|
Name |
Accession |
Description |
Interval |
E-value |
| MopB_DMSOR-BSOR-TMAOR |
cd02769 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
11-619 |
0e+00 |
|
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: 972.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 11 LTSTHWGTYRAKVKNGKVQELIGWENDKDPSPIGPGILDIQDGPTRIDAPMVRKSWLEQGPGSRNDLRGIDPFIEVSWKK 90
Cdd:cd02769 1 PTASHWGAFRARVKDGRIVGVRPFEEDPDPSPLLDGVPDAVYSPTRIKYPMVRRGWLEKGPGSDRSLRGKEEFVRVSWDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 91 AEQLVADELTRVKNTYGNASIFGGSYGWASAGRFHHAQSQLHRFLNCIGGYTRSKFTYSFAAAEAMVPHILGSYRAYLDT 170
Cdd:cd02769 81 ALDLVAAELKRVRKTYGNEAIFGGSYGWSSAGRFHHAQSLLHRFLNLAGGYVGSVGDYSTGAAQVILPHVVGSMEVYTEQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 171 CTSWDLINKNTELFVCFGGIPIKNGQISQGGTGNHYQRKNLVEAANSGIEFINISPLKSDLIDEVKGEWITARPNTDTAL 250
Cdd:cd02769 161 QTSWPVIAEHTELVVAFGADPLKNAQIAWGGIPDHQAYSYLKALKDRGIRFISISPLRDDTAAELGAEWIAIRPGTDVAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 251 MLGLAHTLHVEGLSDKQFLENYTQGFEKFLPYLLGTNDGIEKNADWAASICNIPSSKIKELAHKISSKRTMISVSWSLTR 330
Cdd:cd02769 241 MLALAHTLVTEGLHDKAFLARYTVGFDKFLPYLLGESDGVPKTPEWAAAICGIPAETIRELARRFASKRTMIMAGWSLQR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 331 QDHGEQPFWMAIMLASMVGQIGLPGGGFGFGYSATNYIGGQFKVLPGAAFPQADNKIENFIPVARISDLLLGPGEKFDFD 410
Cdd:cd02769 321 AHHGEQPHWMAVTLAAMLGQIGLPGGGFGFGYHYSNGGGPPRGAAPPPALPQGRNPVSSFIPVARIADMLLNPGKPFDYN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 411 GKTYVYPDTKIVYWAGGNPFHHHQDLNRLIKAWEKPDTIISNEWCWNTLAKRSDIVLPCTTPLERGDIMMTPRDPYVVSM 490
Cdd:cd02769 401 GKKLTYPDIKLVYWAGGNPFHHHQDLNRLIRAWQKPETVIVHEPFWTATARHADIVLPATTSLERNDIGGSGDNRYIVAM 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 491 SKLVEPHGKAKNDYEIFSGIARKMGVEEKFTEGRNQEEWQKWIYKQTFERAAAANIKIPSYEKFREEKWFKIDDPSEPTL 570
Cdd:cd02769 481 KQVVEPVGEARDDYDIFADLAERLGVEEQFTEGRDEMEWLRHLYEESRAQAAARGVEMPSFDEFWAQGYVELPIPEADFV 560
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 142091137 571 MLKDFREDPIKYPLDTQSGKIEIFSQTVSDFKYDDCPGHPVWIEPCEWL 619
Cdd:cd02769 561 RLADFREDPEANPLGTPSGRIEIFSETIAGFGYDDCPGHPTWLEPAEWL 609
|
|
| bisC_fam |
TIGR00509 |
molybdopterin guanine dinucleotide-containing S/N-oxide reductases; This enzyme family shares ... |
14-771 |
0e+00 |
|
molybdopterin guanine dinucleotide-containing S/N-oxide reductases; This enzyme family shares sequence similarity and a requirement for a molydenum cofactor as the only prosthetic group. The form of the cofactor is a single molybdenum atom coordinated by two molybdopterin guanine dinucleotide molecules. Members of the family include biotin sulfoxide reductase, dimethylsulfoxide reductase, and trimethylamine-N-oxide reductase, although a single member may show all those activities and related activities; it may not be possible to resolve the primary function for members of this family by sequence comparison alone. A number of similar molybdoproteins in which the N-terminal region contains a CXXXC motif and may bind an iron-sulfur cluster are excluded from this set, including formate dehydrogenases and nitrate reductases. Also excluded is the A chain of a heteromeric, anaerobic DMSO reductase, which also contains the CXXXC motif.
Pssm-ID: 273110 [Multi-domain] Cd Length: 770 Bit Score: 946.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 14 THWGTYRAKVKNGKVQELIGWENDKDPSPIGPGILDIQDGPTRIDAPMVRKSWLEQGPGSRNDLRGIDPFIEVSWKKAEQ 93
Cdd:TIGR00509 2 SHWGVFTATVQDGRIVAVTPFESDPNPTPMLEGVPDQVYSESRIKYPMVRKGFLENGVKSDRSGRGREEFVRVSWDEALD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 94 LVADELTRVKNTYGNASIFGGSYGWASAGRFHHAQSQLHRFLNCIGGYTRSKFTYSFAAAEAMVPHILGSYRAYLDTcTS 173
Cdd:TIGR00509 82 LVAEELKRVRKTHGPSAIFAGSYGWKSAGRLHNASTLLQRMLNLLGGYVGHAGDYSTGAAQVIMPHVVGDMEVYEQQ-TT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 174 WDLINKNTELFVCFGGIPIKNGQISqGGTGNHYQRKNLVEAANSGIEFINISPLKSDLIDEVKGEWITARPNTDTALMLG 253
Cdd:TIGR00509 161 WPVILENSEVLVLWGADPLKTSQIA-WGIPDHGGYEYLERLKAKGKRVISIDPVRTETVEFFGAEWIPPNPQTDVALMLG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 254 LAHTLHVEGLSDKQFLENYTQGFEKFLPYLLGTNDGIEKNADWAASICNIPSSKIKELAHKISSKRTMISVSWSLTRQDH 333
Cdd:TIGR00509 240 LAHTLVTEGLYDKDFLAKYTSGFEKFLPYLLGETDGTPKTAEWASKITGVPAETIKELARLFASKRTMLAAGWSMQRMQH 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 334 GEQPFWMAIMLASMVGQIGLPGGGFGFGYSatnYIGGQFKVLPGAAFPQADNKI------------ENFIPVARISDLLL 401
Cdd:TIGR00509 320 GEQPHWMLVTLAAMLGQIGLPGGGFGFSYH---YSGGGTPSASGPALSQGSNSVsstagpewddgsASVIPVARISDALL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 402 GPGEKFDFDGKTYVYPDTKIVYWAGGNPFHHHQDLNRLIKAWEKPDTIISNEWCWNTLAKRSDIVLPCTTPLERGDIMMT 481
Cdd:TIGR00509 397 NPGKEIDYNGKELKLPDIKMVYWAGGNPFHHHQDTNRLIKAWRKLETIIVHEPQWTPTAKHADIVLPATTSFERNDLTMA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 482 P--RDPYVVSMSKLVEPHGKAKNDYEIFSGIARKMGVEEKFTEGRNQEEWQKWIYKQTFERAAAANIKIPSYEKFREEKW 559
Cdd:TIGR00509 477 GdySNTGILAMKQVVPPQFEARNDYDIFAALAERLGVEEAFTEGKDEMGWLKHLYEKAAKQAKADGVEMPAFDAFWAEGI 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 560 FKIDDPSEPTLM-LKDFREDPIKYPLDTQSGKIEIFSQTVSDFKYDDCPGHPVWIEPCEWLGQKNK-KFPLHLISNQPKN 637
Cdd:TIGR00509 557 VEFPVPEGADFVrYAAFREDPLLNPLGTPSGLIEIYSKTIAKMGYDDCPGHPTWMEPAEWLGGPRGaKYPLHLISPHPKY 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 638 KLHSQMDHGNYSKSFKIEDREPVEINPNDAKSRGLKNGDIVKLFNDRGSCLAGVIVDEKVMPGVVQISTGAWYDPENPEK 717
Cdd:TIGR00509 637 RLHSQLDHTELRQAYKVQGREPVMIHPDDAAARGIADGDIVRVFNARGQILAGAVVTDGIRKGVVQIHEGAWYDPADVRE 716
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 142091137 718 PNSMCKHGNPNVLTRDKGTSKLGQGPIAHSCLIEIEKYKDKPPKVTAHEPPIII 771
Cdd:TIGR00509 717 PGGLCKYGNPNVLTADIGTSSLAQGNSGNTVLVEIEKYTGPAPPLTAFDQPAAA 770
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
11-619 |
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: 853.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 11 LTSTHWGTYRAKVKNGKVQELIGWENDK-DPSPIGPGILDIQDGPTRIDAPMVRKSWLEQGPGSRnDLRGIDPFIEVSWK 89
Cdd:cd02751 1 PTACHWGPFKAHVKDGVIVRVEPDDTDQpRPCPRGRSVRDRVYSPDRIKYPMKRVGWLGNGPGSR-ELRGEGEFVRISWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 90 KAEQLVADELTRVKNTYGNASIFGGSYGWASAGRFHHAQSQLHRFLNCIGGYTRSKFTYSFAAAEAMVPHILGSYRAYlD 169
Cdd:cd02751 80 EALDLVASELKRIREKYGNEAIFGGSYGWASAGRLHHAQSLLHRFLNLIGGYLGSYGTYSTGAAQVILPHVVGSDEVY-E 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 170 TCTSWDLINKNTELFVCFGGIPIKNGQISQGGtGNHYQRKNLVEAANSGIEFINISPLKSDLIDEVKGEWITARPNTDTA 249
