGGI 247
Cdd:PRK14990 173 GGTMTRSwPPGNTLVARLMNCCGGYLNHYGDYSSAQIAEGLNYTYGGwADGNSPSDIENSKLVVLFGNNPGETRMSGGGV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 248 TYYLEQARERSNARMIVIDPRYTDTAAGREDEWIPIRPGTDAALVAGIAWVLIDENLVDQPFLDKYCVGYDEKTLPEGAP 327
Cdd:PRK14990 253 TYYLEQARQKSNARMIIIDPRYTDTGAGREDEWIPIRPGTDAALVNGLAYVMITENLVDQPFLDKYCVGYDEKTLPASAP 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 328 ANGHYKAYILGQGDDHTAKTPEWASRITGIPADRIVKLAREIGSAKPAYICQGWGPQRQANGELTSRAIAMLPILTGNV- 406
Cdd:PRK14990 333 KNGHYKAYILGEGPDGVAKTPEWASQITGVPADKIIKLAREIGSTKPAFISQGWGPQRHANGEIATRAISMLAILTGNVg 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 407 ---GNSGARESTYTITIERMPLPDNPVKTQISCFSWTDAIARGPEMTALRDGVRGKDKLDVPIKFIWNYAGNTLINQHSD 483
Cdd:PRK14990 413 ingGNSGAREGSYSLPFVRMPTLENPIQTSISMFMWTDAIERGPEMTALRDGVRGKDKLDVPIKMIWNYAGNCLINQHSE 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 484 INKTHDILQDESKCEMIVVIDNFMTSSAKYADIVLPDLMTVEQEDIIPNDYAGNMGYLIFLQPVTAPKFERKPIYWIMSE 563
Cdd:PRK14990 493 INRTHEILQDDKKCELIVVIDCHMTSSAKYADILLPDCTASEQMDFALDASCGNMSYVIFNDQVIKPRFECKTIYEMTSE 572
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 564 VAKRLGpdIHQKFTEGRTQEQWLQYLYAKMLEKDPKLPSYDELKKRGIYKRKDPNGHFVAYKKFRENPEANPLKTPSGKI 643
Cdd:PRK14990 573 LAKRLG--VEQQFTEGRTQEEWMRHLYAQSREAIPELPTFEEFRKQGIFKKRDPQGHHVAYKAFREDPQANPLTTPSGKI 650
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 644 EIYSSKLAEIAATWELEKDETISPLPVYASTFDGWDAPERARFPLQLFGFHFKARTHSSYGNVDVLKAACRQEVWLNPVD 723
Cdd:PRK14990 651 EIYSQALADIAATWELPEGDVIDPLPIYTPGFESYQDPLNKQYPLQLTGFHYKSRVHSTYGNVDVLKAACRQEMWINPLD 730
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 724 AEKRGIKNGDTVRVFNDRGEVRIEAKVTPRIMPGVSAMGQGAWHDANMSgdRVDHGSCINTLTTHRPSPLAKGNPQHTNL 803
Cdd:PRK14990 731 AQKRGINNGDKVRIFNDRGEVHIEAKVTPRMMPGVVALGEGAWYDPDAK--RVDKGGCINVLTTQRPSPLAKGNPSHTNL 808
|
....*.
gi 2278930946 804 VQIEKV 809
Cdd:PRK14990 809 VQVEKV 814
|
|
| MopB_DmsA-EC |
cd02770 |
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
58-677 |
0e+00 |
|
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic dimethylsulfoxide reductase (DMSOR) of Escherichia coli and other related DMSOR-like enzymes. Unlike other DMSOR-like enzymes, this group has a predicted N-terminal iron-sulfur [4Fe-4S] cluster binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239171 [Multi-domain] Cd Length: 617 Bit Score: 969.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 58 WGACSVNCGSRCALRLHVRDNEVYWVETDNTGEDVYGDHQVRACLRGRSIRRRINHPDRLNYPMKRVGKRGEGKFERITW 137
Cdd:cd02770 1 WSACTVNCGGRCPLKAHVKDGVITRIETDDTGDDDPGFHQIRACLRGRSQRKRVYNPDRLKYPMKRVGKRGEGKFVRISW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 138 DEALDTIAASLKDVVANYGNEAVYINYSSGIVGGNITRSSPyaslVARLMNCYGGFLSHYGTYSTAQIACAMPYTYGSND 217
Cdd:cd02770 81 DEALDTIASELKRIIEKYGNEAIYVNYGTGTYGGVPAGRGA----IARLLNLTGGYLNYYGTYSWAQITTATPYTYGAAA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 218 -GNSTSDIENTKLVVMFGNNPAETRMSGGGITYYLEQAReRSNARMIVIDPRYTDTAAGREDEWIPIRPGTDAALVAGIA 296
Cdd:cd02770 157 sGSSLDDLKDSKLVVLFGHNPAETRMGGGGSTYYYLQAK-KAGAKFIVIDPRYTDTAVTLADEWIPIRPGTDAALVAAMA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 297 WVLIDENLVDQPFLDKYCVGYDEKTLPEGAPANGHYKAYILGQGDDHTAKTPEWASRITGIPADRIVKLAREIGSAKPAY 376
Cdd:cd02770 236 YVMITENLHDQAFLDRYCVGFDAEHLPEGAPPNESYKDYVLGTGYDGTPKTPEWASEITGVPAETIRRLAREIATTKPAA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 377 ICQGWGPQRQANGELTSRAIAMLPILTGNVG----NSGARESTYTITIERMPLPDNPVKTQISCFSWTDAIARGPEMTAL 452
Cdd:cd02770 316 ILQGWGPQRHANGEQAARAIMMLAAMTGNVGipggNTGARPGGSAYNGAGLPAGKNPVKTSIPCFMWTDAIERGEEMTAD 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 453 RDGVRGKDKLDVPIKFIWNYAGNTLINQHSDINKTHD-ILQDESKCEMIVVIDNFMTSSAKYADIVLPDLMTVEQEDIIP 531
Cdd:cd02770 396 DGGVKGADKLKSNIKMIWNYAGNTLINQHSDDNNTTRaLLDDESKCEFIVVIDNFMTPSARYADILLPDTTELEREDIVL 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 532 NDYAGNMGYLIFLQPVTAPKFERKPIYWIMSEVAKRLGpdIHQKFTEGRTQEQWLQYLYAKMLEKDPKLPSYDELKKRGI 611
Cdd:cd02770 476 TSNAGMMEYLIYSQKAIEPLYECKSDYEICAELAKRLG--VEDQFTEGKTEQEWLEELYGQTRAKEPGLPTYEEFREKGI 553
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2278930946 612 YKRKDPnGHFVAYKKFRENPEANPLKTPSGKIEIYSSKLAEIAATwELEKDEtISPLPVYASTFDG 677
Cdd:cd02770 554 YRVPRA-LPFVAFEDFREDPENNPLKTPSGKIEIYSKALADMAKT-LPEGDE-IPAIPKYVPAWEG 616
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
41-809 |
0e+00 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 715.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 41 AAAAVKHAVQPPEDTVVWGACSvNCGSRCALRLHVRDNEVYWVETDNTGEDvygdHQVRACLRGRSIRRRINHPDRLNYP 120
Cdd:COG0243 8 AAGAGAAALEAAGTKTVKTTCP-GCGVGCGLGVKVEDGRVVRVRGDPDHPV----NRGRLCAKGAALDERLYSPDRLTYP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 121 MKRVGKRGEGKFERITWDEALDTIAASLKDVVANYGNEAVYInYSSGIVGGNITRSSPYasLVARLMNCYG--GFLSHyG 198
Cdd:COG0243 83 MKRVGPRGSGKFERISWDEALDLIAEKLKAIIDEYGPEAVAF-YTSGGSAGRLSNEAAY--LAQRFARALGtnNLDDN-S 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 199 TYSTAQIACAMPYTYGSNDG-NSTSDIENTKLVVMFGNNPAETrmsGGGITYYLEQARERSNARMIVIDPRYTDTAAgRE 277
Cdd:COG0243 159 RLCHESAVAGLPRTFGSDKGtVSYEDLEHADLIVLWGSNPAEN---HPRLLRRLREAAKKRGAKIVVIDPRRTETAA-IA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 278 DEWIPIRPGTDAALVAGIAWVLIDENLVDQPFLDKYCVGYDEktlpegapanghYKAYIlgqgddhTAKTPEWASRITGI 357
Cdd:COG0243 235 DEWLPIRPGTDAALLLALAHVLIEEGLYDRDFLARHTVGFDE------------LAAYV-------AAYTPEWAAEITGV 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 358 PADRIVKLAREIGSAKPAYICQGWGPQRQANGELTSRAIAMLPILTGNVGNSGArestytitiermplpdnpvktqISCF 437
Cdd:COG0243 296 PAEDIRELAREFATAKPAVILWGMGLQQHSNGTQTVRAIANLALLTGNIGKPGG----------------------GPFS 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 438 SWTDAIARGpemtalrdgvrgkdkLDVPIKFIWNYAGNtLINQHSDINKTHDILQdesKCEMIVVIDNFMTSSAKYADIV 517
Cdd:COG0243 354 LTGEAILDG---------------KPYPIKALWVYGGN-PAVSAPDTNRVREALR---KLDFVVVIDTFLTETARYADIV 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 518 LPDLMTVEQEDIIPNdyaGNMGYLIFLQPVTAPKFERKPIYWIMSEVAKRLGpdIHQKFTEGRTQEQWLQYLYAKMlekD 597
Cdd:COG0243 415 LPATTWLERDDIVTN---SEDRRVHLSRPAVEPPGEARSDWEIFAELAKRLG--FEEAFPWGRTEEDYLRELLEAT---R 486
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 598 PKLPSYDELKKRGIYKRKDPNGHfvaykKFRENpeaNPLKTPSGKIEIYSSKLAeiaatwelekdetISPLPVYASTFDg 677
Cdd:COG0243 487 GRGITFEELREKGPVQLPVPPEP-----AFRND---GPFPTPSGKAEFYSETLA-------------LPPLPRYAPPYE- 544
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 678 WDAPERARFPLQLFGFHFKARTHSSYGNVDVLKAACRQE-VWLNPVDAEKRGIKNGDTVRVFNDRGEVRIEAKVTPRIMP 756
Cdd:COG0243 545 GAEPLDAEYPLRLITGRSRDQWHSTTYNNPRLREIGPRPvVEINPEDAAALGIKDGDLVRVESDRGEVLARAKVTEGIRP 624
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|...
gi 2278930946 757 GVSAMGQGAWHDANMsgdrvDHGSCINTLTTHRPSPLAKGNPQHTNLVQIEKV 809
Cdd:COG0243 625 GVVFAPHGWWYEPAD-----DKGGNVNVLTPDATDPLSGTPAFKSVPVRVEKA 672
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
68-671 |
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: 712.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 68 RCALRLHVRDNEVYWVETDNTgedvygdHQVRACLRGRSIRRRINHPDRLNYPMKRVGK----------RGEGKFERITW 137
Cdd:cd02751 6 WGPFKAHVKDGVIVRVEPDDT-------DQPRPCPRGRSVRDRVYSPDRIKYPMKRVGWlgngpgsrelRGEGEFVRISW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 138 DEALDTIAASLKDVVANYGNEAVYINYSSGIVGGNITRSSpyaSLVARLMNCYGGFLSHYGTYSTAQIACAMPYTYGS-- 215
Cdd:cd02751 79 DEALDLVASELKRIREKYGNEAIFGGSYGWASAGRLHHAQ---SLLHRFLNLIGGYLGSYGTYSTGAAQVILPHVVGSde 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 216 --NDGNSTSDI-ENTKLVVMFGNNPAETRMSGGGI-----TYYLEQARERsNARMIVIDPRYTDTAAGREDEWIPIRPGT 287
Cdd:cd02751 156 vyEQGTSWDDIaEHSDLVVLFGANPLKTRQGGGGGpdhgsYYYLKQAKDA-GVRFICIDPRYTDTAAVLAAEWIPIRPGT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 288 DAALVAGIAWVLIDENLVDQPFLDKYCVGYDEktlpegapanghYKAYILGqGDDHTAKTPEWASRITGIPADRIVKLAR 367
Cdd:cd02751 235 DVALMLAMAHTLITEDLHDQAFLARYTVGFDE------------FKDYLLG-ESDGVPKTPEWAAEITGVPAETIRALAR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 368 EIGSaKPAYICQGWGPQRQANGELTSRAIAMLPILTGNVG------------NSGARESTYTITIERMPLPDNPVKTQIS 435
Cdd:cd02751 302 EIAS-KRTMIAQGWGLQRAHHGEQPAWMLVTLAAMLGQIGlpgggfgfgygySNGGGPPRGGAGGPGLPQGKNPVKDSIP 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 436 CFSWTDAIAR-GPEMTAlrdgvRGKDKLDVPIKFIWNYAGNTLINQHsDINKTHDILQDEskcEMIVVIDNFMTSSAKYA 514
Cdd:cd02751 381 VARIADALLNpGKEFTA-----NGKLKTYPDIKMIYWAGGNPLHHHQ-DLNRLIKALRKD---ETIVVHDIFWTASARYA 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 515 DIVLPDLMTVEQEDIIPNDYAgNMGYLIFLQPVTAPKFERKPIYWIMSEVAKRLGpdIHQKFTEGRTQEQWLQYLY---- 590
Cdd:cd02751 452 DIVLPATTSLERNDIGLTGNY-SNRYLIAMKQAVEPLGEARSDYEIFAELAKRLG--VEEEFTEGRDEMEWLEHLYeetr 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 591 AKMLEKDPKLPSYDELKKRGIYKRKDPNGHFVAYKKFRENPEANPLKTPSGKIEIYSSKLAEIAatwelekDETISPLPV 670
Cdd:cd02751 529 AKAAGPGPELPSFEEFWEKGIVRVPAAPKPFVAFADFREDPEANPLGTPSGKIEIYSETLADFG-------YDDCPGHPT 601
|
.
