|
Name |
Accession |
Description |
Interval |
E-value |
| bisC_fam |
TIGR00509 |
molybdopterin guanine dinucleotide-containing S/N-oxide reductases; This enzyme family shares ... |
37-794 |
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: 1250.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 37 ATHFGPFIAKVQNGVIKDIVPQKSDYNPTMMLKAMADRVYSDSRVKYPCVRKSFLENK-KNHKELRGREEFVRVSWDVAL 115
Cdd:TIGR00509 1 ASHWGVFTATVQDGRIVAVTPFESDPNPTPMLEGVPDQVYSESRIKYPMVRKGFLENGvKSDRSGRGREEFVRVSWDEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 116 DLAAKKLKEIPKEN----IYNASYGgWGHAGSLHRCHHLAWRFFNTtLGGAIGTDGEYSNGAAAKINPMIVGDMEVYSQQ 191
Cdd:TIGR00509 81 DLVAEELKRVRKTHgpsaIFAGSYG-WKSAGRLHNASTLLQRMLNL-LGGYVGHAGDYSTGAAQVIMPHVVGDMEVYEQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 192 TAHEEMIKNCKVYVMWGADLFKCNRIDYFVPNHVNDSYYPKYKRAGIKFISIDPIYTETAQAFNAEWIPIRPNTDVALML 271
Cdd:TIGR00509 159 TTWPVILENSEVLVLWGADPLKTSQIAWGIPDHGGYEYLERLKAKGKRVISIDPVRTETVEFFGAEWIPPNPQTDVALML 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 272 GIMHYLYTSNQYDKAFIAKYTDGFDKFLPYLLGESDKAPKTLEWASQITGVSAEKIKELADLFVSKRTFLAGNWAMQRAQ 351
Cdd:TIGR00509 239 GLAHTLVTEGLYDKDFLAKYTSGFEKFLPYLLGETDGTPKTAEWASKITGVPAETIKELARLFASKRTMLAAGWSMQRMQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 352 YGEQPDWALIVLASMIGQVGLSGGGFGFSMHYGGNaQASSGARivPMISQGHNSVK------------SVIPASRISEAI 419
Cdd:TIGR00509 319 HGEQPHWMLVTLAAMLGQIGLPGGGFGFSYHYSGG-GTPSASG--PALSQGSNSVSstagpewddgsaSVIPVARISDAL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 420 LNPDKEIDFMGKKLKLPKIKMIYNCGADLLGHEADTNELIRALRTLDCVIVHEPWWTPTAKFADIVFASTSTMERDDITF 499
Cdd:TIGR00509 396 LNPGKEIDYNGKELKLPDIKMVYWAGGNPFHHHQDTNRLIKAWRKLETIIVHEPQWTPTAKHADIVLPATTSFERNDLTM 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 500 GGSYSKNVVYAMRKVVEPVYESKDDYEIFRQLALRIGgneTEQKFTESKSYMEWIKSLYEKS------DGPTLKSFDQFW 573
Cdd:TIGR00509 476 AGDYSNTGILAMKQVVPPQFEARNDYDIFAALAERLG---VEEAFTEGKDEMGWLKHLYEKAakqakaDGVEMPAFDAFW 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 574 RDGFVEFEIPENaRKFVRHAKFRQDPINNKLDTESGKIQIFSQKCADFKLTDFKGHPTWFEPAEWLGSKMAETYPFHLIS 653
Cdd:TIGR00509 553 AEGIVEFPVPEG-ADFVRYAAFREDPLLNPLGTPSGLIEIYSKTIAKMGYDDCPGHPTWMEPAEWLGGPRGAKYPLHLIS 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 654 PHPKYRVNSQLDNTWVRNVYKIQGREPVMINELDANKLGIRHGEIVEVFNARGRLLAGAFVTKNIRQGVLSIQKGAWYDP 733
Cdd:TIGR00509 632 PHPKYRLHSQLDHTELRQAYKVQGREPVMIHPDDAAARGIADGDIVRVFNARGQILAGAVVTDGIRKGVVQIHEGAWYDP 711
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1751927289 734 EDGRVRNPRCNAGHVNTLTSLRPTSSMTQAISANTALVNIRRLrRYELvKPYHSISTPSII 794
Cdd:TIGR00509 712 ADVREPGGLCKYGNPNVLTADIGTSSLAQGNSGNTVLVEIEKY-TGPA-PPLTAFDQPAAA 770
|
|
| MopB_DMSOR-BSOR-TMAOR |
cd02769 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
35-639 |
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: 940.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 35 PHATHFGPFIAKVQNGVIKDIVPQKSDYNPTMMLKAMADRVYSDSRVKYPCVRKSFLENKKN-HKELRGREEFVRVSWDV 113
Cdd:cd02769 1 PTASHWGAFRARVKDGRIVGVRPFEEDPDPSPLLDGVPDAVYSPTRIKYPMVRRGWLEKGPGsDRSLRGKEEFVRVSWDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 114 ALDLAAKKLKEIPK----ENIYNASYGgWGHAGSLHRCHHLAWRFFNTTlGGAIGTDGEYSNGAAAKINPMIVGDMEVY- 188
Cdd:cd02769 81 ALDLVAAELKRVRKtygnEAIFGGSYG-WSSAGRFHHAQSLLHRFLNLA-GGYVGSVGDYSTGAAQVILPHVVGSMEVYt 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 189 SQQTAHEEMIKNCKVYVMWGADLFKCNRIDYFV-PNHVNDSYYPKYKRAGIKFISIDPIYTETAQAFNAEWIPIRPNTDV 267
Cdd:cd02769 159 EQQTSWPVIAEHTELVVAFGADPLKNAQIAWGGiPDHQAYSYLKALKDRGIRFISISPLRDDTAAELGAEWIAIRPGTDV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 268 ALMLGIMHYLYTSNQYDKAFIAKYTDGFDKFLPYLLGESDKAPKTLEWASQITGVSAEKIKELADLFVSKRTFLAGNWAM 347
Cdd:cd02769 239 ALMLALAHTLVTEGLHDKAFLARYTVGFDKFLPYLLGESDGVPKTPEWAAAICGIPAETIRELARRFASKRTMIMAGWSL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 348 QRAQYGEQPDWALIVLASMIGQVGLSGGGFGFSMHYGGNAQASSGARIVPMISQGHNSVKSVIPASRISEAILNPDKEID 427
Cdd:cd02769 319 QRAHHGEQPHWMAVTLAAMLGQIGLPGGGFGFGYHYSNGGGPPRGAAPPPALPQGRNPVSSFIPVARIADMLLNPGKPFD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 428 FMGKKLKLPKIKMIYNCGADLLGHEADTNELIRALRTLDCVIVHEPWWTPTAKFADIVFASTSTMERDDITFGGsySKNV 507
Cdd:cd02769 399 YNGKKLTYPDIKLVYWAGGNPFHHHQDLNRLIRAWQKPETVIVHEPFWTATARHADIVLPATTSLERNDIGGSG--DNRY 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 508 VYAMRKVVEPVYESKDDYEIFRQLALRIGGNETeqkFTESKSYMEWIKSLYEKS------DGPTLKSFDQFWRDGFVEFE 581
Cdd:cd02769 477 IVAMKQVVEPVGEARDDYDIFADLAERLGVEEQ---FTEGRDEMEWLRHLYEESraqaaaRGVEMPSFDEFWAQGYVELP 553
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 1751927289 582 IPENarKFVRHAKFRQDPINNKLDTESGKIQIFSQKCADFKLTDFKGHPTWFEPAEWL 639
Cdd:cd02769 554 IPEA--DFVRLADFREDPEANPLGTPSGRIEIFSETIAGFGYDDCPGHPTWLEPAEWL 609
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
35-639 |
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: 849.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 35 PHATHFGPFIAKVQNGVIKDIVPQKSD-YNPTMMLKAMADRVYSDSRVKYPCVRKSFLENKKNHKELRGREEFVRVSWDV 113
Cdd:cd02751 1 PTACHWGPFKAHVKDGVIVRVEPDDTDqPRPCPRGRSVRDRVYSPDRIKYPMKRVGWLGNGPGSRELRGEGEFVRISWDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 114 ALDLAAKKLKEIPK----ENIYNASYGGWGhAGSLHRCHHLAWRFFNTTlGGAIGTDGEYSNGAAAKINPMIVGDMEVYS 189
Cdd:cd02751 81 ALDLVASELKRIREkygnEAIFGGSYGWAS-AGRLHHAQSLLHRFLNLI-GGYLGSYGTYSTGAAQVILPHVVGSDEVYE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 190 QQTAHEEMIKNCKVYVMWGADLFKCNRIDYFVPNHVNDSYYPKYKRAGIKFISIDPIYTETAQAFNAEWIPIRPNTDVAL 269
Cdd:cd02751 159 QGTSWDDIAEHSDLVVLFGANPLKTRQGGGGGPDHGSYYYLKQAKDAGVRFICIDPRYTDTAAVLAAEWIPIRPGTDVAL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 270 MLGIMHYLYTSNQYDKAFIAKYTDGFDKFLPYLLGESDKAPKTLEWASQITGVSAEKIKELADLFVSKRTFLAGNWAMQR 349
Cdd:cd02751 239 MLAMAHTLITEDLHDQAFLARYTVGFDEFKDYLLGESDGVPKTPEWAAEITGVPAETIRALAREIASKRTMIAQGWGLQR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 350 AQYGEQPDWALIVLASMIGQVGLSGGGFGFSMHYGGNAQASSGARIVPMISQGHNSVKSVIPASRISEAILNPDKEIDFM 429
Cdd:cd02751 319 AHHGEQPAWMLVTLAAMLGQIGLPGGGFGFGYGYSNGGGPPRGGAGGPGLPQGKNPVKDSIPVARIADALLNPGKEFTAN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 430 GKKLKLPKIKMIYNCGADLLGHEADTNELIRALRTLDCVIVHEPWWTPTAKFADIVFASTSTMERDDITFGGSYSKNVVY 509
Cdd:cd02751 399 GKLKTYPDIKMIYWAGGNPLHHHQDLNRLIKALRKDETIVVHDIFWTASARYADIVLPATTSLERNDIGLTGNYSNRYLI 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 510 AMRKVVEPVYESKDDYEIFRQLALRIGgneTEQKFTESKSYMEWIKSLYEKSD------GPTLKSFDQFWRDGFVEFEIP 583
Cdd:cd02751 479 AMKQAVEPLGEARSDYEIFAELAKRLG---VEEEFTEGRDEMEWLEHLYEETRakaagpGPELPSFEEFWEKGIVRVPAA 555
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 1751927289 584 EnaRKFVRHAKFRQDPINNKLDTESGKIQIFSQKCADFKLTDFKGHPTWFEPAEWL 639
Cdd:cd02751 556 P--KPFVAFADFREDPEANPLGTPSGKIEIYSETLADFGYDDCPGHPTWIEPWEGL 609
|
|
| PRK15102 |
PRK15102 |
trimethylamine-N-oxide reductase TorA; |
3-773 |
0e+00 |
|
trimethylamine-N-oxide reductase TorA;