Cdd:cd02751 159 QGTSWDDIAEHSDLVVLFGANPLKTRQGGGGG-PDHGSYYYLKQAKDAGVRFICIDPRYTDTAAVLAAEWIPIRPGTDVA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 250 LMLGLAHTLHVEGLSDKQFLENYTQGFEKFLPYLLGTNDGIEKNADWAASICNIPSSKIKELAHKISSKRTMISVSWSLT 329
Cdd:cd02751 238 LMLAMAHTLITEDLHDQAFLARYTVGFDEFKDYLLGESDGVPKTPEWAAEITGVPAETIRALAREIASKRTMIAQGWGLQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 330 RQDHGEQPFWMAIMLASMVGQIGLPGGGFGFGYSATNYIGGQFKVLPGAAFPQADNKIENFIPVARISDLLLGPGEKFDF 409
Cdd:cd02751 318 RAHHGEQPAWMLVTLAAMLGQIGLPGGGFGFGYGYSNGGGPPRGGAGGPGLPQGKNPVKDSIPVARIADALLNPGKEFTA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 410 DGKTYVYPDTKIVYWAGGNPFHHHQDLNRLIKAWEKPDTIISNEWCWNTLAKRSDIVLPCTTPLERGDIMMTPR--DPYV 487
Cdd:cd02751 398 NGKLKTYPDIKMIYWAGGNPLHHHQDLNRLIKALRKDETIVVHDIFWTASARYADIVLPATTSLERNDIGLTGNysNRYL 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 488 VSMSKLVEPHGKAKNDYEIFSGIARKMGVEEKFTEGRNQEEWQKWIYKQTFERAAAANIKIPSYEKFREEKWFKIDDPSE 567
Cdd:cd02751 478 IAMKQAVEPLGEARSDYEIFAELAKRLGVEEEFTEGRDEMEWLEHLYEETRAKAAGPGPELPSFEEFWEKGIVRVPAAPK 557
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 142091137 568 PTLMLKDFREDPIKYPLDTQSGKIEIFSQTVSDFKYDDCPGHPVWIEPCEWL 619
Cdd:cd02751 558 PFVAFADFREDPEANPLGTPSGKIEIYSETLADFGYDDCPGHPTWIEPWEGL 609
|
|
| PRK15102 |
PRK15102 |
trimethylamine-N-oxide reductase TorA; |
11-771 |
0e+00 |
|
trimethylamine-N-oxide reductase TorA;
Pssm-ID: 237909 [Multi-domain] Cd Length: 825 Bit Score: 730.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 11 LTSTHWGTYRAKVKNGKVQELIGWENDKDPSPIGPGILDIQDGPTRIDAPMVRKSWLEQGPGSRNDLRGIDPFIEVSWKK 90
Cdd:PRK15102 45 LTGSHWGAFRAKVKNGRFVEAKPFELDKYPTKMINGIKGHVYNPSRIRYPMVRLDWLRKRHKSDTSQRGDNRFVRVSWDE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 91 AEQLVADELTRVKNTYGNASIFGGSYGWASAGRFHHAQSQLHRFLNCIGGYTRSKFTYSFAAAEAMVPHILGSYRAYlDT 170
Cdd:PRK15102 125 ALDLFYEELERVQKTYGPSALHTGQTGWQSTGQFHSATGHMQRAIGMHGNSVGTVGDYSTGAGQVILPYVLGSTEVY-EQ 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 171 CTSWDLINKNTELFVCFGGIPIKNGQIS-QGGTGNHY----QRKNLVeaANSGIEFINISPLKSDLIDEVKGEWITARPN 245
Cdd:PRK15102 204 GTSWPLILENSKTIVLWGSDPVKNLQVGwNCETHESYaylaQLKEKV--AKGEINVISIDPVVTKTQNYLGCEHLYVNPQ 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 246 TDTALMLGLAHTLHVEGLSDKQFLENYTQGFEKFLPYLLGTNDGIEKNADWAASICNIPSSKIKELAHKISSKRTMISVS 325
Cdd:PRK15102 282 TDVPLMLALAHTLYSENLYDKKFIDNYCLGFEQFLPYLLGEKDGVPKTPEWAEKICGIDAETIRELARQMAKGRTQIIAG 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 326 WSLTRQDHGEQPFWMAIMLASMVGQIGLP--GGGFGFGYSATNYIGGQFkVLPGaAFPQA---------DNK----IENF 390
Cdd:PRK15102 362 WCIQRQQHGEQPYWMGAVLAAMLGQIGLPggGISYGHHYSGIGVPSSGG-AIPG-GFPGNldtgqkpkhDNSdykgYSST 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 391 IPVARISDLLLGPGEKFDFDGKTYVYPDTKIVYWAGGNPFHHHQDLNRLIKAWEKPDTIISNEWCWNTLAKRSDIVLPCT 470
Cdd:PRK15102 440 IPVARFIDAILEPGKTINWNGKKVTLPPLKMMIFSGTNPWHRHQDRNRMKEAFRKLETVVAIDNQWTATCRFADIVLPAC 519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 471 TPLERGDImmtprDPY-------VVSMSKLVEPHGKAKNDYEIFSGIARKMGVEEKFTEGRNQEEWQKWIYKQTfERAAA 543
Cdd:PRK15102 520 TQFERNDI-----DQYgsysnrgIIAMKKVVEPLFESRSDFDIFRELCRRFGREKEYTRGMDEMGWLKRLYQEC-KQQNK 593
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 544 ANIKIPSYEKFREEKWFKIDDPsEPTLMLKDFREDPIKYPLDTQSGKIEIFSQTVSDFKYDDCPGHPVWIEPCEWL--GQ 621
Cdd:PRK15102 594 GKFHMPEFDEFWKKGYVEFGEG-QPWVRHADFREDPELNPLGTPSGLIEIYSRKIADMGYDDCQGHPMWFEKIERShgGP 672
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 622 KNKKFPLHLISNQPKNKLHSQM-DHGNYSKSFKIEDREPVEINPNDAKSRGLKNGDIVKLFNDRGSCLAGVIVDEKVMPG 700
Cdd:PRK15102 673 GSDKYPLWLQSVHPDKRLHSQLcESEELRETYTVQGREPVYINPQDAKARGIKDGDVVRVFNDRGQVLAGAVVSDRYPPG 752
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 142091137 701 VVQISTGAWYDPENPEKPNSMCKHGNPNVLTRDKGTSKLGQGPIAHSCLIEIEKYKDKPPKVTAHEPPIII 771
Cdd:PRK15102 753 VIRIHEGAWYGPDKGGEIGALCTYGDPNTLTLDIGTSQLAQATSAHTCLVEIEKYQGKVPPVTSFNGPVEV 823
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
19-754 |
0e+00 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 550.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 19 YRAKVKNGKVQELIGweNDKDPSPIGP------GILDIQDGPTRIDAPMVRKSwleqgpgsrndLRGIDPFIEVSWKKAE 92
Cdd:COG0243 37 LGVKVEDGRVVRVRG--DPDHPVNRGRlcakgaALDERLYSPDRLTYPMKRVG-----------PRGSGKFERISWDEAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 93 QLVADELTRVKNTYGNASIFGGSYGwASAGRFHHAQSQL-HRFLNCIGG---YTRSkfTYSFAAAEAMVPHILGSYRAyl 168
Cdd:COG0243 104 DLIAEKLKAIIDEYGPEAVAFYTSG-GSAGRLSNEAAYLaQRFARALGTnnlDDNS--RLCHESAVAGLPRTFGSDKG-- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 169 dtCTSWDLInKNTELFVCFGGIPIKNGQIsqggtgnhyQRKNLVEAA-NSGIEFINISPLKSDLIDEVkGEWITARPNTD 247
Cdd:COG0243 179 --TVSYEDL-EHADLIVLWGSNPAENHPR---------LLRRLREAAkKRGAKIVVIDPRRTETAAIA-DEWLPIRPGTD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 248 TALMLGLAHTLHVEGLSDKQFLENYTQGFEKFLPYLlgtndgIEKNADWAASICNIPSSKIKELAHKI-SSKRTMISVSW 326
Cdd:COG0243 246 AALLLALAHVLIEEGLYDRDFLARHTVGFDELAAYV------AAYTPEWAAEITGVPAEDIRELAREFaTAKPAVILWGM 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 327 SLTRQDHGEQPFWMAIMLASMVGQIGLPgggfgfgysatnyiGGQFKVLPGAAfpqadnkIEnfipvarisdlllgpgek 406
Cdd:COG0243 320 GLQQHSNGTQTVRAIANLALLTGNIGKP--------------GGGPFSLTGEA-------IL------------------ 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 407 fdfDGKTYvypDTKIVYWAGGNPFHHHQDLNRLIKAWEKPDTIISNEWCWNTLAKRSDIVLPCTTPLERGDIMMTPRDPY 486
Cdd:COG0243 361 ---DGKPY---PIKALWVYGGNPAVSAPDTNRVREALRKLDFVVVIDTFLTETARYADIVLPATTWLERDDIVTNSEDRR 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 487 VVSMSKLVEPHGKAKNDYEIFSGIARKMGVEEKFTEGRNQEEWQKWIYKQTFERAAaanikipSYEKFREEKWFKIDDPS 566
Cdd:COG0243 435 VHLSRPAVEPPGEARSDWEIFAELAKRLGFEEAFPWGRTEEDYLRELLEATRGRGI-------TFEELREKGPVQLPVPP 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 567 EPTlmlkdFREDPikyPLDTQSGKIEIFSQTVsdfkydDCPGHPVWIEPCEWLGQKNKKFPLHLISNQPKNKLHSQMDhg 646
Cdd:COG0243 508 EPA-----FRNDG---PFPTPSGKAEFYSETL------ALPPLPRYAPPYEGAEPLDAEYPLRLITGRSRDQWHSTTY-- 571
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 647 NYSKSFKIEDREPVEINPNDAKSRGLKNGDIVKLFNDRGSCLAGVIVDEKVMPGVVQISTGAWYDPENpekpnsmCKHGN 726
Cdd:COG0243 572 NNPRLREIGPRPVVEINPEDAAALGIKDGDLVRVESDRGEVLARAKVTEGIRPGVVFAPHGWWYEPAD-------DKGGN 644
|
730 740
....*....|....*....|....*...