gi 2278930946 671 Y 671
Cdd:cd02751 602 W 602
|
|
| MopB_DMSOR-BSOR-TMAOR |
cd02769 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
104-663 |
9.57e-130 |
|
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: 400.49 E-value: 9.57e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 104 GRSIRRRINHPDRLNYPMKRVG-----------KRGEGKFERITWDEALDTIAASLKDVVANYGNEAVYinyssgivGGN 172
Cdd:cd02769 34 LDGVPDAVYSPTRIKYPMVRRGwlekgpgsdrsLRGKEEFVRVSWDEALDLVAAELKRVRKTYGNEAIF--------GGS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 173 ITRSSP-----YASLVARLMNCYGGFLSHYGTYSTAQIACAMPYTYGSNDG----NSTSD--IENTKLVVMFGNNPAETR 241
Cdd:cd02769 106 YGWSSAgrfhhAQSLLHRFLNLAGGYVGSVGDYSTGAAQVILPHVVGSMEVyteqQTSWPviAEHTELVVAFGADPLKNA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 242 MSGGGIT------YYLEQARERsNARMIVIDPRYTDTAAGREDEWIPIRPGTDAALVAGIAWVLIDENLVDQPFLDKYCV 315
Cdd:cd02769 186 QIAWGGIpdhqaySYLKALKDR-GIRFISISPLRDDTAAELGAEWIAIRPGTDVALMLALAHTLVTEGLHDKAFLARYTV 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 316 GYDEktlpegapanghYKAYILGqGDDHTAKTPEWASRITGIPADRIVKLAREIGSaKPAYICQGWGPQRQANGELTSRA 395
Cdd:cd02769 265 GFDK------------FLPYLLG-ESDGVPKTPEWAAAICGIPAETIRELARRFAS-KRTMIMAGWSLQRAHHGEQPHWM 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 396 IAMLPILTGNVG------------NSGARESTYTITIERMPLPDNPVKTQISCFSWTDAIARgPEMTALRDGvrgkDKLD 463
Cdd:cd02769 331 AVTLAAMLGQIGlpgggfgfgyhySNGGGPPRGAAPPPALPQGRNPVSSFIPVARIADMLLN-PGKPFDYNG----KKLT 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 464 VP-IKFIWNyAGNTLINQHSDINKTHDILQdesKCEMIVVIDNFMTSSAKYADIVLPDLMTVEQEDIipnDYAGNMGYLI 542
Cdd:cd02769 406 YPdIKLVYW-AGGNPFHHHQDLNRLIRAWQ---KPETVIVHEPFWTATARHADIVLPATTSLERNDI---GGSGDNRYIV 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 543 FLQPVTAPKFERKPIYWIMSEVAKRLGPDihQKFTEGRTQEQWLQYLY----AKMLEKDPKLPSYDELKKRGIYKRKDPN 618
Cdd:cd02769 479 AMKQVVEPVGEARDDYDIFADLAERLGVE--EQFTEGRDEMEWLRHLYeesrAQAAARGVEMPSFDEFWAQGYVELPIPE 556
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 2278930946 619 GHFVAYKKFRENPEANPLKTPSGKIEIYSSKLAEIA-------ATWeLEKDE 663
Cdd:cd02769 557 ADFVRLADFREDPEANPLGTPSGRIEIFSETIAGFGyddcpghPTW-LEPAE 607
|
|
| PRK15102 |
PRK15102 |
trimethylamine-N-oxide reductase TorA; |
11-808 |
1.39e-109 |
|
trimethylamine-N-oxide reductase TorA;
Pssm-ID: 237909 [Multi-domain] Cd Length: 825 Bit Score: 353.98 E-value: 1.39e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 11 ISRRTLVKstaiGSLALAAGGISLPfGLKSAAAAVKHAVQPPEDTVVWGACSVNCGsrcALRLHVRDNEvyWVETDNTGE 90
Cdd:PRK15102 1 ASRRRFLK----GLGGLSAAGMLGP-SLLTPRSALAAQAAAAETTKEWILTGSHWG---AFRAKVKNGR--FVEAKPFEL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 91 DVYGDHQVRAclrgrsIRRRINHPDRLNYPMKRV-----------GKRGEGKFERITWDEALDTIAASLKDVVANYGNEA 159
Cdd:PRK15102 71 DKYPTKMING------IKGHVYNPSRIRYPMVRLdwlrkrhksdtSQRGDNRFVRVSWDEALDLFYEELERVQKTYGPSA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 160 VYinysSGIVGGNIT---RSSpyASLVARLMNCYGGFLSHYGTYSTAQIACAMPYTYGSND----GNSTSDI-ENTKLVV 231
Cdd:PRK15102 145 LH----TGQTGWQSTgqfHSA--TGHMQRAIGMHGNSVGTVGDYSTGAGQVILPYVLGSTEvyeqGTSWPLIlENSKTIV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 232 MFGNNP---------AETRMSGGgityYLEQARER---SNARMIVIDPRYTDTAAGREDEWIPIRPGTDAALVAGIAWVL 299
Cdd:PRK15102 219 LWGSDPvknlqvgwnCETHESYA----YLAQLKEKvakGEINVISIDPVVTKTQNYLGCEHLYVNPQTDVPLMLALAHTL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 300 IDENLVDQPFLDKYCVGYDEkTLPegapanghykaYILGQgDDHTAKTPEWASRITGIPADRIVKLAREIgSAKPAYICQ 379
Cdd:PRK15102 295 YSENLYDKKFIDNYCLGFEQ-FLP-----------YLLGE-KDGVPKTPEWAEKICGIDAETIRELARQM-AKGRTQIIA 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 380 GWGPQRQANGELTSRAIAMLPILTGNVG------------NSGAREST---------YTITIERMPLPDNP----VKTQI 434
Cdd:PRK15102 361 GWCIQRQQHGEQPYWMGAVLAAMLGQIGlpgggisyghhySGIGVPSSggaipggfpGNLDTGQKPKHDNSdykgYSSTI 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 435 SCFSWTDAIAR-GPEMTAlrdgvRGKDKLDVPIKFIWnYAGNTLINQHSDINKTHDILQdesKCEMIVVIDNFMTSSAKY 513
Cdd:PRK15102 441 PVARFIDAILEpGKTINW-----NGKKVTLPPLKMMI-FSGTNPWHRHQDRNRMKEAFR---KLETVVAIDNQWTATCRF 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 514 ADIVLPDLMTVEQEDI-IPNDYAgNMGyLIFLQPVTAPKFERKPIYWIMSEVAKRLGPdiHQKFTEGRTQEQWLQYLYA- 591
Cdd:PRK15102 512 ADIVLPACTQFERNDIdQYGSYS-NRG-IIAMKKVVEPLFESRSDFDIFRELCRRFGR--EKEYTRGMDEMGWLKRLYQe 587
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 592 --KMLEKDPKLPSYDELKKRGiYKRKDPNGHFVAYKKFRENPEANPLKTPSGKIEIYSSKLAEIA-------ATWeLEKD 662
Cdd:PRK15102 588 ckQQNKGKFHMPEFDEFWKKG-YVEFGEGQPWVRHADFREDPELNPLGTPSGLIEIYSRKIADMGyddcqghPMW-FEKI 665
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 663 EtisplpvyaSTFDGwdaPERARFPLQLFGFHFKARTHSSYGNVDVLKA----ACRQEVWLNPVDAEKRGIKNGDTVRVF 738
Cdd:PRK15102 666 E---------RSHGG---PGSDKYPLWLQSVHPDKRLHSQLCESEELREtytvQGREPVYINPQDAKARGIKDGDVVRVF 733
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2278930946 739 NDRGEVRIEAKVTPRIMPGVSAMGQGAWHDANMSGD--RVDHGSCINTLTTHRP-SPLAKGNPQHTNLVQIEK 808
Cdd:PRK15102 734 NDRGQVLAGAVVSDRYPPGVIRIHEGAWYGPDKGGEigALCTYGDPNTLTLDIGtSQLAQATSAHTCLVEIEK 806
|
|
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
60-669 |
5.66e-107 |
|
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: 337.30 E-value: 5.66e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 60 ACSVNCGSRCALRLHVRDNEVYWVETDntgedvyGDHQVRA---CLRGRSIRRRINHPDRLNYPMKRVGKRGeGKFERIT 136
Cdd:cd02766 3 VCPLDCPDTCSLLVTVEDGRIVRVEGD-------PAHPYTRgfiCAKGARYVERVYSPDRLLTPLKRVGRKG-GQWERIS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 137 WDEALDTIAASLKDVVANYGNEAV-YINYSSGivGGNITRSSPyaslvaRLMNCYGGFLSHYGTY-STAQIAcAMPYTYG 214
Cdd:cd02766 75 WDEALDTIAAKLKEIKAEYGPESIlPYSYAGT--MGLLQRAAR------GRFFHALGASELRGTIcSGAGIE-AQKYDFG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 215 SNDGNSTSDIENTKLVVMFGNNPAETRMSGGGItyyLEQARERsNARMIVIDPRYTDTAAgREDEWIPIRPGTDAALVAG 294
Cdd:cd02766 146 ASLGNDPEDMVNADLIVIWGINPAATNIHLMRI---IQEARKR-GAKVVVIDPYRTATAA-RADLHIQIRPGTDGALALG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 295 IAWVLIDENLVDQPFLDKYCVGYDEktlpegapanghYKAYILgqgddhtAKTPEWASRITGIPADRIVKLAREIGSAKP 374
Cdd:cd02766 221 VAKVLFREGLYDRDFLARHTEGFEE------------LKAHLE-------TYTPEWAAEITGVSAEEIEELARLYGEAKP 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 375 AYICQGWGPQRQANGELTSRAIAMLPILTGNVGNS--GARESTYtitiermplpdnpvktqiscfswtdaiarGPemtal 452
Cdd:cd02766 282 PSIRLGYGMQRYRNGGQNVRAIDALPALTGNIGVPggGAFYSNS-----------------------------GP----- 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 453 rdgvrgkdkldvPIKFIWNYAGNtLINQHSDINKTHDILQDEskCEMIVVIDNFMTSSAKYADIVLPDLMTVEQEDIIpn 532
Cdd:cd02766 328 ------------PVKALWVYNSN-PVAQAPDSNKVRKGLARE--DLFVVVHDQFMTDTARYADIVLPATTFLEHEDVY-- 390
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 533 dyaGNMG--YLIFLQPVTAPKFERKPIYWIMSEVAKRLGpdihqkFTEG---RTQEQWLqylyAKMLEKdpklpsyDELK 607
Cdd:cd02766 391 ---ASYWhyYLQYNEPAIPPPGEARSNTEIFRELAKRLG------FGEPpfeESDEEWL----DQALDG-------TGLP 450
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2278930946 608 KRGIYKRKDPNGHFVAYKKFRenPEANPLKTPSGKIEIYSsklaEIAATWELEkdetisPLP 669
Cdd:cd02766 451 LEGIDLERLLGPRKAGFPLVA--WEDRGFPTPSGKFEFYS----ERAAKRGLP------PLP 500
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
62-568 |
1.03e-103 |
|
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, heterogeneous superfamily of enzymes that, in general, bind molybdopterin as a cofactor. The MopB domain is found in a wide variety of molybdenum- and tungsten-containing enzymes, including formate dehydrogenase-H (Fdh-H) and -N (Fdh-N), several forms of nitrate reductase (Nap, Nas, NarG), dimethylsulfoxide reductase (DMSOR), thiosulfate reductase, formylmethanofuran dehydrogenase, and arsenite oxidase. Molybdenum is present in most of these enzymes in the form of molybdopterin, a modified pterin ring with a dithiolene side chain, which is responsible for ligating the Mo. In many bacterial and archaeal species, molybdopterin is in the form of a dinucleotide, with two molybdopterin dinucleotide units per molybdenum. These proteins can function as monomers, heterodimers, or heterotrimers, depending on the protein and organism. Also included in the MopB superfamily is the eukaryotic/eubacterial protein domain family of the 75-kDa subunit/Nad11/NuoG (second domain) of respiratory complex 1/NADH-quinone oxidoreductase which is postulated to have lost an ancestral formate dehydrogenase activity and only vestigial sequence evidence remains of a molybdopterin binding site.
Pssm-ID: 238218 [Multi-domain] Cd Length: 374 Bit Score: 324.28 E-value: 1.03e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 62 SVNCGSRCALRLHVRDNEVYWVETDntgeDVYGDHQVRACLRGRSIRRRINHPDRLNYPMKRVGKRGegKFERITWDEAL 141
Cdd:cd00368 4 CPFCGVGCGILVYVKDGKVVRIEGD----PNHPVNEGRLCDKGRAGLDGLYSPDRLKYPLIRVGGRG--KFVPISWDEAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 142 DTIAASLKDVVANYGNEAVYINYSSGIVGGNitrsspYASLVARLMNCYGGFLSHYGTYSTAQIACAMPYTYGSNDGNST 221
Cdd:cd00368 78 DEIAEKLKEIREKYGPDAIAFYGGGGASNEE------AYLLQKLLRALGSNNVDSHARLCHASAVAALKAFGGGAPTNTL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 222 SDIENTKLVVMFGNNPAETRMSgggITYYLEQARERsNARMIVIDPRYTDTAAgREDEWIPIRPGTDAALVAGiawvlid 301
Cdd:cd00368 152 ADIENADLILLWGSNPAETHPV---LAARLRRAKKR-GAKLIVIDPRRTETAA-KADEWLPIRPGTDAALALA------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 302 enlvdqpfldkycvgydektlpegapanghykayilgqgddhtaktpEWASRITGIPADRIVKLAREIGSAKPAYICQGW 381
Cdd:cd00368 220 -----------------------------------------------EWAAEITGVPAETIRALAREFAAAKRAVILWGM 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 382 GPQRQANGELTSRAIAMLPILTGNVGNSGArestytitiermplpdnpvktqiscfswtdaiargpemtalrdgvrgkdk 461
Cdd:cd00368 253 GLTQHTNGTQNVRAIANLAALTGNIGRPGG-------------------------------------------------- 282
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 462 ldvpikfIWNYAGNTLINQhsdiNKTHDILQDESKCEMIVVIDNFMTSSAKYADIVLPDLMTVEQEDIipndYAGNMGYL 541
Cdd:cd00368 283 -------GLGPGGNPLVSA----PDANRVRAALKKLDFVVVIDIFMTETAAYADVVLPAATYLEKEGT----YTNTEGRV 347
|
490 500
....*....|....*....|....*..
