|
Name |
Accession |
Description |
Interval |
E-value |
| bisC_fam |
TIGR00509 |
molybdopterin guanine dinucleotide-containing S/N-oxide reductases; This enzyme family shares ... |
13-775 |
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: 1116.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 13 AAHWGPMLVETDGETVFSSRGALATGMENSLQSAVRDQVHSNTRVRFPMVRKGFLASPE-NPQGIRGQDEFVRVSWDEAL 91
Cdd:TIGR00509 1 ASHWGVFTATVQDGRIVAVTPFESDPNPTPMLEGVPDQVYSESRIKYPMVRKGFLENGVkSDRSGRGREEFVRVSWDEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 92 DLIHQQHKRIREAYGPASIFAGSYGWRSNGVLHKASTLLQRYMALAGGYTGHLGDYSTGAAQAIMPYVVGGSEVYQQQTS 171
Cdd:TIGR00509 81 DLVAEELKRVRKTHGPSAIFAGSYGWKSAGRLHNASTLLQRMLNLLGGYVGHAGDYSTGAAQVIMPHVVGDMEVYEQQTT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 172 WPLVLEHSDVVVLWSANPLNTLKIAWNASDEQGLSYFSALRDSGKKLICIDPMRSETVDFFGdkMEWVAPHMGTDVALML 251
Cdd:TIGR00509 161 WPVILENSEVLVLWGADPLKTSQIAWGIPDHGGYEYLERLKAKGKRVISIDPVRTETVEFFG--AEWIPPNPQTDVALML 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 252 GIAHTLVENGWHDEAFLARCTTGYAVFASYLLGESDGIAKTAEWAAEICGVGAAKIRELAAIFHQNTTMLMAGWGMQRQQ 331
Cdd:TIGR00509 239 GLAHTLVTEGLYDKDFLAKYTSGFEKFLPYLLGETDGTPKTAEWASKITGVPAETIKELARLFASKRTMLAAGWSMQRMQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 332 FGEQKHWMIVTLAAMLGQIGTPGGGFGLSYHFSNGGNPTRRSAVLSSMQGSLPGGCDAVDK------IPVARIVEALENP 405
Cdd:TIGR00509 319 HGEQPHWMLVTLAAMLGQIGLPGGGFGFSYHYSGGGTPSASGPALSQGSNSVSSTAGPEWDdgsasvIPVARISDALLNP 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 406 GGAYQHNGMNRHFPDIRFIWWAGGANFTHHQDTNRLIRAWQKPELVVISECFWTAAAKHADIVLPATTSFERNDLTMTGD 485
Cdd:TIGR00509 399 GKEIDYNGKELKLPDIKMVYWAGGNPFHHHQDTNRLIKAWRKLETIIVHEPQWTPTAKHADIVLPATTSFERNDLTMAGD 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 486 YSNQHLVPMKQVVPPRYEARNDFDVFAELSERWekGGYARFTEGKSELQWLETFYNVARQRGANQQVELPPFAEFWqANQ 565
Cdd:TIGR00509 479 YSNTGILAMKQVVPPQFEARNDYDIFAALAERL--GVEEAFTEGKDEMGWLKHLYEKAAKQAKADGVEMPAFDAFW-AEG 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 566 LIEMPeNPDSERFIRFADFCRDPLAHPLKTASGKIEIFSQRIADYGYPDCPGHPMWLEPDEWQGNAEPEQ--LQVLSAHP 643
Cdd:TIGR00509 556 IVEFP-VPEGADFVRYAAFREDPLLNPLGTPSGLIEIYSKTIAKMGYDDCPGHPTWMEPAEWLGGPRGAKypLHLISPHP 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 644 AHRLHSQLNYSSLRELYAVANREPVTIHPDDAQERGIQDGDTVRLWNARGQILAGAVISEGIKPGVICIHEGAWPDLD-- 721
Cdd:TIGR00509 635 KYRLHSQLDHTELRQAYKVQGREPVMIHPDDAAARGIADGDIVRVFNARGQILAGAVVTDGIRKGVVQIHEGAWYDPAdv 714
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 2203217743 722 LTADGICKNGAVNVLTKDLPSSRLGNGCAGNTALAWLEKYNGPELTLTAFEPPA 775
Cdd:TIGR00509 715 REPGGLCKYGNPNVLTADIGTSSLAQGNSGNTVLVEIEKYTGPAPPLTAFDQPA 768
|
|
| MopB_DMSOR-BSOR-TMAOR |
cd02769 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
11-627 |
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: 1011.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 11 LTAAHWGPMLVETDGETVFSSRGALATGMENSLQSAVRDQVHSNTRVRFPMVRKGFLASPEN-PQGIRGQDEFVRVSWDE 89
Cdd:cd02769 1 PTASHWGAFRARVKDGRIVGVRPFEEDPDPSPLLDGVPDAVYSPTRIKYPMVRRGWLEKGPGsDRSLRGKEEFVRVSWDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 90 ALDLIHQQHKRIREAYGPASIFAGSYGWRSNGVLHKASTLLQRYMALAGGYTGHLGDYSTGAAQAIMPYVVGGSEVY-QQ 168
Cdd:cd02769 81 ALDLVAAELKRVRKTYGNEAIFGGSYGWSSAGRFHHAQSLLHRFLNLAGGYVGSVGDYSTGAAQVILPHVVGSMEVYtEQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 169 QTSWPLVLEHSDVVVLWSANPLNTLKIAWN-ASDEQGLSYFSALRDSGKKLICIDPMRSETVDFFGdkMEWVAPHMGTDV 247
Cdd:cd02769 161 QTSWPVIAEHTELVVAFGADPLKNAQIAWGgIPDHQAYSYLKALKDRGIRFISISPLRDDTAAELG--AEWIAIRPGTDV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 248 ALMLGIAHTLVENGWHDEAFLARCTTGYAVFASYLLGESDGIAKTAEWAAEICGVGAAKIRELAAIFHQNTTMLMAGWGM 327
Cdd:cd02769 239 ALMLALAHTLVTEGLHDKAFLARYTVGFDKFLPYLLGESDGVPKTPEWAAAICGIPAETIRELARRFASKRTMIMAGWSL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 328 QRQQFGEQKHWMIVTLAAMLGQIGTPGGGFGLSYHFSNGGNPTRRSAvlsSMQGSLPGGCDAVDKIPVARIVEALENPGG 407
Cdd:cd02769 319 QRAHHGEQPHWMAVTLAAMLGQIGLPGGGFGFGYHYSNGGGPPRGAA---PPPALPQGRNPVSSFIPVARIADMLLNPGK 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 408 AYQHNGMNRHFPDIRFIWWAGGANFTHHQDTNRLIRAWQKPELVVISECFWTAAAKHADIVLPATTSFERNDLTMTGDys 487
Cdd:cd02769 396 PFDYNGKKLTYPDIKLVYWAGGNPFHHHQDLNRLIRAWQKPETVIVHEPFWTATARHADIVLPATTSLERNDIGGSGD-- 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 488 NQHLVPMKQVVPPRYEARNDFDVFAELSERWEKGGYarFTEGKSELQWLETFYNVARQRGANQQVELPPFAEFWQANQLI 567
Cdd:cd02769 474 NRYIVAMKQVVEPVGEARDDYDIFADLAERLGVEEQ--FTEGRDEMEWLRHLYEESRAQAAARGVEMPSFDEFWAQGYVE 551
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 568 EMPENPDserFIRFADFCRDPLAHPLKTASGKIEIFSQRIADYGYPDCPGHPMWLEPDEW 627
Cdd:cd02769 552 LPIPEAD---FVRLADFREDPEANPLGTPSGRIEIFSETIAGFGYDDCPGHPTWLEPAEW 608
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
11-628 |
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: 932.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 11 LTAAHWGPMLVETDGETVFSSRGALATGME-NSLQSAVRDQVHSNTRVRFPMVRKGFLASPENPQGIRGQDEFVRVSWDE 89
Cdd:cd02751 1 PTACHWGPFKAHVKDGVIVRVEPDDTDQPRpCPRGRSVRDRVYSPDRIKYPMKRVGWLGNGPGSRELRGEGEFVRISWDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 90 ALDLIHQQHKRIREAYGPASIFAGSYGWRSNGVLHKASTLLQRYMALAGGYTGHLGDYSTGAAQAIMPYVVGGSEVYQQQ 169
Cdd:cd02751 81 ALDLVASELKRIREKYGNEAIFGGSYGWASAGRLHHAQSLLHRFLNLIGGYLGSYGTYSTGAAQVILPHVVGSDEVYEQG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 170 TSWPLVLEHSDVVVLWSANPLNTLKIAWNASDEQGLSYFSALRDSGKKLICIDPMRSETVDFFGDkmEWVAPHMGTDVAL 249
Cdd:cd02751 161 TSWDDIAEHSDLVVLFGANPLKTRQGGGGGPDHGSYYYLKQAKDAGVRFICIDPRYTDTAAVLAA--EWIPIRPGTDVAL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 250 MLGIAHTLVENGWHDEAFLARCTTGYAVFASYLLGESDGIAKTAEWAAEICGVGAAKIRELAAIFHQNTTMLMAGWGMQR 329
Cdd:cd02751 239 MLAMAHTLITEDLHDQAFLARYTVGFDEFKDYLLGESDGVPKTPEWAAEITGVPAETIRALAREIASKRTMIAQGWGLQR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 330 QQFGEQKHWMIVTLAAMLGQIGTPGGGFGLSYHFSNGGNPTRRSAvlsSMQGSLPGGCDAVDKIPVARIVEALENPGGAY 409
Cdd:cd02751 319 AHHGEQPAWMLVTLAAMLGQIGLPGGGFGFGYGYSNGGGPPRGGA---GGPGLPQGKNPVKDSIPVARIADALLNPGKEF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 410 QHNGMNRHFPDIRFIWWAGGANFTHHQDTNRLIRAWQKPELVVISECFWTAAAKHADIVLPATTSFERNDLTMTGDYSNQ 489
Cdd:cd02751 396 TANGKLKTYPDIKMIYWAGGNPLHHHQDLNRLIKALRKDETIVVHDIFWTASARYADIVLPATTSLERNDIGLTGNYSNR 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 490 HLVPMKQVVPPRYEARNDFDVFAELSERWekGGYARFTEGKSELQWLETFYNVARQRGANQQVELPPFAEFWQANQL-IE 568
Cdd:cd02751 476 YLIAMKQAVEPLGEARSDYEIFAELAKRL--GVEEEFTEGRDEMEWLEHLYEETRAKAAGPGPELPSFEEFWEKGIVrVP 553
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 569 MPENPdserFIRFADFCRDPLAHPLKTASGKIEIFSQRIADYGYPDCPGHPMWLEPDEWQ 628
Cdd:cd02751 554 AAPKP----FVAFADFREDPEANPLGTPSGKIEIYSETLADFGYDDCPGHPTWIEPWEGL 609
|
|
| PRK15102 |
PRK15102 |