gi 142091137 727 PNVLTRDkGTSKLGQGPIAHSCLIEIEK 754
Cdd:COG0243 645 VNVLTPD-ATDPLSGTPAFKSVPVRVEK 671
|
|
| MopB_DmsA-EC |
cd02770 |
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
20-600 |
1.65e-112 |
|
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: 354.71 E-value: 1.65e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 20 RAKVKNGKVQElIGWENDKDPSPIGPGILDIQDG---------PTRIDAPMVRKSWleqgpgsrndlRGIDPFIEVSWKK 90
Cdd:cd02770 15 KAHVKDGVITR-IETDDTGDDDPGFHQIRACLRGrsqrkrvynPDRLKYPMKRVGK-----------RGEGKFVRISWDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 91 AEQLVADELTRVKNTYGNASIF----GGSYGWASAGRfhhaqSQLHRFLNCIGGYTRSKFTYSFAAAEAMVPHILGSYra 166
Cdd:cd02770 83 ALDTIASELKRIIEKYGNEAIYvnygTGTYGGVPAGR-----GAIARLLNLTGGYLNYYGTYSWAQITTATPYTYGAA-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 167 ylDTCTSWDLInKNTELFVCFGGIPiknGQISQGGTGNHYqrkNLVEAANSGIEFINISPLKSDLIDEVKGEWITARPNT 246
Cdd:cd02770 156 --ASGSSLDDL-KDSKLVVLFGHNP---AETRMGGGGSTY---YYLQAKKAGAKFIVIDPRYTDTAVTLADEWIPIRPGT 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 247 DTALMLGLAHTLHVEGLSDKQFLENYTQGF-EKFLP-----------YLLGTN-DGIEKNADWAASICNIPSSKIKELAH 313
Cdd:cd02770 227 DAALVAAMAYVMITENLHDQAFLDRYCVGFdAEHLPegappnesykdYVLGTGyDGTPKTPEWASEITGVPAETIRRLAR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 314 KI-SSKRTMISVSWSLTRQDHGEQPFWMAIMLASMVGQIGLPGGgfgfgySATNYIGGqfKVLPGAAFPQADNKIENFIP 392
Cdd:cd02770 307 EIaTTKPAAILQGWGPQRHANGEQAARAIMMLAAMTGNVGIPGG------NTGARPGG--SAYNGAGLPAGKNPVKTSIP 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 393 VARISDLLLGPGE----KFDFDGKTYVYPDTKIVY-WAGGNPFHHHQDLNRLIKAWEKPDT----IISNEWCWNTLAKRS 463
Cdd:cd02770 379 CFMWTDAIERGEEmtadDGGVKGADKLKSNIKMIWnYAGNTLINQHSDDNNTTRALLDDESkcefIVVIDNFMTPSARYA 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 464 DIVLPCTTPLERGDIMMTPRD---PYVVSMSKLVEPHGKAKNDYEIFSGIARKMGVEEKFTEGRNQEEWQKWIYKQTfer 540
Cdd:cd02770 459 DILLPDTTELEREDIVLTSNAgmmEYLIYSQKAIEPLYECKSDYEICAELAKRLGVEDQFTEGKTEQEWLEELYGQT--- 535
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 541 aAAANIKIPSYEKFREEKWFKIDDPSePTLMLKDFREDPIKYPLDTQSGKIEIFSQTVSD 600
Cdd:cd02770 536 -RAKEPGLPTYEEFREKGIYRVPRAL-PFVAFEDFREDPENNPLKTPSGKIEIYSKALAD 593
|
|
| PRK14990 |
PRK14990 |
anaerobic dimethyl sulfoxide reductase subunit A; Provisional |
54-754 |
4.64e-98 |
|
anaerobic dimethyl sulfoxide reductase subunit A; Provisional
Pssm-ID: 184952 [Multi-domain] Cd Length: 814 Bit Score: 322.36 E-value: 4.64e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 54 PTRIDAPMvrkswleqgpgSRNDLRGIDPFIEVSWKKAEQLVADELTRVKNTYGNASIF----GGSYGWASAGRFHHAQS 129
Cdd:PRK14990 117 PDRLKYPM-----------KRVGARGEGKFERISWEEAYDIIATNMQRLIKEYGNESIYlnygTGTLGGTMTRSWPPGNT 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 130 QLHRFLNCIGGYTRSKFTYSFAAAEAMVPHilgSYRAYLDTCTSWDLinKNTELFVCFGGIPiknGQISQGGTGNHYQRK 209
Cdd:PRK14990 186 LVARLMNCCGGYLNHYGDYSSAQIAEGLNY---TYGGWADGNSPSDI--ENSKLVVLFGNNP---GETRMSGGGVTYYLE 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 210 NLVEAANSgiEFINISPLKSDLIDEVKGEWITARPNTDTALMLGLAHTLHVEGLSDKQFLENYTQGF-EKFLP------- 281
Cdd:PRK14990 258 QARQKSNA--RMIIIDPRYTDTGAGREDEWIPIRPGTDAALVNGLAYVMITENLVDQPFLDKYCVGYdEKTLPasapkng 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 282 ----YLLGT-NDGIEKNADWAASICNIPSSKIKELAHKI-SSKRTMISVSWSLTRQDHGEQPFWMAIMLASMVGQIGLPG 355
Cdd:PRK14990 336 hykaYILGEgPDGVAKTPEWASQITGVPADKIIKLAREIgSTKPAFISQGWGPQRHANGEIATRAISMLAILTGNVGING 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 356 GGFGFGYsatnyigGQFKvLPGAAFPQADNKIENFIPVARISDLL-LGPGEKFDFDG---KTYVYPDTKIVY-WAGGNPF 430
Cdd:PRK14990 416 GNSGARE-------GSYS-LPFVRMPTLENPIQTSISMFMWTDAIeRGPEMTALRDGvrgKDKLDVPIKMIWnYAGNCLI 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 431 HHHQDLNR---LIKAWEKPDTIISNEWCWNTLAKRSDIVLPCTTPLERGDIMMTP---RDPYVVSMSKLVEPHGKAKNDY 504
Cdd:PRK14990 488 NQHSEINRtheILQDDKKCELIVVIDCHMTSSAKYADILLPDCTASEQMDFALDAscgNMSYVIFNDQVIKPRFECKTIY 567
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 505 EIFSGIARKMGVEEKFTEGRNQEEWQKWIYKQTfeRAAAANIkiPSYEKFREEKWFKIDDPSEPTLMLKDFREDPIKYPL 584
Cdd:PRK14990 568 EMTSELAKRLGVEQQFTEGRTQEEWMRHLYAQS--REAIPEL--PTFEEFRKQGIFKKRDPQGHHVAYKAFREDPQANPL 643
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 585 DTQSGKIEIFSQTVSDF-------KYDDCPGHPVWIEPCE-WLGQKNKKFPLHLISNQPKNKLHSQmdHGNYSkSFKIED 656
Cdd:PRK14990 644 TTPSGKIEIYSQALADIaatwelpEGDVIDPLPIYTPGFEsYQDPLNKQYPLQLTGFHYKSRVHST--YGNVD-VLKAAC 720
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 657 REPVEINPNDAKSRGLKNGDIVKLFNDRGSCLAGVIVDEKVMPGVVQISTGAWYDPEnpekPNSMCKHGNPNVLTRDKgT 736
Cdd:PRK14990 721 RQEMWINPLDAQKRGINNGDKVRIFNDRGEVHIEAKVTPRMMPGVVALGEGAWYDPD----AKRVDKGGCINVLTTQR-P 795
|
730
....*....|....*...
gi 142091137 737 SKLGQGPIAHSCLIEIEK 754
Cdd:PRK14990 796 SPLAKGNPSHTNLVQVEK 813
|
|
| MopB_CT_DMSOR-BSOR-TMAOR |
cd02793 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
626-754 |
5.80e-78 |
|
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: 246.78 E-value: 5.80e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 626 FPLHLISNQPKNKLHSQMDHGNYSKSFKIEDREPVEINPNDAKSRGLKNGDIVKLFNDRGSCLAGVIVDEKVMPGVVQIS 705
Cdd:cd02793 1 YPLHLLSNQPATRLHSQLDHGSLSRAYKVQGREPIRINPADAAARGIADGDIVRVFNDRGACLAGAVVTDGIMPGVVQLP 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 142091137 706 TGAWYDPENPEKPNSMCKHGNPNVLTRDKGTSKLGQGPIAHSCLIEIEK 754
Cdd:cd02793 81 TGAWYDPDDPGEPGPLCKHGNPNVLTLDIGTSSLAQGCSAQTCLVQIEK 129
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
16-514 |
4.53e-68 |
|
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: 229.52 E-value: 4.53e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 16 WGTYRAKVKNGKVQELIGWENDKD----PSPIGPGILDIQDGPTRIDAPMVRKSWLEQgpgsrndlrgidpFIEVSWKKA 91
Cdd:cd00368 10 GCGILVYVKDGKVVRIEGDPNHPVnegrLCDKGRAGLDGLYSPDRLKYPLIRVGGRGK-------------FVPISWDEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 92 EQLVADELTRVKNTYGNASIFGGSYGWASAGRFHHAQSqlhRFLNCIGGYTRSKFTYSFAAAEAMVPHILGsyraYLDTC 171
Cdd:cd00368 77 LDEIAEKLKEIREKYGPDAIAFYGGGGASNEEAYLLQK---LLRALGSNNVDSHARLCHASAVAALKAFGG----GAPTN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 172 TSWDLinKNTELFVCFGGIPIKNGQISqggtgNHYQRKnlveAANSGIEFINISPLKSDLIDEVKgEWITARPNTDTALM 251
Cdd:cd00368 150 TLADI--ENADLILLWGSNPAETHPVL-----AARLRR----AKKRGAKLIVIDPRRTETAAKAD-EWLPIRPGTDAALA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 252 lglahtlhveglsdkqflenytqgfekflpyllgtndgiekNADWAASICNIPSSKIKELAHKI-SSKRTMISVSWSLTR 330
Cdd:cd00368 218 -----------------------------------------LAEWAAEITGVPAETIRALAREFaAAKRAVILWGMGLTQ 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 331 QDHGEQPFWMAIMLASMVGQIGLPgggfgfgysatnyiGGQFkvlpgaafpqadnkienfipvarisdlllgpgekfdfd 410
Cdd:cd00368 257 HTNGTQNVRAIANLAALTGNIGRP--------------GGGL-------------------------------------- 284
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 411 gktyvypdtkivyWAGGNPFHHHQDLNRLIKAWEKPDTIISNEWCWNTLAKRSDIVLPCTTPLERGDIMMTPrDPYVVSM 490
Cdd:cd00368 285 -------------GPGGNPLVSAPDANRVRAALKKLDFVVVIDIFMTETAAYADVVLPAATYLEKEGTYTNT-EGRVQLF 350
|
490 500
....*....|....*....|....