gi 2278930946 542 IFLQPVTAPKFERKPIYWIMSEVAKRL 568
Cdd:cd00368 348 QLFRQAVEPPGEARSDWEILRELAKRL 374
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
65-672 |
3.53e-99 |
|
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. The acetylene hydratase of Pelobacter acetylenicus is a tungsten iron-sulfur protein involved in the fermentation of acetylene to ethanol and acetate. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239160 [Multi-domain] Cd Length: 477 Bit Score: 316.17 E-value: 3.53e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 65 CGSRCALRLHVRDNEVYWVETDNTGEDVYGdhqvRACLRGRSIRRRINHPDRLNYPMKRVGKRGEGKFERITWDEALDTI 144
Cdd:cd02759 7 CHSGCGVLVYVKDGKLVKVEGDPNHPTNKG----RLCMRGLAAPEIVYHPDRLLYPLKRVGERGENKWERISWDEALDEI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 145 AASLKDVVANYGNEAVYInYSSGIVGGNITrSSPYASLVARLMNCYGGFLSHYGTYstAQIACAMPYTYGSNDGNSTSDI 224
Cdd:cd02759 83 AEKLAEIKAEYGPESIAT-AVGTGRGTMWQ-DSLFWIRFVRLFGSPNLFLSGESCY--WPRDMAHALTTGFGLGYDEPDW 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 225 ENTKLVVMFGNNPAETrmSGGGITYYLEQARERSnARMIVIDPRYTDTAAgREDEWIPIRPGTDAALVAGIAWVLIDENL 304
Cdd:cd02759 159 ENPECIVLWGKNPLNS--NLDLQGHWLVAAMKRG-AKLIVVDPRLTWLAA-RADLWLPIRPGTDAALALGMLNVIINEGL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 305 VDQPFLDKYCVGYDEktLPEgapangHYKAYilgqgddhtakTPEWASRITGIPADRIVKLAREIGSAKPAYICQGWGPQ 384
Cdd:cd02759 235 YDKDFVENWCYGFEE--LAE------RVQEY-----------TPEKVAEITGVPAEKIRKAARLYATAKPACIQWGLAID 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 385 RQANGELTSRAIAMLPILTGNVGNSGA-RESTYtitiermplpdnpvktqiscfswtdaiargpemtalrdgvrgkdkld 463
Cdd:cd02759 296 QQKNGTQTSRAIAILRAITGNLDVPGGnLLIPY----------------------------------------------- 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 464 vPIKFIWNYAGNTLINQhSDINKTHDILQdesKCEMIVVIDNFMTSSAKYADIVLPDLMTVEQEDIIPNDYAGNMGYLIf 543
Cdd:cd02759 329 -PVKMLIVFGTNPLASY-ADTAPVLEALK---ALDFIVVVDLFMTPTAMLADIVLPVAMSLERPGLRGGFEAENFVQLR- 402
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 544 lQPVTAPKFERKPIYWIMSEVAKRLGPdihqkftegrtqEQWLQYLYAKmlekdpklpsydelkkrgIYKRKDPNGHFVa 623
Cdd:cd02759 403 -QKAVEPYGEAKSDYEIVLELGKRLGP------------EEAEYYKYEK------------------GLLRPDGQPGFN- 450
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 2278930946 624 ykkfrenpeanplkTPSGKIEIYSSKLaeiaatWELEKDetisPLPVYA 672
Cdd:cd02759 451 --------------TPTGKVELYSTML------EELGYD----PLPYYR 475
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
65-795 |
3.04e-94 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 309.51 E-value: 3.04e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 65 CGSRCALRLHVRDNEVYWVETDNtgedvygDHQV---RACLRGRSIRRRINHPDRLNYPMKRVGkrgeGKFERITWDEAL 141
Cdd:COG3383 14 CGVGCGIDLEVKDGKIVKVEGDP-------DHPVnrgRLCVKGRFGFEFVNSPDRLTTPLIRRG----GEFREVSWDEAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 142 DTIAASLKDVVANYGNEAVyinysSGIVGGNITRSSPYasLVARLMNCYGG--FLSHYGTYSTAQIACAMPYTYGSnDG- 218
Cdd:COG3383 83 DLVAERLREIQAEHGPDAV-----AFYGSGQLTNEENY--LLQKLARGVLGtnNIDNNARLCMASAVAGLKQSFGS-DAp 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 219 -NSTSDIENTKLVVMFGNNPAETrmsgggITYYLEQARERsNARMIVIDPRYTDTAAgREDEWIPIRPGTDAALVAGIAW 297
Cdd:COG3383 155 pNSYDDIEEADVILVIGSNPAEAhp---vLARRIKKAKKN-GAKLIVVDPRRTETAR-LADLHLQIKPGTDLALLNGLLH 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 298 VLIDENLVDQPFLDKYCVGYDEktlpegapanghYKAYILGQgddhtakTPEWASRITGIPADRIVKLAREIGSAKPAYI 377
Cdd:COG3383 230 VIIEEGLVDEDFIAERTEGFEE------------LKASVAKY-------TPERVAEITGVPAEDIREAARLIAEAKRAMI 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 378 CQGWGPQRQANGELTSRAIAMLPILTGNVG-------------NS-GARE--------STYtitierMPLPDNPVKTQIS 435
Cdd:COG3383 291 LWGMGVNQHTQGTDNVNAIINLALATGNIGrpgtgpfpltgqnNVqGGRDmgalpnvlPGY------RDVTDPEHRAKVA 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 436 CFSWTDAIARGPEMTA--LRDGV-RGKdkldvpIKFIWNYAGNTLInQHSDINKTHDILqdeSKCEMIVVIDNFMTSSAK 512
Cdd:COG3383 365 DAWGVPPLPDKPGLTAveMFDAIaDGE------IKALWIIGENPAV-SDPDANHVREAL---EKLEFLVVQDIFLTETAE 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 513 YADIVLPDLMTVEQEdiipndyaGNM----GYLIFLQPVTAPKFERKPIYWIMSEVAKRLGPDIHQK-----FTEGRTqe 583
Cdd:COG3383 435 YADVVLPAASWAEKD--------GTFtnteRRVQRVRKAVEPPGEARPDWEIIAELARRLGYGFDYDspeevFDEIAR-- 504
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 584 qwLQYLYAKMlekdpklpSYDELKKRG----IYKRKDPNGHFVAYK-KFrenpeanplKTPSGKieiyssklAEIAATWE 658
Cdd:COG3383 505 --LTPDYSGI--------SYERLEALGgvqwPCPSEDHPGTPRLFTgRF---------PTPDGK--------ARFVPVEY 557
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 659 LEKDETISplpvyastfdgwdaperARFPLQL------FGFHFKARThssyGNVDVLKAACRQE-VWLNPVDAEKRGIKN 731
Cdd:COG3383 558 RPPAELPD-----------------EEYPLVLttgrllDQWHTGTRT----RRSPRLNKHAPEPfVEIHPEDAARLGIKD 616
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2278930946 732 GDTVRVFNDRGEVRIEAKVTPRIMPGVSAMgqgAWHDAnmsgdrvdhGSCINTLTTHRPSPLAK 795
Cdd:COG3383 617 GDLVRVSSRRGEVVLRARVTDRVRPGTVFM---PFHWG---------EGAANALTNDALDPVSK 668
|
|
| MopB_4 |
cd02765 |
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
59-654 |
3.72e-92 |
|
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: 300.55 E-value: 3.72e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 59 GACSVNCGSRCALRLHVRDNEVYWVETdntgEDVYGDHQVRACLRGRSIRRRINHPDRLNYPMKRVGKRGEGKFERITWD 138
Cdd:cd02765 2 TACPPNCGGRCPLKCHVRDGKIVKVEP----NEWPDKTYKRGCTRGLSHLQRVYSPDRLKYPMKRVGERGEGKFERITWD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 139 EALDTIAASLKDVVANYGNEAVYINYSSGIVGGNITRSSpyASLVARLMNCYGGFLSHyGTYSTAQIACAMPYTYGSNDg 218
Cdd:cd02765 78 EALDTIADKLTEAKREYGGKSILWMSSSGDGAILSYLRL--ALLGGGLQDALTYGIDT-GVGQGFNRVTGGGFMPPTNE- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 219 nsTSDIENTKLVVMFGNNPAETRMSGggiTYYLEQARERSnARMIVIDPRYTDTAAgREDEWIPIRPGTDAALVAGIAWV 298
Cdd:cd02765 154 --ITDWVNAKTIIIWGSNILETQFQD---AEFFLDARENG-AKIVVIDPVYSTTAA-KADQWVPIRPGTDPALALGMINY 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 299 LIDENLVDQPFLDKYC-----VGYDEKTL--PEGAPANGHYKAYILGQGDDHTAK------------------------- 346
Cdd:cd02765 227 ILEHNWYDEAFLKSNTsapflVREDNGTLlrQADVTATPAEDGYVVWDTNSDSPEpvaatninpalegeytingvkvhtv 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 347 -----------TPEWASRITGIPADRIVKLAREIGSAKPAYICQGWGPQRQANGELTSRAIAMLPILTGNVGNSGAREST 415
Cdd:cd02765 307 ltalreqaasyPPKAAAEICGLEEAIIETLAEWYATGKPSGIWGFGGVDRYYHSHVFGRTAAILAALTGNIGRVGGGVGQ 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 416 ytitiermplpdnpvktqiscfswtdaiargpemtalrdgvrgkdkldvpIKFIWNyAGNTLINQHSDINKTHDILqdeS 495
Cdd:cd02765 387 --------------------------------------------------IKFMYF-MGSNFLGNQPDRDRWLKVM---K 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 496 KCEMIVVIDNFMTSSAKYADIVLPDLMTVEQEDIIPNDYAGNmgYLIFLQPVTAPKFERKPIYWIMSEVAKRLGPDihQK 575
Cdd:cd02765 413 NLDFIVVVDIFHTPTVRYADIVLPAAHWFEVEDLLVRYTTHP--HVLLQQKAIEPLFESKSDFEIEKGLAERLGLG--DY 488
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 576 FTEgrTQEQWLQylyAKMLEKDPKLP--SYDELKKRGIYKRKD-PNGHFVAYK--KFrenpeanplKTPSGKIEIYSSKL 650
Cdd:cd02765 489 FPK--TPEDYVR---AFMNSDDPALDgiTWEALKEEGIIMRLAtPEDPYVAYLdqKF---------GTPSGKLEFYNEAA 554
|
....
gi 2278930946 651 AEIA 654
Cdd:cd02765 555 PELE 558
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
65-652 |
2.54e-87 |
|
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: 284.19 E-value: 2.54e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 65 CGSRCALRLHVRDNEVYWVEtdntGEDVYGDHQVRACLRGRSIRRRINHPDRLNYPMKRVGKRGEGKFERITWDEALDTI 144
Cdd:cd02755 8 CSSRCGILARVEDGRVVKID----GNPLSPLSRGKLCARGNAGIQLLYDPDRLKKPLIRVGERGEGKFREASWDEALQYI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 145 AASLKDVVANYGNEAVyinyssgIVGGNITRSSPYASLVARLMNCYGGFlSHYGT-YSTAQIACAMPYTYGSNDGNstSD 223
Cdd:cd02755 84 ASKLKEIKEQHGPESV-------LFGGHGGCYSPFFKHFAAAFGSPNIF-SHESTcLASKNLAWKLVIDSFGGEVN--PD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 224 IENTKLVVMFGNNPAEtrmsgGGITYY---LEQARERSnARMIVIDPRYTDTAAgREDEWIPIRPGTDAALVAGIAWVLI 300
Cdd:cd02755 154 FENARYIILFGRNLAE-----AIIVVDarrLMKALENG-AKVVVVDPRFSELAS-KADEWIPIKPGTDLAFVLALIHVLI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 301 DENLVDQPFLDKYCVGYDEktlpegapANGHYKAYilgqgddhtakTPEWASRITGIPADRIVKLAREIG-SAKPAYICQ 379
Cdd:cd02755 227 SENLYDAAFVEKYTNGFEL--------LKAHVKPY-----------TPEWAAQITDIPADTIRRIAREFAaAAPHAVVDP 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 380 GWGPQRQANGELTSRAIAMLPILTGNVGNSGArestytitierMPLPDNPvktqiscfswtdaiarGPemtalrdgvrgk 459
Cdd:cd02755 288 GWRGTFYSNSFQTRRAIAIINALLGNIDKRGG-----------LYYAGSA----------------KP------------ 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 460 dkldVPIKFIWNYAGNTLINQhSDINKTHDILQdesKCEMIVVIDNFMTSSAKYADIVLPDLMTVEQEDIIPNDYAGNMG 539
Cdd:cd02755 329 ----YPIKALFIYRTNPFHSM-PDRARLIKALK---NLDLVVAIDILPSDTALYADVILPEATYLERDEPFSDKGGPAPA 400
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 540 YLIfLQPVTAPKFERKPIYWIMSEVAKRLGpdihqkftegrtqeqwlqylyakmlekdpklpsydelkkrgiykrkdpng 619
Cdd:cd02755 401 VAT-RQRAIEPLYDTRPGWDILKELARRLG-------------------------------------------------- 429
|
570 580 590
....*....|....*....|....*....|...
gi 2278930946 620 hfvaykkfrenpeanPLKTPSGKIEIYSSKLAE 652
Cdd:cd02755 430 ---------------LFGTPSGKIELYSPILAK 447
|
|
| MopB_Nitrate-R-NarG-like |
cd02750 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
54-568 |
5.38e-87 |
|
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: 283.44 E-value: 5.38e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 54 DTVVWGACSVNCGSRCALRLHVRDNEVYWVE--TD--NTGEDvYGDHQVRACLRGRSIRRRINHPDRLNYPMKRVGKRGE 129
Cdd:cd02750 1 DKVVRSTHGVNCTGSCSWNVYVKNGIVTREEqaTDypETPPD-LPDYNPRGCQRGASFSWYLYSPDRVKYPLKRVGARGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 130 GKFERITWDEALDTIAASLKDVVANYGNEAVYInySSGIVG-GNITRSSPYaslvaRLMNCYGG----FLSHYGTYSTAQ 204
Cdd:cd02750 80 GKWKRISWDEALELIADAIIDTIKKYGPDRVIG--FSPIPAmSMVSYAAGS-----RFASLIGGvslsFYDWYGDLPPGS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 205 iacamPYTYG-SNDGNSTSDIENTKLVVMFGNNPAETRMSGggiTYYLEQARERSnARMIVIDPRYTDTAAgREDEWIPI 283
Cdd:cd02750 153 -----PQTWGeQTDVPESADWYNADYIIMWGSNVPVTRTPD---AHFLTEARYNG-AKVVVVSPDYSPSAK-HADLWVPI 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 284 RPGTDAALVAGIAWVLIDENLVDQPFLDKYcvgydeKTLPegapanghYKAYilgqgddhtakTPEWASRITGIPADRIV 363
Cdd:cd02750 223 KPGTDAALALAMAHVIIKEKLYDEDYLKEY------TDLP--------FLVY-----------TPAWQEAITGVPRETVI 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 364 KLAREIGSAKPAYICQGWGPQRQANGELTSRAIAMLPILTGNVGNSGARESTYTitiermplpdnpvktqiscfswtdai 443
Cdd:cd02750 278 RLAREFATNGRSMIIVGAGINHWYHGDLCYRALILLLALTGNEGKNGGGWAHYV-------------------------- 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 444 argPEMTALrdgvrgkdkldvpikFIWnyaGNTLINQHsdiNKTHDILQD--ESKCEMIVVIDNFMTSSAKYADIVLPDL 521
Cdd:cd02750 332 ---GQPRVL---------------FVW---RGNLFGSS---GKGHEYFEDapEGKLDLIVDLDFRMDSTALYSDIVLPAA 387
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 2278930946 522 MTVEQEDIIPNDYAgnmGYLIFLQPVTAPKFERKPIYWIMSEVAKRL 568
Cdd:cd02750 388 TWYEKHDLSTTDMH---PFIHPFSPAVDPLWEAKSDWEIFKALAKKV 431
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
11-809 |