trimethylamine-N-oxide reductase TorA; |
46-774 |
0e+00 |
|
trimethylamine-N-oxide reductase TorA;
Pssm-ID: 237909 [Multi-domain] Cd Length: 825 Bit Score: 814.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 46 AVRDQVHSNTRVRFPMVRKGFLASPENPQGI-RGQDEFVRVSWDEALDLIHQQHKRIREAYGPASIFAGSYGWRSNGVLH 124
Cdd:PRK15102 80 GIKGHVYNPSRIRYPMVRLDWLRKRHKSDTSqRGDNRFVRVSWDEALDLFYEELERVQKTYGPSALHTGQTGWQSTGQFH 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 125 KASTLLQRYMALAGGYTGHLGDYSTGAAQAIMPYVVGGSEVYQQQTSWPLVLEHSDVVVLWSANPLNTLKIAWNASDEQG 204
Cdd:PRK15102 160 SATGHMQRAIGMHGNSVGTVGDYSTGAGQVILPYVLGSTEVYEQGTSWPLILENSKTIVLWGSDPVKNLQVGWNCETHES 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 205 LSYFSALRDSGKK----LICIDPMRSETVDFFGDKMEWVAPHmgTDVALMLGIAHTLVENGWHDEAFLARCTTGYAVFAS 280
Cdd:PRK15102 240 YAYLAQLKEKVAKgeinVISIDPVVTKTQNYLGCEHLYVNPQ--TDVPLMLALAHTLYSENLYDKKFIDNYCLGFEQFLP 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 281 YLLGESDGIAKTAEWAAEICGVGAAKIRELAAIFHQNTTMLMAGWGMQRQQFGEQKHWMIVTLAAMLGQIGTPGGGFGLS 360
Cdd:PRK15102 318 YLLGEKDGVPKTPEWAEKICGIDAETIRELARQMAKGRTQIIAGWCIQRQQHGEQPYWMGAVLAAMLGQIGLPGGGISYG 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 361 YHFSNGGNPTRRSAVLSSMQGSLPGGCDAV----------DKIPVARIVEALENPGGAYQHNGMNRHFPDIRFIWWAGGA 430
Cdd:PRK15102 398 HHYSGIGVPSSGGAIPGGFPGNLDTGQKPKhdnsdykgysSTIPVARFIDAILEPGKTINWNGKKVTLPPLKMMIFSGTN 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 431 NFTHHQDTNRLIRAWQKPELVVISECFWTAAAKHADIVLPATTSFERNDLTMTGDYSNQHLVPMKQVVPPRYEARNDFDV 510
Cdd:PRK15102 478 PWHRHQDRNRMKEAFRKLETVVAIDNQWTATCRFADIVLPACTQFERNDIDQYGSYSNRGIIAMKKVVEPLFESRSDFDI 557
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 511 FAELSERWekGGYARFTEGKSELQWLETFYNVARQRGANqQVELPPFAEFWQANQLiempENPDSERFIRFADFCRDPLA 590
Cdd:PRK15102 558 FRELCRRF--GREKEYTRGMDEMGWLKRLYQECKQQNKG-KFHMPEFDEFWKKGYV----EFGEGQPWVRHADFREDPEL 630
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 591 HPLKTASGKIEIFSQRIADYGYPDCPGHPMWLEPDEW-----QGNAEPEQLQvlSAHPAHRLHSQLNYS-SLRELYAVAN 664
Cdd:PRK15102 631 NPLGTPSGLIEIYSRKIADMGYDDCQGHPMWFEKIERshggpGSDKYPLWLQ--SVHPDKRLHSQLCESeELRETYTVQG 708
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 665 REPVTIHPDDAQERGIQDGDTVRLWNARGQILAGAVISEGIKPGVICIHEGAW--PDLDLTADGICKNGAVNVLTKDLPS 742
Cdd:PRK15102 709 REPVYINPQDAKARGIKDGDVVRVFNDRGQVLAGAVVSDRYPPGVIRIHEGAWygPDKGGEIGALCTYGDPNTLTLDIGT 788
|
730 740 750
....*....|....*....|....*....|..
gi 2203217743 743 SRLGNGCAGNTALAWLEKYNGPELTLTAFEPP 774
Cdd:PRK15102 789 SQLAQATSAHTCLVEIEKYQGKVPPVTSFNGP 820
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
45-760 |
0e+00 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 584.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 45 SAVRDQVHSNTRVRFPMVRKGflaspenpqgIRGQDEFVRVSWDEALDLIHQQHKRIREAYGPASIFAGSYGWRSNGVLH 124
Cdd:COG0243 67 AALDERLYSPDRLTYPMKRVG----------PRGSGKFERISWDEALDLIAEKLKAIIDEYGPEAVAFYTSGGSAGRLSN 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 125 KASTLLQRYMALAG--GYTGHlGDYSTGAAQAIMPYVVGGSEVyqqQTSWPlVLEHSDVVVLWSANPLNTLKIAWNAsde 202
Cdd:COG0243 137 EAAYLAQRFARALGtnNLDDN-SRLCHESAVAGLPRTFGSDKG---TVSYE-DLEHADLIVLWGSNPAENHPRLLRR--- 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 203 qglsYFSALRDSGKKLICIDPMRSETVDFFGdkmEWVAPHMGTDVALMLGIAHTLVENGWHDEAFLARCTTGYAVFASYL 282
Cdd:COG0243 209 ----LREAAKKRGAKIVVIDPRRTETAAIAD---EWLPIRPGTDAALLLALAHVLIEEGLYDRDFLARHTVGFDELAAYV 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 283 lgesdgIAKTAEWAAEICGVGAAKIRELAAIFHQNT-TMLMAGWGMQRQQFGEQKHWMIVTLAAMLGQIGTPGGGFGLSY 361
Cdd:COG0243 282 ------AAYTPEWAAEITGVPAEDIRELAREFATAKpAVILWGMGLQQHSNGTQTVRAIANLALLTGNIGKPGGGPFSLT 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 362 HfsnggnptrrsavlssmqgslpggcdavdkipvarivEALENpGGAYQhngmnrhfpdIRFIWWAGGANFTHHQDTNRL 441
Cdd:COG0243 356 G-------------------------------------EAILD-GKPYP----------IKALWVYGGNPAVSAPDTNRV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 442 IRAWQKPELVVISECFWTAAAKHADIVLPATTSFERNDLTMTgdYSNQHLVPMKQVVPPRYEARNDFDVFAELSERWekG 521
Cdd:COG0243 388 REALRKLDFVVVIDTFLTETARYADIVLPATTWLERDDIVTN--SEDRRVHLSRPAVEPPGEARSDWEIFAELAKRL--G 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 522 GYARFTEGKSELQWLETFYNVARQRGAnqqvelpPFAEFWqANQLIEMPENPDserfirfADFCRDplaHPLKTASGKIE 601
Cdd:COG0243 464 FEEAFPWGRTEEDYLRELLEATRGRGI-------TFEELR-EKGPVQLPVPPE-------PAFRND---GPFPTPSGKAE 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 602 IFSQRIAdygypdCPGHPMWLEPDEWQGNAEPE-QLQVLSAHPAHRLHSQlnYSSLRELYAVANREPVTIHPDDAQERGI 680
Cdd:COG0243 526 FYSETLA------LPPLPRYAPPYEGAEPLDAEyPLRLITGRSRDQWHST--TYNNPRLREIGPRPVVEINPEDAAALGI 597
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 681 QDGDTVRLWNARGQILAGAVISEGIKPGVICIHEGAWPDLDLtadgiCKNGAVNVLTKDlPSSRLGNGCAGNTALAWLEK 760
Cdd:COG0243 598 KDGDLVRVESDRGEVLARAKVTEGIRPGVVFAPHGWWYEPAD-----DKGGNVNVLTPD-ATDPLSGTPAFKSVPVRVEK 671
|
|
| MopB_DmsA-EC |
cd02770 |
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
46-609 |
7.36e-135 |
|
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: 412.87 E-value: 7.36e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 46 AVRDQVHSNTRVRFPMVRKGFlaspenpqgiRGQDEFVRVSWDEALDLIHQQHKRIREAYGPASIFAGsYGWRSNGVLHK 125
Cdd:cd02770 49 SQRKRVYNPDRLKYPMKRVGK----------RGEGKFVRISWDEALDTIASELKRIIEKYGNEAIYVN-YGTGTYGGVPA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 126 ASTLLQRYMALAGGYTGHLGDYSTGAAQAIMPYVVGGSEvyqqQTSWPLVLEHSDVVVLWSANPLNTLKIAWNasdeQGL 205
Cdd:cd02770 118 GRGAIARLLNLTGGYLNYYGTYSWAQITTATPYTYGAAA----SGSSLDDLKDSKLVVLFGHNPAETRMGGGG----STY 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 206 SYFSALRdSGKKLICIDPMRSETVDFFGDkmEWVAPHMGTDVALMLGIAHTLVENGWHDEAFLARCTTGY---------- 275
Cdd:cd02770 190 YYLQAKK-AGAKFIVIDPRYTDTAVTLAD--EWIPIRPGTDAALVAAMAYVMITENLHDQAFLDRYCVGFdaehlpegap 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 276 --AVFASYLLGE-SDGIAKTAEWAAEICGVGAAKIRELAA-IFHQNTTMLMAGWGMQRQQFGEQKHWMIVTLAAMLGQIG 351
Cdd:cd02770 267 pnESYKDYVLGTgYDGTPKTPEWASEITGVPAETIRRLAReIATTKPAAILQGWGPQRHANGEQAARAIMMLAAMTGNVG 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 352 TPGGGFGLSyhfsnGGNPTRRSAVLSSMQGSLPggcdavDKIPVARIVEALENPG----GAYQHNGMNRHFPDIRFIW-W 426
Cdd:cd02770 347 IPGGNTGAR-----PGGSAYNGAGLPAGKNPVK------TSIPCFMWTDAIERGEemtaDDGGVKGADKLKSNIKMIWnY 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 427 AGGANFTHHQDTNRLIRAWQ----KPELVVISECFWTAAAKHADIVLPATTSFERNDLTMTGDYSNQH-LVPMKQVVPPR 501
Cdd:cd02770 416 AGNTLINQHSDDNNTTRALLddesKCEFIVVIDNFMTPSARYADILLPDTTELEREDIVLTSNAGMMEyLIYSQKAIEPL 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 502 YEARNDFDVFAELSERWekGGYARFTEGKSELQWLETFYNVARQRGAnqqvELPPFAEFwqanQLIEMPENPDSERFIRF 581
Cdd:cd02770 496 YECKSDYEICAELAKRL--GVEDQFTEGKTEQEWLEELYGQTRAKEP----GLPTYEEF----REKGIYRVPRALPFVAF 565
|
570 580
....*....|....*....|....*...