gi 142091137 491 SKLVEPHGKAKNDYEIFSGIARKM 514
Cdd:cd00368 351 RQAVEPPGEARSDWEILRELAKRL 374
|
|
| MopB_CT_DMSOR-like |
cd02777 |
The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
626-754 |
6.94e-66 |
|
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: 214.37 E-value: 6.94e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 626 FPLHLISNQPKNKLHSQMDH-GNYSKSFKIEDREPVEINPNDAKSRGLKNGDIVKLFNDRGSCLAGVIVDEKVMPGVVQI 704
Cdd:cd02777 1 YPLQLISPHPKRRLHSQLDNvPWLREAYKVKGREPVWINPLDAAARGIKDGDIVRVFNDRGAVLAGARVTDRIMPGVVAL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 142091137 705 STGAWYDPENpekPNSMCKHGNPNVLTRDKGTSKLGQGPIAHSCLIEIEK 754
Cdd:cd02777 81 PEGAWYDPDD---NGGLDKGGNPNVLTSDIPTSKLAQGNPANTCLVEIEK 127
|
|
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
54-597 |
3.39e-46 |
|
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: 172.43 E-value: 3.39e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 54 PTRIDAPMVRkswleQGPGSRNdlrgidpFIEVSWKKAEQLVADELTRVKNTYGNASIFGGSYgwasAGRFHHAQSQLHR 133
Cdd:cd02766 53 PDRLLTPLKR-----VGRKGGQ-------WERISWDEALDTIAAKLKEIKAEYGPESILPYSY----AGTMGLLQRAARG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 134 FLNCIGGYTRSKFTYSFAAAEAmvphilgsyrAY-LDTCTSW-----DLINKNteLFVCFGGIPIKNgqisqggtgNHYQ 207
Cdd:cd02766 117 RFFHALGASELRGTICSGAGIE----------AQkYDFGASLgndpeDMVNAD--LIVIWGINPAAT---------NIHL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 208 RKNLVEAANSGIEFINISPLKS---DLIDEVkgewITARPNTDTALMLGLAHTLHVEGLSDKQFLENYTQGFEKFLPYLL 284
Cdd:cd02766 176 MRIIQEARKRGAKVVVIDPYRTataARADLH----IQIRPGTDGALALGVAKVLFREGLYDRDFLARHTEGFEELKAHLE 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 285 gtndgiEKNADWAASICNIPSSKIKELAHKI-SSKRTMISVSWSLTRQDHGEQPFWMAIMLASMVGQIGLPgggfgfgys 363
Cdd:cd02766 252 ------TYTPEWAAEITGVSAEEIEELARLYgEAKPPSIRLGYGMQRYRNGGQNVRAIDALPALTGNIGVP--------- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 364 atnyiGGqfkvlpGAafpqadnkienfipvarisdlLLGPGEkfdfdgktyvyPDTKIVYWAGGNPFHHHQDLNRLIKAW 443
Cdd:cd02766 317 -----GG------GA---------------------FYSNSG-----------PPVKALWVYNSNPVAQAPDSNKVRKGL 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 444 EKPD-TIISNEWCWNTLAKRSDIVLPCTTPLERGDIMMTPRDPYVVSMSKLVEPHGKAKNDYEIFSGIARKMGVEEKFTE 522
Cdd:cd02766 354 AREDlFVVVHDQFMTDTARYADIVLPATTFLEHEDVYASYWHYYLQYNEPAIPPPGEARSNTEIFRELAKRLGFGEPPFE 433
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 142091137 523 gRNQEEWQkwiykqtfeRAAAANIKIPSyekfreekwFKIDDPSEPTLMLKDFREDPIKYP-LDTQSGKIEIFSQT 597
Cdd:cd02766 434 -ESDEEWL---------DQALDGTGLPL---------EGIDLERLLGPRKAGFPLVAWEDRgFPTPSGKFEFYSER 490
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
56-513 |
8.23e-46 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 167.58 E-value: 8.23e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 56 RIDAPMVRkswleqgpgsrndlRGIDPFIEVSWKKAEQLVADELTRVKNTYGNASIF--GGSYGWASAGRFHHAQSQLHR 133
Cdd:pfam00384 1 RLKYPMVR--------------RGDGKFVRVSWDEALDLIAKKLKRIIKKYGPDAIAinGGSGGLTDVESLYALKKLLNR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 134 FLNCIGGYTRSKFTYSFAAAEAmVPHILGSYRAYLDTCTSWDlinkNTELFVCFGGIPIKNGQIsqggtGNHYQRKnlvE 213
Cdd:pfam00384 67 LGSKNGNTEDHNGDLCTAAAAA-FGSDLRSNYLFNSSIADIE----NADLILLIGTNPREEAPI-----LNARIRK---A 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 214 AANSGIEFINISPlKSDLIDEVkgEWITARPNTDTALMLGLAHTLHVEGLSDKQFlenytqgfekflpyllgtndgiekn 293
Cdd:pfam00384 134 ALKGKAKVIVIGP-RLDLTYAD--EHLGIKPGTDLALALAGAHVFIKELKKDKDF------------------------- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 294 adwaasicnipsskikelahkisSKRTMISVSWSLTRQDHGEQPFWMAIMLASMVGQIGLPGGGfgfgysatnyiGGQFK 373
Cdd:pfam00384 186 -----------------------APKPIIIVGAGVLQRQDGEAIFRAIANLADLTGNIGRPGGG-----------WNGLN 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 374 VLPGAAFPQADNKIeNFIPVARISDLLLGPGEKfdfdgktyvypDTKIVYWAGGNPFHHHQDLNRLIKAWEKPDTIISNE 453
Cdd:pfam00384 232 ILQGAASPVGALDL-GLVPGIKSVEMINAIKKG-----------GIKVLYLLGNNPFVTHADENRVVKALQKLDLFVVYD 299
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 142091137 454 WCWNT-LAKRSDIVLPCTTPLERGDIMMTPRDPyVVSMSKLVEPHGKAKNDYEIFSGIARK 513
Cdd:pfam00384 300 GHHGDkTAKYADVILPAAAYTEKNGTYVNTEGR-VQSTKQAVPPPGEAREDWKILRALSEV 359
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
19-704 |
1.62e-43 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 167.75 E-value: 1.62e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 19 YRAKVKNGKVQELIGWENdkdpSPIGPGIL--------DIQDGPTRIDAPMVRKSwleqgpgsrndlrgiDPFIEVSWKK 90
Cdd:COG3383 20 IDLEVKDGKIVKVEGDPD----HPVNRGRLcvkgrfgfEFVNSPDRLTTPLIRRG---------------GEFREVSWDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 91 AEQLVADELTRVKNTYGNASIfgGSYGwaSAGRFHHAQSQLHRFL------NCIGGYTRSkFTYSFAAAEAMVphiLGSy 164
Cdd:COG3383 81 ALDLVAERLREIQAEHGPDAV--AFYG--SGQLTNEENYLLQKLArgvlgtNNIDNNARL-CMASAVAGLKQS---FGS- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 165 raylDTCT-SWDLInKNTELFVCFGGIPikngqisqggTGNH---YQRknLVEAANSGIEFINISPLKSDLiDEVKGEWI 240
Cdd:COG3383 152 ----DAPPnSYDDI-EEADVILVIGSNP----------AEAHpvlARR--IKKAKKNGAKLIVVDPRRTET-ARLADLHL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 241 TARPNTDTALMLGLAHTLHVEGLSDKQFLENYTQGFEKFLpyllgtnDGIEKNA-DWAASICNIPSSKIKELAHKI-SSK 318
Cdd:COG3383 214 QIKPGTDLALLNGLLHVIIEEGLVDEDFIAERTEGFEELK-------ASVAKYTpERVAEITGVPAEDIREAARLIaEAK 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 319 RTMISVSWSLTRQDHGEQPFWMAIMLASMVGQIGLPgggfgfgYSATNYIGGQFKV------------LPG---AAFPQA 383
Cdd:COG3383 287 RAMILWGMGVNQHTQGTDNVNAIINLALATGNIGRP-------GTGPFPLTGQNNVqggrdmgalpnvLPGyrdVTDPEH 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 384 DNKIENFIPVARISDlllGPG----EKFDF--DGKTyvypdtKIVYWAGGNPFHHHQDLNRLIKAWEKPDTIISNEWCWN 457
Cdd:COG3383 360 RAKVADAWGVPPLPD---KPGltavEMFDAiaDGEI------KALWIIGENPAVSDPDANHVREALEKLEFLVVQDIFLT 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 458 TLAKRSDIVLPCTTPLERGDIMM-TPRDpyvVSMS-KLVEPHGKAKNDYEIFSGIARKMGVEekFTEGRNQEEWQKWiyk 535
Cdd:COG3383 431 ETAEYADVVLPAASWAEKDGTFTnTERR---VQRVrKAVEPPGEARPDWEIIAELARRLGYG--FDYDSPEEVFDEI--- 502
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 536 qtfeRAAAANIKIPSYEKFREEK---W--FKIDDPSEPTLMLKDFRedpikypldTQSGKIEIfsqtvsdfkyddcpgHP 610
Cdd:COG3383 503 ----ARLTPDYSGISYERLEALGgvqWpcPSEDHPGTPRLFTGRFP---------TPDGKARF---------------VP 554
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 611 V-WIEPCEwlgQKNKKFPLHLISNQPKNKLHSQMDHGNYSKSFKIEDREPVEINPNDAKSRGLKNGDIVKLFNDRGSCLA 689
Cdd:COG3383 555 VeYRPPAE---LPDEEYPLVLTTGRLLDQWHTGTRTRRSPRLNKHAPEPFVEIHPEDAARLGIKDGDLVRVSSRRGEVVL 631
|
730
....*....|....*
gi 142091137 690 GVIVDEKVMPGVVQI 704
Cdd:COG3383 632 RARVTDRVRPGTVFM 646
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
21-686 |
1.66e-40 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 159.45 E-value: 1.66e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 21 AKVKNGKVQELIGweNDKDPSPI-------GPGILDIQDgPTRIDAPMVRKswleqGPgsrndlRGIDPFIEVSWKKAEQ 93
Cdd:PRK15488 59 ARVVNGKNVFIQG--NPKAKSFGtkvcargGSGHSLLYD-PQRIVKPLKRV-----GE------RGEGKWQEISWDEAYQ 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 94 LVADELTRVKNTYGNASI-FGGSYGWASAGRFHHAQS-----QLHRFLNCIGGYTrskftysfAAAEAMVPHILGsyray 167
Cdd:PRK15488 125 EIAAKLNAIKQQHGPESVaFSSKSGSLSSHLFHLATAfgspnTFTHASTCPAGYA--------IAAKVMFGGKLK----- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 168 LDTCTSWDLINKNTELFvcfGGIPIKngqisqggtgnhYQRKNLVEAANSGIEFINISPLKSDLIDEVKgEWITARPNTD 247
Cdd:PRK15488 192 RDLANSKYIINFGHNLY---EGINMS------------DTRGLMTAQMEKGAKLVVFEPRFSVVASKAD-EWHAIRPGTD 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 248 TALMLGLAHTLHVEGLSDKQFLENYTQGFEKFLPYLLgtndgiEKNADWAASICNIPSSKIKELAHKISSKRTMISVSWS 327
Cdd:PRK15488 256 LAVVLALCHVLIEENLYDKAFVERYTSGFEELAASVK------EYTPEWAEAISDVPADDIRRIARELAAAAPHAIVDFG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 328 lTRQDHGEQPFWM--AIMLAS-MVGQI----GLPGGGFGFGYsatNYIGGQfKVLPGAAFPqadnKIENF--IPVARIsD 398
Cdd:PRK15488 330 -HRATFTPEEFDMrrAIFAANvLLGNIerkgGLYFGKNASVY---NKLAGE-KVAPTLAKP----GVKGMpkPTAKRI-D 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 399 LLlgpGEKFDF----------------DGKTYvypdtKIVYW--AGGNPFHHHQDLNRLIKAWEKPDTIISNEWCWNTLA 460
Cdd:PRK15488 400 LV---GEQFKYiaagggvvqsiidatlTQKPY-----QIKGWvmSRHNPMQTVTDRADVVKALKKLDLVVVCDVYLSESA 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 461 KRSDIVLPCTTPLErgdimmtpRDPYVVSMS----------KLVEPHGKAKNDYEIFSGIARKMGVEEKFTeGRNQEEWQ 530
Cdd:PRK15488 472 AYADVVLPESTYLE--------RDEEISDKSgknpayalrqRVVEPIGDTKPSWQIFKELGEKMGLGQYYP-WQDMETLQ 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 531 KwiykqtfeRAAAANIKIpsYEKFREEKWFKIDDP---SEPTlMLKDFREdpiKYP----------------LDTQSGKI 591
Cdd:PRK15488 543 L--------YQVNGDHAL--LKELKKKGYVSFGVPlllREPK-MVAKFVA---RYPnakavdedgtygsqlkFKTPSGKI 608
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 592 EIFSQTVSDFkyddCPGHPVwiepcewLGQKN----KKFPLHLIsnQPKNKLHSQMDHGNYSKSFKIEDREPVEINPNDA 667
Cdd:PRK15488 609 ELFSAKLEAL----APGYGV-------PRYRDvalkKEDELYFI--QGKVAVHTNGATQNVPLLANLMSDNAVWIHPQTA 675
|
730
....*....|....*....