4.36e-80 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 273.08 E-value: 4.36e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 11 ISRRTLVKSTAIGSlALAAGGISLPFGLksaaAAVKHAVQPPEDTVVWGACSVnCGSRCALRLHVRDNEVYWVETDNTGE 90
Cdd:PRK15488 3 LSRRDFLKGAGAGC-AACALGSLLPGAL----AANEIAQLKGKTKLTPSICEM-CSTRCPIEARVVNGKNVFIQGNPKAK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 91 DVYGdhqvRACLRGRSIRRRINHPDRLNYPMKRVGKRGEGKFERITWDEALDTIAASLKDVVANYGNEAVYINYSSGIVG 170
Cdd:PRK15488 77 SFGT----KVCARGGSGHSLLYDPQRIVKPLKRVGERGEGKWQEISWDEAYQEIAAKLNAIKQQHGPESVAFSSKSGSLS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 171 GNITR-SSPYASlvarlMNCYGGFLSHYGTYstaQIAC-AMpytYGsndGNSTSDIENTKLVVMFGNNPAEtrmsggGI- 247
Cdd:PRK15488 153 SHLFHlATAFGS-----PNTFTHASTCPAGY---AIAAkVM---FG---GKLKRDLANSKYIINFGHNLYE------GIn 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 248 ---TYYLEQARERSNARMIVIDPRYTdTAAGREDEWIPIRPGTDAALVAGIAWVLIDENLVDQPFLDKYCVGYDEktlpe 324
Cdd:PRK15488 213 msdTRGLMTAQMEKGAKLVVFEPRFS-VVASKADEWHAIRPGTDLAVVLALCHVLIEENLYDKAFVERYTSGFEE----- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 325 gapanghYKAYIlgqgddhTAKTPEWASRITGIPADRIVKLAREIGSAKPAYICQgWGPQ---RQANGELTsRAIAMLPI 401
Cdd:PRK15488 287 -------LAASV-------KEYTPEWAEAISDVPADDIRRIARELAAAAPHAIVD-FGHRatfTPEEFDMR-RAIFAANV 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 402 LTGNVGNSG--------------ARESTY----TITIERMPlpdNPVKTQIscfswtDAIARGPEMTALRDGVRgKDKLD 463
Cdd:PRK15488 351 LLGNIERKGglyfgknasvynklAGEKVAptlaKPGVKGMP---KPTAKRI------DLVGEQFKYIAAGGGVV-QSIID 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 464 V-------PIKFIWNYAGNTLINQhSDINKTHDILQdesKCEMIVVIDNFMTSSAKYADIVLPDLMTVEQ-EDIipNDYA 535
Cdd:PRK15488 421 AtltqkpyQIKGWVMSRHNPMQTV-TDRADVVKALK---KLDLVVVCDVYLSESAAYADVVLPESTYLERdEEI--SDKS 494
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 536 G-NMGYLIfLQPVTAPKFERKPIYWIMSEVAKRLGPDihqKFTEGRTQEQWLQYlyakMLEKDPKLpsYDELKKRGiykr 614
Cdd:PRK15488 495 GkNPAYAL-RQRVVEPIGDTKPSWQIFKELGEKMGLG---QYYPWQDMETLQLY----QVNGDHAL--LKELKKKG---- 560
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 615 kdpnghFVAYKK---FREN----------PEANP------------LKTPSGKIEIYSSKLAEIAAtwelekdetisplp 669
Cdd:PRK15488 561 ------YVSFGVpllLREPkmvakfvaryPNAKAvdedgtygsqlkFKTPSGKIELFSAKLEALAP-------------- 620
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 670 vyastfdGWDAPERARFPL----QLFGFHFKA--RTHSSYGNVDVL-----KAAcrqeVWLNPVDAEKRGIKNGDTVRVF 738
Cdd:PRK15488 621 -------GYGVPRYRDVALkkedELYFIQGKVavHTNGATQNVPLLanlmsDNA----VWIHPQTAGKLGIKNGDEIRLE 689
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2278930946 739 NDRGEVRIEAKVTPRIMPGV--SAMGQGAWHDANMSGDRvdHGSCINTLTTHRPSPLAkGNPQHTNLVQIEKV 809
Cdd:PRK15488 690 NSVGKEKGKALVTPGIRPDTlfAYMGFGSKNKELTRATG--KGIHCGNLLPHVTSPVS-GTNVHTTGVTLSKA 759
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
116-567 |
4.47e-71 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 237.68 E-value: 4.47e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 116 RLNYPMKRvgkRGEGKFERITWDEALDTIAASLKDVVANYGNEAVYINYSSGivGGNITRSSPYAS-LVARLMNCYGGFL 194
Cdd:pfam00384 1 RLKYPMVR---RGDGKFVRVSWDEALDLIAKKLKRIIKKYGPDAIAINGGSG--GLTDVESLYALKkLLNRLGSKNGNTE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 195 SHYGTYSTAQIACA-MPYTYGSNDGNSTSDIENTKLVVMFGNNPAETRMSGGGITYyleQARERSNARMIVIDPRYTdta 273
Cdd:pfam00384 76 DHNGDLCTAAAAAFgSDLRSNYLFNSSIADIENADLILLIGTNPREEAPILNARIR---KAALKGKAKVIVIGPRLD--- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 274 AGREDEWIPIRPGTDAALVAGIAWVLIDENLVDQPFLDKycvgydektlpegapanghykayilgqgddhtaktpewasr 353
Cdd:pfam00384 150 LTYADEHLGIKPGTDLALALAGAHVFIKELKKDKDFAPK----------------------------------------- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 354 itgipadrivklareigsakpAYICQGWGPQRQANGELTSRAIAMLPILTGNVGNSGARESTYTI---TIERMPLPDNPV 430
Cdd:pfam00384 189 ---------------------PIIIVGAGVLQRQDGEAIFRAIANLADLTGNIGRPGGGWNGLNIlqgAASPVGALDLGL 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 431 KTQISCFSWTDAIARGPemtalrdgvrgkdkldvpiKFIWNYAGNTLINQHSDINKTHDILQdesKCEMIVVIDNFM-TS 509
Cdd:pfam00384 248 VPGIKSVEMINAIKKGG-------------------IKVLYLLGNNPFVTHADENRVVKALQ---KLDLFVVYDGHHgDK 305
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2278930946 510 SAKYADIVLPDLMTVEQEDIIPNDyagnMGYLIFLQPVTAPKFERKPIYWIMSEVAKR 567
Cdd:pfam00384 306 TAKYADVILPAAAYTEKNGTYVNT----EGRVQSTKQAVPPPGEAREDWKILRALSEV 359
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
65-580 |
7.10e-69 |
|
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to nitrite. Monomeric Nas is located in the cytoplasm and participates in nitrogen assimilation. Dimeric Nap is located in the periplasm and is coupled to quinol oxidation via a membrane-anchored tetraheme cytochrome. Members of the MopB_Nitrate-R-NapA CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239155 [Multi-domain] Cd Length: 565 Bit Score: 237.89 E-value: 7.10e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 65 CGSRCALRLHVRDNEVYWVETDNtgedvygDHQV---RACLRGRSIRRRINHPDRLNYPMKRvgkRGEGKFERITWDEAL 141
Cdd:cd02754 7 CGVGCGVEIGVKDGKVVAVRGDP-------EHPVnrgRLCIKGLNLHKTLNGPERLTRPLLR---RNGGELVPVSWDEAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 142 DTIAASLKDVVANYGNEAVYInYSSGivggNITRSSPYAslVARLMNcyGGFLS-HYGTYST---AQIACAMPYTYGSnD 217
Cdd:cd02754 77 DLIAERFKAIQAEYGPDSVAF-YGSG----QLLTEEYYA--ANKLAK--GGLGTnNIDTNSRlcmASAVAGYKRSFGA-D 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 218 G--NSTSDIENTKLVVMFGNNPAETRmsggGITY-YLEQARE-RSNARMIVIDPRYTDTAAgREDEWIPIRPGTDAALVA 293
Cdd:cd02754 147 GppGSYDDIEHADCFFLIGSNMAECH----PILFrRLLDRKKaNPGAKIIVVDPRRTRTAD-IADLHLPIRPGTDLALLN 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 294 GIAWVLIDENLVDQPFLDKYCVGYDEKTlpegapanghykayilgqgdDHTAK-TPEWASRITGIPADRIVKLAREIGSA 372
Cdd:cd02754 222 GLLHVLIEEGLIDRDFIDAHTEGFEELK--------------------AFVADyTPEKVAEITGVPEADIREAARLFGEA 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 373 KPAYICQGWGPQRQANGELTSRAIAMLPILTGNVG-------------NS-GARESTYTIT------------------- 419
Cdd:cd02754 282 RKVMSLWTMGVNQSTQGTAANNAIINLHLATGKIGrpgsgpfsltgqpNAmGGREVGGLANllpghrsvnnpehraevak 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 420 ---IERMPLPDNPVKTQISCFswtDAIARGpemtalrdgvrgkdkldvPIKFIWNYAGNTLinqHS--DINKTHDILQde 494
Cdd:cd02754 362 fwgVPEGTIPPKPGLHAVEMF---EAIEDG------------------EIKALWVMCTNPA---VSlpNANRVREALE-- 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 495 sKCEMIVVIDNFMTS-SAKYADIVLPDLMTVEQEDIIpndyaGNM-GYLIFLQPVTAPKFERKPIYWIMSEVAKRLGP-- 570
Cdd:cd02754 416 -RLEFVVVQDAFADTeTAEYADLVLPAASWGEKEGTM-----TNSeRRVSLLRAAVEPPGEARPDWWILADVARRLGFge 489
|
570 580
....*....|....*....|.
gi 2278930946 571 -----------DIHQKFTEGR 580
Cdd:cd02754 490 lfpytspeevfEEYRRLSRGR 510
|
|
| MopB_Arsenate-R |
cd02757 |
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ... |
64-652 |
4.08e-68 |
|
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other related proteins. These members belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239158 [Multi-domain] Cd Length: 523 Bit Score: 234.64 E-value: 4.08e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 64 NCGSRCALRLHVRDNEVYWVEtdntGEDVYGDHQVRACLRGRSIRRRINHPDRLNYPMKRVGKRG----EGKFERITWDE 139
Cdd:cd02757 8 GCTAWCGLQAYVEDGRVTKVE----GNPLHPGSRGRLCAKGHLGLQQVYDPDRILYPMKRTNPRKgrdvDPKFVPISWDE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 140 ALDTIAASLKDVVANygNEAVYINYSSGIVGGNitrsspYASLVARLMNCYG--GFLSHYGTYSTAQiACAMPYTYGSND 217
Cdd:cd02757 84 ALDTIADKIRALRKE--NEPHKIMLHRGRYGHN------NSILYGRFTKMIGspNNISHSSVCAESE-KFGRYYTEGGWD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 218 GNStSDIENTKLVVMFGNNPAEtrmSGGGITYYLEQARERSN-ARMIVIDPRYTDTAAgREDEWIPIRPGTDAALVAGIA 296
Cdd:cd02757 155 YNS-YDYANAKYILFFGADPLE---SNRQNPHAQRIWGGKMDqAKVVVVDPRLSNTAA-KADEWLPIKPGEDGALALAIA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 297 WVLIDENLVDQPFLDKYCVGYD----EKTLPEGAPANGHYKAYILGQGDDHTAKTPEWASRITGIPADRIVKLAREIGSA 372
Cdd:cd02757 230 HVILTEGLWDKDFVGDFVDGKNyfkaGETVDEESFKEKSTEGLVKWWNLELKDYTPEWAAKISGIPAETIERVAREFATA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 373 KPAYICQGW-GPQRQANGELTSRAIAMLPILTGNVGNSGARES-TYTITIERM-PLPDNPVKTQISCFSWTDAIArgpem 449
Cdd:cd02757 310 APAAAAFTWrGATMQNRGSYNSMACHALNGLVGSIDSKGGLCPnMGVPKIKVYfTYLDNPVFSNPDGMSWEEALA----- 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 450 talrdgvrgkdklDVPIkfiwnyagntlinqhsdinkthdilqdeskcemIVVIDNFMTSSAKYADIVLPDLMTVEQEDI 529
Cdd:cd02757 385 -------------KIPF---------------------------------HVHLSPFMSETTYFADIVLPDGHHFERWDV 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 530 IPNdYAGNMGYLIFLQPVTAPKFERKPIYWIMSEVAKRLGPDIHqkftegrtqEQWLQYLYAKMLEKDPklpsydelkkr 609
Cdd:cd02757 419 MSQ-ENNLHPWLSIRQPVVKSLGEVREETEILIELAKKLDPKGS---------DGMKRYAPGQFKDPET----------- 477
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 2278930946 610 giykrKDPNGHfvaykKFrenpeANPLKTPSGKIEIYSSKLAE 652
Cdd:cd02757 478 -----GKNNRW-----EF-----ENVFPTETGKFEFYSETLKK 505
|
|
| MopB_CT_DmsA-EC |
cd02794 |
The MopB_CT_DmsA-EC CD includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
686-808 |
3.88e-66 |
|
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: 215.23 E-value: 3.88e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 686 FPLQLFGFHFKARTHSSYGNVDVLKAACRQEVWLNPVDAEKRGIKNGDTVRVFNDRGEVRIEAKVTPRIMPGVSAMGQGA 765
Cdd:cd02794 1 YPLQLIGWHYKRRTHSTFDNVPWLREAFPQEVWINPLDAAARGIKDGDRVLVFNDRGKVIRPVKVTERIMPGVVALPQGA 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2278930946 766 WHDanMSGDRVDHGSCINTLTTHRPSPLAKGNPQHTNLVQIEK 808
Cdd:cd02794 81 WYE--PDANGIDKGGCINTLTGLRPSPLAKGNPQHTNLVQVEK 121
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
65-569 |
8.12e-63 |
|
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: 219.78 E-value: 8.12e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 65 CGSRCALRLHVRDNEVYWVEtdntGEDVYGDHQVRACLRGRSIRRRINHPDRLNYPMKRVgkrgEGKFERITWDEALDTI 144
Cdd:cd02753 7 CGVGCGLELWVKDNKIVGVE----PVKGHPVNRGKLCVKGRFGFDFVNSKDRLTKPLIRK----NGKFVEASWDEALSLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 145 AASLKDVVANYGNEAVYinyssGIVGGNITRSSPYasLVARLM----------NCyggflSHYGTYSTAQiacAMPYTYG 214
Cdd:cd02753 79 ASRLKEIKDKYGPDAIA-----FFGSAKCTNEENY--LFQKLAravggtnnvdHC-----ARLCHSPTVA---GLAETLG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 215 SN-DGNSTSDIENTKLVVMFGNNPAETRMSgggITYYLEQARERSnARMIVIDPRYTDTAAgREDEWIPIRPGTDAALVA 293
Cdd:cd02753 144 SGaMTNSIADIEEADVILVIGSNTTEAHPV---IARRIKRAKRNG-AKLIVADPRRTELAR-FADLHLQLRPGTDVALLN 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 294 GIAWVLIDENLVDQPFLDKYCVGYDEKTLpegapangHYKAYilgqgddhtakTPEWASRITGIPADRIVKLAREIGSAK 373
Cdd:cd02753 219 AMAHVIIEEGLYDEEFIEERTEGFEELKE--------IVEKY-----------TPEYAERITGVPAEDIREAARMYATAK 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 374 PAYICQGWGPQRQANGELTSRAIAMLPILTGNVGNSGARestytitieRMPLP-DNPVktQISCfswtdaiargpEMTAL 452
Cdd:cd02753 280 SAAILWGMGVTQHSHGTDNVMALSNLALLTGNIGRPGTG---------VNPLRgQNNV--QGAC-----------DMGAL 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 453 RDgvrgkdklDVP--IKFIWNYAGNTLINqHSDINKTHDILqdeSKCEMIVVIDNFMTSSAKYADIVLPDLMTVEQEDII 530
Cdd:cd02753 338 PN--------VLPgyVKALYIMGENPALS-DPNTNHVRKAL---ESLEFLVVQDIFLTETAELADVVLPAASFAEKDGTF 405
|
490 500 510
....*....|....*....|....*....|....*....