gi 2203217743 582 ADFCRDPLAHPLKTASGKIEIFSQRIAD 609
Cdd:cd02770 566 EDFREDPENNPLKTPSGKIEIYSKALAD 593
|
|
| PRK14990 |
PRK14990 |
anaerobic dimethyl sulfoxide reductase subunit A; Provisional |
46-760 |
1.38e-100 |
|
anaerobic dimethyl sulfoxide reductase subunit A; Provisional
Pssm-ID: 184952 [Multi-domain] Cd Length: 814 Bit Score: 328.91 E-value: 1.38e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 46 AVRDQVHSNTRVRFPMVRkgflaspenpQGIRGQDEFVRVSWDEALDLIHQQHKRIREAYGPASIFAgSYGWRS-NGVLH 124
Cdd:PRK14990 109 SMRRRVYNPDRLKYPMKR----------VGARGEGKFERISWEEAYDIIATNMQRLIKEYGNESIYL-NYGTGTlGGTMT 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 125 KA----STLLQRYMALAGGYTGHLGDYSTGAAQAIMPYVVGGsevYQQQTSwPLVLEHSDVVVLWSANPLNTlkiawnAS 200
Cdd:PRK14990 178 RSwppgNTLVARLMNCCGGYLNHYGDYSSAQIAEGLNYTYGG---WADGNS-PSDIENSKLVVLFGNNPGET------RM 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 201 DEQGLSYF--SALRDSGKKLICIDPMRSETVDffGDKMEWVAPHMGTDVALMLGIAHTLVENGWHDEAFLARCTTGY--- 275
Cdd:PRK14990 248 SGGGVTYYleQARQKSNARMIIIDPRYTDTGA--GREDEWIPIRPGTDAALVNGLAYVMITENLVDQPFLDKYCVGYdek 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 276 ---------AVFASYLLGE-SDGIAKTAEWAAEICGVGAAKIRELA-AIFHQNTTMLMAGWGMQRQQFGEQKHWMIVTLA 344
Cdd:PRK14990 326 tlpasapknGHYKAYILGEgPDGVAKTPEWASQITGVPADKIIKLArEIGSTKPAFISQGWGPQRHANGEIATRAISMLA 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 345 AMLGQIGTPGGGFGL---SYHFSNGGNPTRRSAVLSSMqgSLPGGCDAVDKIPVariVEALENpgGAyqhNGMNRHFPDI 421
Cdd:PRK14990 406 ILTGNVGINGGNSGAregSYSLPFVRMPTLENPIQTSI--SMFMWTDAIERGPE---MTALRD--GV---RGKDKLDVPI 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 422 RFIW-WAGGANFTHHQDTNR---LIRAWQKPELVVISECFWTAAAKHADIVLPATTSFERNDLTMTGDYSN-QHLVPMKQ 496
Cdd:PRK14990 476 KMIWnYAGNCLINQHSEINRtheILQDDKKCELIVVIDCHMTSSAKYADILLPDCTASEQMDFALDASCGNmSYVIFNDQ 555
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 497 VVPPRYEARNDFDVFAELSERWekGGYARFTEGKSELQWLETFYNVARQrganQQVELPPFAEFWQanQLIEMPENPDSE 576
Cdd:PRK14990 556 VIKPRFECKTIYEMTSELAKRL--GVEQQFTEGRTQEEWMRHLYAQSRE----AIPELPTFEEFRK--QGIFKKRDPQGH 627
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 577 RfIRFADFCRDPLAHPLKTASGKIEIFSQRIAD----YGYPD----------CPGHPMWLEPDEWQgnaepEQLQVLSAH 642
Cdd:PRK14990 628 H-VAYKAFREDPQANPLTTPSGKIEIYSQALADiaatWELPEgdvidplpiyTPGFESYQDPLNKQ-----YPLQLTGFH 701
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 643 PAHRLHSqlNYSSLRELYAvANREPVTIHPDDAQERGIQDGDTVRLWNARGQILAGAVISEGIKPGVICIHEGAWPDLDl 722
Cdd:PRK14990 702 YKSRVHS--TYGNVDVLKA-ACRQEMWINPLDAQKRGINNGDKVRIFNDRGEVHIEAKVTPRMMPGVVALGEGAWYDPD- 777
|
730 740 750
....*....|....*....|....*....|....*...
gi 2203217743 723 tADGICKNGAVNVLTKDLPSSrLGNGCAGNTALAWLEK 760
Cdd:PRK14990 778 -AKRVDKGGCINVLTTQRPSP-LAKGNPSHTNLVQVEK 813
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
56-517 |
1.33e-98 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 309.72 E-value: 1.33e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 56 RVRFPMVRkgflaspenpqgiRGQDEFVRVSWDEALDLIHQQHKRIREAYGPASIF--AGSYGWRSNGVLHKASTLLQRY 133
Cdd:pfam00384 1 RLKYPMVR-------------RGDGKFVRVSWDEALDLIAKKLKRIIKKYGPDAIAinGGSGGLTDVESLYALKKLLNRL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 134 MALAGGYTGHLGDYSTGAAQAimpyvVGGSEVYQQQ-TSWPLVLEHSDVVVLWSANPLNTLKIAWNAsdeqglSYFSALR 212
Cdd:pfam00384 68 GSKNGNTEDHNGDLCTAAAAA-----FGSDLRSNYLfNSSIADIENADLILLIGTNPREEAPILNAR------IRKAALK 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 213 DsGKKLICIDPMRSETVDffgdkMEWVAPHMGTDVALMLGIAHTLVENGWHDEAFLARcttgyavfasyllgesdgiakt 292
Cdd:pfam00384 137 G-KAKVIVIGPRLDLTYA-----DEHLGIKPGTDLALALAGAHVFIKELKKDKDFAPK---------------------- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 293 aewaaeicgvgaakirelAAIFhqnttmlmAGWGMQRQQFGEQKHWMIVTLAAMLGQIGTPGGGFGLSYHFSNGGNPTRR 372
Cdd:pfam00384 189 ------------------PIII--------VGAGVLQRQDGEAIFRAIANLADLTGNIGRPGGGWNGLNILQGAASPVGA 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 373 SAVlssmqGSLPGGcdavdkipvaRIVEALENPggayqhngmnrHFPDIRFIWWAGGANFTHHQDTNRLIRAWQKPELVV 452
Cdd:pfam00384 243 LDL-----GLVPGI----------KSVEMINAI-----------KKGGIKVLYLLGNNPFVTHADENRVVKALQKLDLFV 296
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2203217743 453 ISECFW-TAAAKHADIVLPATTSFERNDLTMTGDYSNQHlvpMKQVVPPRYEARNDFDVFAELSER 517
Cdd:pfam00384 297 VYDGHHgDKTAKYADVILPAAAYTEKNGTYVNTEGRVQS---TKQAVPPPGEAREDWKILRALSEV 359
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
46-517 |
1.92e-83 |
|
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: 270.35 E-value: 1.92e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 46 AVRDQVHSNTRVRFPMVRKGflaspenpqgirGQDEFVRVSWDEALDLIHQQHKRIREAYGPASIFAGSYGWRSNGVLHK 125
Cdd:cd00368 44 AGLDGLYSPDRLKYPLIRVG------------GRGKFVPISWDEALDEIAEKLKEIREKYGPDAIAFYGGGGASNEEAYL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 126 ASTLLqryMALAGGYTGHLGDYSTGAAQAIMPYVVGGSevyqQQTSWPlVLEHSDVVVLWSANPLNTLKIAWnasdeqgl 205
Cdd:cd00368 112 LQKLL---RALGSNNVDSHARLCHASAVAALKAFGGGA----PTNTLA-DIENADLILLWGSNPAETHPVLA-------- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 206 SYFSALRDSGKKLICIDPMRSETVDFFgdkMEWVAPHMGTDVALMLgiahtlvengwhdeaflarcttgyavfasyllge 285
Cdd:cd00368 176 ARLRRAKKRGAKLIVIDPRRTETAAKA---DEWLPIRPGTDAALAL---------------------------------- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 286 sdgiaktAEWAAEICGVGAAKIRELAAIFHQN-TTMLMAGWGMQRQQFGEQKHWMIVTLAAMLGQIGTPGGGFGLsyhfs 364
Cdd:cd00368 219 -------AEWAAEITGVPAETIRALAREFAAAkRAVILWGMGLTQHTNGTQNVRAIANLAALTGNIGRPGGGLGP----- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 365 nGGNPtrrsavlssmqgslpggcdavdkipvarivealenpggayqhngmnrhfpdirfiwwagganFTHHQDTNRLIRA 444
Cdd:cd00368 287 -GGNP--------------------------------------------------------------LVSAPDANRVRAA 303
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2203217743 445 WQKPELVVISECFWTAAAKHADIVLPATTSFERNDLTMTGDYsnqHLVPMKQVVPPRYEARNDFDVFAELSER 517
Cdd:cd00368 304 LKKLDFVVVIDIFMTETAAYADVVLPAATYLEKEGTYTNTEG---RVQLFRQAVEPPGEARSDWEILRELAKR 373
|
|
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
51-616 |
3.23e-71 |
|
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: 241.77 E-value: 3.23e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 51 VHSNTRVRFPMVRKGflaspenpqgiRGQDEFVRVSWDEALDLIHQQHKRIREAYGPASI----FAGSYGWRSNGVLHka 126
Cdd:cd02766 50 VYSPDRLLTPLKRVG-----------RKGGQWERISWDEALDTIAAKLKEIKAEYGPESIlpysYAGTMGLLQRAARG-- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 127 stllqrYMALAGGYTGHLGDYSTGAAQAIMPYVVGgsevyqqqTSW---PLVLEHSDVVVLWSANPlntlkiAWNASdeQ 203
Cdd:cd02766 117 ------RFFHALGASELRGTICSGAGIEAQKYDFG--------ASLgndPEDMVNADLIVIWGINP------AATNI--H 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 204 GLSYFSALRDSGKKLICIDPMRSETVDFfGDKMEWVAPhmGTDVALMLGIAHTLVENGWHDEAFLARCTTGYAVFASYLL 283
Cdd:cd02766 175 LMRIIQEARKRGAKVVVIDPYRTATAAR-ADLHIQIRP--GTDGALALGVAKVLFREGLYDRDFLARHTEGFEELKAHLE 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 284 gesdgiAKTAEWAAEICGVGAAKIRELAAIF-HQNTTMLMAGWGMQRQQFGEQK-HWmIVTLAAMLGQIGTPGGGFglsy 361
Cdd:cd02766 252 ------TYTPEWAAEITGVSAEEIEELARLYgEAKPPSIRLGYGMQRYRNGGQNvRA-IDALPALTGNIGVPGGGA---- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 362 HFSNGGnptrrsavlssmqgslpggcdavdkipvarivealenpggayqhngmnrhfPDIRFIWWAGGANFTHHQDTNRL 441
Cdd:cd02766 321 FYSNSG---------------------------------------------------PPVKALWVYNSNPVAQAPDSNKV 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 442 IRAWQKP-ELVVISECFWTAAAKHADIVLPATTSFERNDLtmTGDYSNQHLVPMKQVVPPRYEARNDFDVFAELSERWEK 520
Cdd:cd02766 350 RKGLAREdLFVVVHDQFMTDTARYADIVLPATTFLEHEDV--YASYWHYYLQYNEPAIPPPGEARSNTEIFRELAKRLGF 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 521 GGYarFTEGkSELQWLEtfynvarqrGANQQVELPPFAEfwqanqliempenpDSERFIRFADFCRDPLAHP---LKTAS 597
Cdd:cd02766 428 GEP--PFEE-SDEEWLD---------QALDGTGLPLEGI--------------DLERLLGPRKAGFPLVAWEdrgFPTPS 481
|
570
....*....|....*....