Pssm-ID: 237909 [Multi-domain] Cd Length: 825 Bit Score: 722.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 3 ISRRSIL----TKIPIALASTNVLKAVGVFEKVESIPHAT--------HFGPFIAKVQNGVIKDIVPQKSDYNPTMMLKA 70
Cdd:PRK15102 1 ASRRRFLkglgGLSAAGMLGPSLLTPRSALAAQAAAAETTkewiltgsHWGAFRAKVKNGRFVEAKPFELDKYPTKMING 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 71 MADRVYSDSRVKYPCVRKSFLenKKNHK---ELRGREEFVRVSWDVALDLAAKKLKEIPKEniynasYGGWG-HAGslhr 146
Cdd:PRK15102 81 IKGHVYNPSRIRYPMVRLDWL--RKRHKsdtSQRGDNRFVRVSWDEALDLFYEELERVQKT------YGPSAlHTG---- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 147 chHLAWR----FFNTTL---------GGAIGTDGEYSNGAAAKINPMIVGDMEVYSQQTAHEEMIKNCKVYVMWGADLFK 213
Cdd:PRK15102 149 --QTGWQstgqFHSATGhmqraigmhGNSVGTVGDYSTGAGQVILPYVLGSTEVYEQGTSWPLILENSKTIVLWGSDPVK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 214 CNRIDYFVPNHVNDSYYP----KYKRAGIKFISIDPIYTETAQAFNAEWIPIRPNTDVALMLGIMHYLYTSNQYDKAFIA 289
Cdd:PRK15102 227 NLQVGWNCETHESYAYLAqlkeKVAKGEINVISIDPVVTKTQNYLGCEHLYVNPQTDVPLMLALAHTLYSENLYDKKFID 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 290 KYTDGFDKFLPYLLGESDKAPKTLEWASQITGVSAEKIKELADLFVSKRTFLAGNWAMQRAQYGEQPDWALIVLASMIGQ 369
Cdd:PRK15102 307 NYCLGFEQFLPYLLGEKDGVPKTPEWAEKICGIDAETIRELARQMAKGRTQIIAGWCIQRQQHGEQPYWMGAVLAAMLGQ 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 370 VGLSGGGFGFSMHYGGNAQASSGARI------------VPMI-SQGHNSVKSVIPASRISEAILNPDKEIDFMGKKLKLP 436
Cdd:PRK15102 387 IGLPGGGISYGHHYSGIGVPSSGGAIpggfpgnldtgqKPKHdNSDYKGYSSTIPVARFIDAILEPGKTINWNGKKVTLP 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 437 KIKMIYNCGADLLGHEADTNELIRALRTLDCVIVHEPWWTPTAKFADIVFASTSTMERDDITFGGSYSKNVVYAMRKVVE 516
Cdd:PRK15102 467 PLKMMIFSGTNPWHRHQDRNRMKEAFRKLETVVAIDNQWTATCRFADIVLPACTQFERNDIDQYGSYSNRGIIAMKKVVE 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 517 PVYESKDDYEIFRQLALRIGgneTEQKFTESKSYMEWIKSLYE--------KSDGPtlkSFDQFWRDGFVEFEIPENark 588
Cdd:PRK15102 547 PLFESRSDFDIFRELCRRFG---REKEYTRGMDEMGWLKRLYQeckqqnkgKFHMP---EFDEFWKKGYVEFGEGQP--- 617
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 589 FVRHAKFRQDPINNKLDTESGKIQIFSQKCADFKLTDFKGHPTWFEPAEWL-GSKMAETYPFHLISPHPKYRVNSQL-DN 666
Cdd:PRK15102 618 WVRHADFREDPELNPLGTPSGLIEIYSRKIADMGYDDCQGHPMWFEKIERShGGPGSDKYPLWLQSVHPDKRLHSQLcES 697
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 667 TWVRNVYKIQGREPVMINELDANKLGIRHGEIVEVFNARGRLLAGAFVTKNIRQGVLSIQKGAWYDPEDGRVRNPRCNAG 746
Cdd:PRK15102 698 EELRETYTVQGREPVYINPQDAKARGIKDGDVVRVFNDRGQVLAGAVVSDRYPPGVIRIHEGAWYGPDKGGEIGALCTYG 777
|
810 820
....*....|....*....|....*..
gi 1751927289 747 HVNTLTSLRPTSSMTQAISANTALVNI 773
Cdd:PRK15102 778 DPNTLTLDIGTSQLAQATSAHTCLVEI 804
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
42-777 |
0e+00 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 554.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 42 PFIAKVQNGVIKDIVPQKSdyNPTMMLK------AMADRVYSDSRVKYPCVRKSflenkknhkeLRGREEFVRVSWDVAL 115
Cdd:COG0243 36 GLGVKVEDGRVVRVRGDPD--HPVNRGRlcakgaALDERLYSPDRLTYPMKRVG----------PRGSGKFERISWDEAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 116 DLAAKKLKEIPKEniYN----ASYGGWGHAGSLHRC-HHLAWRFFNttlggAIGTDGEYSNG-----AAAKINPMIVGDM 185
Cdd:COG0243 104 DLIAEKLKAIIDE--YGpeavAFYTSGGSAGRLSNEaAYLAQRFAR-----ALGTNNLDDNSrlcheSAVAGLPRTFGSD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 186 EVysqqTAHEEMIKNCKVYVMWGADLFKCNRIDYfvpNHVNDSYypkyKRAGIKFISIDPIYTETAQAFNaEWIPIRPNT 265
Cdd:COG0243 177 KG----TVSYEDLEHADLIVLWGSNPAENHPRLL---RRLREAA----KKRGAKIVVIDPRRTETAAIAD-EWLPIRPGT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 266 DVALMLGIMHYLYTSNQYDKAFIAKYTDGFDKFLPYLlgesdkAPKTLEWASQITGVSAEKIKELADLFV-SKRTFLAGN 344
Cdd:COG0243 245 DAALLLALAHVLIEEGLYDRDFLARHTVGFDELAAYV------AAYTPEWAAEITGVPAEDIRELAREFAtAKPAVILWG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 345 WAMQRAQYGEQPDWALIVLASMIGQVGLSgggfgfsmhyGGNAQASSGarivpmisqghnsvksvipasrisEAILNpdk 424
Cdd:COG0243 319 MGLQQHSNGTQTVRAIANLALLTGNIGKP----------GGGPFSLTG------------------------EAILD--- 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 425 eidfmGKKlklPKIKMIYNCGADLLGHEADTNELIRALRTLDCVIVHEPWWTPTAKFADIVFASTSTMERDDITfgGSYS 504
Cdd:COG0243 362 -----GKP---YPIKALWVYGGNPAVSAPDTNRVREALRKLDFVVVIDTFLTETARYADIVLPATTWLERDDIV--TNSE 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 505 KNVVYAMRKVVEPVYESKDDYEIFRQLALRIGgneTEQKFTESKSYMEWIKSLYEKSDGPTLkSFDQFWRDGFVEFEIPE 584
Cdd:COG0243 432 DRRVHLSRPAVEPPGEARSDWEIFAELAKRLG---FEEAFPWGRTEEDYLRELLEATRGRGI-TFEELREKGPVQLPVPP 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 585 NARkfvrhakFRQDpinNKLDTESGKIQIFSQKCAdfkltdFKGHPTWFEPAEWlGSKMAETYPFHLISPHPKYRVNSQL 664
Cdd:COG0243 508 EPA-------FRND---GPFPTPSGKAEFYSETLA------LPPLPRYAPPYEG-AEPLDAEYPLRLITGRSRDQWHSTT 570
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 665 DNtwVRNVYKIQGREPVMINELDANKLGIRHGEIVEVFNARGRLLAGAFVTKNIRQGVLSIQKGAWYDPEDGRvrnprcn 744
Cdd:COG0243 571 YN--NPRLREIGPRPVVEINPEDAAALGIKDGDLVRVESDRGEVLARAKVTEGIRPGVVFAPHGWWYEPADDK------- 641
|
730 740 750
....*....|....*....|....*....|...
gi 1751927289 745 AGHVNTLTSLRpTSSMTQAISANTALVNIRRLR 777
Cdd:COG0243 642 GGNVNVLTPDA-TDPLSGTPAFKSVPVRVEKAA 673
|
|
| MopB_DmsA-EC |
cd02770 |
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
74-628 |
2.06e-117 |
|
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: 368.19 E-value: 2.06e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 74 RVYSDSRVKYPCVRKsflenkknHKelRGREEFVRVSWDVALDLAAKKLKEIPK----ENIYNaSYGGwGHAGSLhRCHH 149
Cdd:cd02770 53 RVYNPDRLKYPMKRV--------GK--RGEGKFVRISWDEALDTIASELKRIIEkygnEAIYV-NYGT-GTYGGV-PAGR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 150 LAWRFFNTTLGGAIGTDGEYSNGAAAKINPMIVGDMEVYSQQTAheemIKNCKVYVMWGADLfKCNRIDYFVPNHvndsY 229
Cdd:cd02770 120 GAIARLLNLTGGYLNYYGTYSWAQITTATPYTYGAAASGSSLDD----LKDSKLVVLFGHNP-AETRMGGGGSTY----Y 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 230 YPKYKRAGIKFISIDPIYTETAQAFNAEWIPIRPNTDVALMLGIMHYLYTSNQYDKAFIAKYTDGFD-KFLP-------- 300
Cdd:cd02770 191 YLQAKKAGAKFIVIDPRYTDTAVTLADEWIPIRPGTDAALVAAMAYVMITENLHDQAFLDRYCVGFDaEHLPegappnes 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 301 ---YLLGE-SDKAPKTLEWASQITGVSAEKIKELA-DLFVSKRTFLAGNWAMQRAQYGEQPDWALIVLASMIGQVGLSgg 375
Cdd:cd02770 271 ykdYVLGTgYDGTPKTPEWASEITGVPAETIRRLArEIATTKPAAILQGWGPQRHANGEQAARAIMMLAAMTGNVGIP-- 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 376 gfgfsmhyGGNAQASSG--ARIVPMISQGHNSVKSVIPASRISEAILNPDKEIDFMGK-----KLKLPkIKMIYN-CGAD 447
Cdd:cd02770 349 --------GGNTGARPGgsAYNGAGLPAGKNPVKTSIPCFMWTDAIERGEEMTADDGGvkgadKLKSN-IKMIWNyAGNT 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 448 LLGHEADTNELIRALR--TLDC--VIVHEPWWTPTAKFADIVFASTSTMERDDI-TFGGSYSKNVVYAMRKVVEPVYESK 522
Cdd:cd02770 420 LINQHSDDNNTTRALLddESKCefIVVIDNFMTPSARYADILLPDTTELEREDIvLTSNAGMMEYLIYSQKAIEPLYECK 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 523 DDYEIFRQLALRIGgneTEQKFTESKSYMEWIKSLYEKS--DGPTLKSFDQFWRDGFVEFEIpenARKFVRHAKFRQDPI 600
Cdd:cd02770 500 SDYEICAELAKRLG---VEDQFTEGKTEQEWLEELYGQTraKEPGLPTYEEFREKGIYRVPR---ALPFVAFEDFREDPE 573
|
570 580
....*....|....*....|....*...