gi 2278930946 531 PNdyagNMGYLIFLQPVTAPKFERKPIYWIMSEVAKRLG 569
Cdd:cd02753 406 TN----TERRVQRVRKAVEPPGEARPDWEIIQELANRLG 440
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
61-655 |
1.91e-57 |
|
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: 205.71 E-value: 1.91e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 61 CSVNCGsrcaLRLHVRDNEVYWVETDNtgedvygDHQVRA---CLRGRSIRRRINHPDRLNYPMKRVGkrgeGKFERITW 137
Cdd:cd02762 7 CEANCG----LVVTVEDGRVASIRGDP-------DDPLSKgyiCPKAAALGDYQNDPDRLRTPMRRRG----GSFEEIDW 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 138 DEALDTIAASLKDVVANYGNEAVyinyssGIVGGNitrssPYASLVARLMncYGGFL------SHYGTYSTAQiacAMP- 210
Cdd:cd02762 72 DEAFDEIAERLRAIRARHGGDAV------GVYGGN-----PQAHTHAGGA--YSPALlkalgtSNYFSAATAD---QKPg 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 211 -----YTYGSNDGNSTSDIENTKLVVMFGNNPAETR---MSGGGITYYLEQARERSnARMIVIDPRYTDTAAgREDEWIP 282
Cdd:cd02762 136 hfwsgLMFGHPGLHPVPDIDRTDYLLILGANPLQSNgslRTAPDRVLRLKAAKDRG-GSLVVIDPRRTETAK-LADEHLF 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 283 IRPGTDAALVAGIAWVLIDENLVDQPFLDKYCVGYDektlpegapangHYKAYIlgqgddhTAKTPEWASRITGIPADRI 362
Cdd:cd02762 214 VRPGTDAWLLAAMLAVLLAEGLTDRRFLAEHCDGLD------------EVRAAL-------AEFTPEAYAPRCGVPAETI 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 363 VKLAREIGSAKPAYICQGWGPQRQANGELTSRAIAMLPILTGNVGnsgaRESTYTITIERMPLPDNPVKTQISCFSWTDA 442
Cdd:cd02762 275 RRLAREFAAAPSAAVYGRLGVQTQLFGTLCSWLVKLLNLLTGNLD----RPGGAMFTTPALDLVGQTSGRTIGRGEWRSR 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 443 IARGPEMTALRDGVRGKDKLDVP----IKFIWNYAGNTLinqHS--DINKTHDILQdesKCEMIVVIDNFMTSSAKYADI 516
Cdd:cd02762 351 VSGLPEIAGELPVNVLAEEILTDgpgrIRAMIVVAGNPV---LSapDGARLEAALG---GLEFMVSVDVYMTETTRHADY 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 517 VLPDLMTVEQEDIipnDYAGnmgyliFLQPVTAPKFeRKPIywimsevakrLGPdihqkftEGRTQEQWlqYLYAKMLEK 596
Cdd:cd02762 425 ILPPASQLEKPHA---TFFN------LEFPRNAFRY-RRPL----------FPP-------PPGTLPEW--EILARLVEA 475
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2278930946 597 dpklpsYDELKKRGIYkrKDPNGHFVAYKKFRENP-----------EANPLKTPSGKIEIYSSK-LAEIAA 655
Cdd:cd02762 476 ------LDAVLRAGFY--GERAGGTLLLAALLERPsgvdlgpltprLWQRLRTPDGRIHLAPPElLDELRR 538
|
|
| MopB_CT_DMSOR-like |
cd02777 |
The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
686-808 |
9.05e-55 |
|
The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide reductase (BSOR), trimethylamine N-oxide reductase (TMAOR) and other related proteins. DMSOR always catalyzes the reduction of DMSO to dimethylsulfide, but its cellular location and oligomerization state are organism-dependent. For example, in Rhodobacter sphaeriodes and Rhodobacter capsulatus, it is an 82-kDa monomeric soluble protein found in the periplasmic space; in E. coli, it is membrane-bound and exists as a heterotrimer. BSOR catalyzes the reduction of biotin sulfixode to biotin, and is unique among Mo enzymes because no additional auxiliary proteins or cofactors are required. TMAOR is similar to DMSOR, but its only natural substrate is TMAO. Also included in this group is the pyrogallol-phloroglucinol transhydroxylase from Pelobacter acidigallici. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239178 [Multi-domain] Cd Length: 127 Bit Score: 184.71 E-value: 9.05e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 686 FPLQLFGFHFKARTHSSYGNVDVLKAAC----RQEVWLNPVDAEKRGIKNGDTVRVFNDRGEVRIEAKVTPRIMPGVSAM 761
Cdd:cd02777 1 YPLQLISPHPKRRLHSQLDNVPWLREAYkvkgREPVWINPLDAAARGIKDGDIVRVFNDRGAVLAGARVTDRIMPGVVAL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2278930946 762 GQGAWHDAnMSGDRVDHGSCINTLTTHRPSP-LAKGNPQHTNLVQIEK 808
Cdd:cd02777 81 PEGAWYDP-DDNGGLDKGGNPNVLTSDIPTSkLAQGNPANTCLVEIEK 127
|
|
| MopB_2 |
cd02763 |
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
65-569 |
1.78e-44 |
|
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins
Pssm-ID: 239164 [Multi-domain] Cd Length: 679 Bit Score: 171.17 E-value: 1.78e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 65 CGSRCALRLHVRDNEVYWVEtdntGEDvygDHQVRA---CLRGRSIRRRINHPDRLNYPMKRVGKRGEGKFERITWDEAL 141
Cdd:cd02763 7 CACRCGIRVHLRDGKVRYIK----GNP---DHPLNKgviCAKGSSGIMKQYSPARLTKPLLRKGPRGSGQFEEIEWEEAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 142 DTIAASLKDVVAnygneavyinyssgivggniTRSSPYASLVAR--LMNCYGGFLSHYGT--------YSTAQIACAMPY 211
Cdd:cd02763 80 SIATKRLKAARA--------------------TDPKKFAFFTGRdqMQALTGWFAGQFGTpnyaahggFCSVNMAAGGLY 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 212 TYGSNDGN-STSDIENTKLVVMFG------NNPAETRMsgggityyleQARERSNARMIVIDPRYTDTAAgREDEWIPIR 284
Cdd:cd02763 140 SIGGSFWEfGGPDLEHTKYFMMIGvaedhhSNPFKIGI----------QKLKRRGGKFVAVNPVRTGYAA-IADEWVPIK 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 285 PGTDAALVAGIAWVLIDENLVDQPFLDKYcvgydektlpEGAPANGHYkayilgqgddhtakTPEWASRITGIPADRIVK 364
Cdd:cd02763 209 PGTDGAFILALAHELLKAGLIDWEFLKRY----------TNAAELVDY--------------TPEWVEKITGIPADTIRR 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 365 LAREIGSAK-------PAYICQGWGPQRQ------------------ANGELTSRAIAMLPILTGNVGNSGA--RESTYT 417
Cdd:cd02763 265 IAKELGVTArdqpielPIAWTDVWGRKHEkitgrpvsfhamrgiaahSNGFQTIRALFVLMMLLGTIDRPGGfrHKPPYP 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 418 ITIERMPLP--------------------------------DNPVKTQiSCFSWTDAIA-RGPEMTALRDGVRGKdklDV 464
Cdd:cd02763 345 RHIPPLPKPpkipsadkpftplygpplgwpaspddllvdedGNPLRID-KAYSWEYPLAaHGCMQNVITNAWRGD---PY 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 465 PIKFIWNYAGNTLINQHSDINKTHDILQD-----ESKCEMIVVIDNFMTSSAKYADIVLPDLMTVEQEDII------PND 533
Cdd:cd02763 421 PIDTLMIYMANMAWNSSMNTPEVREMLTDkdasgNYKIPFIIVCDAFYSEMVAFADLVLPDTTYLERHDAMslldrpISE 500
|
570 580 590
....*....|....*....|....*....|....*.
gi 2278930946 534 YAGNMGYLifLQPVTAPKFERKPIYWIMSEVAKRLG 569
Cdd:cd02763 501 ADGPVDAI--RVPIVEPKGDVKPFQEVLIELGTRLG 534
|
|
| MopB_Formate-Dh-Na-like |
cd02752 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
55-569 |
1.17e-42 |
|
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate respiration in bacteria such as in the E. coli formate dehydrogenase N (Fdh-N). Fdh-N is a membrane protein that is a complex of three different subunits and is the major electron donor to the nitrate respiratory chain. Also included in this CD is the Desulfovibrio gigas tungsten formate dehydrogenase, DgW-FDH. In contrast to Fdh-N, which is a functional heterotrimer, DgW-FDH is a heterodimer. The DgW-FDH complex is composed of a large subunit carrying the W active site and one [4Fe-4S] center, and a small subunit that harbors a series of three [4Fe-4S] clusters as well as a putative vacant binding site for a fourth cluster. The smaller subunit is not included in this alignment. Members of the MopB_Formate-Dh-Na-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239153 [Multi-domain] Cd Length: 649 Bit Score: 165.27 E-value: 1.17e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 55 TVVWGACSVNCGsrcaLRLHVRDNEVYWVETDNtgedvygDHQVR---ACLRGRSIRRRINHPDRLNYPMKRVGkrGEGK 131
Cdd:cd02752 1 RTICPYCSVGCG----LIAYVQNGVWVHQEGDP-------DHPVNrgsLCPKGAALRDFVHSPKRLKYPMYRAP--GSGK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 132 FERITWDEALDTIAASLKD-------------VVANyGNEAVYINYSSGIvggnitrSSPYASLVARLMNCYG-GFLSHY 197
Cdd:cd02752 68 WEEISWDEALDEIARKMKDirdasfveknaagVVVN-RPDSIAFLGSAKL-------SNEECYLIRKFARALGtNNLDHQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 198 GT--YSTAQIACAMPYTYGSNDgNSTSDIENTKLVVMFGNNPAETRMSGggiTYYLEQARERSNARMIVIDPRYTDTAAg 275
Cdd:cd02752 140 ARiuHSPTVAGLANTFGRGAMT-NSWNDIKNADVILVMGGNPAEAHPVS---FKWILEAKEKNGAKLIVVDPRFTRTAA- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 276 REDEWIPIRPGTDAALVAGIAWVLIdenlvdqpfldKYcvgydektlpegapanghykayilgqgddhtakTPEWASRIT 355
Cdd:cd02752 215 KADLYVPIRSGTDIAFLGGMINYII-----------RY---------------------------------TPEEVEDIC 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 356 GIPADRIVKLAREIGS----AKPAYI--CQGWgpQRQANGELTSRAIAMLPILTGNVGNSGArestytitiermplpdnp 429
Cdd:cd02752 251 GVPKEDFLKVAEMFAAtgrpDKPGTIlyAMGW--TQHTVGSQNIRAMCILQLLLGNIGVAGG------------------ 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 430 vktqiscfswtdaiargpEMTALR--DGVRGKDKLDVpikfIWN-----YAGNTLINQHSDINKTHDILqdeSKCEMIVV 502
Cdd:cd02752 311 ------------------GVNALRghSNVQGATDLGL----LSHnlpgyLGGQNPNSSFPNANKVRRAL---DKLDWLVV 365
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 503 IDNFMTSSAKYAD-------------IVLPDLMTVEQEDIIPN-DYAGNMGYliflqPVTAPKFERKPIYWIMSEVAKRL 568
Cdd:cd02752 366 IDPFPTETAAFWKnpgmdpksiqtevFLLPAACQYEKEGSITNsGRWLQWRY-----KVVEPPGEAKSDGDILVELAKRL 440
|
.
gi 2278930946 569 G 569
Cdd:cd02752 441 G 441
|
|
| MopB_Tetrathionate-Ra |
cd02758 |
The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other ... |
99-569 |
1.28e-35 |
|
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: 144.79 E-value: 1.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 99 RACLRGRSIRRRINHPDRLNYPMKRVGKRGEGKFERITWDEALDTI----------------AASLKDVVAN-----YG- 156
Cdd:cd02758 66 TACARGNAGLQYLYDPYRVLQPLKRVGPRGSGKWKPISWEQLIEEVveggdlfgeghveglkAIRDLDTPIDpdhpdLGp 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 157 --NEAVYINyssgivggniTRSSPYASLVARLM-NCYG--GFLSHyGTYstaqiaCAMPYTYGS------NDGNS--TSD 223
Cdd:cd02758 146 kaNQLLYTF----------GRDEGRTPFIKRFAnQAFGtvNFGGH-GSY------CGLSYRAGNgalmndLDGYPhvKPD 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 224 IENTKLVVMFGNNPAE-----TRMSGggityYLEQARERSNARMIVIDPRY--TDTAAGREDEWIPIRPGTDAALVAGIA 296
Cdd:cd02758 209 FDNAEFALFIGTSPAQagnpfKRQAR-----RLAEARTEGNFKYVVVDPVLpnTTSAAGENIRWVPIKPGGDGALAMAMI 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 297 WVLIDENlvdqpfldkycvGYDEKTL----PEGAPANGhykaYILGQGDDH-----TAKTP--------------EWAsR 353
Cdd:cd02758 284 RWIIENE------------RYNAEYLsipsKEAAKAAG----EPSWTNATHlvitvRVKSAlqllkeeafsysleEYA-E 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 354 ITGIPADRIVKLAREIGSA--KPAYICQgwGPQRQANGELTSRAIAMLPILTGNV---------------GNSGARE--- 413
Cdd:cd02758 347 ICGVPEAKIIELAKEFTSHgrAAAVVHH--GGTMHSNGFYNAYAIRMLNALIGNLnwkggllmsgggfadNSAGPRYdfk 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 414 --------STYTITIERMPLPDNP-----VKTQISCF----SWTD-AIARGPEM-TALRDGvrgkdkLDVPIKFIWNYAG 474
Cdd:cd02758 425 kffgevkpWGVPIDRSKKAYEKTSeykrkVAAGENPYpakrPWYPlTPELYTEViASAAEG------YPYKLKALILWMA 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 475 NTLINQHSDINKTHDILQDESKCEMIVVIDNFMTSSAKYADIVLPDLMTVEQEDIipndyAGNMGYLIFL-----QPVTA 549
Cdd:cd02758 499 NPVYGAPGLVKQVEEKLKDPKKLPLFIAIDAFINETSAYADYIVPDTTYYESWGF-----STPWGGVPTKastarWPVIA 573
|
570 580
....*....|....*....|....*.
gi 2278930946 550 PKFERK----PIY-WIMS-EVAKRLG 569
Cdd:cd02758 574 PLTEKTanghPVSmESFLiDLAKALG 599
|
|
| MopB_CT_DMSOR-BSOR-TMAOR |
cd02793 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
686-808 |
7.39e-33 |
|
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: 123.13 E-value: 7.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 686 FPLQLFGFHFKARTHSSYGNVDVLKAAC---RQEVWLNPVDAEKRGIKNGDTVRVFNDRGEVRIEAKVTPRIMPGVSAMG 762
Cdd:cd02793 1 YPLHLLSNQPATRLHSQLDHGSLSRAYKvqgREPIRINPADAAARGIADGDIVRVFNDRGACLAGAVVTDGIMPGVVQLP 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2278930946 763 QGAWHDANMSGDRVD---HGsCINTLTTHRP-SPLAKGNPQHTNLVQIEK 808
Cdd:cd02793 81 TGAWYDPDDPGEPGPlckHG-NPNVLTLDIGtSSLAQGCSAQTCLVQIEK 129
|
|
| MopB_ydeP |
cd02767 |
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
116-411 |
4.97e-32 |
|
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: 132.05 E-value: 4.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 116 RLNYPMKRvgKRGEGKFERITWDEALDTIAASLKdvvANYGNEAVYinYSSGivggnitRSSPYASLVARL-MNCYG--- 191
Cdd:cd02767 64 RLTYPMRY--DAGSDHYRPISWDEAFAEIAARLR---ALDPDRAAF--YTSG-------RASNEAAYLYQLfARAYGtnn 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 192 ----GFLSHYGTystaqiACAMPYTYGSndGNST---SDIENTKLVVMFGNNPAET--RMsgggiTYYLEQARERSnARM 262
Cdd:cd02767 130 lpdcSNMCHEPS------SVGLKKSIGV--GKGTvslEDFEHTDLIFFIGQNPGTNhpRM-----LHYLREAKKRG-GKI 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 263 IVIDP-------RYTDTAAGRE---------DEWIPIRPGTDAALVAGIAWVLIDE-----NLVDQPFLDKYCVGYDEkt 321
Cdd:cd02767 196 IVINPlrepgleRFANPQNPESmltggtkiaDEYFQVRIGGDIALLNGMAKHLIERddepgNVLDHDFIAEHTSGFEE-- 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 322 lpegapanghYKAYILGQgddhtaktpEWAS--RITGIPADRIVKLAREIGSAKPAYICQGWGPQRQANGELTSRAIAML 399
Cdd:cd02767 274 ----------YVAALRAL---------SWDEieRASGLSREEIEAFAAMYAKSERVVFVWGMGITQHAHGVDNVRAIVNL 334
|
330
....*....|..
gi 2278930946 400 PILTGNVGNSGA 411
Cdd:cd02767 335 ALLRGNIGRPGA 346
|
|
| Molydop_binding |
pfam01568 |
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
688-803 |
2.13e-27 |
|
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: 106.97 E-value: 2.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 688 LQLFGFHFKARTHSSYGNVDVLKAACRQE--VWLNPVDAEKRGIKNGDTVRVFNDRGEVRIEAKVTPRIMPGVSAMGQGA 765
Cdd:pfam01568 1 LYLITGRVLGQYHSQTRTRRVLRLAKPEPevVEIHPEDAAALGIKDGDLVEVTSRRGSVVVRAKVTDRVRPGVVFMPFGW 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 2278930946 766 WHDAnmsgdrvdHGSCINTLTTHRPSPLAKGNPQHTNL 803
Cdd:pfam01568 81 WYEP--------RGGNANALTDDATDPLSGGPEFKTCA 110
|
|
| MopB_CT |
cd02775 |
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a ... |
696-800 |
2.61e-26 |
|
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a large, diverse, heterogeneous superfamily of enzymes that, in general, bind molybdopterin as a cofactor. The MopB domain is found in a wide variety of molybdenum- and tungsten-containing enzymes, including formate dehydrogenase-H (Fdh-H) and -N (Fdh-N), several forms of nitrate reductase (Nap, Nas, NarG), dimethylsulfoxide reductase (DMSOR), thiosulfate reductase, formylmethanofuran dehydrogenase, and arsenite oxidase. Molybdenum is present in most of these enzymes in the form of molybdopterin, a modified pterin ring with a dithiolene side chain, which is responsible for ligating the Mo. In many bacterial and archaeal species, molybdopterin is in the form of a dinucleotide, with two molybdopterin dinucleotide units per molybdenum. These proteins can function as monomers, heterodimers, or heterotrimers, depending on the protein and organism. Also included in the MopB superfamily is the eukaryotic/eubacterial protein domain family of the 75-kDa subunit/Nad11/NuoG (second domain) of respiratory complex 1/NADH-quinone oxidoreductase which is postulated to have lost an ancestral formate dehydrogenase activity and only vestigial sequence evidence remains of a molybdopterin binding site. This hierarchy is of the conserved MopB_CT domain present in many, but not all, MopB homologs.