gi 2203217743 598 GKIEIFSQRIADYGYPDCP 616
Cdd:cd02766 482 GKFEFYSERAAKRGLPPLP 500
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
49-739 |
6.00e-69 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 240.17 E-value: 6.00e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 49 DQVHSNTRVRFPMVRKGflaspenpqgirgqDEFVRVSWDEALDLIHQQHKRIREAYGPASIfaGSYGwrSNGVLHKAST 128
Cdd:COG3383 54 EFVNSPDRLTTPLIRRG--------------GEFREVSWDEALDLVAERLREIQAEHGPDAV--AFYG--SGQLTNEENY 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 129 LLQRYMALAGGyTGHLgDYSTGAAQAimPYVVGGSEV---------YQQqtswplvLEHSDVVVLWSANPLNTLKIAWna 199
Cdd:COG3383 116 LLQKLARGVLG-TNNI-DNNARLCMA--SAVAGLKQSfgsdappnsYDD-------IEEADVILVIGSNPAEAHPVLA-- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 200 sdeqglSYFSALRDSGKKLICIDPMRSETVDFFGdkmEWVAPHMGTDVALMLGIAHTLVENGWHDEAFLARCTTGYAVFA 279
Cdd:COG3383 183 ------RRIKKAKKNGAKLIVVDPRRTETARLAD---LHLQIKPGTDLALLNGLLHVIIEEGLVDEDFIAERTEGFEELK 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 280 SYLLGEsdgiakTAEWAAEICGVGAAKIRELAAIFHQ-NTTMLMAGWGMQRQQFGEQKHWMIVTLAAMLGQIGTPGGGfg 358
Cdd:COG3383 254 ASVAKY------TPERVAEITGVPAEDIREAARLIAEaKRAMILWGMGVNQHTQGTDNVNAIINLALATGNIGRPGTG-- 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 359 lsYHFSNGGNPTRRSAVLSSMQGSLPGGCDAVDKIPVARI-----VEAL-ENPG-GAYQ-----HNGmnrhfpDIRFIWW 426
Cdd:COG3383 326 --PFPLTGQNNVQGGRDMGALPNVLPGYRDVTDPEHRAKVadawgVPPLpDKPGlTAVEmfdaiADG------EIKALWI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 427 AgGANFTH-HQDTNRLIRAWQKPELVVISECFWTAAAKHADIVLPATTSFERnDLTMTGdySNQHLVPMKQVVPPRYEAR 505
Cdd:COG3383 398 I-GENPAVsDPDANHVREALEKLEFLVVQDIFLTETAEYADVVLPAASWAEK-DGTFTN--TERRVQRVRKAVEPPGEAR 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 506 NDFDVFAELSERWEKG-GYARFTEGKSELQWL-ETFYNVARQRGANQQVELPPFAEfwqanqliemPENPDSERFirFAD 583
Cdd:COG3383 474 PDWEIIAELARRLGYGfDYDSPEEVFDEIARLtPDYSGISYERLEALGGVQWPCPS----------EDHPGTPRL--FTG 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 584 -FCrdplahplkTASGKIEIFsqriadygypdcpghpmwlePDEWQGNAEPeqlqVLSAHPAH----RLHSQLNYSSL-- 656
Cdd:COG3383 542 rFP---------TPDGKARFV--------------------PVEYRPPAEL----PDEEYPLVlttgRLLDQWHTGTRtr 588
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 657 --RELYAVANREPVTIHPDDAQERGIQDGDTVRLWNARGQILAGAVISEGIKPGVICI--HegaWPDldltadgicknGA 732
Cdd:COG3383 589 rsPRLNKHAPEPFVEIHPEDAARLGIKDGDLVRVSSRRGEVVLRARVTDRVRPGTVFMpfH---WGE-----------GA 654
|
....*..
gi 2203217743 733 VNVLTKD 739
Cdd:COG3383 655 ANALTND 661
|
|
| MopB_CT_DMSOR-BSOR-TMAOR |
cd02793 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
635-760 |
7.38e-62 |
|
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: 203.64 E-value: 7.38e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 635 QLQVLSAHPAHRLHSQLNYSSLRELYAVANREPVTIHPDDAQERGIQDGDTVRLWNARGQILAGAVISEGIKPGVICIHE 714
Cdd:cd02793 2 PLHLLSNQPATRLHSQLDHGSLSRAYKVQGREPIRINPADAAARGIADGDIVRVFNDRGACLAGAVVTDGIMPGVVQLPT 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2203217743 715 GAWPDLDL--TADGICKNGAVNVLTKDLPSSRLGNGCAGNTALAWLEK 760
Cdd:cd02793 82 GAWYDPDDpgEPGPLCKHGNPNVLTLDIGTSSLAQGCSAQTCLVQIEK 129
|
|
| MopB_CT_DMSOR-like |
cd02777 |
The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
636-760 |
1.86e-56 |
|
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: 188.95 E-value: 1.86e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 636 LQVLSAHPAHRLHSQL-NYSSLRELYAVANREPVTIHPDDAQERGIQDGDTVRLWNARGQILAGAVISEGIKPGVICIHE 714
Cdd:cd02777 3 LQLISPHPKRRLHSQLdNVPWLREAYKVKGREPVWINPLDAAARGIKDGDIVRVFNDRGAVLAGARVTDRIMPGVVALPE 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2203217743 715 GAWPDLDLTaDGICKNGAVNVLTKDLPSSRLGNGCAGNTALAWLEK 760
Cdd:cd02777 83 GAWYDPDDN-GGLDKGGNPNVLTSDIPTSKLAQGNPANTCLVEIEK 127
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
46-624 |
3.70e-52 |
|
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: 188.67 E-value: 3.70e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 46 AVRDQVHSNTRVRFPMVRKGflaspenpqgIRGQDEFVRVSWDEALDLIHQQHKRIREAYGPASIfAGSYGWRSNGVLhk 125
Cdd:cd02759 44 AAPEIVYHPDRLLYPLKRVG----------ERGENKWERISWDEALDEIAEKLAEIKAEYGPESI-ATAVGTGRGTMW-- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 126 ASTLLQRYMALAGG-----YTGHLGDYSTGAAQAIMPYVVGGSEVyqqqTSWplvlEHSDVVVLWSANPLNTlkiaWNas 200
Cdd:cd02759 111 QDSLFWIRFVRLFGspnlfLSGESCYWPRDMAHALTTGFGLGYDE----PDW----ENPECIVLWGKNPLNS----NL-- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 201 DEQGlSYFSALRDSGKKLICIDPMRSETVDffgDKMEWVAPHMGTDVALMLGIAHTLVENGWHDEAFLARCTTGYAVFAS 280
Cdd:cd02759 177 DLQG-HWLVAAMKRGAKLIVVDPRLTWLAA---RADLWLPIRPGTDAALALGMLNVIINEGLYDKDFVENWCYGFEELAE 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 281 YLlgesdgIAKTAEWAAEICGVGAAKIRELAAIFHQNTTMLMAgWG--MQRQQFGEQKHWMIVTLAAMLGQIGTPGGGFG 358
Cdd:cd02759 253 RV------QEYTPEKVAEITGVPAEKIRKAARLYATAKPACIQ-WGlaIDQQKNGTQTSRAIAILRAITGNLDVPGGNLL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 359 LSYhfsnggnptrrsavlssmqgslpggcdavdkipvarivealenpggayqhngmnrhfpDIRFIWWAGGANFTHHQDT 438
Cdd:cd02759 326 IPY----------------------------------------------------------PVKMLIVFGTNPLASYADT 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 439 NRLIRAWQKPELVVISECFWTAAAKHADIVLPATTSFERNDLtMTGDYSNQHLVPMKQVVPPRYEARNDFDVFAELSERW 518
Cdd:cd02759 348 APVLEALKALDFIVVVDLFMTPTAMLADIVLPVAMSLERPGL-RGGFEAENFVQLRQKAVEPYGEAKSDYEIVLELGKRL 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 519 ekgGYARFTEGKSElqwletfynvarqRGANQQVELPPFAefwqanqliempenpdserfirfadfcrdplahplkTASG 598
Cdd:cd02759 427 ---GPEEAEYYKYE-------------KGLLRPDGQPGFN------------------------------------TPTG 454
|
570 580
....*....|....*....|....*.
gi 2203217743 599 KIEIFSQRIADYGYPDCPGHPmwlEP 624
Cdd:cd02759 455 KVELYSTMLEELGYDPLPYYR---EP 477
|
|
| Fdh-alpha |
TIGR01591 |
formate dehydrogenase, alpha subunit, archaeal-type; This model describes a subset of formate ... |
49-739 |
1.61e-51 |
|
formate dehydrogenase, alpha subunit, archaeal-type; This model describes a subset of formate dehydrogenase alpha chains found mainly archaea but also in alpha and gamma proteobacteria and a small number of gram positive bacteria. The alpha chain contains domains for molybdopterin dinucleotide binding and molybdopterin oxidoreductase (pfam01568 and pfam00384, respectively). The holo-enzyme also contains beta and gamma subunits. The enzyme catalyzes the oxidation of formate (produced from pyruvate during anaerobic growth) to carbon dioxide with the concomitant release of two electrons and two protons. The enzyme's purpose is to allow growth on formate in some circumstances and, in the case of FdhH in gamma proteobacteria, to pass electrons to hydrogenase (by which process acid is neutralized). This model is well-defined, with only a single fragmentary sequence falling between trusted and noise. The alpha subunit of a version of nitrate reductase is closely related.