gi 142091137 668 KSRGLKNGDIVKLFNDRGS 686
Cdd:PRK15488 676 GKLGIKNGDEIRLENSVGK 694
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
21-515 |
1.23e-31 |
|
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: 128.95 E-value: 1.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 21 AKVKNGKVQELIGweNDKDPS------PIGPGILDIQDGPTRIDAPMVRKSwlEQGPGSrndlrgidpFIEVSWKKAEQL 94
Cdd:cd02755 16 ARVEDGRVVKIDG--NPLSPLsrgklcARGNAGIQLLYDPDRLKKPLIRVG--ERGEGK---------FREASWDEALQY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 95 VADELTRVKNTYGNASIFGGSYGwasagrfhHAQSQLHRFLNCIGGytrskfTYSFAAAEAMVPhiLGSYRAYLDTCTSW 174
Cdd:cd02755 83 IASKLKEIKEQHGPESVLFGGHG--------GCYSPFFKHFAAAFG------SPNIFSHESTCL--ASKNLAWKLVIDSF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 175 ------DLinKNTELFVCFGgipiKNGqisqGGTGNHYQRKNLVEAANSGIEFINISPLKSDLIDEVKgEWITARPNTDT 248
Cdd:cd02755 147 ggevnpDF--ENARYIILFG----RNL----AEAIIVVDARRLMKALENGAKVVVVDPRFSELASKAD-EWIPIKPGTDL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 249 ALMLGLAHTLHVEGLSDKQFLENYTQGFEKFlpyllgtNDGIEK-NADWAASICNIPSSKIKELAHKI--SSKRTMISVS 325
Cdd:cd02755 216 AFVLALIHVLISENLYDAAFVEKYTNGFELL-------KAHVKPyTPEWAAQITDIPADTIRRIAREFaaAAPHAVVDPG 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 326 WSLTRQDHGEQpFWMAI-MLASMVGQIGLPgggfgfgysatnyiGGQFkvlpgaafpqadnkienfipvarisdlllgpg 404
Cdd:cd02755 289 WRGTFYSNSFQ-TRRAIaIINALLGNIDKR--------------GGLY-------------------------------- 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 405 ekfdFDGKTYVYPdTKIVYWAGGNPFHHHQDLNRLIKAWEKPDTIISNEWCWNTLAKRSDIVLPCTTPLERGDIMMTPRD 484
Cdd:cd02755 322 ----YAGSAKPYP-IKALFIYRTNPFHSMPDRARLIKALKNLDLVVAIDILPSDTALYADVILPEATYLERDEPFSDKGG 396
|
490 500 510
....*....|....*....|....*....|...
gi 142091137 485 --PYVVSMSKLVEPHGKAKNDYEIFSGIARKMG 515
Cdd:cd02755 397 paPAVATRQRAIEPLYDTRPGWDILKELARRLG 429
|
|
| MopB_Nitrate-R-NarG-like |
cd02750 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
19-529 |
2.89e-31 |
|
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: 127.82 E-value: 2.89e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 19 YRAKVKNGkvqeLIGWEND-KDPSPIGPGILDIQD--------------GPTRIDAPMVRKSwleqgpgsrndLRGIDPF 83
Cdd:cd02750 18 WNVYVKNG----IVTREEQaTDYPETPPDLPDYNPrgcqrgasfswylySPDRVKYPLKRVG-----------ARGEGKW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 84 IEVSWKKAEQLVADELTRVKNTYGNASIFGGSyGWASAGRFHHAQSqlHRFLNCIGGYTRSKFTYsFAAAEAMVPHILGS 163
Cdd:cd02750 83 KRISWDEALELIADAIIDTIKKYGPDRVIGFS-PIPAMSMVSYAAG--SRFASLIGGVSLSFYDW-YGDLPPGSPQTWGE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 164 YRaylDTCTSWDLINknTELFVCFGgipiKNgqISQGGTGN-HYqrknLVEAANSGIEFINISP------LKSDLidevk 236
Cdd:cd02750 159 QT---DVPESADWYN--ADYIIMWG----SN--VPVTRTPDaHF----LTEARYNGAKVVVVSPdyspsaKHADL----- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 237 geWITARPNTDTALMLGLAHTLHVEGLSDKQFLENYTQgfekfLPYLLGTndgieknADWAASICNIPSSKIKELAHKI- 315
Cdd:cd02750 219 --WVPIKPGTDAALALAMAHVIIKEKLYDEDYLKEYTD-----LPFLVYT-------PAWQEAITGVPRETVIRLAREFa 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 316 SSKRTMISVSWSLTRQDHGEQPFWMAIMLASMVGQIGLPgggfgfgysatnyiGGqfkvlpGAAfpqadnkienfipvar 395
Cdd:cd02750 285 TNGRSMIIVGAGINHWYHGDLCYRALILLLALTGNEGKN--------------GG------GWA---------------- 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 396 isdlllgpgekfdfdgkTYVY-PDTKIVYWagGNPFHHHQDLNRLIKA--WEKPDTIISNEWCWNTLAKRSDIVLPCTTP 472
Cdd:cd02750 329 -----------------HYVGqPRVLFVWR--GNLFGSSGKGHEYFEDapEGKLDLIVDLDFRMDSTALYSDIVLPAATW 389
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 142091137 473 LERGDIMMTPRDPYVVSMSKLVEPHGKAKNDYEIFSGIARKmgVEEKFTEGRNQ----EEW 529
Cdd:cd02750 390 YEKHDLSTTDMHPFIHPFSPAVDPLWEAKSDWEIFKALAKK--VPWRTLTGRQQfyldHDW 448
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
20-615 |
3.05e-31 |
|
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: 128.19 E-value: 3.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 20 RAKVKNGKVQELIGwendkDPS-PIGPGIL--------DIQDGPTRIDAPMVRKswleqGPgsrndlRGIDPFIEVSWKK 90
Cdd:cd02759 14 LVYVKDGKLVKVEG-----DPNhPTNKGRLcmrglaapEIVYHPDRLLYPLKRV-----GE------RGENKWERISWDE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 91 AEQLVADELTRVKNTYGNASIfggsYGWASAGRFHHAQSQL--HRFLNCIG--GYTRSkfTYSFAAAEAMVPHILGSYRA 166
Cdd:cd02759 78 ALDEIAEKLAEIKAEYGPESI----ATAVGTGRGTMWQDSLfwIRFVRLFGspNLFLS--GESCYWPRDMAHALTTGFGL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 167 YLDTcTSWdlinKNTELFVCFGGIPIKNGQISQGGTgnhyqrknLVEAANSGIEFINISP------LKSDLidevkgeWI 240
Cdd:cd02759 152 GYDE-PDW----ENPECIVLWGKNPLNSNLDLQGHW--------LVAAMKRGAKLIVVDPrltwlaARADL-------WL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 241 TARPNTDTALMLGLAHTLHVEGLSDKQFLENYTQGFEKFLPYLlgtndgIEKNADWAASICNIPSSKIKELAHKISSKRT 320
Cdd:cd02759 212 PIRPGTDAALALGMLNVIINEGLYDKDFVENWCYGFEELAERV------QEYTPEKVAEITGVPAEKIRKAARLYATAKP 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 321 MiSVSWSLT--RQDHGEQPFWMAIMLASMVGQIGLPgggfgfgysatnyiGGQFkVLP---GAAFPQADNKIENfipvar 395
Cdd:cd02759 286 A-CIQWGLAidQQKNGTQTSRAIAILRAITGNLDVP--------------GGNL-LIPypvKMLIVFGTNPLAS------ 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 396 isdlllgpgekfdfdgktyvYPDTKIVYWAGGN-PFHHHQDLnrlikaWEKPDtiisnewcwntlAKRSDIVLPCTTPLE 474
Cdd:cd02759 344 --------------------YADTAPVLEALKAlDFIVVVDL------FMTPT------------AMLADIVLPVAMSLE 385
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 475 RGDIMMT--PRDPYVVSmSKLVEPHGKAKNDYEIFSGIARKMGveekftegrnqeewqkwiykqtferaaaanikipsYE 552
Cdd:cd02759 386 RPGLRGGfeAENFVQLR-QKAVEPYGEAKSDYEIVLELGKRLG-----------------------------------PE 429
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 142091137 553 KFREEKWFKIDDpseptlmlkdfREDPiKYPLDTQSGKIEIFSQTVSDFKYDDCPGHpvwIEP 615
Cdd:cd02759 430 EAEYYKYEKGLL-----------RPDG-QPGFNTPTGKVELYSTMLEELGYDPLPYY---REP 477
|
|
| Molydop_binding |
pfam01568 |
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
628-749 |
1.12e-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: 107.74 E-value: 1.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 628 LHLISNQPKNKLHSQMDHGNYSkSFKIEDREPVEINPNDAKSRGLKNGDIVKLFNDRGSCLAGVIVDEKVMPGVVQISTG 707
Cdd:pfam01568 1 LYLITGRVLGQYHSQTRTRRVL-RLAKPEPEVVEIHPEDAAALGIKDGDLVEVTSRRGSVVVRAKVTDRVRPGVVFMPFG 79
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 142091137 708 AWYDPenpekpnsmcKHGNPNVLTRDkGTSKLGQGPIAHSCL 749
Cdd:pfam01568 80 WWYEP----------RGGNANALTDD-ATDPLSGGPEFKTCA 110
|
|
| MopB_CT_DmsA-EC |
cd02794 |
The MopB_CT_DmsA-EC CD includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
626-754 |
2.00e-26 |
|
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: 104.68 E-value: 2.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 626 FPLHLISNQPKNKLHSQmdHGNYSKSFKIEDREpVEINPNDAKSRGLKNGDIVKLFNDRGSCLAGVIVDEKVMPGVVQIS 705
Cdd:cd02794 1 YPLQLIGWHYKRRTHST--FDNVPWLREAFPQE-VWINPLDAAARGIKDGDRVLVFNDRGKVIRPVKVTERIMPGVVALP 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 142091137 706 TGAWYDPENpekpNSMCKHGNPNVLTRDKgTSKLGQGPIAHSCLIEIEK 754
Cdd:cd02794 78 QGAWYEPDA----NGIDKGGCINTLTGLR-PSPLAKGNPQHTNLVQVEK 121
|
|
| MopB_4 |
cd02765 |
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
54-615 |
2.03e-26 |
|
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: 114.50 E-value: 2.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 54 PTRIDAPMVRKSwlEQGPGSrndlrgidpFIEVSWKKAEQLVADELTRVKNTYGNASIfggsyGWASAGRFHHAQSQLHr 133
Cdd:cd02765 53 PDRLKYPMKRVG--ERGEGK---------FERITWDEALDTIADKLTEAKREYGGKSI-----LWMSSSGDGAILSYLR- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 134 fLNCIGGYTRSKFTYSF--AAAEAMVPHILGSYRAYLDTCTSWdlinKNTELFVCFGGIPIKNGQisqggTGNHYqrknL 211