Pssm-ID: 239176 [Multi-domain] Cd Length: 101 Bit Score: 103.55 E-value: 2.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 696 KARTHSSY-GNVDVLKAACRQE-VWLNPVDAEKRGIKNGDTVRVFNDRGEVRIEAKVTPRIMPGVSAMGQGAWHdanmsg 773
Cdd:cd02775 2 RDHFHSGTrTRNPWLRELAPEPvVEINPEDAAALGIKDGDLVRVESRRGSVVLRAKVTDGVPPGVVFLPHGWGH------ 75
|
90 100
....*....|....*....|....*..
gi 2278930946 774 dRVDHGSCINTLTTHRPSPLAKGNPQH 800
Cdd:cd02775 76 -RGGRGGNANVLTPDALDPPSGGPAYK 101
|
|
| MopB_Phenylacetyl-CoA-OR |
cd02760 |
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large ... |
64-569 |
1.08e-25 |
|
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large subunit (PadB2), and other related proteins. The phenylacetyl-CoA:acceptor oxidoreductase has been characterized as a membrane-bound molybdenum-iron-sulfur enzyme involved in anaerobic metabolism of phenylalanine in the denitrifying bacterium Thauera aromatica. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239161 [Multi-domain] Cd Length: 760 Bit Score: 113.53 E-value: 1.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 64 NCGSRCALRLH-VRDNEVYWVETDNTGEDVYgDHQVRACLRGRSIRRRINHPDRLNYPMKRVG-KRGEGK---FERITWD 138
Cdd:cd02760 6 NCVAGPDFMAVkVVDGVATEIEPNFAAEDIH-PARGRVCVKAYGLVQKTYNPNRVLQPMKRTNpKKGRNEdpgFVPISWD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 139 EALDTIAASLKDV-VANYGNEAVYINYSSGIVGGNITrsspyaslvARLMNCYGGFLSHYGT----YSTAQIAC--AMPY 211
Cdd:cd02760 85 EALDLVAAKLRRVrEKGLLDEKGLPRLAATFGHGGTP---------AMYMGTFPAFLAAWGPidfsFGSGQGVKcvHSEH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 212 TYGSNDGNSTS---DIENTKLVVMFGNNpaeTRMSGGGITYYLE-QARERSnARMIVIDPRYTDTAAgREDEWIPIRPGT 287
Cdd:cd02760 156 LYGEFWHRAFTvaaDTPLANYVISFGSN---VEASGGPCAVTRHaDARVRG-YKRVQVEPHLSVTGA-CSAEWVPIRPKT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 288 DAALVAGIAWVLIDE---NLVDQPFL-DK----YCVGYDEKTLPEgaPANG----------------HYKAYILGQGD-- 341
Cdd:cd02760 231 DPAFMFAMIHVMVHEqglGKLDVPFLrDRtsspYLVGPDGLYLRD--AATGkplvwdersgravpfdTRGAVPAVAGDfa 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 342 -----------------------------DHTAK-TPEWASRITGIPADRIVKLARE------IGSA----------KPA 375
Cdd:cd02760 309 vdgavsvdaddetaihqgvegttaftmlvEHMRKyTPEWAESICDVPAATIRRIAREflenasIGSTievdgvtlpyRPV 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 376 YICQGWGPQRQANGELTSRAIAMLPILTGNVGNSGAREST-------------------------YTITIERMPLPDNPV 430
Cdd:cd02760 389 AVTLGKSVNNGWGAFECCWARTLLATLVGALEVPGGTLGTtvrlnrphddrlasvkpgedgfmaqGFNPTDKEHWVVKPT 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 431 KTQISCF--------SWTDAIarGPEMTA---LRDgVRGKDKLDVPIK-FIW-NYAGNTLINqhsdINKTHDILQDESKC 497
Cdd:cd02760 469 GRNAHRTlvpivgnsAWSQAL--GPTQLAwmfLRE-VPLDWKFELPTLpDVWfNYRTNPAIS----FWDTATLVDNIAKF 541
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2278930946 498 EMIVVIDNFMTSSAKYADIVLPDLMTVEQEDII---PNDYAGNMGY---LIFLQPVTAPKFERKPIYWIMSEVAKRLG 569
Cdd:cd02760 542 PFTVSFAYTEDETNWMADVLLPEATDLESLQMIkvgGTKFVEQFWEhrgVVLRQPAVEPQGEARDFTWISTELAKRTG 619
|
|
| MopB_CT_4 |
cd02785 |
The MopB_CT_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
685-809 |
2.83e-22 |
|
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: 92.81 E-value: 2.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 685 RFPLQLFGFHFKARTHSSYGNVDVLKAACRQ-EVWLNPVDAEKRGIKNGDTVRVFNDRGEVRIEAKVTPRIMPGVSAMGQ 763
Cdd:cd02785 1 KYPLACIQRHSRFRVHSQFSNVPWLLELQPEpRVKINPIDAAARGIAHGDLVEVYNDRGSVVCKAKVDDGIQPGVVTAEQ 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2278930946 764 GAWHDANMSGDrvdhgscINTLTTHRPSPLAKGNPQ-----HTNLVQIEKV 809
Cdd:cd02785 81 GWWSRYFQEGS-------LQDLTSPFVNPVHEYIYGpnsafYDTLVEVRKA 124
|
|
| PRK14991 |
PRK14991 |
tetrathionate reductase subunit TtrA; |
100-767 |
4.38e-22 |
|
tetrathionate reductase subunit TtrA;
Pssm-ID: 237883 [Multi-domain] Cd Length: 1031 Bit Score: 102.38 E-value: 4.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 100 ACLRGRSIRRRINHPDRLNYPMKRVGKRGEGKFERITWDEALDTIA--------------ASLKDVV-----AN--YG-- 156
Cdd:PRK14991 141 ACARGNAMLEQLDSPYRVLQPLKRVGKRGSGKWQRISFEQLVEEVVeggdlfgeghvdglRAIRDLDtpidaKNpeYGpk 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 157 -NEAVYINyssgivGGNITRsspyASLVARLM-NCYGGF-LSHYGTYstaqiaCAMPYTYGSN------DGNS--TSDIE 225
Cdd:PRK14991 221 aNQLLVTN------ASDEGR----DAFIKRFAfNSFGTRnFGNHGSY------CGLAYRAGSGalmgdlDKNPhvKPDWD 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 226 NTKLVVMFGNNPAEtrmSGGGityYLEQARERSNARM------IVIDPR---YTDTAAGREDEWIPIRPGTDAALVAG-I 295
Cdd:PRK14991 285 NVEFALFIGTSPAQ---SGNP---FKRQARQLANARTrgnfeyVVVAPAlplSSSLAAGDNNRWLPIRPGTDSALAMGmI 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 296 AWVlIDENLVDQPFLD--------------------------------KYCVGYDEKTLPEGAPANGHYKAYILGQGD-- 341
Cdd:PRK14991 359 RWI-IDNQRYNADYLAqpgvaamqaageaswtnathlviadpghprygQFLRASDLGLPFEGEARGDGEDTLVVDAADge 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 342 --DHTAKTP---------------------------EWASRIT--------GIPADRIVKLAREIGS--AKPAYICQGwG 382
Cdd:PRK14991 438 lvPATQAQParlfveqyvtladgqrvrvksslqllkEAARKLSlaeyseqcGVPEAQIIALAEEFTShgRKAAVISHG-G 516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 383 pQRQANGELTSRAIAMLPILTGNVGNSG------------ARESTYTIT------------IERMPLP------------ 426
Cdd:PRK14991 517 -TMSGNGFYNAWAIMMLNALIGNLNLKGgvvvgggkfpgfGDGPRYNLAsfagkvkpkgvsLSRSKFPyeksseyrrkve 595
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 427 --DNPVKTQISCFSwtdaiARGPEMTA-LRDGVRGkdkLDVPIKFIWNYAGNTLINQHSDINKTHDILQDESKCEMIVVI 503
Cdd:PRK14991 596 agQSPYPAKAPWYP-----FVAGLLTEmLTAALEG---YPYPLKAWINHMSNPIYGVPGLRAVIEEKLKDPKKLPLFISI 667
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 504 DNFMTSSAKYADIVLPDLMTVEQEDIIPnDYAGNMGYLIFLQ-PVTAPKFER----KPIYW--IMSEVAKRLG-P---DI 572
Cdd:PRK14991 668 DAFINETTALADYIVPDTHTYESWGFTA-PWGGVPTKASTARwPVVEPRTAKtadgQPVCMesFLIAVAKRLQlPgfgDN 746
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 573 HQKFTEGRTQ-----EQWlqYLYA----KMLEKDPK----------------LPSY------DELKKRG-IYKRkdpNGH 620
Cdd:PRK14991 747 AIKDAQGNTHplnraEDF--YLRGaaniAYLGKTPVadasdedialtgvsriLPALqatlkpDEVRRVAfIYAR---GGR 821
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 621 FVAYKK-FRENPEANPLKTPsgkIEIYSsklAEIAATWELEKDETISPLPVYAST--FDGWDAPER---ARFPLQLFGfh 694
Cdd:PRK14991 822 FAPAESaYDEERMGNRWKKP---LQIWN---EDVAAARHSMTGERYSGCPTWYPPrlADGTPLREQfpeSQWPLLLIS-- 893
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2278930946 695 FKARTHSSYGN-VDVLKAACRQE-VWLNPVDAEKRGIKNGDTVRVFNDRGEVRIEAKVTPRIMPGVSAMGQGAWH 767
Cdd:PRK14991 894 FKSNLMSSMSIaSPRLRQVKPANpVALNPQDAARLGIQHGDRVRISTPGGSVVAQASVLNGVMPGVIAIEHGYGH 968
|
|
| PRK13532 |
PRK13532 |
nitrate reductase catalytic subunit NapA; |
11-614 |
8.02e-21 |
|
nitrate reductase catalytic subunit NapA;
Pssm-ID: 237416 [Multi-domain] Cd Length: 830 Bit Score: 98.05 E-value: 8.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 11 ISRRTLVKSTAIGSLALAAGgISLPfglksaaAAVKHAVQPPEDTVVW--GACSVnCGSRCALRLHVRDNEVYWVETD-- 86
Cdd:PRK13532 3 LSRRDFMKANAAAAAAAAAG-LSLP-------AVANAVVGSAQTAIKWdkAPCRF-CGTGCGVLVGTKDGRVVATQGDpd 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 87 ---NTGEDvygdhqvraCLRGRSIRRRINHPDRLNYPMKRVgKRGE----GKFERITWDEALDTIAASLKDVVANYGNEA 159
Cdd:PRK13532 74 apvNRGLN---------CIKGYFLSKIMYGKDRLTQPLLRM-KDGKydkeGEFTPVSWDQAFDVMAEKFKKALKEKGPTA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 160 VyinyssGIVG-GNITRSSPYASlvARLMNcyGGFLSH--------------YGTYSTAQIACAMpytyGSNDgnstsDI 224
Cdd:PRK13532 144 V------GMFGsGQWTIWEGYAA--SKLMK--AGFRSNnidpnarhcmasavVGFMRTFGIDEPM----GCYD-----DI 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 225 ENTKLVVMFGNNPAE------TRMSGggityyleqaRERSN--ARMIVIDP---RYTDTAagreDEWIPIRPGTDAALVA 293
Cdd:PRK13532 205 EAADAFVLWGSNMAEmhpilwSRVTD----------RRLSNpdVKVAVLSTfehRSFELA----DNGIIFTPQTDLAILN 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 294 GIAWVLIDENLVDQPFLDKYCV--------GYD-------EKTLPEGAPANGH-------YKAYIlgqgDDHTAktpEWA 351
Cdd:PRK13532 271 YIANYIIQNNAVNWDFVNKHTNfrkgatdiGYGlrpthplEKAAKNPGTAGKSepisfeeFKKFV----APYTL---EKT 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 352 SRITGIPADRIVKLArEIGSAKPAYICQGW--GPQRQANGELTSRAIAMLPILTGNV---GNSG------------ARE- 413
Cdd:PRK13532 344 AKMSGVPKEQLEQLA-KLYADPNRKVVSFWtmGFNQHTRGVWANNLVYNIHLLTGKIstpGNGPfsltgqpsacgtAREv 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 414 STYTitiERMP---LPDNPVKTQIscfswTDAIARGPEMT--------------ALRDGVrgkdkldvpIKFIWNYAGNt 476
Cdd:PRK13532 423 GTFS---HRLPadmVVTNPKHREI-----AEKIWKLPEGTippkpgyhavaqdrMLKDGK---------LNAYWVMCNN- 484
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 477 liNQHSDINKTHDILQDESKCE-MIVVIDNFMTSSAKYADIVLPDLMTVEQEdiipNDYaGN------MGYliflQPVTA 549
Cdd:PRK13532 485 --NMQAGPNINEERLPGWRNPDnFIVVSDPYPTVSALAADLILPTAMWVEKE----GAY-GNaerrtqFWR----QQVKA 553
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2278930946 550 PKfERKPIYWIMSEVAKRlgpdihqkFTegrTQEQWLQYLYAKMLE-KDPKLpsYDELKKRGIYKR 614
Cdd:PRK13532 554 PG-EAKSDLWQLVEFSKR--------FK---TEEVWPEELLAKKPEyRGKTL--YDVLFANGQVDK 605
|
|
| MopB_CT_3 |
cd02786 |
The MopB_CT_3 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
686-806 |
2.33e-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: 2.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 686 FPLQLFGFHFKARTHSSYGNVDVL-KAACRQEVWLNPVDAEKRGIKNGDTVRVFNDRGEVRIEAKVTPRIMPGVsAMGQG 764
Cdd:cd02786 1 YPLRLITPPAHNFLNSTFANLPELrAKEGEPTLLIHPADAAARGIADGDLVVVFNDRGSVTLRAKVTDDVPPGV-VVAEG 79
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2278930946 765 AWHDANMSGdrvdhGSCINTLTTHRPSPLAKGNPQHTNLVQI 806
Cdd:cd02786 80 GWWREHSPD-----GRGVNALTSARLTDLGGGSTFHDTRVEV 116
|
|
| MopB_CT_Fdh-Nap-like |
cd00508 |
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and ... |
684-795 |
8.18e-17 |
|
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: 77.16 E-value: 8.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 684 ARFPL------QLFGFHFKARThssyGNVDVLKAACRQE-VWLNPVDAEKRGIKNGDTVRVFNDRGEVRIEAKVTPRIMP 756
Cdd:cd00508 1 EEYPLvlttgrLLEHWHTGTMT----RRSPRLAALAPEPfVEIHPEDAARLGIKDGDLVRVSSRRGSVVVRARVTDRVRP 76
|
90 100 110
....*....|....*....|....*....|....*....