Pssm-ID: 130652 [Multi-domain] Cd Length: 671 Bit Score: 191.14 E-value: 1.61e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 49 DQVHSNTRVRFPMVRKGflaspenpqgirgqDEFVRVSWDEALDLIHQQHKRIREAYGPASI--FAGSYGWRSNGVlhka 126
Cdd:TIGR01591 46 EFINSKDRLTTPLIREG--------------DKFREVSWDEAISYIAEKLKEIKEKYGPDSIgfIGSSRGTNEENY---- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 127 stLLQRyMALAGGYTG---HLGDYSTGAAQAIMPYVVGGSEVYQQQTSwplvLEHSDVVVLWSANPLNTLKIAwnasdeq 203
Cdd:TIGR01591 108 --LLQK-LARAVIGTNnvdNCARVCHGPSVAGLKQTVGIGAMSNTISE----IENADLIVIIGYNPAESHPVV------- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 204 gLSYFSALRDSGKKLICIDPMRSETVDfFGDkmEWVAPHMGTDVALMLGIAHTLVENGWHDEAFLARCTTGYAVFASyll 283
Cdd:TIGR01591 174 -AQYLKNAKRNGAKIIVIDPRKTETAK-IAD--LHIPLKPGTDIALLNAMANVIIEEGLYDKAFIEKRTEGFEEFRE--- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 284 gesdGIAK-TAEWAAEICGVGAAKIRELAAIFHQ-NTTMLMAGWGMQRQQFGEQKHWMIVTLAAMLGQIGTPGGG----- 356
Cdd:TIGR01591 247 ----IVKGyTPEYVEDITGVPADLIREAARMYAKaGSAAILWGMGVTQHSQGVETVMALINLAMLTGNIGKPGGGvnplr 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 357 ----------FGLSYHFSNGGNPTRRSAV---LSSMQGSLPGGCDavdkiPVARIVEALEnpggAYQHNgmnrhfpDIRF 423
Cdd:TIGR01591 323 gqnnvqgacdMGALPDFLPGYQPVSDEEVrekFAKAWGVVKLPAE-----PGLRIPEMID----AAADG-------DVKA 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 424 IWWAGGANFTHHQDTNRLIRAWQKPELVVISECFWTAAAKHADIVLPATTSFERNDLTMTGDYSNQHLvpmKQVVPPRYE 503
Cdd:TIGR01591 387 LYIMGEDPLQSDPNTSKVRKALEKLELLVVQDIFMTETAKYADVVLPAAAWLEKEGTFTNAERRIQRF---FKAVEPKGE 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 504 ARNDFDVFAELSER----WEKGGYARFTEGKSELQWLetFYNVARQRganqqVELPPFAEfWQANqliEMPENPDSERFI 579
Cdd:TIGR01591 464 SKPDWEIIQELANAlgldWNYNHPQEIMDEIRELTPL--FAGLTYER-----LDELGSLQ-WPCN---DSDASPTSYLYK 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 580 -RFAdfcrdplahplkTASGKIEIFSQRiadygypdcpghpmWLEPDEWQGNAEPEQLQVLsahpahRLHSQLNYSSL-R 657
Cdd:TIGR01591 533 dKFA------------TPDGKAKFIPLE--------------WVAPIEEPDDEYPLILTTG------RVLTHYNVGEMtR 580
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 658 ELYAVANREP---VTIHPDDAQERGIQDGDTVRLWNARGQILAGAVISEGIKPGVICIHEGAWpdldltadgickNGAVN 734
Cdd:TIGR01591 581 RVAGLRRLSPepyVEINTEDAKKLGIKDGDLVKVKSRRGEITLRAKVSDRVNKGAIYITMHFW------------DGAVN 648
|
....*
gi 2203217743 735 VLTKD 739
Cdd:TIGR01591 649 NLTTD 653
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
56-527 |
6.20e-48 |
|
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: 178.96 E-value: 6.20e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 56 RVRFPMVRkgflaspenpqgiRGQDEFVRVSWDEALDLIHQQHKRIREAYGPASIfagsygwrsnGVLHKASTLLQRYMA 135
Cdd:cd02754 54 RLTRPLLR-------------RNGGELVPVSWDEALDLIAERFKAIQAEYGPDSV----------AFYGSGQLLTEEYYA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 136 LAGGYTGHLG----DYSTG--AAQAIMPYV--VGGSEV---YQQqtswplvLEHSDVVVLWSANPLNTLKIAWnasdeqg 204
Cdd:cd02754 111 ANKLAKGGLGtnniDTNSRlcMASAVAGYKrsFGADGPpgsYDD-------IEHADCFFLIGSNMAECHPILF------- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 205 lSYFSALRDS--GKKLICIDPMRSETVDFfGDKmeWVAPHMGTDVALMLGIAHTLVENGWHDEAFLARCTTGYAVFASYL 282
Cdd:cd02754 177 -RRLLDRKKAnpGAKIIVVDPRRTRTADI-ADL--HLPIRPGTDLALLNGLLHVLIEEGLIDRDFIDAHTEGFEELKAFV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 283 lgesdgiAK-TAEWAAEICGVGAAKIRELAAIFHQNTTmLMAGWGM---QRQQfGEQKHWMIVTLAAMLGQIGTPGGGFg 358
Cdd:cd02754 253 -------ADyTPEKVAEITGVPEADIREAARLFGEARK-VMSLWTMgvnQSTQ-GTAANNAIINLHLATGKIGRPGSGP- 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 359 lsyhFSNGGNPTRRSAVLSSMQGSLPGGCDAVD------------KIPVARIVEAlenPGGAY--QHNGMNRHfpDIRFI 424
Cdd:cd02754 323 ----FSLTGQPNAMGGREVGGLANLLPGHRSVNnpehraevakfwGVPEGTIPPK---PGLHAveMFEAIEDG--EIKAL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 425 WWAGGANFTHHQDTNRLIRAWQKPELVVISECFW-TAAAKHADIVLPATTSFERnDLTMTGdySNQHLVPMKQVVPPRYE 503
Cdd:cd02754 394 WVMCTNPAVSLPNANRVREALERLEFVVVQDAFAdTETAEYADLVLPAASWGEK-EGTMTN--SERRVSLLRAAVEPPGE 470
|
490 500
....*....|....*....|....
gi 2203217743 504 ARNDFDVFAELSERWEKGGYARFT 527
Cdd:cd02754 471 ARPDWWILADVARRLGFGELFPYT 494
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
49-517 |
7.35e-47 |
|
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: 174.71 E-value: 7.35e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 49 DQVHSNTRVRFPMVRKGflaspenpqgirgqDEFVRVSWDEALDLIHQQHKRIREAYGPASI--FAGSYGwrSNgvlhKA 126
Cdd:cd02753 47 DFVNSKDRLTKPLIRKN--------------GKFVEASWDEALSLVASRLKEIKDKYGPDAIafFGSAKC--TN----EE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 127 STLLQRyMALAGGYTGHLgDYSTGAAQAimPYVVGGSEVYQQQTSWPLV--LEHSDVVVLWSANPLNTLKIAwnasdeqG 204
Cdd:cd02753 107 NYLFQK-LARAVGGTNNV-DHCARLCHS--PTVAGLAETLGSGAMTNSIadIEEADVILVIGSNTTEAHPVI-------A 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 205 LSYFSALRdSGKKLICIDPMRSETVDFfGDKmeWVAPHMGTDVALMLGIAHTLVENGWHDEAFLARCTTGYAVFASYLLg 284
Cdd:cd02753 176 RRIKRAKR-NGAKLIVADPRRTELARF-ADL--HLQLRPGTDVALLNAMAHVIIEEGLYDEEFIEERTEGFEELKEIVE- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 285 esdgiAKTAEWAAEICGVGAAKIRELAAIFHQ-NTTMLMAGWGMQRQQFGEQKHWMIVTLAAMLGQIGTPGGgfglsyhf 363
Cdd:cd02753 251 -----KYTPEYAERITGVPAEDIREAARMYATaKSAAILWGMGVTQHSHGTDNVMALSNLALLTGNIGRPGT-------- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 364 snGGNPTRRsavlssmQGSLPGGCDAvdkipvarivealenpgGAYQHngmnrHFPD-IRFIWWAgGANFTH-HQDTNRL 441
Cdd:cd02753 318 --GVNPLRG-------QNNVQGACDM-----------------GALPN-----VLPGyVKALYIM-GENPALsDPNTNHV 365
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2203217743 442 IRAWQKPELVVISECFWTAAAKHADIVLPATTSFERNdltmtGDYSN--QHLVPMKQVVPPRYEARNDFDVFAELSER 517
Cdd:cd02753 366 RKALESLEFLVVQDIFLTETAELADVVLPAASFAEKD-----GTFTNteRRVQRVRKAVEPPGEARPDWEIIQELANR 438
|
|
| MopB_4 |
cd02765 |
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
50-624 |
2.24e-44 |
|
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: 168.81 E-value: 2.24e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 50 QVHSNTRVRFPMVRKGFlaspenpqgiRGQDEFVRVSWDEALDLIHQQHKRIREAYGPASIfagsyGWR-SNGVLHKAST 128
Cdd:cd02765 49 RVYSPDRLKYPMKRVGE----------RGEGKFERITWDEALDTIADKLTEAKREYGGKSI-----LWMsSSGDGAILSY 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 129 LLQRyMALAGGYTGHLGDYSTGAAQAIMPyVVGGSEVYQQQTSWPLVleHSDVVVLWSANPLntlkiawnASDEQGLSYF 208
Cdd:cd02765 114 LRLA-LLGGGLQDALTYGIDTGVGQGFNR-VTGGGFMPPTNEITDWV--NAKTIIIWGSNIL--------ETQFQDAEFF 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 209 SALRDSGKKLICIDPMRSETvdffGDKME-WVAPHMGTDVALMLGIAHTLVENGWHDEAFLARCTT-------------- 273
Cdd:cd02765 182 LDARENGAKIVVIDPVYSTT----AAKADqWVPIRPGTDPALALGMINYILEHNWYDEAFLKSNTSapflvredngtllr 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 274 -----------GYAVF----ASY-----------LLGE--SDG-------------IAK-TAEWAAEICGVGAAKIRELA 311