Cdd:cd02765 116 -LALLGGGLQDALTYGIdtGVGQGFNRVTGGGFMPPTNEITDW----VNAKTIIIWGSNILETQF-----QDAEF----F 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 212 VEAANSGIEFINISPLKSDLIdEVKGEWITARPNTDTALMLGLAHTLHVEGLSDKQFLENYT-------QGFEKFL---- 280
Cdd:cd02765 182 LDARENGAKIVVIDPVYSTTA-AKADQWVPIRPGTDPALALGMINYILEHNWYDEAFLKSNTsapflvrEDNGTLLrqad 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 281 -----------------------------PYLLG--TNDGI--------------EKNADWAASICNIPSSKIKELAHKI 315
Cdd:cd02765 261 vtatpaedgyvvwdtnsdspepvaatninPALEGeyTINGVkvhtvltalreqaaSYPPKAAAEICGLEEAIIETLAEWY 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 316 SS-KRTMISVSWSLTRQDHGEQPFWMAIMLASMVGQIGLPGGgfgfgysatnyIGGQFKVLpgaafpqadnkienfipva 394
Cdd:cd02765 341 ATgKPSGIWGFGGVDRYYHSHVFGRTAAILAALTGNIGRVGG-----------GVGQIKFM------------------- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 395 risdlllgpgekfdfdgktyvypdtkivyWAGGNPFHHHQ-DLNRLIKAWEKPDTIISNEWCWNTLAKRSDIVLPCTTPL 473
Cdd:cd02765 391 -----------------------------YFMGSNFLGNQpDRDRWLKVMKNLDFIVVVDIFHTPTVRYADIVLPAAHWF 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 474 ERGDIMMT-PRDPYVVSMSKLVEPHGKAKNDYEIFSGIARKMGVEEKFTEgrNQEEW-QKWIykqTFERAAAANIkipSY 551
Cdd:cd02765 442 EVEDLLVRyTTHPHVLLQQKAIEPLFESKSDFEIEKGLAERLGLGDYFPK--TPEDYvRAFM---NSDDPALDGI---TW 513
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 142091137 552 EKFREEKwfkiddpsepTLMLKDFREDPIKYPLD----TQSGKIEIFSQtvsDFKYDDCpGHPVWIEP 615
Cdd:cd02765 514 EALKEEG----------IIMRLATPEDPYVAYLDqkfgTPSGKLEFYNE---AAPELEE-ALPLPEEP 567
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
49-572 |
3.97e-26 |
|
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: 113.86 E-value: 3.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 49 DIQDGPTRIDAPMVRkswleqgpgsrndlRGIDPFIEVSWKKAEQLVADELTRVKNTYGNASIfggsyGWASAGRFH--- 125
Cdd:cd02754 47 KTLNGPERLTRPLLR--------------RNGGELVPVSWDEALDLIAERFKAIQAEYGPDSV-----AFYGSGQLLtee 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 126 -HAQSQLHRFL---NCIGGYTR-------SKFTYSFAAAEAMvphilGSYRayldtctswDLinKNTELFVCFG-----G 189
Cdd:cd02754 108 yYAANKLAKGGlgtNNIDTNSRlcmasavAGYKRSFGADGPP-----GSYD---------DI--EHADCFFLIGsnmaeC 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 190 IPIKNGQIsqggtgnhYQRKnlveAANSGIEFINISPLKS---DLIDEvkgeWITARPNTDTALMLGLAHTLHVEGLSDK 266
Cdd:cd02754 172 HPILFRRL--------LDRK----KANPGAKIIVVDPRRTrtaDIADL----HLPIRPGTDLALLNGLLHVLIEEGLIDR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 267 QFLENYTQGFEKFLpyllgtnDGIEK-NADWAASICNIPSSKIKELAHKISSKRTMISVsWS--LTRQDHGEQPFWMAIM 343
Cdd:cd02754 236 DFIDAHTEGFEELK-------AFVADyTPEKVAEITGVPEADIREAARLFGEARKVMSL-WTmgVNQSTQGTAANNAIIN 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 344 LASMVGQIGLPgggfgfgYSATNYIGGQFKVLPG------AAFPQADNKIENFIPVARISDLLLGPGEKFDFD-GKTYVY 416
Cdd:cd02754 308 LHLATGKIGRP-------GSGPFSLTGQPNAMGGrevgglANLLPGHRSVNNPEHRAEVAKFWGVPEGTIPPKpGLHAVE 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 417 PDTKI------VYW-AGGNPFHHHQDLNRLIKAWEKPDTIISNEWCWNT-LAKRSDIVLPCTTPLERgDIMMTPRDPYVV 488
Cdd:cd02754 381 MFEAIedgeikALWvMCTNPAVSLPNANRVREALERLEFVVVQDAFADTeTAEYADLVLPAASWGEK-EGTMTNSERRVS 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 489 SMSKLVEPHGKAKNDYEIFSGIARKMGVEEKFTEGRNQEEWQKWiykQTFERAAAANIKIPSYEKFREE--KWFKIDDPS 566
Cdd:cd02754 460 LLRAAVEPPGEARPDWWILADVARRLGFGELFPYTSPEEVFEEY---RRLSRGRGADLSGLSYERLRDGgvQWPCPDGPP 536
|
....*.
gi 142091137 567 EPTLML 572
Cdd:cd02754 537 EGTRRL 542
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
18-522 |
1.03e-23 |
|
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: 105.76 E-value: 1.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 18 TYRAKVKNGKVQELIGWENdkdpSPIGPGIL--------DIQDGPTRIDAPMVRKSwleqgpgsrndlrgiDPFIEVSWK 89
Cdd:cd02753 12 GLELWVKDNKIVGVEPVKG----HPVNRGKLcvkgrfgfDFVNSKDRLTKPLIRKN---------------GKFVEASWD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 90 KAEQLVADELTRVKNTYGNASIfggsygwasagrfhhaqsqlhrflnciGGYTRSKFT----YSFaaaEAMVPHILGSYR 165
Cdd:cd02753 73 EALSLVASRLKEIKDKYGPDAI---------------------------AFFGSAKCTneenYLF---QKLARAVGGTNN 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 166 ayLDTCT-------------------SWDLIN--KNTELFVCFGGIPikngqisqggTGNH---YQRknLVEAANSGIEF 221
Cdd:cd02753 123 --VDHCArlchsptvaglaetlgsgaMTNSIAdiEEADVILVIGSNT----------TEAHpviARR--IKRAKRNGAKL 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 222 INISPLKSDLIdEVKGEWITARPNTDTALMLGLAHTLHVEGLSDKQFLENYTQGFEKFLpyllgtnDGIEKNA-DWAASI 300
Cdd:cd02753 189 IVADPRRTELA-RFADLHLQLRPGTDVALLNAMAHVIIEEGLYDEEFIEERTEGFEELK-------EIVEKYTpEYAERI 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 301 CNIPSSKIKELAHKISSKRTMIsVSWSL--TRQDHGEQPFwMAIM-LASMVGQIGLPGggfgfgySATNYIGGQFKVlPG 377
Cdd:cd02753 261 TGVPAEDIREAARMYATAKSAA-ILWGMgvTQHSHGTDNV-MALSnLALLTGNIGRPG-------TGVNPLRGQNNV-QG 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 378 AAfpqadnkienfipvarisdlllgpgekfDFDGKTYVYPD-TKIVYWAGGNPFHHHQDLNRLIKAWEKPDTIISNEWCW 456
Cdd:cd02753 331 AC----------------------------DMGALPNVLPGyVKALYIMGENPALSDPNTNHVRKALESLEFLVVQDIFL 382
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 142091137 457 NTLAKRSDIVLPCTTPLER-GDIMMTPRDpyVVSMSKLVEPHGKAKNDYEIFSGIARKMG-------VEEKFTE 522
Cdd:cd02753 383 TETAELADVVLPAASFAEKdGTFTNTERR--VQRVRKAVEPPGEARPDWEIIQELANRLGypgfyshPEEIFDE 454
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
23-514 |
1.98e-22 |
|
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: 102.09 E-value: 1.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 23 VKNGKVQELIGweNDKDP------SPIGPGILDIQDGPTRIDAPMVRKswleqgPGSrndlrgidpFIEVSWKKAEQLVA 96
Cdd:cd02762 17 VEDGRVASIRG--DPDDPlskgyiCPKAAALGDYQNDPDRLRTPMRRR------GGS---------FEEIDWDEAFDEIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 97 DELTRVKNTYGNASIfgGSYGWASAGRFHHAQSQLHRFLNCIGgyTRSKFTysfAAAEAMVPHILGSYRAY--LDTCTSW 174
Cdd:cd02762 80 ERLRAIRARHGGDAV--GVYGGNPQAHTHAGGAYSPALLKALG--TSNYFS---AATADQKPGHFWSGLMFghPGLHPVP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 175 DLinKNTELFVCFGGIPIkngqISQGGTGNHYQRKNLVEAANS-GIEFINISPLKSDlIDEVKGEWITARPNTDTALMLG 253
Cdd:cd02762 153 DI--DRTDYLLILGANPL----QSNGSLRTAPDRVLRLKAAKDrGGSLVVIDPRRTE-TAKLADEHLFVRPGTDAWLLAA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 254 LAHTLHVEGLSDKQFLENYTQGFEKFLPYLLgtndgiEKNADWAASICNIPSSKIKELAHKISSKRTM-----ISVSwsl 328
Cdd:cd02762 226 MLAVLLAEGLTDRRFLAEHCDGLDEVRAALA------EFTPEAYAPRCGVPAETIRRLAREFAAAPSAavygrLGVQ--- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 329 tRQDHGEQPFWMAIMLASMVGQIGLPGGGFGFGySATNYIGgqFKVLPGAAFPQADNKIENF------IPVARISDLLLG 402
Cdd:cd02762 297 -TQLFGTLCSWLVKLLNLLTGNLDRPGGAMFTT-PALDLVG--QTSGRTIGRGEWRSRVSGLpeiageLPVNVLAEEILT 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 403 PGEKfdfdgktyvYPDTKIVYwaGGNPFHHHQDLNRLIKAWEKPDTIISNEWCWNTLAKRSDIVLPCTTPLERGDI---- 478
Cdd:cd02762 373 DGPG---------RIRAMIVV--AGNPVLSAPDGARLEAALGGLEFMVSVDVYMTETTRHADYILPPASQLEKPHAtffn 441
|
490 500 510
....*....|....*....|....*....|....*.
gi 142091137 479 MMTPRDpYVVSMSKLVEPHGKAKNDYEIFSGIARKM 514
Cdd:cd02762 442 LEFPRN-AFRYRRPLFPPPPGTLPEWEILARLVEAL 476
|
|
| MopB_CT |
cd02775 |
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a ... |
639-744 |
4.04e-22 |
|
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: 91.61 E-value: 4.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 639 LHSQMDHGNYSkSFKIEDREPVEINPNDAKSRGLKNGDIVKLFNDRGSCLAGVIVDEKVMPGVVQISTGAWYDpenpekp 718
Cdd:cd02775 5 FHSGTRTRNPW-LRELAPEPVVEINPEDAAALGIKDGDLVRVESRRGSVVLRAKVTDGVPPGVVFLPHGWGHR------- 76
|
90 100
....*....|....*....|....*.