gi 2278930946 757 GVSAMgqgAWHDANMSGdrvdhGSCINTLTTHRPSPLAK 795
Cdd:cd00508 77 GTVFM---PFHWGGEVS-----GGAANALTNDALDPVSG 107
|
|
| 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 ... |
64-519 |
2.62e-14 |
|
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: 76.27 E-value: 2.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 64 NCGSRCALRLHVRDNEVYWVETDNTGEDvygdHQVRACLRGRSIRRRINHPDRLNYPMKRVGkrgeGKFERITWDEALDT 143
Cdd:cd02771 6 HCSVGCNISLGERYGELRRVENRYNGAV----NHYFLCDRGRFGYGYVNSRDRLTQPLIRRG----GTLVPVSWNEALDV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 144 IAASLKDVVANYGneavyinyssGIVGGNITRSSPYAslVARLMNCYGG--FLSHYGTYSTAQIACAMPYTYGSNDgnst 221
Cdd:cd02771 78 AAARLKEAKDKVG----------GIGSPRASNESNYA--LQKLVGAVLGtnNVDHRARRLIAEILRNGPIYIPSLR---- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 222 sDIENTKLVVMFGNNPAETrmsGGGITYYLEQARERSNARMIVIDPRYTDTAAGREDewIPIRPGTDAALVAgiawvlid 301
Cdd:cd02771 142 -DIESADAVLVLGEDLTQT---APRIALALRQAARRKAVELAALSGIPKWQDAAVRN--IAQGAKSPLFIVN-------- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 302 enlVDQPFLDKYcVGYDEKTLPEGAPAnghykayiLGQGDDHtAKTPEWASRITGIPADRIVKLAREIGSAKPAYICQGW 381
Cdd:cd02771 208 ---ALATRLDDI-AAESIRASPGGQAR--------LGAALAR-AVDASAAGVSGLAPKEKAARIAARLTGAKKPLIVSGT 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 382 GPQRQANGELTSRAIAMLPILTGNVGNSGARESTYTITIErmPLPDNPVKTQIScfswTDAIArgpemTALRDGvrGKDK 461
Cdd:cd02771 275 LSGSLELIKAAANLAKALKRRGENAGLTLAVEEGNSPGLL--LLGGHVTEPGLD----LDGAL-----AALEDG--SADA 341
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2278930946 462 LDVpikfiwnyAGNTLINQHSDInkthDILQDESKCEMIVVIDNFMTSSAKYADIVLP 519
Cdd:cd02771 342 LIV--------LGNDLYRSAPER----RVEAALDAAEFVVVLDHFLTETAERADVVLP 387
|
|
| NarG |
COG5013 |
Nitrate reductase alpha subunit [Energy production and conversion, Inorganic ion transport and ... |
63-314 |
4.60e-14 |
|
Nitrate reductase alpha subunit [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 444037 [Multi-domain] Cd Length: 1231 Bit Score: 76.40 E-value: 4.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 63 VNC-GSrCALRLHVRDNEVYWvETDNT-----GEDvYGDHQVRACLRGRSIRRRINHPDRLNYPMKR------------- 123
Cdd:COG5013 55 VNCtGS-CSWKVYVKDGIITW-ETQQTdyprtGPD-LPNYEPRGCPRGASFSWYTYSPTRVKYPYVRgvllelwrearar 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 124 ---------------------VGKRGEGKFERITWDEALDTIAASLKDVVANYGNEAVY----------INYSSGivggn 172
Cdd:COG5013 132 hgdpveawasivedpekrrryKSARGKGGFVRATWDEANEIIAAANVYTIKKYGPDRVAgfspipamsmVSYAAG----- 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 173 itrsspyaslvARLMNCYGG-FLSHYGTYstAQIACAMPYTYG-SNDGNSTSDIENTKLVVMFGNNPAETRmsgggiT-- 248
Cdd:COG5013 207 -----------ARFLSLIGGvMLSFYDWY--ADLPPASPQVWGeQTDVPESADWYNSGYLIMWGSNVPQTR------Tpd 267
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2278930946 249 -YYLEQARERSnARMIVIDPRYTDtAAGREDEWIPIRPGTDAALVAGIAWVLIDENLVDQ--PFLDKYC 314
Cdd:COG5013 268 aHFMTEARYKG-TKVVVVSPDYAE-NTKFADEWLPPKQGTDAALAMAMGHVILKEFHVDRqvPYFTDYA 334
|
|
| MopB_CT_Nitrate-R-NarG-like |
cd02776 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
687-793 |
5.93e-14 |
|
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under anaerobic conditions in the presence of nitrate, E. coli synthesizes the cytoplasmic membrane-bound quinol-nitrate oxidoreductase (NarGHI), which reduces nitrate to nitrite and forms part of a redox loop generating a proton-motive force. Found in prokaryotes and some archaea, NarGHI usually functions as a heterotrimer. The alpha chain contains the molybdenum cofactor-containing Mo-bisMGD catalytic subunit. This CD (MopB_CT_Nitrate-R-NarG-like) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239177 [Multi-domain] Cd Length: 141 Bit Score: 69.71 E-value: 5.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 687 PLQLFGFHFKARTHSSYGNVDVLKAACRQE--VWLNPVDAEKRGIKNGDTVRVFNDRGEVRIEAKVTPRIMPGVSAM--G 762
Cdd:cd02776 1 PLNYLTPHGKWSIHSTYRDNLLMLRLQRGGpvVWMNPKDAAELGIKDNDWVEVFNDNGVVVARAKVSPRIPRGTVFMyhA 80
|
90 100 110
....*....|....*....|....*....|.
gi 2278930946 763 QGAWHDANMSGDRVDHGSCINTLTTHRPSPL 793
Cdd:cd02776 81 QERHVNVPGSKLTGKRGGIHNSVTRVRIKPT 111
|
|
| Molybdop_Fe4S4 |
pfam04879 |
Molybdopterin oxidoreductase Fe4S4 domain; This domain is found in formate dehydrogenase H for ... |
54-113 |
1.33e-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: 65.78 E-value: 1.33e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 54 DTVVWGACSvNCGSRCALRLHVRDNEVYWVETDNTGEDVYGdhqvRACLRGRSIRRRINH 113
Cdd:pfam04879 1 MKVVKTICP-YCGVGCGLEVHVKDGKIVKVEGDPDHPVNEG----RLCVKGRFGYERVYN 55
|
|
| MopB_CT_Acetylene-hydratase |
cd02781 |
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related ... |
685-808 |
2.69e-13 |
|
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. The acetylene hydratase of Pelobacter acetylenicus is a tungsten iron-sulfur protein involved in the fermentation of acetylene to ethanol and acetate. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239182 [Multi-domain] Cd Length: 130 Bit Score: 67.33 E-value: 2.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 685 RFPLQLF-----GFHFkartHSSYGNVDVLKAACRQ-EVWLNPVDAEKRGIKNGDTVRVFNDRGEVRIEAKVTPRIMPGV 758
Cdd:cd02781 1 EYPLILTtgarsYYYF----HSEHRQLPSLRELHPDpVAEINPETAAKLGIADGDWVWVETPRGRARQKARLTPGIRPGV 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2278930946 759 sAMGQGAWHDANMSGDRVDHGSC----INTLTTHRPS-PLAKGNPQHTNLVQIEK 808
Cdd:cd02781 77 -VRAEHGWWYPEREAGEPALGGVwesnANALTSDDWNdPVSGSSPLRSMLCKIYK 130
|
|
| MopB_Arsenite-Ox |
cd02756 |
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the ... |
83-568 |
1.27e-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: 71.36 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 83 VETDNTGEDVY-------------GDHQVRACLRGRSIRRRINHP--DRLNYPMKRVGkrgeGKFERITWDEALDTIAAS 147
Cdd:cd02756 69 VVVTQDGREVYivivpdkecpvnsGNYSTRGGTNAERIWSPDNRVgeTRLTTPLVRRG----GQLQPTTWDDAIDLVARV 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 148 LKDVVANYGNE-AVYINYSSGIVGGnitrsspyaslvarlmncyGGFLSHYGT-----YSTAQIACAMPY--TYGSN--- 216
Cdd:cd02756 145 IKGILDKDGNDdAVFASRFDHGGGG-------------------GGFENNWGVgkfffMALQTPFVRIHNrpAYNSEvha 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 217 --------DGNSTSDIENTKLVVMFGNNPAETRMsgggiTYYLE---------------QARERSN----ARMIVIDPRY 269
Cdd:cd02756 206 tremgvgeLNNSYEDARLADTIVLWGNNPYETQT-----VYFLNhwlpnlrgatvsekqQWFPPGEpvppGRIIVVDPRR 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 270 TDT------AAGREDEW-IPIRPGTDAALVAGIAWVLIDenlvdqpfldkycvGYDEkTLPEgapanghykayilgqgdd 342
Cdd:cd02756 281 TETvhaaeaAAGKDRVLhLQVNPGTDTALANAIARYIYE--------------SLDE-VLAE------------------ 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 343 htaktpewASRITGIPADRIVKLA-----REIGSAKPAYIC---QG--WGPQR-QANGeltsrAIAMLPILTGNVGNSG- 410
Cdd:cd02756 328 --------AEQITGVPRAQIEKAAdwiakPKEGGYRKRVMFeyeKGiiWGNDNyRPIY-----SLVNLAIITGNIGRPGt 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 411 --ARESTYTITIERMPLPDNPVKTQISCFSWTD------------AIARGPEMTALrDGVRGKDKLDVPIKFIWNYAGNT 476
Cdd:cd02756 395 gcVRQGGHQEGYVRPPPPPPPWYPQYQYAPYIDqllisgkgkvlwVIGCDPYKTTP-NAQRLRETINHRSKLVTDAVEAA 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 477 LINQHSDINKTHDILQD--ESKCEMIVVIDNFMTSSAKYADIVLPDLMTVEQEDIIPNdyaGNMGYLIFLQPVTAPKFER 554
Cdd:cd02756 474 LYAGTYDREAMVCLIGDaiQPGGLFIVVQDIYPTKLAEDAHVILPAAANGEMNETSMN---GHERRLRLYEKFMDPPGEA 550
|
570
....*....|....
gi 2278930946 555 KPIYWIMSEVAKRL 568
Cdd:cd02756 551 MPDWWIAAMIANRI 564
|
|
| MopB_CT_Thiosulfate-R-like |
cd02778 |
The MopB_CT_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, ... |
689-808 |
1.54e-12 |
|
The MopB_CT_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and other related proteins. Thiosulfate reductase catalyzes the cleavage of sulfur-sulfur bonds in thiosulfate. Polysulfide reductase is a membrane-bound enzyme that catalyzes the reduction of polysulfide using either hydrogen or formate as the electron donor. Also included in this CD is the phenylacetyl-CoA:acceptor oxidoreductase, large subunit (PadB2), which has been characterized as a membrane-bound molybdenum-iron-sulfur enzyme involved in anaerobic metabolism of phenylalanine in the denitrifying bacterium Thauera aromatica. The MopB_CT_Thiosulfate-R-like CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239179 [Multi-domain] Cd Length: 123 Bit Score: 64.99 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 689 QLFGFHFKA--RTHSSYGNVDVLKAACR-QEVWLNPVDAEKRGIKNGDTVRVFNDRGEVRIEAKVTPRIMPGVSAM--GQ 763
Cdd:cd02778 1 EFRLIYGKSpvHTHGHTANNPLLHELTPeNTLWINPETAARLGIKDGDRVEVSSARGKVTGKARLTEGIRPDTVFMphGF 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2278930946 764 GAWHDANMSGDRvdHGSCINTLTTHRPSPLAKGNPQHTNLVQIEK 808
Cdd:cd02778 81 GHWAPALSRAYG--GGVNDNNLLPGSTEPVSGGAGLQEFTVTVRK 123
|
|
| MopB_CT_Nitrate-R-NapA-like |
cd02791 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
684-809 |
4.54e-12 |
|
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: 63.75 E-value: 4.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 684 ARFPLQL------FGFHFKARThssyGNVDVL-KAACRQEVWLNPVDAEKRGIKNGDTVRVFNDRGEVRIEAKVTPRIMP 756
Cdd:cd02791 1 AEYPLWLntgrvrDQWHTMTRT----GRVPRLnAHVPEPYVEIHPEDAARLGLKEGDLVRVTSRRGEVVLRVRVTDRVRP 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2278930946 757 GVSAMgqgAWHDANMSGDrvdhGSCINTLTTHRPSPLAKgnpQ----HTnLVQIEKV 809
Cdd:cd02791 77 GEVFV---PMHWGDQFGR----SGRVNALTLDATDPVSG---QpefkHC-AVRIEKV 122
|
|
| MopB_CT_Tetrathionate_Arsenate-R |
cd02780 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate ... |
686-768 |
4.86e-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: 64.24 E-value: 4.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 686 FPLQLFGFHFKARTHSSYGNVDVLKAACRQEVWLNPVDAEKRGIKNGDTVRVFNDRGEVRIEAKVTPRIMPGVSAM--GQ 763
Cdd:cd02780 1 YPFILVTFKSNLNSHRSANAPWLKEIKPENPVWINPEDAAKLGIKTGDRVRVVTPGGSVVGKAKVTEGVRPGVVAIehGY 80
|
....*
gi 2278930946 764 GAWHD 768
Cdd:cd02780 81 GHWAY 85
|
|
| MopB_PHLH |
cd02764 |
The MopB_PHLH CD includes a group of related uncharacterized putative hydrogenase-like ... |
114-556 |
5.96e-12 |
|
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: 69.05 E-value: 5.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 114 PDRLNYPMKRVGKRGEGKferITWDEALDTIAASLKdvvANYGNEAVYInySSGIVGGNITRSspyasLVARLMNCYGGF 193
Cdd:cd02764 97 PDRAQGPLRRGIDGAYVA---SDWADFDAKVAEQLK---AVKDGGKLAV--LSGNVNSPTTEA-----LIGDFLKKYPGA 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 194 LSH-YGTYSTAQIACAMPYTYGsNDGNSTSDIENTKLVVMFGNNPAETRMSGGGITYYLEQAR----ERSNARMIVIDPR 268
Cdd:cd02764 164 KHVvYDPLSAEDVNEAWQASFG-KDVVPGYDFDKAEVIVSIDADFLGSWISAIRHRHDFAAKRrlgaEEPMSRLVAAESV 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 269 YTDTAAGrEDEWIPIRPGTDAALVAGIAWVLIdenlvdqpfldkycvgydekTLPEGAPANGHYKAYILgqgddhtAKTP 348
Cdd:cd02764 243 YTLTGAN-ADVRLAIRPSQEKAFALGLAHKLI--------------------KKGAGSSLPDFFRALNL-------AFKP 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 349 EWASRITGIPADRIVKLAREIGSAKPAYICQGwgpqrqanGELTSRAIAMLPILtGNVGNSGARESTYTITIERmPLPDN 428
Cdd:cd02764 295 AKVAELTVDLDKALAALAKALAAAGKSLVVAG--------SELSQTAGADTQVA-VNALNSLLGNDGKTVDHAR-PIKGG 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 429 PVKTQISCFSWTDAIARGpemtalrdgvrgkdklDVPIKFIWnyagntlinqhsDINKTHDILQDE------SKCEMIVV 502
Cdd:cd02764 365 ELGNQQDLKALASRINAG----------------KVSALLVY------------DVNPVYDLPQGLgfakalEKVPLSVS 416
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2278930946 503 IDNFMTSSAKYADIVLPDLMTVEQEDiipnDYAGNMGYLIFLQPVTAPKFERKP 556
Cdd:cd02764 417 FGDRLDETAMLCDWVAPMSHGLESWG----DAETPDGTYSICQPVIAPLFDTRS 466
|
|
| MopB_CT_Formate-Dh_H |
cd02790 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
693-761 |
1.57e-11 |
|
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: 61.87 E-value: 1.57e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 693 FHFKARTHSsyGNVDVLKAACRQE-VWLNPVDAEKRGIKNGDTVRVFNDRGEVRIEAKVTPRIMPGVSAM 761
Cdd:cd02790 14 YHYHTGTMT--RRAEGLDAIAPEEyVEINPEDAKRLGIEDGEKVRVSSRRGSVEVRARVTDRVPEGVVFM 81
|
|
| MopB_CT_1 |
cd02782 |
The MopB_CT_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
719-809 |
4.40e-11 |
|
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: 60.87 E-value: 4.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 719 LNPVDAEKRGIKNGDTVRVFNDRGEVRIEAKVTPRIMPGVSAMGQGAWHDA-NMSGDRVDHGSCINTLT--THRpSPLAk 795
Cdd:cd02782 37 IHPDDAAALGLADGDKVRVTSAAGSVEAEVEVTDDMMPGVVSLPHGWGHDYpGVSGAGSRPGVNVNDLTddTQR-DPLS- 114
|
90
....*....|....*
gi 2278930946 796 GNPQHTNL-VQIEKV 809
Cdd:cd02782 115 GNAAHNGVpVRLARV 129
|
|
| MopB_NADH-Q-OR-NuoG2 |
cd02768 |
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone ... |
62-240 |
9.49e-11 |
|
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone oxidoreductase (NADH-Q-OR)/respiratory complex I/NADH dehydrogenase-1 (NDH-1). The NADH-Q-OR is the first energy-transducting complex in the respiratory chains of many prokaryotes and eukaryotes. Mitochondrial complex I and its bacterial counterpart, NDH-1, function as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. The atomic structure of complex I is not known and the mechanisms of electron transfer and proton pumping are not established. The nad11 gene codes for the largest (75-kDa) subunit of the mitochondrial NADH:ubiquinone oxidoreductase, it constitutes the electron input part of the enzyme, or the so-called NADH dehydrogenase fragment. In Escherichia coli, this subunit is encoded by the nuoG gene, and is part of the 14 distinct subunits constituting the 'minimal' functional enzyme. The nad11 gene is nuclear-encoded in animals, plants, and fungi, but is still encoded in the mitochondrial genome of some protists. The Nad11/NuoG subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain family belongs to the molybdopterin_binding (MopB) superfamily of proteins. Bacterial type II NADH-quinone oxidoreductases and NQR-type sodium-motive NADH-quinone oxidoreductases are not homologs of this domain family.