Cdd:cd02765 258 qadvtatpaedGYVVWdtnsDSPepvaatninpaLEGEytINGvkvhtvltalreqAASyPPKAAAEICGLEEAIIETLA 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 312 AIFHQN-TTMLMAGWGMQRQQFGEQKHWMIVTLAAMLGQIGTPGGGFGlsyhfsnggnptrrsavlssmqgslpggcdav 390
Cdd:cd02765 338 EWYATGkPSGIWGFGGVDRYYHSHVFGRTAAILAALTGNIGRVGGGVG-------------------------------- 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 391 dkipvarivealenpggayqhngmnrhfpDIRFIWWaGGANFTHHQDTNRLIRAWQKP-ELVVISECFWTAAAKHADIVL 469
Cdd:cd02765 386 -----------------------------QIKFMYF-MGSNFLGNQPDRDRWLKVMKNlDFIVVVDIFHTPTVRYADIVL 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 470 PATTSFERNDLTMTgdYSNQ-HLVPMKQVVPPRYEARNDFDVFAELSERWEKGGYarFTEGKSElqWLETFYNVARQRGA 548
Cdd:cd02765 436 PAAHWFEVEDLLVR--YTTHpHVLLQQKAIEPLFESKSDFEIEKGLAERLGLGDY--FPKTPED--YVRAFMNSDDPALD 509
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2203217743 549 NQQVELppfaefWQANQLIeMPENPDSERFIRFADfcrdplaHPLKTASGKIEIFSQRIAdygyPDCPGHPMWLEP 624
Cdd:cd02765 510 GITWEA------LKEEGII-MRLATPEDPYVAYLD-------QKFGTPSGKLEFYNEAAP----ELEEALPLPEEP 567
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
7-516 |
3.32e-43 |
|
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: 164.88 E-value: 3.32e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 7 RYSVLTAAHWGpMLVETDGETVFSSRG----ALATGMENSLQSAVRDQVHSNTRVRFPMVRKGflaspenpqgirgqDEF 82
Cdd:cd02762 2 RACILCEANCG-LVVTVEDGRVASIRGdpddPLSKGYICPKAAALGDYQNDPDRLRTPMRRRG--------------GSF 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 83 VRVSWDEALDLIHQQHKRIREAYGPASIfaGSYGWRSNGVLHKAST---LLQRYMALAGGYTGHLGDYSTGAAQAIMPYV 159
Cdd:cd02762 67 EEIDWDEAFDEIAERLRAIRARHGGDAV--GVYGGNPQAHTHAGGAyspALLKALGTSNYFSAATADQKPGHFWSGLMFG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 160 VGGSEVYQQqtswplvLEHSDVVVLWSANPLNTLKIAWNASDEQGLsyFSALRDSGKKLICIDPMRSETVDFFGdkmEWV 239
Cdd:cd02762 145 HPGLHPVPD-------IDRTDYLLILGANPLQSNGSLRTAPDRVLR--LKAAKDRGGSLVVIDPRRTETAKLAD---EHL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 240 APHMGTDVALMLGIAHTLVENGWHDEAFLARCTTGYAVFASYLLgesdgiAKTAEWAAEICGVGAAKIRELAAIFHQNTT 319
Cdd:cd02762 213 FVRPGTDAWLLAAMLAVLLAEGLTDRRFLAEHCDGLDEVRAALA------EFTPEAYAPRCGVPAETIRRLAREFAAAPS 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 320 MLMAG-WGMQRQQFGEQKHWMIVTLAAMLGQIGTPGGG----FGLSYHFSNGGNPTRRSAVLS--SMQGSLPGgcdavdK 392
Cdd:cd02762 287 AAVYGrLGVQTQLFGTLCSWLVKLLNLLTGNLDRPGGAmfttPALDLVGQTSGRTIGRGEWRSrvSGLPEIAG------E 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 393 IPVARIVEALENPGGAyqhngmnrhfpDIRFIWWAGGANFTHHQDTNRLIRAWQKPELVVISECFWTAAAKHADIVLPAT 472
Cdd:cd02762 361 LPVNVLAEEILTDGPG-----------RIRAMIVVAGNPVLSAPDGARLEAALGGLEFMVSVDVYMTETTRHADYILPPA 429
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 2203217743 473 TSFERNDLTMTGDYSNQHLVPMKQ-VVPPRYEARNDFDVFAELSE 516
Cdd:cd02762 430 SQLEKPHATFFNLEFPRNAFRYRRpLFPPPPGTLPEWEILARLVE 474
|
|
| MopB_Nitrate-R-NarG-like |
cd02750 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
51-517 |
2.45e-42 |
|
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: 160.56 E-value: 2.45e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 51 VHSNTRVRFPMVRKGflaspenpqgIRGQDEFVRVSWDEALDLIHQQHKRIREAYGPASIFaGSYGWRSNGVLHKASTLl 130
Cdd:cd02750 61 LYSPDRVKYPLKRVG----------ARGEGKWKRISWDEALELIADAIIDTIKKYGPDRVI-GFSPIPAMSMVSYAAGS- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 131 qRYMALAGGYTGHL----GDYSTGAAQaimpyvvggseVYQQQTSWPLVLE--HSDVVVLWSANPLNTlkiawNASDEQg 204
Cdd:cd02750 129 -RFASLIGGVSLSFydwyGDLPPGSPQ-----------TWGEQTDVPESADwyNADYIIMWGSNVPVT-----RTPDAH- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 205 lsYFSALRDSGKKLICIDPMRSETVDfFGDkmEWVAPHMGTDVALMLGIAHTLVENGWHDEAFLARCTT-GYAVFasyll 283
Cdd:cd02750 191 --FLTEARYNGAKVVVVSPDYSPSAK-HAD--LWVPIKPGTDAALALAMAHVIIKEKLYDEDYLKEYTDlPFLVY----- 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 284 gesdgiakTAEWAAEICGVGAAKIRELAAIFHQN-TTMLMAGWGMQRQQFGEQKHWMIVTLAAMLGQIGTPGGGfglsyh 362
Cdd:cd02750 261 --------TPAWQEAITGVPRETVIRLAREFATNgRSMIIVGAGINHWYHGDLCYRALILLLALTGNEGKNGGG------ 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 363 fsnggnptrrsavLSSMQGSlpggcdavdkiPVARIVEAlENPGGayQHNGMNRHFPDIrfiwwagganfthhqdtnrli 442
Cdd:cd02750 327 -------------WAHYVGQ-----------PRVLFVWR-GNLFG--SSGKGHEYFEDA--------------------- 358
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2203217743 443 rAWQKPELVVISECFWTAAAKHADIVLPATTSFERNDLTMTGDYSNQHlvPMKQVVPPRYEARNDFDVFAELSER 517
Cdd:cd02750 359 -PEGKLDLIVDLDFRMDSTALYSDIVLPAATWYEKHDLSTTDMHPFIH--PFSPAVDPLWEAKSDWEIFKALAKK 430
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
24-715 |
1.28e-40 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 159.83 E-value: 1.28e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 24 DGETVFSSRGALATGMENSL---QSAVRDQVHSNTRVRFPMVRKGflaspenpqgIRGQDEFVRVSWDEALDLIHQQHKR 100
Cdd:PRK15488 63 NGKNVFIQGNPKAKSFGTKVcarGGSGHSLLYDPQRIVKPLKRVG----------ERGEGKWQEISWDEAYQEIAAKLNA 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 101 IREAYGPASI-FAGSYGWRSNGVLHKAStllqrymalAGGYTGHLGDYSTGAAQaimpYVVGGSEVYQqqTSWPLVLEHS 179
Cdd:PRK15488 133 IKQQHGPESVaFSSKSGSLSSHLFHLAT---------AFGSPNTFTHASTCPAG----YAIAAKVMFG--GKLKRDLANS 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 180 DVVVLWSANplntLKIAWNASDEQGLsyFSALRDSGKKLICIDPMRSetvdFFGDKM-EWVAPHMGTDVALMLGIAHTLV 258
Cdd:PRK15488 198 KYIINFGHN----LYEGINMSDTRGL--MTAQMEKGAKLVVFEPRFS----VVASKAdEWHAIRPGTDLAVVLALCHVLI 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 259 ENGWHDEAFLARCTTGYAVFASYLLgesdgiAKTAEWAAEICGVGAAKIRELAAIFHQNTTMLMAGWGmQRQQFGEQKHW 338
Cdd:PRK15488 268 EENLYDKAFVERYTSGFEELAASVK------EYTPEWAEAISDVPADDIRRIARELAAAAPHAIVDFG-HRATFTPEEFD 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 339 M---IVTLAAMLGQIGTPGG-GFGLSYHFSNGGNPTRRSAVLSSMqgslpgGCDAVDKIPVARIVEALE-----NPGGA- 408
Cdd:PRK15488 341 MrraIFAANVLLGNIERKGGlYFGKNASVYNKLAGEKVAPTLAKP------GVKGMPKPTAKRIDLVGEqfkyiAAGGGv 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 409 -------------YQHNG--MNRHFPdirfiwwagganFTHHQDTNRLIRAWQKPELVVISECFWTAAAKHADIVLPATT 473
Cdd:PRK15488 415 vqsiidatltqkpYQIKGwvMSRHNP------------MQTVTDRADVVKALKKLDLVVVCDVYLSESAAYADVVLPEST 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 474 SFERNDltMTGDYSNQHLVPM--KQVVPPRYEARNDFDVFAELSERWEKGGYarFT-EGKSELQWLETFYNVA-----RQ 545
Cdd:PRK15488 483 YLERDE--EISDKSGKNPAYAlrQRVVEPIGDTKPSWQIFKELGEKMGLGQY--YPwQDMETLQLYQVNGDHAllkelKK 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 546 RGanqqvelppFAEFwqaNQLIEMPENPDSERFIRfadfcRDPLAHP------------LKTASGKIEIFSQRI----AD 609
Cdd:PRK15488 559 KG---------YVSF---GVPLLLREPKMVAKFVA-----RYPNAKAvdedgtygsqlkFKTPSGKIELFSAKLealaPG 621
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 610 YGYPDCpgHPMWL-EPDEW---QGNAepeqlqvlsahPAH-RLHSQlNYSSLRELYAvanREPVTIHPDDAQERGIQDGD 684
Cdd:PRK15488 622 YGVPRY--RDVALkKEDELyfiQGKV-----------AVHtNGATQ-NVPLLANLMS---DNAVWIHPQTAGKLGIKNGD 684
|
730 740 750
....*....|....*....|....*....|.