gi 142091137 719 nsMCKHGNPNVLTRDKGTSKLGQGPI 744
Cdd:cd02775 77 --GGRGGNANVLTPDALDPPSGGPAY 100
|
|
| MopB_CT_4 |
cd02785 |
The MopB_CT_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
625-754 |
1.82e-19 |
|
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: 84.73 E-value: 1.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 625 KFPLHLISNQPKNKLHSQmdHGNYSKSFKIEDREPVEINPNDAKSRGLKNGDIVKLFNDRGSCLAGVIVDEKVMPGVVQI 704
Cdd:cd02785 1 KYPLACIQRHSRFRVHSQ--FSNVPWLLELQPEPRVKINPIDAAARGIAHGDLVEVYNDRGSVVCKAKVDDGIQPGVVTA 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 142091137 705 STGAW--YDPEnpekpnsmckhGNPNVLTRD--KGTSKLGQGPIA--HSCLIEIEK 754
Cdd:cd02785 79 EQGWWsrYFQE-----------GSLQDLTSPfvNPVHEYIYGPNSafYDTLVEVRK 123
|
|
| MopB_CT_3 |
cd02786 |
The MopB_CT_3 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
626-752 |
9.84e-17 |
|
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: 76.55 E-value: 9.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 626 FPLHLISNQPKNKLHSQMdhGNYSKSFKIEDREPVEINPNDAKSRGLKNGDIVKLFNDRGSCLAGVIVDEKVMPGVVqIS 705
Cdd:cd02786 1 YPLRLITPPAHNFLNSTF--ANLPELRAKEGEPTLLIHPADAAARGIADGDLVVVFNDRGSVTLRAKVTDDVPPGVV-VA 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 142091137 706 TGAWYDPENPEkpnsmckHGNPNVLTRDKGTSkLGQGPIAHSCLIEI 752
Cdd:cd02786 78 EGGWWREHSPD-------GRGVNALTSARLTD-LGGGSTFHDTRVEV 116
|
|
| MopB_Arsenate-R |
cd02757 |
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ... |
54-514 |
1.09e-14 |
|
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: 77.48 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 54 PTRIDAPMVRKswleqGPgsrNDLRGIDP-FIEVSWKKAEQLVADEL--TRVKNTYGNASIFGGSYGwasagrfHHAQSQ 130
Cdd:cd02757 54 PDRILYPMKRT-----NP---RKGRDVDPkFVPISWDEALDTIADKIraLRKENEPHKIMLHRGRYG-------HNNSIL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 131 LHRFLNCIGGYTRSKFTYSFAAAEAMVPHILGSYRAYldtcTSWDLINKNTELFvcFGGIPIKNGQISqggtgNHYQRKn 210
Cdd:cd02757 119 YGRFTKMIGSPNNISHSSVCAESEKFGRYYTEGGWDY----NSYDYANAKYILF--FGADPLESNRQN-----PHAQRI- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 211 lVEAANSGIEFINISP------LKSDlidevkgEWITARPNTDTALMLGLAHTLHVEGLSDKQFLENYTQGFEKFLPYLL 284
Cdd:cd02757 187 -WGGKMDQAKVVVVDPrlsntaAKAD-------EWLPIKPGEDGALALAIAHVILTEGLWDKDFVGDFVDGKNYFKAGET 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 285 GTNDGIE-----------------KNADWAASICNIPSSKIKELAHKI-SSKRTMISVSW-SLTRQDHGeqpfWMAIM-- 343
Cdd:cd02757 259 VDEESFKeksteglvkwwnlelkdYTPEWAAKISGIPAETIERVAREFaTAAPAAAAFTWrGATMQNRG----SYNSMac 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 344 --LASMVGQIGLPgggfgfgysatnyiGGqfkVLPGAAFPqadnKIENFIpvarisdlllgpgekFDFDGKTYVYPDTKI 421
Cdd:cd02757 335 haLNGLVGSIDSK--------------GG---LCPNMGVP----KIKVYF---------------TYLDNPVFSNPDGMS 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 422 VYWAGGN-PFHHHQDLNrlikawekpdtiisnewcWNTLAKRSDIVLPCTTPLERGDIMMTPRD--PYVVSMSKLVEPHG 498
Cdd:cd02757 379 WEEALAKiPFHVHLSPF------------------MSETTYFADIVLPDGHHFERWDVMSQENNlhPWLSIRQPVVKSLG 440
|
490
....*....|....*.
gi 142091137 499 KAKNDYEIFSGIARKM 514
Cdd:cd02757 441 EVREETEILIELAKKL 456
|
|
| MopB_2 |
cd02763 |
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
20-315 |
5.52e-14 |
|
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: 75.64 E-value: 5.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 20 RAKVKNGKVQELIGweNDKDPSPIG-------PGILDiQDGPTRIDAPMVRKswleqGPgsrndlRGIDPFIEVSWKKAE 92
Cdd:cd02763 14 RVHLRDGKVRYIKG--NPDHPLNKGvicakgsSGIMK-QYSPARLTKPLLRK-----GP------RGSGQFEEIEWEEAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 93 QLVADELTRVKNTygNASIFGGSYGwasagrfhHAQSQlhrflnCIGGYTRSKF-TYSFAA---------AEAMVPHILG 162
Cdd:cd02763 80 SIATKRLKAARAT--DPKKFAFFTG--------RDQMQ------ALTGWFAGQFgTPNYAAhggfcsvnmAAGGLYSIGG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 163 SYRAYLDTctSWDlinkNTELFVCFGgipikngqISQGGTGNHYQRkNLVEAANSGIEFINISPLKSDLiDEVKGEWITA 242
Cdd:cd02763 144 SFWEFGGP--DLE----HTKYFMMIG--------VAEDHHSNPFKI-GIQKLKRRGGKFVAVNPVRTGY-AAIADEWVPI 207
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 142091137 243 RPNTDTALMLGLAHTLHVEGLSDKQFLENYTQGfekflPYLlgtndgIEKNADWAASICNIPSSKIKELAHKI 315
Cdd:cd02763 208 KPGTDGAFILALAHELLKAGLIDWEFLKRYTNA-----AEL------VDYTPEWVEKITGIPADTIRRIAKEL 269
|
|
| MopB_CT_Acetylene-hydratase |
cd02781 |
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related ... |
659-754 |
2.34e-12 |
|
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: 64.64 E-value: 2.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 659 PVEINPNDAKSRGLKNGDIVKLFNDRGSCLAGVIVDEKVMPGVVQISTGAWYDPENPEKPNSM-CKHGNPNVLTRDKGTS 737
Cdd:cd02781 34 VAEINPETAAKLGIADGDWVWVETPRGRARQKARLTPGIRPGVVRAEHGWWYPEREAGEPALGgVWESNANALTSDDWND 113
|
90
....*....|....*..
gi 142091137 738 KLGQGPIAHSCLIEIEK 754
Cdd:cd02781 114 PVSGSSPLRSMLCKIYK 130
|
|
| MopB_CT_Tetrathionate_Arsenate-R |
cd02780 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate ... |
626-707 |
7.39e-12 |
|
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate reductase, subunit A, (TtrA); respiratory arsenate As(V) reductase, catalytic subunit (ArrA); and other related proteins.
Pssm-ID: 239181 [Multi-domain] Cd Length: 143 Bit Score: 63.47 E-value: 7.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 626 FPLHLISnqPKNKLHSQMDHGNYS-KSFKIEDrePVEINPNDAKSRGLKNGDIVKLFNDRGSCLAGVIVDEKVMPGVVQI 704
Cdd:cd02780 1 YPFILVT--FKSNLNSHRSANAPWlKEIKPEN--PVWINPEDAAKLGIKTGDRVRVVTPGGSVVGKAKVTEGVRPGVVAI 76
|
...
gi 142091137 705 STG 707
Cdd:cd02780 77 EHG 79
|
|
| Molybdopterin_N |
pfam18364 |
Molybdopterin oxidoreductase N-terminal domain; This is the N-terminal domain of pfam00384 ... |
12-49 |
3.66e-11 |
|
Molybdopterin oxidoreductase N-terminal domain; This is the N-terminal domain of pfam00384 found in a number of molybdopterin-containing oxidoreductases such as dimethyl sulfoxide/trimethylamine N-oxide reductase, also known as DMSO reductase (EC:1.7.2.3, EC:1.8.5.3).
Pssm-ID: 465726 [Multi-domain] Cd Length: 41 Bit Score: 58.18 E-value: 3.66e-11
10 20 30
....*....|....*....|....*....|....*...
gi 142091137 12 TSTHWGTYRAKVKNGKVQELIGWENDKDPSPIGPGILD 49
Cdd:pfam18364 1 TASHWGAFRAVVKDGRIVGVEPFEGDPDPSPLLQGVPD 38
|
|
| MopB_ydeP |
cd02767 |
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
56-354 |
1.65e-10 |
|
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: 64.25 E-value: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 56 RIDAPMVRKswleqgpgsrndlRGIDPFIEVSWKKAEQLVADELtrvKNTYGNASIFGGS--------YGWASAGRFHHA 127
Cdd:cd02767 64 RLTYPMRYD-------------AGSDHYRPISWDEAFAEIAARL---RALDPDRAAFYTSgrasneaaYLYQLFARAYGT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 128 QSqlhrFLNCiggytrSKFTYSfaAAEAMVPHILGSYRAyldTCTSWDLINknTELFVCFGGIPikngqisqggtGNHYQ 207
Cdd:cd02767 128 NN----LPDC------SNMCHE--PSSVGLKKSIGVGKG---TVSLEDFEH--TDLIFFIGQNP-----------GTNHP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 208 R--KNLVEAANSGIEFINISPLK----------SDLIDEVKG------EWITARPNTDTALMLGLAHTLH-----VEGLS 264
Cdd:cd02767 180 RmlHYLREAKKRGGKIIVINPLRepglerfanpQNPESMLTGgtkiadEYFQVRIGGDIALLNGMAKHLIerddePGNVL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 265 DKQFLENYTQGFEKFLPYLLGTN-DGIEKnadwaasICNIPSSKIKELA-HKISSKRTMISVSWSLTRQDHGEQPFWMAI 342
Cdd:cd02767 260 DHDFIAEHTSGFEEYVAALRALSwDEIER-------ASGLSREEIEAFAaMYAKSERVVFVWGMGITQHAHGVDNVRAIV 332
|
330
....*....|..