gi 1751927289 601 NNKLDTESGKIQIFSQKCADFKLTDFKG 628
Cdd:cd02770 574 NNPLKTPSGKIEIYSKALADMAKTLPEG 601
|
|
| PRK14990 |
PRK14990 |
anaerobic dimethyl sulfoxide reductase subunit A; Provisional |
69-776 |
4.81e-94 |
|
anaerobic dimethyl sulfoxide reductase subunit A; Provisional
Pssm-ID: 184952 [Multi-domain] Cd Length: 814 Bit Score: 311.96 E-value: 4.81e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 69 KAMADRVYSDSRVKYPCVRKSflenkknhkeLRGREEFVRVSWDVALDLAAKKL----KEIPKENIYnASYGGWGHAGSL 144
Cdd:PRK14990 108 RSMRRRVYNPDRLKYPMKRVG----------ARGEGKFERISWEEAYDIIATNMqrliKEYGNESIY-LNYGTGTLGGTM 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 145 HRC----HHLAWRFFNTTlGGAIGTDGEYSNGA-AAKINPMIVGDMEVYSQQTaheemIKNCKVYVMWGADlfkcnridy 219
Cdd:PRK14990 177 TRSwppgNTLVARLMNCC-GGYLNHYGDYSSAQiAEGLNYTYGGWADGNSPSD-----IENSKLVVLFGNN--------- 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 220 fvPNHVNDS-----YYPKYKRA--GIKFISIDPIYTETAQAFNAEWIPIRPNTDVALMLGIMHYLYTSNQYDKAFIAKYT 292
Cdd:PRK14990 242 --PGETRMSgggvtYYLEQARQksNARMIIIDPRYTDTGAGREDEWIPIRPGTDAALVNGLAYVMITENLVDQPFLDKYC 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 293 DGFD-KFLP-----------YLLGE-SDKAPKTLEWASQITGVSAEKIKELA-DLFVSKRTFLAGNWAMQRAQYGEQPDW 358
Cdd:PRK14990 320 VGYDeKTLPasapknghykaYILGEgPDGVAKTPEWASQITGVPADKIIKLArEIGSTKPAFISQGWGPQRHANGEIATR 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 359 ALIVLASMIGQVGLSgggfgfsmhyGGNAQASSGARIVPM--ISQGHNSVKSVIPASRISEAI-LNPDKEI---DFMGK- 431
Cdd:PRK14990 400 AISMLAILTGNVGIN----------GGNSGAREGSYSLPFvrMPTLENPIQTSISMFMWTDAIeRGPEMTAlrdGVRGKd 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 432 KLKLPkIKMIYN-CGADLLGHEAD---TNELIRALRTLDCVIVHEPWWTPTAKFADIVFASTSTMERDDITFGGSySKNV 507
Cdd:PRK14990 470 KLDVP-IKMIWNyAGNCLINQHSEinrTHEILQDDKKCELIVVIDCHMTSSAKYADILLPDCTASEQMDFALDAS-CGNM 547
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 508 VYAM--RKVVEPVYESKDDYEIFRQLALRIGgneTEQKFTESKSYMEWIKSLYEKSDG--PTLKSFDQFWRDGFVEFEIP 583
Cdd:PRK14990 548 SYVIfnDQVIKPRFECKTIYEMTSELAKRLG---VEQQFTEGRTQEEWMRHLYAQSREaiPELPTFEEFRKQGIFKKRDP 624
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 584 ENARkfVRHAKFRQDPINNKLDTESGKIQIFSQKCADFKLT------DFKGHPTWFEPA-EWLGSKMAETYPFHLISPHP 656
Cdd:PRK14990 625 QGHH--VAYKAFREDPQANPLTTPSGKIEIYSQALADIAATwelpegDVIDPLPIYTPGfESYQDPLNKQYPLQLTGFHY 702
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 657 KYRVNSQLDNTwvrNVYKIQGREPVMINELDANKLGIRHGEIVEVFNARGRLLAGAFVTKNIRQGVLSIQKGAWYDPEDG 736
Cdd:PRK14990 703 KSRVHSTYGNV---DVLKAACRQEMWINPLDAQKRGINNGDKVRIFNDRGEVHIEAKVTPRMMPGVVALGEGAWYDPDAK 779
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 1751927289 737 RVRnprcNAGHVNTLTSLRPtSSMTQAISANTALVNIRRL 776
Cdd:PRK14990 780 RVD----KGGCINVLTTQRP-SPLAKGNPSHTNLVQVEKV 814
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
42-535 |
1.84e-74 |
|
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: 246.86 E-value: 1.84e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 42 PFIAKVQNGVIKDIVPQKSD----YNPTMMLKAMADRVYSDSRVKYPCVRKSflenkknhkelrGREEFVRVSWDVALDL 117
Cdd:cd00368 12 GILVYVKDGKVVRIEGDPNHpvneGRLCDKGRAGLDGLYSPDRLKYPLIRVG------------GRGKFVPISWDEALDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 118 AAKKLKEIPKENIYNASYGGWGHAGSLHRCHHLAWRFFNtTLGGAIGTDGEYSNGAAAKINPMivgdMEVYSQQTAHEEm 197
Cdd:cd00368 80 IAEKLKEIREKYGPDAIAFYGGGGASNEEAYLLQKLLRA-LGSNNVDSHARLCHASAVAALKA----FGGGAPTNTLAD- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 198 IKNCKVYVMWGADLFKCNRIDYfvpnhvndSYYPKYKRAGIKFISIDPIYTETAqAFNAEWIPIRPNTDVALMLGimhyl 277
Cdd:cd00368 154 IENADLILLWGSNPAETHPVLA--------ARLRRAKKRGAKLIVIDPRRTETA-AKADEWLPIRPGTDAALALA----- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 278 ytsnqydkafiakytdgfdkflpyllgesdkapktlEWASQITGVSAEKIKELADLF-VSKRTFLAGNWAMQRAQYGEQP 356
Cdd:cd00368 220 ------------------------------------EWAAEITGVPAETIRALAREFaAAKRAVILWGMGLTQHTNGTQN 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 357 DWALIVLASMIGQVGLSgggfgfsmhyGGNAQAssgarivpmisqghnsvksvipasriseailnpdkeidfmgkklklp 436
Cdd:cd00368 264 VRAIANLAALTGNIGRP----------GGGLGP----------------------------------------------- 286
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 437 kikmiyncGADLLGHEADTNELIRALRTLDCVIVHEPWWTPTAKFADIVFASTSTMERDDITFGGSyskNVVYAMRKVVE 516
Cdd:cd00368 287 --------GGNPLVSAPDANRVRAALKKLDFVVVIDIFMTETAAYADVVLPAATYLEKEGTYTNTE---GRVQLFRQAVE 355
|
490
....*....|....*....
gi 1751927289 517 PVYESKDDYEIFRQLALRI 535
Cdd:cd00368 356 PPGEARSDWEILRELAKRL 374
|
|
| MopB_CT_DMSOR-BSOR-TMAOR |
cd02793 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
647-775 |
8.70e-71 |
|
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: 227.90 E-value: 8.70e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 647 YPFHLISPHPKYRVNSQLDNTWVRNVYKIQGREPVMINELDANKLGIRHGEIVEVFNARGRLLAGAFVTKNIRQGVLSIQ 726
Cdd:cd02793 1 YPLHLLSNQPATRLHSQLDHGSLSRAYKVQGREPIRINPADAAARGIADGDIVRVFNDRGACLAGAVVTDGIMPGVVQLP 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1751927289 727 KGAWYDPEDGRVRNPRCNAGHVNTLTSLRPTSSMTQAISANTALVNIRR 775
Cdd:cd02793 81 TGAWYDPDDPGEPGPLCKHGNPNVLTLDIGTSSLAQGCSAQTCLVQIEK 129
|
|
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
70-620 |
2.32e-66 |
|
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: 229.06 E-value: 2.32e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 70 AMADRVYSDSRVKYPCVRKSflenkknhkelRGREEFVRVSWDVALDLAAKKLKEIPKENIYNA--SYGGWGHAGSLHRc 147
Cdd:cd02766 45 RYVERVYSPDRLLTPLKRVG-----------RKGGQWERISWDEALDTIAAKLKEIKAEYGPESilPYSYAGTMGLLQR- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 148 hHLAWRFFNttLGGAIGTDGEYSNGAAAKINPMIVGDMevYSqqtAHEEMIKNCKVYVMWGADLFKCNrIDYFvpNHVNd 227
Cdd:cd02766 113 -AARGRFFH--ALGASELRGTICSGAGIEAQKYDFGAS--LG---NDPEDMVNADLIVIWGINPAATN-IHLM--RIIQ- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 228 syypKYKRAGIKFISIDPIYTETAqAFNAEWIPIRPNTDVALMLGIMHYLYTSNQYDKAFIAKYTDGFDKFLPYLLgesd 307
Cdd:cd02766 181 ----EARKRGAKVVVIDPYRTATA-ARADLHIQIRPGTDGALALGVAKVLFREGLYDRDFLARHTEGFEELKAHLE---- 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 308 kaPKTLEWASQITGVSAEKIKELADLFV-SKRTFLAGNWAMQRAQYGEQPDWALIVLASMIGQVGlsgggfgfsmHYGGN 386
Cdd:cd02766 252 --TYTPEWAAEITGVSAEEIEELARLYGeAKPPSIRLGYGMQRYRNGGQNVRAIDALPALTGNIG----------VPGGG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 387 AQAS-SGARIVPMISQGHNSVkSVIPasriseailnpdkeidfmgkklklpkikmiyncgadllgheaDTNELIRAL-RT 464
Cdd:cd02766 320 AFYSnSGPPVKALWVYNSNPV-AQAP------------------------------------------DSNKVRKGLaRE 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 465 LDCVIVHEPWWTPTAKFADIVFASTSTMERDDI--TFGGSYsknVVYAmRKVVEPVYESKDDYEIFRQLALRIGgnETEQ 542
Cdd:cd02766 357 DLFVVVHDQFMTDTARYADIVLPATTFLEHEDVyaSYWHYY---LQYN-EPAIPPPGEARSNTEIFRELAKRLG--FGEP 430
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1751927289 543 KFTESKsyMEWIKSLYEKSDGPTlksfdqfwrdgfveFEIPENARKFVRHAKFRQDPI-NNKLDTESGKIQIFSQKCAD 620
Cdd:cd02766 431 PFEESD--EEWLDQALDGTGLPL--------------EGIDLERLLGPRKAGFPLVAWeDRGFPTPSGKFEFYSERAAK 493
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
43-723 |
2.18e-60 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 216.67 E-value: 2.18e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 43 FIAKVQNGVIKDIVPQKSDYNPTMML----KAMADRVYSDSRVKYPCVRKSflenkknhkelrgrEEFVRVSWDVALDLA 118
Cdd:COG3383 20 IDLEVKDGKIVKVEGDPDHPVNRGRLcvkgRFGFEFVNSPDRLTTPLIRRG--------------GEFREVSWDEALDLV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 119 AKKLKEIPKEniYNA-SYGGWGHAGSLHRCHHLAWRFFNTTLGGA-IGTDGEYSNGAAAKINPMIVGdmevYSQQTAHEE 196
Cdd:COG3383 86 AERLREIQAE--HGPdAVAFYGSGQLTNEENYLLQKLARGVLGTNnIDNNARLCMASAVAGLKQSFG----SDAPPNSYD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 197 MIKNCKVYVMWGADLFKCNRIdyfVPNHVNDSyypkyKRAGIKFISIDPIYTETAQaFNAEWIPIRPNTDVALMLGIMHY 276
Cdd:COG3383 160 DIEEADVILVIGSNPAEAHPV---LARRIKKA-----KKNGAKLIVVDPRRTETAR-LADLHLQIKPGTDLALLNGLLHV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 277 LYTSNQYDKAFIAKYTDGFDKFLPYLlgesdkAPKTLEWASQITGVSAEKIKELADLFV-SKRTFLAgnWAM---QRAQy 352
Cdd:COG3383 231 IIEEGLVDEDFIAERTEGFEELKASV------AKYTPERVAEITGVPAEDIREAARLIAeAKRAMIL--WGMgvnQHTQ- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 353 GEQPDWALIVLASMIGQVglsgggfgfsmhyG------------GNAQassGAR---IVPMISQGHNSVKSviPASR-IS 416
Cdd:COG3383 302 GTDNVNAIINLALATGNI-------------GrpgtgpfpltgqNNVQ---GGRdmgALPNVLPGYRDVTD--PEHRaKV 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 417 EAILN----PDKE---IDFMGKKLKLPKIKMIYNCGADLLGHEADTNELIRALRTLDCVIVHEPWWTPTAKFADIVFAST 489
Cdd:COG3383 364 ADAWGvpplPDKPgltAVEMFDAIADGEIKALWIIGENPAVSDPDANHVREALEKLEFLVVQDIFLTETAEYADVVLPAA 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 490 STMERDditfgGSYSkNV---VYAMRKVVEPVYESKDDYEIFRQLALRIGGnetEQKFTESKSYMEWIKSL--------Y 558
Cdd:COG3383 444 SWAEKD-----GTFT-NTerrVQRVRKAVEPPGEARPDWEIIAELARRLGY---GFDYDSPEEVFDEIARLtpdysgisY 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 559 EKSDGPTLksfdQFWrdGFVEFEIPENARKFvrhakfrqdpiNNKLDTESGKiqifsqkcADFKLTDfkghptWFEPAEw 638
Cdd:COG3383 515 ERLEALGG----VQW--PCPSEDHPGTPRLF-----------TGRFPTPDGK--------ARFVPVE------YRPPAE- 562
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 639 lgsKMAETYPFHLISPhpkyRVNSQLDN-TWVRNVYKIQGREP---VMINELDANKLGIRHGEIVEVFNARGRLLAGAFV 714
Cdd:COG3383 563 ---LPDEEYPLVLTTG----RLLDQWHTgTRTRRSPRLNKHAPepfVEIHPEDAARLGIKDGDLVRVSSRRGEVVLRARV 635
|
....*....