gi 2203217743 685 TVRLWNARGQILAGAVISEGIKPGVICIHEG 715
Cdd:PRK15488 685 EIRLENSVGKEKGKALVTPGIRPDTLFAYMG 715
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
56-533 |
2.25e-36 |
|
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: 142.82 E-value: 2.25e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 56 RVRFPMVRKGflaspenpqgIRGQDEFVRVSWDEALDLIHQQHKRIREAYGPASIFAGSYGwrsngvlHKASTLLQRYMA 135
Cdd:cd02755 55 RLKKPLIRVG----------ERGEGKFREASWDEALQYIASKLKEIKEQHGPESVLFGGHG-------GCYSPFFKHFAA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 136 LAG--GYTGHLGDYSTGAAQAI--MPYVVGGSEVYQqqtswplvLEHSDVVVLWSANPLNTLKIAwnasdeQGLSYFSAL 211
Cdd:cd02755 118 AFGspNIFSHESTCLASKNLAWklVIDSFGGEVNPD--------FENARYIILFGRNLAEAIIVV------DARRLMKAL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 212 RdSGKKLICIDPMRSETVDFfGDkmEWVAPHMGTDVALMLGIAHTLVENGWHDEAFLARCTTGYAVFAsyllgesDGIAK 291
Cdd:cd02755 184 E-NGAKVVVVDPRFSELASK-AD--EWIPIKPGTDLAFVLALIHVLISENLYDAAFVEKYTNGFELLK-------AHVKP 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 292 -TAEWAAEICGVGAAKIRELAAIF--HQNTTMLMAGWGMQRQQFGEQKHWMIVTLAAMLGQIGTPGGGFglsyhFSNGGN 368
Cdd:cd02755 253 yTPEWAAQITDIPADTIRRIAREFaaAAPHAVVDPGWRGTFYSNSFQTRRAIAIINALLGNIDKRGGLY-----YAGSAK 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 369 PTRRSAVLSsmqgslpggcdavdkipvarivealenpggaYQHNGMNrhfpdirfiwwagganftHHQDTNRLIRAWQKP 448
Cdd:cd02755 328 PYPIKALFI-------------------------------YRTNPFH------------------SMPDRARLIKALKNL 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 449 ELVVISECFWTAAAKHADIVLPATTSFERNDLTMTGDYSNQHLVPMKQVVPPRYEARNDFDVFAELSERWekGGYARFTe 528
Cdd:cd02755 359 DLVVAIDILPSDTALYADVILPEATYLERDEPFSDKGGPAPAVATRQRAIEPLYDTRPGWDILKELARRL--GLFGTPS- 435
|
....*
gi 2203217743 529 GKSEL 533
Cdd:cd02755 436 GKIEL 440
|
|
| MopB_CT_DmsA-EC |
cd02794 |
The MopB_CT_DmsA-EC CD includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
636-760 |
2.99e-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: 112.77 E-value: 2.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 636 LQVLSAHPAHRLHSQL-NYSSLRElyavANREPVTIHPDDAQERGIQDGDTVRLWNARGQILAGAVISEGIKPGVICIHE 714
Cdd:cd02794 3 LQLIGWHYKRRTHSTFdNVPWLRE----AFPQEVWINPLDAAARGIKDGDRVLVFNDRGKVIRPVKVTERIMPGVVALPQ 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2203217743 715 GAWPDLDltADGICKNGAVNVLTKDLPSSrLGNGCAGNTALAWLEK 760
Cdd:cd02794 79 GAWYEPD--ANGIDKGGCINTLTGLRPSP-LAKGNPQHTNLVQVEK 121
|
|
| MopB_Arsenate-R |
cd02757 |
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ... |
50-523 |
1.47e-26 |
|
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: 114.46 E-value: 1.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 50 QVHSNTRVRFPMVRKgflaspeNPQGIRGQD-EFVRVSWDEALDLIHQQHKRIREAYGPA--SIFAGSYGwrsngvlHKA 126
Cdd:cd02757 50 QVYDPDRILYPMKRT-------NPRKGRDVDpKFVPISWDEALDTIADKIRALRKENEPHkiMLHRGRYG-------HNN 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 127 STLLQRYMALAGGyTGHLGDYSTGAAQAIM-PYVVGGSEVYQQQTswplvLEHSDVVVLWSANPL-------NTLKIaWN 198
Cdd:cd02757 116 SILYGRFTKMIGS-PNNISHSSVCAESEKFgRYYTEGGWDYNSYD-----YANAKYILFFGADPLesnrqnpHAQRI-WG 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 199 ASDEQGlsyfsalrdsgkKLICIDPMRSETVDFfgdKMEWVAPHMGTDVALMLGIAHTLVENGWHDEAFLARCTTGYAVF 278
Cdd:cd02757 189 GKMDQA------------KVVVVDPRLSNTAAK---ADEWLPIKPGEDGALALAIAHVILTEGLWDKDFVGDFVDGKNYF 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 279 ASYLLGESDGIA-----------------KTAEWAAEICGVGAAKIRELAAIFHQNTTMLMAgwgmqrqqfgeqkhwmiv 341
Cdd:cd02757 254 KAGETVDEESFKeksteglvkwwnlelkdYTPEWAAKISGIPAETIERVAREFATAAPAAAA------------------ 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 342 tlaamlgqigtpgggfglsyHFSNGGNPTRRSAVLSSMQGSLPGgcdavdkipvarIVEALENPGGAYQHNGMnrhfPDI 421
Cdd:cd02757 316 --------------------FTWRGATMQNRGSYNSMACHALNG------------LVGSIDSKGGLCPNMGV----PKI 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 422 R-FIWWAGGANFThHQDTNRLIRAWQKPELVVISECFWTAAAKHADIVLPATTSFERNDLTMTGDYSNQHLVPMKQVVPP 500
Cdd:cd02757 360 KvYFTYLDNPVFS-NPDGMSWEEALAKIPFHVHLSPFMSETTYFADIVLPDGHHFERWDVMSQENNLHPWLSIRQPVVKS 438
|
490 500
....*....|....*....|...
gi 2203217743 501 RYEARNDFDVFAELSERWEKGGY 523
Cdd:cd02757 439 LGEVREETEILIELAKKLDPKGS 461
|
|
| Molydop_binding |
pfam01568 |
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
636-739 |
1.13e-23 |
|
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: 96.19 E-value: 1.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 636 LQVLSAHPAHRLHSQLNYSSLRELYAVAnREPVTIHPDDAQERGIQDGDTVRLWNARGQILAGAVISEGIKPGVICIHEG 715
Cdd:pfam01568 1 LYLITGRVLGQYHSQTRTRRVLRLAKPE-PEVVEIHPEDAAALGIKDGDLVEVTSRRGSVVVRAKVTDRVRPGVVFMPFG 79
|
90 100
....*....|....*....|....
gi 2203217743 716 AWPDldltadgiCKNGAVNVLTKD 739
Cdd:pfam01568 80 WWYE--------PRGGNANALTDD 95
|
|
| MopB_CT |
cd02775 |
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a ... |
643-744 |
7.51e-23 |
|
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a large, diverse, heterogeneous superfamily of enzymes that, in general, bind molybdopterin as a cofactor. The MopB domain is found in a wide variety of molybdenum- and tungsten-containing enzymes, including formate dehydrogenase-H (Fdh-H) and -N (Fdh-N), several forms of nitrate reductase (Nap, Nas, NarG), dimethylsulfoxide reductase (DMSOR), thiosulfate reductase, formylmethanofuran dehydrogenase, and arsenite oxidase. Molybdenum is present in most of these enzymes in the form of molybdopterin, a modified pterin ring with a dithiolene side chain, which is responsible for ligating the Mo. In many bacterial and archaeal species, molybdopterin is in the form of a dinucleotide, with two molybdopterin dinucleotide units per molybdenum. These proteins can function as monomers, heterodimers, or heterotrimers, depending on the protein and organism. Also included in the MopB superfamily is the eukaryotic/eubacterial protein domain family of the 75-kDa subunit/Nad11/NuoG (second domain) of respiratory complex 1/NADH-quinone oxidoreductase which is postulated to have lost an ancestral formate dehydrogenase activity and only vestigial sequence evidence remains of a molybdopterin binding site. This hierarchy is of the conserved MopB_CT domain present in many, but not all, MopB homologs.
Pssm-ID: 239176 [Multi-domain] Cd Length: 101 Bit Score: 93.54 E-value: 7.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 643 PAHRLHSQLnYSSLRELYAVANREPVTIHPDDAQERGIQDGDTVRLWNARGQILAGAVISEGIKPGVICIHEGAWPDldl 722
Cdd:cd02775 1 LRDHFHSGT-RTRNPWLRELAPEPVVEINPEDAAALGIKDGDLVRVESRRGSVVLRAKVTDGVPPGVVFLPHGWGHR--- 76
|
90 100
....*....|....*....|..