gi 142091137 343 MLASMVGQIGLP 354
Cdd:cd02767 333 NLALLRGNIGRP 344
|
|
| MopB_CT_Fdh-Nap-like |
cd00508 |
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and ... |
660-702 |
5.42e-10 |
|
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: 57.52 E-value: 5.42e-10
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 142091137 660 VEINPNDAKSRGLKNGDIVKLFNDRGSCLAGVIVDEKVMPGVV 702
Cdd:cd00508 37 VEIHPEDAARLGIKDGDLVRVSSRRGSVVVRARVTDRVRPGTV 79
|
|
| MopB_CT_Formate-Dh_H |
cd02790 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
654-712 |
2.84e-09 |
|
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 with the release of a proton and two electrons. It is a component of the anaerobic formate hydrogen lyase complex. The E. coli formate dehydrogenase H (Fdh-H) is a monomer composed of a single polypeptide chain with a Mo active site region and a [4Fe-4S] center. This CD (MopB_CT_Formate-Dh_H) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239191 [Multi-domain] Cd Length: 116 Bit Score: 55.32 E-value: 2.84e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 654 IEDREPVEINPNDAKSRGLKNGDIVKLFNDRGSCLAGVIVDEKVMPGVVQIS-----------TGAWYDP 712
Cdd:cd02790 31 IAPEEYVEINPEDAKRLGIEDGEKVRVSSRRGSVEVRARVTDRVPEGVVFMPfhfaeaaanllTNAALDP 100
|
|
| MopB_CT_Nitrate-R-NapA-like |
cd02791 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
658-702 |
7.17e-09 |
|
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to nitrite. Monomeric Nas is located in the cytoplasm and participates in nitrogen assimilation. Dimeric Nap is located in the periplasm and is coupled to quinol oxidation via a membrane-anchored tetraheme cytochrome. This CD (MopB_CT_Nitrate-R-Nap) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs
Pssm-ID: 239192 [Multi-domain] Cd Length: 122 Bit Score: 54.50 E-value: 7.17e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 142091137 658 EP-VEINPNDAKSRGLKNGDIVKLFNDRGSCLAGVIVDEKVMPGVV 702
Cdd:cd02791 34 EPyVEIHPEDAARLGLKEGDLVRVTSRRGEVVLRVRVTDRVRPGEV 79
|
|
| MopB_CT_Arsenite-Ox |
cd02779 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of Arsenite oxidase ... |
654-709 |
1.09e-08 |
|
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: 53.62 E-value: 1.09e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 142091137 654 IEDREP---VEINPNDAKSRGLKNGDIVKLFNDRGSCLAGVIVDEKVMPGVVQISTGAW 709
Cdd:cd02779 26 IAERVPlpyIEVNPEDAKREGLKNGDLVEVYNDYGSTTAMAYVTNTVKPGQTFMLMAHP 84
|
|
| MopB_CT_Formate-Dh-Na-like |
cd02792 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
624-702 |
1.78e-07 |
|
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate respiration in bacteria such as in the E. coli formate dehydrogenase N (Fdh-N). Fdh-N is a membrane protein that is a complex of three different subunits and is the major electron donor to the nitrate respiratory chain. Also included in this CD is the Desulfovibrio gigas tungsten formate dehydrogenase, DgW-FDH. In contrast to Fdh-N, which is a functional heterotrimer, DgW-FDH is a heterodimer. The DgW-FDH complex is composed of a large subunit carrying the W active site and one [4Fe-4S] center, and a small subunit that harbors a series of three [4Fe-4S] clusters as well as a putative vacant binding site for a fourth cluster. The smaller subunit is not included in this alignment. This CD (MopB_CT_Formate-Dh-Na-like) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239193 [Multi-domain] Cd Length: 122 Bit Score: 50.30 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 624 KKFPLHLISNQPKNKLHSqmdhGNYSKSFK-IEDREP---VEINPNDAKSRGLKNGDIVKLFNDRGSCLAGVIVDEKVMP 699
Cdd:cd02792 1 EEFPLVLTTGRLTEHFHG----GNMTRNSPyLAELQPemfVEISPELAAERGIKNGDMVWVSSPRGKIKVKALVTDRVKP 76
|
...
gi 142091137 700 GVV 702
Cdd:cd02792 77 HEV 79
|
|
| PRK14991 |
PRK14991 |
tetrathionate reductase subunit TtrA; |
627-707 |
7.69e-07 |
|
tetrathionate reductase subunit TtrA;
Pssm-ID: 237883 [Multi-domain] Cd Length: 1031 Bit Score: 52.69 E-value: 7.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 627 PLHLISNqpKNKLHSQMDHGNySKSFKIEDREPVEINPNDAKSRGLKNGDIVKLFNDRGSCLAGVIVDEKVMPGVVQIST 706
Cdd:PRK14991 888 PLLLISF--KSNLMSSMSIAS-PRLRQVKPANPVALNPQDAARLGIQHGDRVRISTPGGSVVAQASVLNGVMPGVIAIEH 964
|
.
gi 142091137 707 G 707
Cdd:PRK14991 965 G 965
|
|
| MopB_CT_Nitrate-R-NarG-like |
cd02776 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
659-732 |
1.16e-06 |
|
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: 48.53 E-value: 1.16e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 142091137 659 PVEINPNDAKSRGLKNGDIVKLFNDRGSCLAGVIVDEKVMPGVVqISTGAWYDPENPEKPNSMCKHGNP-NVLTR 732
Cdd:cd02776 32 VVWMNPKDAAELGIKDNDWVEVFNDNGVVVARAKVSPRIPRGTV-FMYHAQERHVNVPGSKLTGKRGGIhNSVTR 105
|
|
| MopB_Formate-Dh-Na-like |
cd02752 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
21-539 |
7.11e-06 |
|
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate respiration in bacteria such as in the E. coli formate dehydrogenase N (Fdh-N). Fdh-N is a membrane protein that is a complex of three different subunits and is the major electron donor to the nitrate respiratory chain. Also included in this CD is the Desulfovibrio gigas tungsten formate dehydrogenase, DgW-FDH. In contrast to Fdh-N, which is a functional heterotrimer, DgW-FDH is a heterodimer. The DgW-FDH complex is composed of a large subunit carrying the W active site and one [4Fe-4S] center, and a small subunit that harbors a series of three [4Fe-4S] clusters as well as a putative vacant binding site for a fourth cluster. The smaller subunit is not included in this alignment. 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: 49.71 E-value: 7.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 21 AKVKNGKvqeLIGWENDKDpSPI--------GPGILDIQDGPTRIDAPMVRKswleqgPGSrndlrgiDPFIEVSWKKAE 92
Cdd:cd02752 15 AYVQNGV---WVHQEGDPD-HPVnrgslcpkGAALRDFVHSPKRLKYPMYRA------PGS-------GKWEEISWDEAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 93 QLVADEL--TRVKNTYGNASIFGGSYGWASAGRFHHAQsqlhrfLNCIGGYTRSKFTYSFAA----AEAMVPHI-----L 161
Cdd:cd02752 78 DEIARKMkdIRDASFVEKNAAGVVVNRPDSIAFLGSAK------LSNEECYLIRKFARALGTnnldHQARIUHSptvagL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 162 GSYRAYLDTCTSWDLInKNTELFVCFGGIPIKNGQISQggtgnhyqrKNLVEA-ANSGIEFINISP------LKSDLide 234
Cdd:cd02752 152 ANTFGRGAMTNSWNDI-KNADVILVMGGNPAEAHPVSF---------KWILEAkEKNGAKLIVVDPrftrtaAKADL--- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 235 vkgeWITARPNTDTALMLGLAHtlHVeglsdkqflenytqgfekfLPYllgTNDGIEknadwaaSICNIPSSKI----KE 310
Cdd:cd02752 219 ----YVPIRSGTDIAFLGGMIN--YI-------------------IRY---TPEEVE-------DICGVPKEDFlkvaEM 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 311 LAHKISSKRTMISVsWSL--TRQDHGEQPFWMAIMLASMVGQIGLPgggfgfgysatnyiGGQFKVLPGAafpqaDNkIE 388
Cdd:cd02752 264 FAATGRPDKPGTIL-YAMgwTQHTVGSQNIRAMCILQLLLGNIGVA--------------GGGVNALRGH-----SN-VQ 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 389 NFIPVARISDLLlgPGekfdfdgktyvypdtkivYWAGGNPFHHHQDLNRLIKAWEKPDT-----IISNEWC--WN---- 457
Cdd:cd02752 323 GATDLGLLSHNL--PG------------------YLGGQNPNSSFPNANKVRRALDKLDWlvvidPFPTETAafWKnpgm 382
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 458 TLAKRSD--IVLPCTTPLER-GDIMMTPRdpYVVSMSKLVEPHGKAKNDYEIFSGIARKMGVEEKFTEGRNQEEWQKWIY 534
Cdd:cd02752 383 DPKSIQTevFLLPAACQYEKeGSITNSGR--WLQWRYKVVEPPGEAKSDGDILVELAKRLGFLYEKEGGAFPEPITKWNY 460
|
....*
gi 142091137 535 KQTFE 539
Cdd:cd02752 461 GYGDE 465
|
|
| MopB_CT_1 |
cd02782 |
The MopB_CT_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
653-733 |
1.21e-05 |
|
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: 45.46 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 653 KIEDREPVEINPNDAKSRGLKNGDIVKLFNDRGSCLAGVIVDEKVMPGVVQISTGAWYDPENPEKPNSmcKHG-NPNVLT 731
Cdd:cd02782 28 KGRNRCTLRIHPDDAAALGLADGDKVRVTSAAGSVEAEVEVTDDMMPGVVSLPHGWGHDYPGVSGAGS--RPGvNVNDLT 105
|
..
gi 142091137 732 RD 733
Cdd:cd02782 106 DD 107
|
|
| MopB_CT_Thiosulfate-R-like |
cd02778 |
The MopB_CT_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, ... |
660-754 |
1.72e-05 |
|
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: 44.96 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 142091137 660 VEINPNDAKSRGLKNGDIVKLFNDRGSCLAGVIVDEKVMPGVVQISTGawYDPENPEKPNSMCKHGNPNVLTRDkGTSKL 739
Cdd:cd02778 32 LWINPETAARLGIKDGDRVEVSSARGKVTGKARLTEGIRPDTVFMPHG--FGHWAPALSRAYGGGVNDNNLLPG-STEPV 108
|
90
....*....|....*
gi 142091137 740 GQGPIAHSCLIEIEK 754
Cdd:cd02778 109 SGGAGLQEFTVTVRK 123
|
|
| MopB_CT_ydeP |
cd02787 |
The MopB_CT_ydeP CD includes a group of related uncharacterized bacterial ... |
657-715 |
2.51e-03 |
|
The MopB_CT_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative 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: 239188 [Multi-domain] Cd Length: 112 Bit Score: 38.41 E-value: 2.51e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 142091137 657 REPVEINPNDAKSRGLKNGDIVKLFNDRG-----SCLAGVIVDEKVMPGVVQistgAWYdPE-NP 715
Cdd:cd02787 30 RDVVFMNPDDIARLGLKAGDRVDLESAFGdgqgrIVRGFRVVEYDIPRGCLA----AYY-PEgNV 89
|
|
| |