gi 1751927289 715 TKNIRQGVL 723
Cdd:COG3383 636 TDRVRPGTV 644
|
|
| MopB_CT_DMSOR-like |
cd02777 |
The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
647-775 |
3.74e-60 |
|
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: 199.35 E-value: 3.74e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 647 YPFHLISPHPKYRVNSQLDN-TWVRNVYKIQGREPVMINELDANKLGIRHGEIVEVFNARGRLLAGAFVTKNIRQGVLSI 725
Cdd:cd02777 1 YPLQLISPHPKRRLHSQLDNvPWLREAYKVKGREPVWINPLDAAARGIKDGDIVRVFNDRGAVLAGARVTDRIMPGVVAL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1751927289 726 QKGAWYDPEDGrvrNPRCNAGHVNTLTSLRPTSSMTQAISANTALVNIRR 775
Cdd:cd02777 81 PEGAWYDPDDN---GGLDKGGNPNVLTSDIPTSKLAQGNPANTCLVEIEK 127
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
45-543 |
6.63e-53 |
|
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: 190.98 E-value: 6.63e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 45 AKVQNGVIKDIVPQKSDYNPTMML----KAMADRVYSDSRVKYPCvrksflenkKNHKElRGREEFVRVSWDVALDLAAK 120
Cdd:cd02759 15 VYVKDGKLVKVEGDPNHPTNKGRLcmrgLAAPEIVYHPDRLLYPL---------KRVGE-RGENKWERISWDEALDEIAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 121 KLKEIPK----ENIynASYGGWGHAGSLHrCHHLAWRFFNTTLGGAIGTDGEYSNGAAAKINPMIVGDMEVYSqqtahEE 196
Cdd:cd02759 85 KLAEIKAeygpESI--ATAVGTGRGTMWQ-DSLFWIRFVRLFGSPNLFLSGESCYWPRDMAHALTTGFGLGYD-----EP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 197 MIKNCKVYVMWGADLFKCNRIdyFVPNHVNDSyypkyKRAGIKFISIDPIYTETAQAfnAE-WIPIRPNTDVALMLGIMH 275
Cdd:cd02759 157 DWENPECIVLWGKNPLNSNLD--LQGHWLVAA-----MKRGAKLIVVDPRLTWLAAR--ADlWLPIRPGTDAALALGMLN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 276 YLYTSNQYDKAFIAKYTDGFDKFLPYLlgesdkAPKTLEWASQITGVSAEKIKELADLFV-SKRTFLAGNWAMQRAQYGE 354
Cdd:cd02759 228 VIINEGLYDKDFVENWCYGFEELAERV------QEYTPEKVAEITGVPAEKIRKAARLYAtAKPACIQWGLAIDQQKNGT 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 355 QPDWALIVLASMIGQVGLSgggfgfsmhyGGNaqassgaRIVPmisqghnsvksvipasriseailnpdkeidfmgkklk 434
Cdd:cd02759 302 QTSRAIAILRAITGNLDVP----------GGN-------LLIP------------------------------------- 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 435 lPKIKMIYNCGADLLGHEADTNELIRALRTLDCVIVHEPWWTPTAKFADIVFASTSTMERDDITfGGSYSKNVVYAMRKV 514
Cdd:cd02759 328 -YPVKMLIVFGTNPLASYADTAPVLEALKALDFIVVVDLFMTPTAMLADIVLPVAMSLERPGLR-GGFEAENFVQLRQKA 405
|
490 500
....*....|....*....|....*....
gi 1751927289 515 VEPVYESKDDYEIFRQLALRIGGNETEQK 543
Cdd:cd02759 406 VEPYGEAKSDYEIVLELGKRLGPEEAEYY 434
|
|
| MopB_4 |
cd02765 |
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
47-635 |
1.29e-49 |
|
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: 183.83 E-value: 1.29e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 47 VQNGVIKDIVPQK---SDYnPTMMLKAM--ADRVYSDSRVKYPCVRKSflenkknhkeLRGREEFVRVSWDVALDLAAKK 121
Cdd:cd02765 18 VRDGKIVKVEPNEwpdKTY-KRGCTRGLshLQRVYSPDRLKYPMKRVG----------ERGEGKFERITWDEALDTIADK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 122 LKEIpKENIYNASYGGWGHAGSLHRCHHLAWRFFNTTLGGAIGTDGEYsnGAAAKINPMIVGDMEVysqqTAHEEM-IKN 200
Cdd:cd02765 87 LTEA-KREYGGKSILWMSSSGDGAILSYLRLALLGGGLQDALTYGIDT--GVGQGFNRVTGGGFMP----PTNEITdWVN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 201 CKVYVMWGADLFKcnridyfvpNHVNDS-YYPKYKRAGIKFISIDPIYTETAqAFNAEWIPIRPNTDVALMLGIMHYLYT 279
Cdd:cd02765 160 AKTIIIWGSNILE---------TQFQDAeFFLDARENGAKIVVIDPVYSTTA-AKADQWVPIRPGTDPALALGMINYILE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 280 SNQYDKAFIAKYTDGfdkflPYLLGESDKapKTLEWASQITGVSAEKIKELADLFVSKRTF--------LAGNWAMQ--- 348
Cdd:cd02765 230 HNWYDEAFLKSNTSA-----PFLVREDNG--TLLRQADVTATPAEDGYVVWDTNSDSPEPVaatninpaLEGEYTINgvk 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 349 --------RAQYGEQPDWALIVLASMIGQVGLSGGGFGFSMhyGGNAQASSGAriVPMISQGHNSVKSVipasriseAIL 420
Cdd:cd02765 303 vhtvltalREQAASYPPKAAAEICGLEEAIIETLAEWYATG--KPSGIWGFGG--VDRYYHSHVFGRTA--------AIL 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 421 -----NPDKEIDFMGkklklpKIKMIYNCGADLLGHEADTNELIRALRTLDCVIVHEPWWTPTAKFADIVFASTSTMERD 495
Cdd:cd02765 371 aaltgNIGRVGGGVG------QIKFMYFMGSNFLGNQPDRDRWLKVMKNLDFIVVVDIFHTPTVRYADIVLPAAHWFEVE 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 496 DITFGGSYSKNVVYAmRKVVEPVYESKDDYEIFRQLALRIGgneTEQKFTESKSymEWIKsLYEKSDGPTLKSFDqfWrD 575
Cdd:cd02765 445 DLLVRYTTHPHVLLQ-QKAIEPLFESKSDFEIEKGLAERLG---LGDYFPKTPE--DYVR-AFMNSDDPALDGIT--W-E 514
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1751927289 576 GFVEfeipenaRKFVRHAKFRQDPINNKLD----TESGKIQIFSQKCADFKltdfKGHPTWFEP 635
Cdd:cd02765 515 ALKE-------EGIIMRLATPEDPYVAYLDqkfgTPSGKLEFYNEAAPELE----EALPLPEEP 567
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
69-558 |
3.32e-49 |
|
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: 181.64 E-value: 3.32e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 69 KAMADRVYSDSRVKYPCVRKsflenkknhkelrgREEFVRVSWDVALDLAAKKLKEIPKENIYNASYGgwghagslhrch 148
Cdd:cd02753 43 RFGFDFVNSKDRLTKPLIRK--------------NGKFVEASWDEALSLVASRLKEIKDKYGPDAIAF------------ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 149 hlawrffnttLGGAIGTDGEysNGAAAKINPMIVGDMEV--------------------YSQQTAHEEMIKNCKVYVMWG 208
Cdd:cd02753 97 ----------FGSAKCTNEE--NYLFQKLARAVGGTNNVdhcarlchsptvaglaetlgSGAMTNSIADIEEADVILVIG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 209 ADLFKcnridyfvpNH-VNDSYYPKYKRAGIKFISIDPIYTETAQaFNAEWIPIRPNTDVALMLGIMHYLYTSNQYDKAF 287
Cdd:cd02753 165 SNTTE---------AHpVIARRIKRAKRNGAKLIVADPRRTELAR-FADLHLQLRPGTDVALLNAMAHVIIEEGLYDEEF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 288 IAKYTDGFDKFLpyllgESDKApKTLEWASQITGVSAEKIKELADLFVSKRTfLAGNWAMQRAQY--GEQPDWALIVLAS 365
Cdd:cd02753 235 IEERTEGFEELK-----EIVEK-YTPEYAERITGVPAEDIREAARMYATAKS-AAILWGMGVTQHshGTDNVMALSNLAL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 366 MIGQVglsgggfgfsmhyggnaqASSGARIVPMisQGHNSVKSvipASriseailnpdkeiDFMGKKLKLPK-IKMIYNC 444
Cdd:cd02753 308 LTGNI------------------GRPGTGVNPL--RGQNNVQG---AC-------------DMGALPNVLPGyVKALYIM 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 445 GADLLGHEADTNELIRALRTLDCVIVHEPWWTPTAKFADIVFASTSTMERDditfgGSYSkNV---VYAMRKVVEPVYES 521
Cdd:cd02753 352 GENPALSDPNTNHVRKALESLEFLVVQDIFLTETAELADVVLPAASFAEKD-----GTFT-NTerrVQRVRKAVEPPGEA 425
|
490 500 510
....*....|....*....|....*....|....*..