Pssm-ID: 239169 [Multi-domain] Cd Length: 386 Bit Score: 64.61 E-value: 9.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 62 SVNCGSRCALRLHVRDNEV-------------YWVeTDNTgedvygdhqvRACLRGrsirrrINHPDRLNYPMKRVGkrg 128
Cdd:cd02768 4 DVHDALGSNIRVDVRGGEVmrilpreneaineEWI-SDKG----------RFGYDG------LNSRQRLTQPLIKKG--- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 129 eGKFERITWDEALDTIAASLKDVVANygneAVyinysSGIVGGNITRSSPYAslVARLMNCYG-GFLSHYGTYSTAQIAC 207
Cdd:cd02768 64 -GKLVPVSWEEALKTVAEGLKAVKGD----KI-----GGIAGPRADLESLFL--LKKLLNKLGsNNIDHRLRQSDLPADN 131
|
170 180 190
....*....|....*....|....*....|...
gi 2278930946 208 AMPYTYGSNdgNSTSDIENTKLVVMFGNNPAET 240
Cdd:cd02768 132 RLRGNYLFN--TSIAEIEEADAVLLIGSNLRKE 162
|
|
| MopB_CT_Formate-Dh-Na-like |
cd02792 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
717-808 |
1.70e-10 |
|
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: 59.16 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 717 VWLNPVDAEKRGIKNGDTVRVFNDRGEVRIEAKVTPRIMPGVSAMgqgAWHDANMSGDRvdhGSCINTLTTHRPSPLAkg 796
Cdd:cd02792 37 VEISPELAAERGIKNGDMVWVSSPRGKIKVKALVTDRVKPHEVGI---PYHWGGMGLVI---GDSANTLTPYVGDPNT-- 108
|
90
....*....|....
gi 2278930946 797 NPQHTN--LVQIEK 808
Cdd:cd02792 109 QTPEYKafLVNIEK 122
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
62-149 |
3.27e-10 |
|
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production and conversion]; NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) is part of the Pathway/BioSystem: NADH dehydrogenase
Pssm-ID: 440657 [Multi-domain] Cd Length: 453 Bit Score: 63.32 E-value: 3.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 62 SVNCGSRCALRLHVRDNEVYWVE-TDNtgEDVYGDHqvrACLRGRSIRRRINHPDRLNYPMKRVGkrgeGKFERITWDEA 140
Cdd:COG1034 222 CPHCSVGCNIRVDVRGGKVYRVLpREN--EAVNEEW---LCDKGRFGYDGLNSPDRLTRPLVRKD----GELVEASWEEA 292
|
....*....
gi 2278930946 141 LDTIAASLK 149
Cdd:COG1034 293 LAAAAEGLK 301
|
|
| Molybdop_Fe4S4 |
smart00926 |
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is ... |
54-113 |
1.52e-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: 54.18 E-value: 1.52e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2278930946 54 DTVVWGACSVnCGSRCALRLHVRDNEVYWVETDNtgedvygDHQV---RACLRGRSIRRRINH 113
Cdd:smart00926 1 EKWVPTVCPL-CGVGCGLLVEVKDGRVVRVRGDP-------DHPVnrgRLCPKGRAGLEQVYS 55
|
|
| FwdD |
COG1153 |
Formylmethanofuran dehydrogenase subunit D [Energy production and conversion]; |
718-771 |
6.36e-08 |
|
Formylmethanofuran dehydrogenase subunit D [Energy production and conversion];
Pssm-ID: 440767 [Multi-domain] Cd Length: 127 Bit Score: 51.78 E-value: 6.36e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2278930946 718 WLNPVDAEKRGIKNGDTVRVFNDRGEVRIEAKVTPRIMPGVSAMGQGAWhdANM 771
Cdd:COG1153 34 ELNPEDMKKLGIKEGDKVKVTSEYGEVVVKAKESEDLHPGLVFIPMGPW--ANA 85
|
|
| FwdB |
COG1029 |
Formylmethanofuran dehydrogenase subunit B [Energy production and conversion]; |
65-293 |
1.00e-06 |
|
Formylmethanofuran dehydrogenase subunit B [Energy production and conversion];
Pssm-ID: 440652 [Multi-domain] Cd Length: 428 Bit Score: 52.16 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 65 CGSRC-ALRLHVRDNEVywVETDNtgedvygdhqvrACLRGRSIRRRINHPDRLNYPMKRvgkrgegkFERITWDEALDT 143
Cdd:COG1029 13 CGCLCdDLEVEVEGGKI--VVVKN------------ACAIGAAKFERAVSDHRITSPRIR--------GKEVSLEEAIDK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 144 IAaslkDVVANYGNEAVYinyssgivGGNITrSSPYASLVARLMNCYGGFLSHYGTystaqiACAMPYTYGSND-GNSTS 222
Cdd:COG1029 71 AA----EILANAKRPLIY--------GLSST-DCEAMRAGLALAERVGAVVDNTAS------VCHGPSLLALQDvGWPTC 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 223 DIENTK----LVVMFGNNPAET------RMSGGGITYYLEQARERSnaRMIVIDPRYTDTAAgREDEWIPIRPGTDAALV 292
Cdd:COG1029 132 TLGEVKnradVIIYWGCNPVHAhprhmsRYSVFPRGFFTPKGRKDR--TVIVVDPRPTDTAK-VADLHLQVKPGRDYEVL 208
|
.
gi 2278930946 293 A 293
Cdd:COG1029 209 S 209
|
|
| MopB_CT_FmdC-FwdD |
cd02789 |
The MopB_FmdC-FwdD CD includes the C-terminus of subunit C of molybdenum formylmethanofuran ... |
692-798 |
1.75e-05 |
|
The MopB_FmdC-FwdD CD includes the C-terminus of subunit C of molybdenum formylmethanofuran dehydrogenase (FmdC) and subunit D of tungsten formylmethanofuran dehydrogenase (FwdD), and other related proteins. Formylmethanofuran dehydrogenase catalyzes the first step in methane formation from CO2 in methanogenic archaea and some eubacteria. Members of this CD belong to the molybdopterin_binding superfamily of proteins. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239190 [Multi-domain] Cd Length: 106 Bit Score: 44.34 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 692 GFHFKARTHSSYgnvDVLKAAcrqEVWLNPVDAEKRGIKNGDTVRVFNDRGEVRIEAKVTPRIMPGVSAMGQGAWhdANM 771
Cdd:cd02789 14 GRIIEGGNKLTY---EVDACA---YCEINPEDYKLLGKPEGDKVKVTSEFGEVVVFAKENEGVPEGMVFIPMGPW--ANV 85
|
90 100
....*....|....*....|....*..
gi 2278930946 772 SGDRVDHGScintltthrPSPLAKGNP 798
Cdd:cd02789 86 VVDPYTDST---------GSPIFKGVP 103
|
|
| MopB_CT_Arsenite-Ox |
cd02779 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of Arsenite oxidase ... |
719-766 |
3.40e-05 |
|
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of Arsenite oxidase (Arsenite-Ox) and related proteins. Arsenite oxidase oxidizes arsenite to the less toxic arsenate; it transfers the electrons obtained from the oxidation of arsenite towards the soluble periplasmic electron carriers cytochrome c and/or amicyanin.
Pssm-ID: 239180 [Multi-domain] Cd Length: 115 Bit Score: 43.99 E-value: 3.40e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2278930946 719 LNPVDAEKRGIKNGDTVRVFNDRGEVRIEAKVTPRIMPGVSAMGQGAW 766
Cdd:cd02779 37 VNPEDAKREGLKNGDLVEVYNDYGSTTAMAYVTNTVKPGQTFMLMAHP 84
|
|
| MopB_CT_NDH-1_NuoG2-N7 |
cd02788 |
MopB_CT_NDH-1_NuoG2-N7: C-terminal region of the NuoG-like subunit (of the variant with a ... |
704-765 |
6.42e-05 |
|
MopB_CT_NDH-1_NuoG2-N7: C-terminal region of the NuoG-like subunit (of the variant with a [4Fe-4S] cluster, N7) of the NADH-quinone oxidoreductase/NADH dehydrogenase-1 (NDH-1) found in various bacteria. The NDH-1 is the first energy-transducting complex in the respiratory chain and functions as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. In Escherichia coli NDH-1, the largest subunit is encoded by the nuoG gene, and is part of the 14 distinct subunits constituting the functional enzyme. The NuoG subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain, is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Unique to this group, compared to the other prokaryotic and eukaryotic groups in this domain protein family (NADH-Q-OR-NuoG2), is an N-terminal [4Fe-4S] cluster (N7/N1c) present in the second domain and a C-terminal region (this CD) homologous to the formate dehydrogenase C-terminal molybdopterin_binding (MopB) region.
Pssm-ID: 239189 [Multi-domain] Cd Length: 96 Bit Score: 42.30 E-value: 6.42e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2278930946 704 GNVDVLKAACRQEVW-LNPVDAEKRGIKNGDTVRVFNDRGEVRIEAKVTPRIMPGVS--AMGQGA 765
Cdd:cd02788 17 QRSPVIAERAPAPYArLSPADAARLGLADGDLVEFSLGDGTLTLPVQISKYLPAGVVglPLGAGF 81
|
|
| MopB_NDH-1_NuoG2 |
cd02772 |
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase ... |
71-160 |
2.34e-04 |
|
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase/NADH dehydrogenase-1 (NDH-1), found in beta- and gammaproteobacteria. The NDH-1 is the first energy-transducting complex in the respiratory chain and functions as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. In Escherichia coli NDH-1, the largest subunit is encoded by the nuoG gene, and is part of the 14 distinct subunits constituting the functional enzyme. The NuoG subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain belongs to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239173 [Multi-domain] Cd Length: 414 Bit Score: 44.27 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 71 LRLHVRDNEVYWV---ETDNTGEDVYGDhqvraclRGRSIRRRINHPDRLNYPMKRVGkrgeGKFERITWDEALDTIAAS 147
Cdd:cd02772 13 LVVHVKNNKVMRVvprENEAINECWLSD-------RDRFSYEGLNSEDRLTKPMIKKD----GQWQEVDWETALEYVAEG 81
|
90
....*....|...
gi 2278930946 148 LKDVVANYGNEAV 160
Cdd:cd02772 82 LSAIIKKHGADQI 94
|
|
| MopB_Res-Cmplx1_Nad11 |
cd02773 |
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone ... |
116-237 |
7.88e-04 |
|
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone oxidoreductase/respiratory complex I/NADH dehydrogenase-1(NDH-1) of eukaryotes and the Nqo3/G subunit of alphaproteobacteria NDH-1. The NADH-quinone oxidoreductase is the first energy-transducting complex in the respiratory chains of many prokaryotes and eukaryotes. Mitochondrial complex I and its bacterial counterpart, NDH-1, function as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. The nad11 gene codes for the largest (75 kDa) subunit of the mitochondrial NADH:ubiquinone oxidoreductase, it constitutes the electron input part of the enzyme, or the so-called NADH dehydrogenase fragment. In Paracoccus denitrificans, this subunit is encoded by the nqo3 gene, and is part of the 14 distinct subunits constituting the 'minimal' functional enzyme. The Nad11/Nqo3 subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain belongs to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239174 [Multi-domain] Cd Length: 375 Bit Score: 42.64 E-value: 7.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278930946 116 RLNYPMKRvgkrGEGKFERITWDEALDTIAASLKdvvANYGNEAVyinyssGIVGGnitrSSPYASLVA--RLMNCYGGf 193
Cdd:cd02773 53 RLDKPYIR----KNGKLKPATWEEALAAIAKALK---GVKPDEIA------AIAGD----LADVESMVAlkDLLNKLGS- 114
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2278930946 194 lshyGTYSTAQIACAMPYTYGSN-DGNST-SDIENTKLVVMFGNNP 237
Cdd:cd02773 115 ----ENLACEQDGPDLPADLRSNyLFNTTiAGIEEADAVLLVGTNP 156
|
|
| |