gi 1751927289 522 KDDYEIFRQLALRIGGNeteQKFTESKSYMEWIKSLY 558
Cdd:cd02753 426 RPDWEIIQELANRLGYP---GFYSHPEEIFDEIARLT 459
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
42-536 |
9.43e-48 |
|
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: 175.95 E-value: 9.43e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 42 PFIAKVQNGVIKDIVPqksdyNPTMMLK---------AMADRVYSDSRVKYPCVRKsflenkknhkELRGREEFVRVSWD 112
Cdd:cd02755 13 GILARVEDGRVVKIDG-----NPLSPLSrgklcargnAGIQLLYDPDRLKKPLIRV----------GERGEGKFREASWD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 113 VALDLAAKKLKEI-PKENIYNASYGGWGHAGSlhrcHHLawRFFNTTLGGAIGTDGE----YSNGAAAKINPMIVGDMEV 187
Cdd:cd02755 78 EALQYIASKLKEIkEQHGPESVLFGGHGGCYS----PFF--KHFAAAFGSPNIFSHEstclASKNLAWKLVIDSFGGEVN 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 188 YSqqtaheemIKNCKVYVMWGAdlfkcNRIDYFVPNHVNDsyYPKYKRAGIKFISIDPIYTETAqAFNAEWIPIRPNTDV 267
Cdd:cd02755 152 PD--------FENARYIILFGR-----NLAEAIIVVDARR--LMKALENGAKVVVVDPRFSELA-SKADEWIPIKPGTDL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 268 ALMLGIMHYLYTSNQYDKAFIAKYTDGFDKFLPyllgesDKAPKTLEWASQITGVSAEKIKELAdlfvskRTFLAgnwAM 347
Cdd:cd02755 216 AFVLALIHVLISENLYDAAFVEKYTNGFELLKA------HVKPYTPEWAAQITDIPADTIRRIA------REFAA---AA 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 348 QRAQYgeQPDWalivlasmigqvglsgggfgfsmhyggnaqassgarivpMISQGHNSVKsvipaSRISEAILNP----- 422
Cdd:cd02755 281 PHAVV--DPGW---------------------------------------RGTFYSNSFQ-----TRRAIAIINAllgni 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 423 DKEID-FMGKKLKLPKIKMIYNCGADLLGHEADTNELIRALRTLDCVIVHEPWWTPTAKFADIVFASTSTMERDDITFGG 501
Cdd:cd02755 315 DKRGGlYYAGSAKPYPIKALFIYRTNPFHSMPDRARLIKALKNLDLVVAIDILPSDTALYADVILPEATYLERDEPFSDK 394
|
490 500 510
....*....|....*....|....*....|....*
gi 1751927289 502 SYSKNVVYAMRKVVEPVYESKDDYEIFRQLALRIG 536
Cdd:cd02755 395 GGPAPAVATRQRAIEPLYDTRPGWDILKELARRLG 429
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
1-723 |
1.73e-46 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 177.94 E-value: 1.73e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 1 MSISRRSIL-------------TKIPIALASTNVLKAVGVFEKVESIPHATHFG-PFIAKVQNGviKDIVPQKSDYNPTM 66
Cdd:PRK15488 1 MSLSRRDFLkgagagcaacalgSLLPGALAANEIAQLKGKTKLTPSICEMCSTRcPIEARVVNG--KNVFIQGNPKAKSF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 67 MLKAMA------DRVYSDSRVKYPCVRKSflenkknhkeLRGREEFVRVSWDVALDLAAKKLKEIPK----ENIYNASYG 136
Cdd:PRK15488 79 GTKVCArggsghSLLYDPQRIVKPLKRVG----------ERGEGKWQEISWDEAYQEIAAKLNAIKQqhgpESVAFSSKS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 137 GW--GHAgslhrcHHLAwrffnttlgGAIGTDGEYSNGA--------AAKInpMIVGDMEvysqqtaheEMIKNCKVYVM 206
Cdd:PRK15488 149 GSlsSHL------FHLA---------TAFGSPNTFTHAStcpagyaiAAKV--MFGGKLK---------RDLANSKYIIN 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 207 WGADLFKcnridyfvpnHVNDSYYPKYKRA----GIKFISIDPIYTETAQAFNaEWIPIRPNTDVALMLGIMHYLYTSNQ 282
Cdd:PRK15488 203 FGHNLYE----------GINMSDTRGLMTAqmekGAKLVVFEPRFSVVASKAD-EWHAIRPGTDLAVVLALCHVLIEENL 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 283 YDKAFIAKYTDGFDKFLPYLlgesdkAPKTLEWASQITGVSAEKIKELADLFVS-----------KRTFLAGNWAMQRaq 351
Cdd:PRK15488 272 YDKAFVERYTSGFEELAASV------KEYTPEWAEAISDVPADDIRRIARELAAaaphaivdfghRATFTPEEFDMRR-- 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 352 ygeqpdwALIVLASMIGQVglsggGFGFSMHYGGNAQ---ASSGARIVP--------------------------MISQG 402
Cdd:PRK15488 344 -------AIFAANVLLGNI-----ERKGGLYFGKNASvynKLAGEKVAPtlakpgvkgmpkptakridlvgeqfkYIAAG 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 403 HNSVKSVIpasrisEAILNpdkeidfmgkklKLP-KIKMIYNCGADLLGHEADTNELIRALRTLDCVIVHEPWWTPTAKF 481
Cdd:PRK15488 412 GGVVQSII------DATLT------------QKPyQIKGWVMSRHNPMQTVTDRADVVKALKKLDLVVVCDVYLSESAAY 473
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 482 ADIVFASTSTMERDDiTFGGSYSKNVVYAMR-KVVEPVYESKDDYEIFRQLALRIGGNEteqkftesksYMEW--IKS-- 556
Cdd:PRK15488 474 ADVVLPESTYLERDE-EISDKSGKNPAYALRqRVVEPIGDTKPSWQIFKELGEKMGLGQ----------YYPWqdMETlq 542
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 557 LYEKSDGPTLksFDQFWRDGFVEFEIP------ENARKFVRH---AKFRQDpiNN------KLDTESGKIQIFSQKCAdf 621
Cdd:PRK15488 543 LYQVNGDHAL--LKELKKKGYVSFGVPlllrepKMVAKFVARypnAKAVDE--DGtygsqlKFKTPSGKIELFSAKLE-- 616
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 622 KLTDFKGHPTwFEPAewlgsKMAETYPFHLISPHPKYRVNSQLDNtwVRNVYKIQGREPVMINELDANKLGIRHGEIVEV 701
Cdd:PRK15488 617 ALAPGYGVPR-YRDV-----ALKKEDELYFIQGKVAVHTNGATQN--VPLLANLMSDNAVWIHPQTAGKLGIKNGDEIRL 688
|
810 820
....*....|....*....|..
gi 1751927289 702 FNARGRLLAGAFVTKNIRQGVL 723
Cdd:PRK15488 689 ENSVGKEKGKALVTPGIRPDTL 710
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
80-532 |
2.89e-44 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 163.34 E-value: 2.89e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 80 RVKYPCVRksflenkknhkelRGREEFVRVSWDVALDLAAKKLKEIPKE-----NIYNASYGGWGHAGSLHRCHHLAWRF 154
Cdd:pfam00384 1 RLKYPMVR-------------RGDGKFVRVSWDEALDLIAKKLKRIIKKygpdaIAINGGSGGLTDVESLYALKKLLNRL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 155 FNTTlGGAIGTDGEYSNGAAAkinpmIVGDMEVYSQQ-TAHEEMIKNCKVYVMWGADLFKCNRIdyfvpnhVNDSYYPKY 233
Cdd:pfam00384 68 GSKN-GNTEDHNGDLCTAAAA-----AFGSDLRSNYLfNSSIADIENADLILLIGTNPREEAPI-------LNARIRKAA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 234 KRAGIKFISIDPIYTETaqaFNAEWIPIRPNTDVALMLGIMHYLYTSNQYDKAFIAKytdgfdkflpyllgesdkapktl 313
Cdd:pfam00384 135 LKGKAKVIVIGPRLDLT---YADEHLGIKPGTDLALALAGAHVFIKELKKDKDFAPK----------------------- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 314 ewASQITGvsaekikeladlfvskrtflagnWAMQRAQYGEQPDWALIVLASMIGQVGLSGGGFGFSMHYGGNAqASSGA 393
Cdd:pfam00384 189 --PIIIVG-----------------------AGVLQRQDGEAIFRAIANLADLTGNIGRPGGGWNGLNILQGAA-SPVGA 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 394 RIVPmisqghnsvksvipasriseaiLNPDKEIDFMGKKLKLPKIKMIYNCGADLLGHEADTNELIRALRTLDCVIVHEP 473
Cdd:pfam00384 243 LDLG----------------------LVPGIKSVEMINAIKKGGIKVLYLLGNNPFVTHADENRVVKALQKLDLFVVYDG 300
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 474 -WWTPTAKFADIVFASTSTMERDDITFGGSYSknvVYAMRKVVEPVYESKDDYEIFRQLA 532
Cdd:pfam00384 301 hHGDKTAKYADVILPAAAYTEKNGTYVNTEGR---VQSTKQAVPPPGEAREDWKILRALS 357
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
75-536 |
1.29e-35 |
|
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: 142.75 E-value: 1.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 75 VYSDSRVKYPCVRksflenkknhkelRGREEFVRVSWDVALDLAAKKLKEIPKEniynasYG----GWGHAGSLhrchhL 150
Cdd:cd02754 49 LNGPERLTRPLLR-------------RNGGELVPVSWDEALDLIAERFKAIQAE------YGpdsvAFYGSGQL-----L 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 151 AWRFFntTLG----GAIGTDGEYSNG----AAAkinpmIVGDMEVY--SQQTAHEEMIKNCKVYVMWGADLFKCNRIDYf 220
Cdd:cd02754 105 TEEYY--AANklakGGLGTNNIDTNSrlcmASA-----VAGYKRSFgaDGPPGSYDDIEHADCFFLIGSNMAECHPILF- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 221 vpNHVNDSyypKYKRAGIKFISIDPIYTETAQafNAE-WIPIRPNTDVALMLGIMHYLYTSNQYDKAFIAKYTDGFDKFL 299
Cdd:cd02754 177 --RRLLDR---KKANPGAKIIVVDPRRTRTAD--IADlHLPIRPGTDLALLNGLLHVLIEEGLIDRDFIDAHTEGFEELK 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 300 PYLlgesdkAPKTLEWASQITGVSAEKIKELADLFVSKRTFLAgNWAM---QRAQyGEQPDWALIVLA------------ 364
Cdd:cd02754 250 AFV------ADYTPEKVAEITGVPEADIREAARLFGEARKVMS-LWTMgvnQSTQ-GTAANNAIINLHlatgkigrpgsg 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 365 --SMIGQvglsgggfgfsmhygGNAQassGARIVPMISQ---GHNSVKSviPASR-ISEAILN--PDKEIDFMG------ 430
Cdd:cd02754 322 pfSLTGQ---------------PNAM---GGREVGGLANllpGHRSVNN--PEHRaEVAKFWGvpEGTIPPKPGlhavem 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 431 -KKLKLPKIKMIYNCGADLLGHEADTNELIRALRTLDCVIVHEPWW-TPTAKFADIVFASTSTMERDditfgGSY--SKN 506
Cdd:cd02754 382 fEAIEDGEIKALWVMCTNPAVSLPNANRVREALERLEFVVVQDAFAdTETAEYADLVLPAASWGEKE-----GTMtnSER 456
|
490 500 510
....*....|....*....|....*....|
gi 1751927289 507 VVYAMRKVVEPVYESKDDYEIFRQLALRIG 536
Cdd:cd02754 457 RVSLLRAAVEPPGEARPDWWILADVARRLG 486
|
|
| MopB_Nitrate-R-NarG-like |
cd02750 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
47-535 |
1.68e-30 |
|
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: 125.89 E-value: 1.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 47 VQNGVIK---------DIVPQKSDYNPTMMLK--AMADRVYSDSRVKYPCVRKsflenkknhkELRGREEFVRVSWDVAL 115
Cdd:cd02750 22 VKNGIVTreeqatdypETPPDLPDYNPRGCQRgaSFSWYLYSPDRVKYPLKRV----------GARGEGKWKRISWDEAL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 116 DLAAKKLKEIPK----ENIYNASygGWGHAGSLHrchHLAW-RFfnTTLGGAIGTDgeysngaaakINPMIvGDMEVYSQ 190
Cdd:cd02750 92 ELIADAIIDTIKkygpDRVIGFS--PIPAMSMVS---YAAGsRF--ASLIGGVSLS----------FYDWY-GDLPPGSP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 191 QT---AHEEMIK----NCKVYVMWGADLFKCNRIDYfvpnHvndsYYPKYKRAGIKFISIDPIYTETAqAFNAEWIPIRP 263
Cdd:cd02750 154 QTwgeQTDVPESadwyNADYIIMWGSNVPVTRTPDA----H----FLTEARYNGAKVVVVSPDYSPSA-KHADLWVPIKP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 264 NTDVALMLGIMHYLYTSNQYDKAFIAKYTDgfdkfLPYLLgesdkapKTLEWASQITGVSAEKIKELADLFV-SKRTFLA 342
Cdd:cd02750 225 GTDAALALAMAHVIIKEKLYDEDYLKEYTD-----LPFLV-------YTPAWQEAITGVPRETVIRLAREFAtNGRSMII 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 343 GNWAMQRAQYGEQPDWALIVLASMIGqvglsgggfgfsmhyggnAQASSGARIVPMISQghnsvksvipasriseailnp 422
Cdd:cd02750 293 VGAGINHWYHGDLCYRALILLLALTG------------------NEGKNGGGWAHYVGQ--------------------- 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 423 dkeidfmgkklklPKIKMIYncGADLLGHEADTNELI-RALR-TLDCVIVHEPWWTPTAKFADIVFASTSTMERDDI--T 498
Cdd:cd02750 334 -------------PRVLFVW--RGNLFGSSGKGHEYFeDAPEgKLDLIVDLDFRMDSTALYSDIVLPAATWYEKHDLstT 398
|
490 500 510
....*....|....*....|....*....|....*..
gi 1751927289 499 FGGSYsknvVYAMRKVVEPVYESKDDYEIFRQLALRI 535
Cdd:cd02750 399 DMHPF----IHPFSPAVDPLWEAKSDWEIFKALAKKV 431
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
100-535 |
1.17e-29 |
|
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: 124.43 E-value: 1.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 100 LRGREEFVRVSWDVALDLAAKKLKEIPKENIYNAS--YGGWG----HAGSLHrchhlawrffNTTLGGAIGTDGEYSNGA 173
Cdd:cd02762 60 RRRGGSFEEIDWDEAFDEIAERLRAIRARHGGDAVgvYGGNPqahtHAGGAY----------SPALLKALGTSNYFSAAT 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 174 AAKInPMIVGDMEVYSQQTAHE-EMIKNCKVYVMWGADLFKCNRIDYFVPNHVNDSYYPKyKRAGiKFISIDPIYTETAq 252
Cdd:cd02762 130 ADQK-PGHFWSGLMFGHPGLHPvPDIDRTDYLLILGANPLQSNGSLRTAPDRVLRLKAAK-DRGG-SLVVIDPRRTETA- 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 253 AFNAEWIPIRPNTDVALMLGIMHYLYTSNQYDKAFIAKYTDGFDKFLPYLlgesdkAPKTLEWASQITGVSAEKIKELA- 331
Cdd:cd02762 206 KLADEHLFVRPGTDAWLLAAMLAVLLAEGLTDRRFLAEHCDGLDEVRAAL------AEFTPEAYAPRCGVPAETIRRLAr 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 332 DLFVSKRTFLAGNWAMQRAQYGEQPDWALIVLASMIGQVGLSgggfgfsmhyGGNAQASSGARIVPMISQ---------- 401
Cdd:cd02762 280 EFAAAPSAAVYGRLGVQTQLFGTLCSWLVKLLNLLTGNLDRP----------GGAMFTTPALDLVGQTSGrtigrgewrs 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 402 ---GHNSVKSVIPASRISEAILNPDkeidfmGKKLKlpkiKMIYNCGADLLGHeADTNELIRALRTLDCVIVHEPWWTPT 478
Cdd:cd02762 350 rvsGLPEIAGELPVNVLAEEILTDG------PGRIR----AMIVVAGNPVLSA-PDGARLEAALGGLEFMVSVDVYMTET 418
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1751927289 479 AKFADIVFASTSTMERDDITFGGS-YSKNVVYAMRKVVEPVYESKDDYEIFRQLALRI 535
Cdd:cd02762 419 TRHADYILPPASQLEKPHATFFNLeFPRNAFRYRRPLFPPPPGTLPEWEILARLVEAL 476
|
|
| MopB_Arsenate-R |
cd02757 |
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ... |
70-535 |
1.40e-29 |
|
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: 124.09 E-value: 1.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 70 AMADRVYSDSRVKYPCVRKsfleNKKNHKELRGreEFVRVSWDVALDLAAKKLKEIPKENI---YNASYGGWGHAGSLHr 146
Cdd:cd02757 46 LGLQQVYDPDRILYPMKRT----NPRKGRDVDP--KFVPISWDEALDTIADKIRALRKENEphkIMLHRGRYGHNNSIL- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 147 chhlAWRFFNttlggAIGTDGEYSNGA----AAKINPMIVGDMEVYSQQTaheemIKNCKVYVMWGADLFKCNRidyFVP 222
Cdd:cd02757 119 ----YGRFTK-----MIGSPNNISHSSvcaeSEKFGRYYTEGGWDYNSYD-----YANAKYILFFGADPLESNR---QNP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 223 NHVNDSyypKYKRAGIKFISIDPIYTETAqAFNAEWIPIRPNTDVALMLGIMHYLYTSNQYDKAFIAKYTDGFDKFLP-Y 301
Cdd:cd02757 182 HAQRIW---GGKMDQAKVVVVDPRLSNTA-AKADEWLPIKPGEDGALALAIAHVILTEGLWDKDFVGDFVDGKNYFKAgE 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 302 LLGESDKAPK----------------TLEWASQITGVSAEKIKELADLFV-SKRTFLAGNW---AMQ-RAQYGEQPDWAL 360
Cdd:cd02757 258 TVDEESFKEKsteglvkwwnlelkdyTPEWAAKISGIPAETIERVAREFAtAAPAAAAFTWrgaTMQnRGSYNSMACHAL 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 361 IVLASMIGQVglsgggfgfsmhyGGNAQASSGARIVPMISQGHNSVKSvipasriseailNPdkeidfmgkklklpkikm 440
Cdd:cd02757 338 NGLVGSIDSK-------------GGLCPNMGVPKIKVYFTYLDNPVFS------------NP------------------ 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 441 iyncgadllgheaDTNELIRALRTLDCVIVHEPWWTPTAKFADIVFASTSTMERDDITFGGSYSKNVVYAMRKVVEPVYE 520
Cdd:cd02757 375 -------------DGMSWEEALAKIPFHVHLSPFMSETTYFADIVLPDGHHFERWDVMSQENNLHPWLSIRQPVVKSLGE 441
|
490
....*....|....*
gi 1751927289 521 SKDDYEIFRQLALRI 535
Cdd:cd02757 442 VREETEILIELAKKL 456
|
|
| MopB_CT_DmsA-EC |
cd02794 |
The MopB_CT_DmsA-EC CD includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
647-775 |
9.75e-29 |
|
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: 111.23 E-value: 9.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 647 YPFHLISPHPKYRVNSQLDN-TWVRNVYkiqgREPVMINELDANKLGIRHGEIVEVFNARGRLLAGAFVTKNIRQGVLSI 725
Cdd:cd02794 1 YPLQLIGWHYKRRTHSTFDNvPWLREAF----PQEVWINPLDAAARGIKDGDRVLVFNDRGKVIRPVKVTERIMPGVVAL 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1751927289 726 QKGAWYDPEDGRVrnprCNAGHVNTLTSLRPtSSMTQAISANTALVNIRR 775
Cdd:cd02794 77 PQGAWYEPDANGI----DKGGCINTLTGLRP-SPLAKGNPQHTNLVQVEK 121
|
|
| Molydop_binding |
pfam01568 |
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
649-770 |
3.60e-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: 106.20 E-value: 3.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 649 FHLISPHPKYRVNSQLDNTWVRNVYKIQGrEPVMINELDANKLGIRHGEIVEVFNARGRLLAGAFVTKNIRQGVLSIQKG 728
Cdd:pfam01568 1 LYLITGRVLGQYHSQTRTRRVLRLAKPEP-EVVEIHPEDAAALGIKDGDLVEVTSRRGSVVVRAKVTDRVRPGVVFMPFG 79
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1751927289 729 AWYDPedgrvrnprcNAGHVNTLTSlRPTSSMTQAISANTAL 770
Cdd:pfam01568 80 WWYEP----------RGGNANALTD-DATDPLSGGPEFKTCA 110
|
|
| MopB_2 |
cd02763 |
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
76-331 |
5.79e-20 |
|
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: 94.90 E-value: 5.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 76 YSDSRVKYPCVRKsflenkknhkELRGREEFVRVSWDVALDLAAKKLKEIPKENIYN-ASYGGWGHAGSLhrchhlawrf 154
Cdd:cd02763 50 YSPARLTKPLLRK----------GPRGSGQFEEIEWEEAFSIATKRLKAARATDPKKfAFFTGRDQMQAL---------- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 155 fNTTLGGAIGTDGEYSNGAAAKINPMIVGDMEV-YSQQTAHEEMIKNCKVYVMWG-ADLFKCNRIDYFVPnhvndsyypK 232
Cdd:cd02763 110 -TGWFAGQFGTPNYAAHGGFCSVNMAAGGLYSIgGSFWEFGGPDLEHTKYFMMIGvAEDHHSNPFKIGIQ---------K 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 233 YKRAGIKFISIDPIYTETAqAFNAEWIPIRPNTDVALMLGIMHYLYTSNQYDKAFIAKYTDGfdkflPYLLgesDKAPkt 312
Cdd:cd02763 180 LKRRGGKFVAVNPVRTGYA-AIADEWVPIKPGTDGAFILALAHELLKAGLIDWEFLKRYTNA-----AELV---DYTP-- 248
|
250
....*....|....*....
gi 1751927289 313 lEWASQITGVSAEKIKELA 331
Cdd:cd02763 249 -EWVEKITGIPADTIRRIA 266
|
|
| MopB_CT_4 |
cd02785 |
The MopB_CT_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
647-776 |
6.30e-20 |
|
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: 86.27 E-value: 6.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 647 YPFHLISPHPKYRVNSQ-LDNTWVRnvyKIQGREPVMINELDANKLGIRHGEIVEVFNARGRLLAGAFVTKNIRQGVLSI 725
Cdd:cd02785 2 YPLACIQRHSRFRVHSQfSNVPWLL---ELQPEPRVKINPIDAAARGIAHGDLVEVYNDRGSVVCKAKVDDGIQPGVVTA 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1751927289 726 QKGAW--YDPEdgrvrnprcnaGHVNTLTS--LRPTS-SMTQAISA-NTALVNIRRL 776
Cdd:cd02785 79 EQGWWsrYFQE-----------GSLQDLTSpfVNPVHeYIYGPNSAfYDTLVEVRKA 124
|
|
| MopB_Formate-Dh-Na-like |
cd02752 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
43-536 |
2.80e-19 |
|
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: 92.85 E-value: 2.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 43 FIAKVQNGVIkdiVPQKSDY-NP----TMMLK--AMADRVYSDSRVKYPCVRKSflenkknhkelrGREEFVRVSWDVAL 115
Cdd:cd02752 13 LIAYVQNGVW---VHQEGDPdHPvnrgSLCPKgaALRDFVHSPKRLKYPMYRAP------------GSGKWEEISWDEAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 116 DLAAKKLKEIPKENIYNASYGGWghagSLHRCHHLAWrffnttLGGAiGTDGE----YSNGAA----------AKIN--P 179
Cdd:cd02752 78 DEIARKMKDIRDASFVEKNAAGV----VVNRPDSIAF------LGSA-KLSNEecylIRKFARalgtnnldhqARIUhsP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 180 MIVGDMEV--YSQQTAHEEMIKNCKVYVMWGadlfkCNRIDyfvpNH-VNDSYYPKYK-RAGIKFISIDPIYTETAqAFN 255
Cdd:cd02752 147 TVAGLANTfgRGAMTNSWNDIKNADVILVMG-----GNPAE----AHpVSFKWILEAKeKNGAKLIVVDPRFTRTA-AKA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 256 AEWIPIRPNTDVALMLGIMHYlytsnqydkafIAKYTdgfdkflpyllgesdkaPKTLEwasQITGVSAEKIKELADLFV 335
Cdd:cd02752 217 DLYVPIRSGTDIAFLGGMINY-----------IIRYT-----------------PEEVE---DICGVPKEDFLKVAEMFA 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 336 SKR------TFLagnWAMQRAQ--YGEQpdwalIVLASMIGQvglsgggfgfsMHYGGNAQASSGARIVpmisQGHNSVK 407
Cdd:cd02752 266 ATGrpdkpgTIL---YAMGWTQhtVGSQ-----NIRAMCILQ-----------LLLGNIGVAGGGVNAL----RGHSNVQ 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 408 SVipasriSEAILNPDkeidfmgkklKLPKikmiYNCGADLLGHEADTNELIRALRTLDCVIVHEPWWTPTAKFADIvfA 487
Cdd:cd02752 323 GA------TDLGLLSH----------NLPG----YLGGQNPNSSFPNANKVRRALDKLDWLVVIDPFPTETAAFWKN--P 380
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1751927289 488 STSTMERDDITF----GGSYSK--NVVYAMR------KVVEPVYESKDDYEIFRQLALRIG 536
Cdd:cd02752 381 GMDPKSIQTEVFllpaACQYEKegSITNSGRwlqwryKVVEPPGEAKSDGDILVELAKRLG 441
|
|
| MopB_CT |
cd02775 |
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a ... |
656-758 |
5.69e-18 |
|
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: 79.67 E-value: 5.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 656 PKYRVNSQLDnTWVRNVYKIQGREPVMINELDANKLGIRHGEIVEVFNARGRLLAGAFVTKNIRQGVLSIQKGAWYDPED 735
Cdd:cd02775 1 LRDHFHSGTR-TRNPWLRELAPEPVVEINPEDAAALGIKDGDLVRVESRRGSVVLRAKVTDGVPPGVVFLPHGWGHRGGR 79
|
90 100
....*....|....*....|...
gi 1751927289 736 GrvrnprcnaGHVNTLTSLRPTS 758
Cdd:cd02775 80 G---------GNANVLTPDALDP 93
|
|
| MopB_CT_3 |
cd02786 |
The MopB_CT_3 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
647-757 |
6.57e-15 |
|
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: 71.54 E-value: 6.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 647 YPFHLISPHPKYRVNSQLDNTwvRNVYKIQGREPVMINELDANKLGIRHGEIVEVFNARGRLLAGAFVTKNIRQGVLSIQ 726
Cdd:cd02786 1 YPLRLITPPAHNFLNSTFANL--PELRAKEGEPTLLIHPADAAARGIADGDLVVVFNDRGSVTLRAKVTDDVPPGVVVAE 78
|
90 100 110
....*....|....*....|....*....|.
gi 1751927289 727 KGaWYDPEDGRVRNprcnaghVNTLTSLRPT 757
Cdd:cd02786 79 GG-WWREHSPDGRG-------VNALTSARLT 101
|
|
| MopB_Phenylacetyl-CoA-OR |
cd02760 |
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large ... |
46-304 |
3.09e-11 |
|
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: 66.92 E-value: 3.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 46 KVQNGVIKDIVP--QKSDYNPT---MMLKA--MADRVYSDSRVKYPCVRKsfleNKKnhkelRGREE---FVRVSWDVAL 115
Cdd:cd02760 17 KVVDGVATEIEPnfAAEDIHPArgrVCVKAygLVQKTYNPNRVLQPMKRT----NPK-----KGRNEdpgFVPISWDEAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 116 DLAAKKLKEIPKENIYNasyggwgHAGSLHRchhlawrffnTTLGGAIGTDGEYSNGAAAKINPMIVGDMEVYSQQ---T 192
Cdd:cd02760 88 DLVAAKLRRVREKGLLD-------EKGLPRL----------AATFGHGGTPAMYMGTFPAFLAAWGPIDFSFGSGQgvkC 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 193 AHEEMIKNCKVYVMW--GADLFKCNRIDYFVPN-HVNDSYYPKYKRA-----GIKFISIDPIYTETAqAFNAEWIPIRPN 264
Cdd:cd02760 151 VHSEHLYGEFWHRAFtvAADTPLANYVISFGSNvEASGGPCAVTRHAdarvrGYKRVQVEPHLSVTG-ACSAEWVPIRPK 229
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1751927289 265 TDVALMLGIMHYLYTS---NQYDKAFIAKYTDGfdkflPYLLG 304
Cdd:cd02760 230 TDPAFMFAMIHVMVHEqglGKLDVPFLRDRTSS-----PYLVG 267
|
|
| Molybdopterin_N |
pfam18364 |
Molybdopterin oxidoreductase N-terminal domain; This is the N-terminal domain of pfam00384 ... |
36-76 |
3.64e-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: 58.56 E-value: 3.64e-11
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1751927289 36 HATHFGPFIAKVQNGVIKDIVPQKSDYNPTMMLKAMADRVY 76
Cdd:pfam18364 1 TASHWGAFRAVVKDGRIVGVEPFEGDPDPSPLLQGVPDAVY 41
|
|
| MopB_CT_Fdh-Nap-like |
cd00508 |
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and ... |
645-775 |
1.30e-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: 59.44 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 645 ETYPFHLISphpkYRVNSQLdNTWV--RNVYKIQGREP---VMINELDANKLGIRHGEIVEVFNARGRLLAGAFVTKNIR 719
Cdd:cd00508 1 EEYPLVLTT----GRLLEHW-HTGTmtRRSPRLAALAPepfVEIHPEDAARLGIKDGDLVRVSSRRGSVVVRARVTDRVR 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1751927289 720 QGVLSIqkgAWYDPEDGRVRNprcnaghVNTLTS--LRPTSSMTQaisANTALVNIRR 775
Cdd:cd00508 76 PGTVFM---PFHWGGEVSGGA-------ANALTNdaLDPVSGQPE---FKACAVRIEK 120
|
|
| MopB_Tetrathionate-Ra |
cd02758 |
The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other ... |
182-368 |
3.29e-10 |
|
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: 63.52 E-value: 3.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 182 VGDMEVYSQQTAHeemIKNCKVYVMWGADlfkcnridyfvPNHVNDSYYPKYKR-------AGIKFISIDPIYTETAQAF 254
Cdd:cd02758 196 MNDLDGYPHVKPD---FDNAEFALFIGTS-----------PAQAGNPFKRQARRlaearteGNFKYVVVDPVLPNTTSAA 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 255 --NAEWIPIRPNTDVALMLGIMHYLYTSNQYDKAFI------AKYTDGFDKF--LPYL------------LGESDKApKT 312
Cdd:cd02758 262 geNIRWVPIKPGGDGALAMAMIRWIIENERYNAEYLsipskeAAKAAGEPSWtnATHLvitvrvksalqlLKEEAFS-YS 340
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1751927289 313 LEWASQITGVSAEKIKELADLFVS--KRTFLAGNWAMQrAQYGEQPDWALIVLASMIG 368
Cdd:cd02758 341 LEEYAEICGVPEAKIIELAKEFTShgRAAAVVHHGGTM-HSNGFYNAYAIRMLNALIG 397
|
|
| MopB_CT_Tetrathionate_Arsenate-R |
cd02780 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate ... |
647-742 |
4.80e-10 |
|
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: 58.46 E-value: 4.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 647 YPFHLISPHPKYRVNSQLDNTWVrnvYKIQGREPVMINELDANKLGIRHGEIVEVFNARGRLLAGAFVTKNIRQGVLSIQ 726
Cdd:cd02780 1 YPFILVTFKSNLNSHRSANAPWL---KEIKPENPVWINPEDAAKLGIKTGDRVRVVTPGGSVVGKAKVTEGVRPGVVAIE 77
|
90
....*....|....*...
gi 1751927289 727 KGA--WydpEDGRVRNPR 742
Cdd:cd02780 78 HGYghW---AYGAVASTI 92
|
|
| MopB_ydeP |
cd02767 |
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
101-370 |
9.48e-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: 61.94 E-value: 9.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 101 RGREEFVRVSWDVALDLAAKKLKEI-PKENIYNASYGGWGHAGSLHRchhLAWRFFNTT----------------LGGAI 163
Cdd:cd02767 73 AGSDHYRPISWDEAFAEIAARLRALdPDRAAFYTSGRASNEAAYLYQ---LFARAYGTNnlpdcsnmchepssvgLKKSI 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 164 GTdgeysnGAAakinpmivgdmevysqqTAHEEMIKNCKVYVMWGADlfkcnridyfvP--NH-VNDSYYPKYKRAGIKF 240
Cdd:cd02767 150 GV------GKG-----------------TVSLEDFEHTDLIFFIGQN-----------PgtNHpRMLHYLREAKKRGGKI 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 241 ISIDPiYTETA-QAFnaeWIP-------------------IRPNTDVALMLGIMHYL-----YTSNQYDKAFIAKYTDGF 295
Cdd:cd02767 196 IVINP-LREPGlERF---ANPqnpesmltggtkiadeyfqVRIGGDIALLNGMAKHLierddEPGNVLDHDFIAEHTSGF 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 296 DKFLPYLlgesdkapKTLEWAS--QITGVSAEKIKELADLFV-SKRTFLAgnWAMQRAQ--YGEQPDWALIVLASMIGQV 370
Cdd:cd02767 272 EEYVAAL--------RALSWDEieRASGLSREEIEAFAAMYAkSERVVFV--WGMGITQhaHGVDNVRAIVNLALLRGNI 341
|
|
| PRK14991 |
PRK14991 |
tetrathionate reductase subunit TtrA; |
626-728 |
1.44e-08 |
|
tetrathionate reductase subunit TtrA;
Pssm-ID: 237883 [Multi-domain] Cd Length: 1031 Bit Score: 58.47 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 626 FKGHPTWFEPAEWLGSKMAETY-----PFHLISphpkYRVN--SQLDNTWVRnVYKIQGREPVMINELDANKLGIRHGEI 698
Cdd:PRK14991 861 YSGCPTWYPPRLADGTPLREQFpesqwPLLLIS----FKSNlmSSMSIASPR-LRQVKPANPVALNPQDAARLGIQHGDR 935
|
90 100 110
....*....|....*....|....*....|
gi 1751927289 699 VEVFNARGRLLAGAFVTKNIRQGVLSIQKG 728
Cdd:PRK14991 936 VRISTPGGSVVAQASVLNGVMPGVIAIEHG 965
|
|
| MopB_CT_Nitrate-R-NarG-like |
cd02776 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
648-757 |
2.32e-08 |
|
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: 53.54 E-value: 2.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 648 PFHLISPHPKYRVNSqldnTWVRNVYKI---QGREPVMINELDANKLGIRHGEIVEVFNARGRLLAGAFVTKNIRQGVLS 724
Cdd:cd02776 1 PLNYLTPHGKWSIHS----TYRDNLLMLrlqRGGPVVWMNPKDAAELGIKDNDWVEVFNDNGVVVARAKVSPRIPRGTVF 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1751927289 725 IQKgaWYDPEDGRVRNPRC--NAGHVNTLTSLRPT 757
Cdd:cd02776 77 MYH--AQERHVNVPGSKLTgkRGGIHNSVTRVRIK 109
|
|
| MopB_CT_Acetylene-hydratase |
cd02781 |
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related ... |
647-755 |
2.84e-08 |
|
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: 53.08 E-value: 2.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 647 YPFHLISPHPKYR-VNSQLdntwvRNVYKIQGREP---VMINELDANKLGIRHGEIVEVFNARGRLLAGAFVTKNIRQGV 722
Cdd:cd02781 2 YPLILTTGARSYYyFHSEH-----RQLPSLRELHPdpvAEINPETAAKLGIADGDWVWVETPRGRARQKARLTPGIRPGV 76
|
90 100 110
....*....|....*....|....*....|....
gi 1751927289 723 LSIQKGAWYD-PEDGRVRNPRCNAGHVNTLTSLR 755
Cdd:cd02781 77 VRAEHGWWYPeREAGEPALGGVWESNANALTSDD 110
|
|
| MopB_CT_Formate-Dh_H |
cd02790 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
645-725 |
4.31e-07 |
|
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: 49.16 E-value: 4.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 645 ETYPFHLISP----HpkYRVNSQLDNTWVRNVykIQGREPVMINELDANKLGIRHGEIVEVFNARGRLLAGAFVTKNIRQ 720
Cdd:cd02790 1 EEYPLVLTTGrvlyH--YHTGTMTRRAEGLDA--IAPEEYVEINPEDAKRLGIEDGEKVRVSSRRGSVEVRARVTDRVPE 76
|
....*
gi 1751927289 721 GVLSI 725
Cdd:cd02790 77 GVVFM 81
|
|
| MopB_CT_1 |
cd02782 |
The MopB_CT_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
666-753 |
9.42e-07 |
|
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: 48.54 E-value: 9.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 666 NTWVRNVYKIQGREP---VMINELDANKLGIRHGEIVEVFNARGRLLAGAFVTKNIRQGVLSIQKGaW---YDPEDGRVR 739
Cdd:cd02782 17 NSWLHNDPRLVKGRNrctLRIHPDDAAALGLADGDKVRVTSAAGSVEAEVEVTDDMMPGVVSLPHG-WghdYPGVSGAGS 95
|
90
....*....|....
gi 1751927289 740 NPRCNaghVNTLTS 753
Cdd:cd02782 96 RPGVN---VNDLTD 106
|
|
| PRK13532 |
PRK13532 |
nitrate reductase catalytic subunit NapA; |
76-347 |
1.73e-06 |
|
nitrate reductase catalytic subunit NapA;
Pssm-ID: 237416 [Multi-domain] Cd Length: 830 Bit Score: 51.82 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 76 YSDSRVKYPCVRKSfleNKKNHKElrGreEFVRVSWDVALDLAAKKLKEIPKENIYNA----SYGGW----GHAGS-LHR 146
Cdd:PRK13532 93 YGKDRLTQPLLRMK---DGKYDKE--G--EFTPVSWDQAFDVMAEKFKKALKEKGPTAvgmfGSGQWtiweGYAASkLMK 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 147 ChhlawrffnttlggaigtdGEYSNGaaakINP-----M---IVGDMEVYSqqtAHEEM-----IKNCKVYVMWGADLFK 213
Cdd:PRK13532 166 A-------------------GFRSNN----IDPnarhcMasaVVGFMRTFG---IDEPMgcyddIEAADAFVLWGSNMAE 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 214 CNRIDYfvpNHVNDsyypkyKRAGIKFISIDPIYTETAQAFNAEWIPI--RPNTDVALMLGIMHYLYTSNQYDKAFIAKY 291
Cdd:PRK13532 220 MHPILW---SRVTD------RRLSNPDVKVAVLSTFEHRSFELADNGIifTPQTDLAILNYIANYIIQNNAVNWDFVNKH 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 292 T-------------------------------------DGFDKFLpyllgesdkAPKTLEWASQITGVSAEKIKELADLF 334
Cdd:PRK13532 291 TnfrkgatdigyglrpthplekaaknpgtagksepisfEEFKKFV---------APYTLEKTAKMSGVPKEQLEQLAKLY 361
|
330
....*....|...
gi 1751927289 335 VSKRTFLAGNWAM 347
Cdd:PRK13532 362 ADPNRKVVSFWTM 374
|
|
| MopB_CT_Formate-Dh-Na-like |
cd02792 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
645-775 |
2.09e-06 |
|
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate respiration in bacteria such as in the E. coli formate dehydrogenase N (Fdh-N). Fdh-N is a membrane protein that is a complex of three different subunits and is the major electron donor to the nitrate respiratory chain. Also included in this CD is the Desulfovibrio gigas tungsten formate dehydrogenase, DgW-FDH. In contrast to Fdh-N, which is a functional heterotrimer, DgW-FDH is a heterodimer. The DgW-FDH complex is composed of a large subunit carrying the W active site and one [4Fe-4S] center, and a small subunit that harbors a series of three [4Fe-4S] clusters as well as a putative vacant binding site for a fourth cluster. The smaller subunit is not included in this alignment. This CD (MopB_CT_Formate-Dh-Na-like) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239193 [Multi-domain] Cd Length: 122 Bit Score: 47.22 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 645 ETYPFHLISphpkYRVNSQLdNTWV--RNVYKIQGREPVM---INELDANKLGIRHGEIVEVFNARGRLLAGAFVTKNIR 719
Cdd:cd02792 1 EEFPLVLTT----GRLTEHF-HGGNmtRNSPYLAELQPEMfveISPELAAERGIKNGDMVWVSSPRGKIKVKALVTDRVK 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 720 QGVLSI---QKGAWYDPEDGrvrnprcnaghVNTLTSLRP-TSSMTQAisANTALVNIRR 775
Cdd:cd02792 76 PHEVGIpyhWGGMGLVIGDS-----------ANTLTPYVGdPNTQTPE--YKAFLVNIEK 122
|
|
| MopB_CT_Nitrate-R-NapA-like |
cd02791 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
679-723 |
5.21e-06 |
|
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: 46.41 E-value: 5.21e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1751927289 679 EPVM-INELDANKLGIRHGEIVEVFNARGRLLAGAFVTKNIRQGVL 723
Cdd:cd02791 34 EPYVeIHPEDAARLGLKEGDLVRVTSRRGEVVLRVRVTDRVRPGEV 79
|
|
| MopB_CT_Thiosulfate-R-like |
cd02778 |
The MopB_CT_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, ... |
648-775 |
6.43e-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: 43.03 E-value: 6.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 648 PFHLISPHPKYRVNSQLDNTWVRNvyKIQGREPVMINELDANKLGIRHGEIVEVFNARGRLLAGAFVTKNIRQGVLSI-- 725
Cdd:cd02778 1 EFRLIYGKSPVHTHGHTANNPLLH--ELTPENTLWINPETAARLGIKDGDRVEVSSARGKVTGKARLTEGIRPDTVFMph 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1751927289 726 QKGAWYDPEDgrvRNPRCNaGHVNTLT--SLRPTSSmtqAISANTALVNIRR 775
Cdd:cd02778 79 GFGHWAPALS---RAYGGG-VNDNNLLpgSTEPVSG---GAGLQEFTVTVRK 123
|
|
| PRK09939 |
PRK09939 |
acid resistance putative oxidoreductase YdeP; |
235-407 |
1.40e-04 |
|
acid resistance putative oxidoreductase YdeP;
Pssm-ID: 182156 [Multi-domain] Cd Length: 759 Bit Score: 45.42 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 235 RAGIKFISIDPIYTETAQAFNAEWIP-----------------IRPNTDVALMLGIMHYLYTSNQ----------YDKAF 287
Cdd:PRK09939 235 KRGAKMIAINPLQERGLERFTAPQNPfemltnsetqlasayynVRIGGDMALLKGMMRLLIERDDaasaagrpslLDDEF 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 288 IAKYTDGFDKFLPYLLGEsdkapktlEWA--SQITGVSAEKIKELADLFVS-KRTFLAGNWAMQRAQYGEQPDWALIVLA 364
Cdd:PRK09939 315 IQTHTVGFDELRRDVLNS--------EWKdiERISGLSQTQIAELADAYAAaERTIICYGMGITQHEHGTQNVQQLVNLL 386
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1751927289 365 SMIGQVGlsgggfgfsmhyggnaqaSSGARIVPMisQGHNSVK 407
Cdd:PRK09939 387 LMKGNIG------------------KPGAGICPL--RGHSNVQ 409
|
|
| PRK14991 |
PRK14991 |
tetrathionate reductase subunit TtrA; |
245-289 |
1.72e-04 |
|
tetrathionate reductase subunit TtrA;
Pssm-ID: 237883 [Multi-domain] Cd Length: 1031 Bit Score: 45.37 E-value: 1.72e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1751927289 245 PIYTETAQAFNAEWIPIRPNTDVALMLGIMHYLYTSNQYDKAFIA 289
Cdd:PRK14991 329 PLSSSLAAGDNNRWLPIRPGTDSALAMGMIRWIIDNQRYNADYLA 373
|
|
| NarG |
COG5013 |
Nitrate reductase alpha subunit [Energy production and conversion, Inorganic ion transport and ... |
75-119 |
3.89e-04 |
|
Nitrate reductase alpha subunit [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 444037 [Multi-domain] Cd Length: 1231 Bit Score: 44.04 E-value: 3.89e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1751927289 75 VYSDSRVKYPCVRKSFL----ENKKNH--------------------KELRGREEFVRVSWDVALDLAA 119
Cdd:COG5013 106 TYSPTRVKYPYVRGVLLelwrEARARHgdpveawasivedpekrrryKSARGKGGFVRATWDEANEIIA 174
|
|
| MopB_CT_Arsenite-Ox |
cd02779 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of Arsenite oxidase ... |
657-730 |
6.72e-04 |
|
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of Arsenite oxidase (Arsenite-Ox) and related proteins. Arsenite oxidase oxidizes arsenite to the less toxic arsenate; it transfers the electrons obtained from the oxidation of arsenite towards the soluble periplasmic electron carriers cytochrome c and/or amicyanin.
Pssm-ID: 239180 [Multi-domain] Cd Length: 115 Bit Score: 40.13 E-value: 6.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 657 KYRVNSQLDNT-WV-----RNVYKIQGREP---VMINELDANKLGIRHGEIVEVFNARGRLLAGAFVTKNIRQGVLSIQK 727
Cdd:cd02779 2 KYWVNNGRANIiWQtayhdQNNSEIAERVPlpyIEVNPEDAKREGLKNGDLVEVYNDYGSTTAMAYVTNTVKPGQTFMLM 81
|
...
gi 1751927289 728 GAW 730
Cdd:cd02779 82 AHP 84
|
|
| MopB_CT_ydeP |
cd02787 |
The MopB_CT_ydeP CD includes a group of related uncharacterized bacterial ... |
670-734 |
2.25e-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: 2.25e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 670 RNVYKiqGREPVMINELDANKLGIRHGEIVEVFNARG-----RLLAGAFVTKNIRQGVLsiqkGAWYdPE 734
Cdd:cd02787 24 RGVFG--RRDVVFMNPDDIARLGLKAGDRVDLESAFGdgqgrIVRGFRVVEYDIPRGCL----AAYY-PE 86
|
|
| 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 ... |
422-537 |
7.61e-03 |
|
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: 39.68 E-value: 7.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751927289 422 PDKEIDFMGKKLKLPKIKMIYNCGADLLGHeADTNELIRALRTLDCVIVHEPWWTPTAKFADIVFASTSTMERDD--ITF 499
Cdd:cd02771 323 PGLDLDGALAALEDGSADALIVLGNDLYRS-APERRVEAALDAAEFVVVLDHFLTETAERADVVLPAASFAEKSGtfVNY 401
|
90 100 110
....*....|....*....|....*....|....*....
gi 1751927289 500 GGSYSK-NVVYAmrkvvEPVYESKDDYEIFRQLALRIGG 537
Cdd:cd02771 402 EGRAQRfFKAYD-----DPAGDARSDWRWLHALAAKLGG 435
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