gi 2203217743 723 tadgICKNGAVNVLTKDLPSSR 744
Cdd:cd02775 77 ----GGRGGNANVLTPDALDPP 94
|
|
| MopB_ydeP |
cd02767 |
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
56-599 |
1.66e-21 |
|
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: 99.30 E-value: 1.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 56 RVRFPMVRKgflaspenpqgiRGQDEFVRVSWDEALDLIHQQHKRIReaygPASIFAGSYGWRSNgvlhKASTLLQRYMA 135
Cdd:cd02767 64 RLTYPMRYD------------AGSDHYRPISWDEAFAEIAARLRALD----PDRAAFYTSGRASN----EAAYLYQLFAR 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 136 LAGgyTGHLGDYS------TGAAqaiMPYVVG---GSEVYQQqtswplvLEHSDVVVLWSANPLNtlkiawnaSDEQGLS 206
Cdd:cd02767 124 AYG--TNNLPDCSnmchepSSVG---LKKSIGvgkGTVSLED-------FEHTDLIFFIGQNPGT--------NHPRMLH 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 207 YFSALRDSGKKLICIDPMRsET--VDF-----------FGDKM--EWVAPHMGTDVALMLGIAHTLVEN-----GWHDEA 266
Cdd:cd02767 184 YLREAKKRGGKIIVINPLR-EPglERFanpqnpesmltGGTKIadEYFQVRIGGDIALLNGMAKHLIERddepgNVLDHD 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 267 FLARCTTGYAVFASYLlgesdgiaKTAEWaAEI---CGVGAAKIRELAAIFHQNTTMLMAgWGMQRQQ--FGEQKHWMIV 341
Cdd:cd02767 263 FIAEHTSGFEEYVAAL--------RALSW-DEIeraSGLSREEIEAFAAMYAKSERVVFV-WGMGITQhaHGVDNVRAIV 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 342 TLAAMLGQIGTPGGGFG-LSYHfSN-------GGNPTRRSAVLSSMqgslpggcDAVDKIPVAR-----IVEALENpgga 408
Cdd:cd02767 333 NLALLRGNIGRPGAGLMpIRGH-SNvqgdrtmGITEKPFPEFLDAL--------EEVFGFTPPRdpgldTVEAIEA---- 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 409 yQHNGmnrhfpDIRFIWWAGGANFTHHQDTNRLIRAWQKPELVV-ISECFWTAAAKHAD--IVLPATTSFERnDLTMTGD 485
Cdd:cd02767 400 -ALEG------KVKAFISLGGNFAEAMPDPAATEEALRRLDLTVhVATKLNRSHLVHGEeaLILPCLGRTEI-DMQAGGA 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 486 YSNQHLVPMKQVV-------PPRYEARNDFDVFAELSErwekggyARFTEGKSELQWLETFYnvARQRGANQQVELPPFA 558
Cdd:cd02767 472 QAVTVEDSMSMTHtsrgrlkPASRVLLSEEAIVAGIAG-------ARLGEAKPEWEILVEDY--DRIRDEIAAVIYEGFA 542
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 2203217743 559 EFwqaNQLIEMPenpdsERFIRfadfCRDPLAHPLKTASGK 599
Cdd:cd02767 543 DF---NQRGDQP-----GGFHL----PNGARERKFNTPSGK 571
|
|
| MopB_Formate-Dh-Na-like |
cd02752 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
31-521 |
9.69e-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: 90.92 E-value: 9.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 31 SRGAL-ATGmenslqSAVRDQVHSNTRVRFPMVRKGflaspenpqgirGQDEFVRVSWDEALDLIHQQHKRIREAYGPAS 109
Cdd:cd02752 34 NRGSLcPKG------AALRDFVHSPKRLKYPMYRAP------------GSGKWEEISWDEALDEIARKMKDIRDASFVEK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 110 IFAGSYGWRSNGVLHKAST--------LLQRYMALAG-GYTGH---LGDYSTGAAqaimpyvVGGSEVYQQQT-SWpLVL 176
Cdd:cd02752 96 NAAGVVVNRPDSIAFLGSAklsneecyLIRKFARALGtNNLDHqarIUHSPTVAG-------LANTFGRGAMTnSW-NDI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 177 EHSDVVVLWSANPLNTLKIawnasdeqGLSYFSALRDS-GKKLICIDPMRSETV---DFFgdkmewVAPHMGTDVALMLG 252
Cdd:cd02752 168 KNADVILVMGGNPAEAHPV--------SFKWILEAKEKnGAKLIVVDPRFTRTAakaDLY------VPIRSGTDIAFLGG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 253 IAHTLVEngwhdeaflarcttgYavfasyllgesdgiakTAEWAAEICGVGAAKIRELAAIFHQNTTMLMAG---WGMQR 329
Cdd:cd02752 234 MINYIIR---------------Y----------------TPEEVEDICGVPKEDFLKVAEMFAATGRPDKPGtilYAMGW 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 330 QQ--FGEQkhwmIVTLAAM----LGQIGTPGGG-FGLSYHfsnggnptrrsavlSSMQGSLPGGCDAvDKIPvariveal 402
Cdd:cd02752 283 TQhtVGSQ----NIRAMCIlqllLGNIGVAGGGvNALRGH--------------SNVQGATDLGLLS-HNLP-------- 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 403 enpgGAYqhngmnrhfpdirfiwwaGGANF-THHQDTNRLIRAWQKPELVVISECFWTAAA----KHAD---------IV 468
Cdd:cd02752 336 ----GYL------------------GGQNPnSSFPNANKVRRALDKLDWLVVIDPFPTETAafwkNPGMdpksiqtevFL 393
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2203217743 469 LPATTSFERNdltmtGDYSNQH--LVPMKQVVPPRYEARNDFDVFAELSER------WEKG 521
Cdd:cd02752 394 LPAACQYEKE-----GSITNSGrwLQWRYKVVEPPGEAKSDGDILVELAKRlgflyeKEGG 449
|
|
| MopB_CT_4 |
cd02785 |
The MopB_CT_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
635-719 |
1.33e-18 |
|
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: 82.41 E-value: 1.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 635 QLQVLSAHPAHRLHSQ-LNYSSLRELyavaNREP-VTIHPDDAQERGIQDGDTVRLWNARGQILAGAVISEGIKPGVICI 712
Cdd:cd02785 3 PLACIQRHSRFRVHSQfSNVPWLLEL----QPEPrVKINPIDAAARGIAHGDLVEVYNDRGSVVCKAKVDDGIQPGVVTA 78
|
....*..
gi 2203217743 713 HEGAWPD 719
Cdd:cd02785 79 EQGWWSR 85
|
|
| MopB_CT_3 |
cd02786 |
The MopB_CT_3 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
643-749 |
5.76e-17 |
|
The MopB_CT_3 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239187 [Multi-domain] Cd Length: 116 Bit Score: 77.32 E-value: 5.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 643 PAH-RLHSqlNYSSLRELYAVANREPVTIHPDDAQERGIQDGDTVRLWNARGQILAGAVISEGIKPGVIcIHEGAWPDLd 721
Cdd:cd02786 9 PAHnFLNS--TFANLPELRAKEGEPTLLIHPADAAARGIADGDLVVVFNDRGSVTLRAKVTDDVPPGVV-VAEGGWWRE- 84
|
90 100
....*....|....*....|....*...
gi 2203217743 722 LTADGIckngAVNVLTKDLPSSRLGNGC 749
Cdd:cd02786 85 HSPDGR----GVNALTSARLTDLGGGST 108
|
|
| MopB_2 |
cd02763 |
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
50-517 |
5.65e-14 |
|
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins
Pssm-ID: 239164 [Multi-domain] Cd Length: 679 Bit Score: 75.64 E-value: 5.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 50 QVHSNTRVRFPMVRKGflaspenpqgIRGQDEFVRVSWDEALDLIHQQHKRIReAYGPA--SIFAGS------YGWRSNg 121
Cdd:cd02763 48 KQYSPARLTKPLLRKG----------PRGSGQFEEIEWEEAFSIATKRLKAAR-ATDPKkfAFFTGRdqmqalTGWFAG- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 122 vlhKASTLlqrymalagGYTGHLGDYSTGAAqAIMPYVVGGSevyqqqtSWPLV---LEHSDVVVLWSA---NPLNTLKI 195
Cdd:cd02763 116 ---QFGTP---------NYAAHGGFCSVNMA-AGGLYSIGGS-------FWEFGgpdLEHTKYFMMIGVaedHHSNPFKI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 196 AwnasdeqglsyFSALRDSGKKLICIDPMRSetvDFFGDKMEWVAPHMGTDVALMLGIAHTLVENGWHDEAFLARCTTGy 275
Cdd:cd02763 176 G-----------IQKLKRRGGKFVAVNPVRT---GYAAIADEWVPIKPGTDGAFILALAHELLKAGLIDWEFLKRYTNA- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 276 AVFASYllgesdgiakTAEWAAEICGVGAAKIRELAA-----IFHQNTTMLMA---GWGmqrqqfgeQKHWMI----VTL 343
Cdd:cd02763 241 AELVDY----------TPEWVEKITGIPADTIRRIAKelgvtARDQPIELPIAwtdVWG--------RKHEKItgrpVSF 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 344 AAMLgqigtpgggfGLSYHfSNGGNPTRRSAVLSSMQGSL--PGGCDAvdKIPVARIVEALENPGGAYQHN-------GM 414
Cdd:cd02763 303 HAMR----------GIAAH-SNGFQTIRALFVLMMLLGTIdrPGGFRH--KPPYPRHIPPLPKPPKIPSADkpftplyGP 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 415 NRHFP-----------------DIRFIW-----------------WAGG-----------AN--FTHHQDTNRLIRA--- 444
Cdd:cd02763 370 PLGWPaspddllvdedgnplriDKAYSWeyplaahgcmqnvitnaWRGDpypidtlmiymANmaWNSSMNTPEVREMltd 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 445 ------WQKPELVVIsECFWTAAAKHADIVLPATTSFERNDLTMTGDYSNQHL--------VPmkqVVPPRYEARNDFDV 510
Cdd:cd02763 450 kdasgnYKIPFIIVC-DAFYSEMVAFADLVLPDTTYLERHDAMSLLDRPISEAdgpvdairVP---IVEPKGDVKPFQEV 525
|
....*..
gi 2203217743 511 FAELSER 517
Cdd:cd02763 526 LIELGTR 532
|
|
| MopB_Tetrathionate-Ra |
cd02758 |
The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other ... |
8-371 |
2.18e-13 |
|
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: 73.92 E-value: 2.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 8 YSVLTAAHWGPMlvetdgETVFSSRGALATGMENSLQ---------SAVRDQVHSNTRVRFPMVRKGflaspenPqgiRG 78
Cdd:cd02758 32 YHPLNTAPSLPY------NTPLKESLYLSLVGENGLKaratacargNAGLQYLYDPYRVLQPLKRVG-------P---RG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 79 QDEFVRVSWDEALDLI-----------HQQHKRIREAYGPASIFAGSYGWRSNGVL------HKASTLLQRYMALAGGYT 141
Cdd:cd02758 96 SGKWKPISWEQLIEEVveggdlfgeghVEGLKAIRDLDTPIDPDHPDLGPKANQLLytfgrdEGRTPFIKRFANQAFGTV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 142 GHLGdySTGAAQaiMPYVVGGSEVYQQQTSWPLV---LEHSDVVVLWSANPLNtlkiAWNASDEQGLSYFSALRDSGKKL 218
Cdd:cd02758 176 NFGG--HGSYCG--LSYRAGNGALMNDLDGYPHVkpdFDNAEFALFIGTSPAQ----AGNPFKRQARRLAEARTEGNFKY 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 219 ICIDPMRSETVDFFGDKMEWVAPHMGTDVALMLGIAHTLVENGWHDEAFLARCTT------GYAVF--ASYL-------- 282
Cdd:cd02758 248 VVVDPVLPNTTSAAGENIRWVPIKPGGDGALAMAMIRWIIENERYNAEYLSIPSKeaakaaGEPSWtnATHLvitvrvks 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 283 ----LGESdGIAKTAEWAAEICGVGAAKIRELAAIF--HQNTTMLMAGWGMQRQQfGEQKHWMIVTLAAMLGQIGTPGGG 356
Cdd:cd02758 328 alqlLKEE-AFSYSLEEYAEICGVPEAKIIELAKEFtsHGRAAAVVHHGGTMHSN-GFYNAYAIRMLNALIGNLNWKGGL 405
|
410
....*....|....*
gi 2203217743 357 FGLSYHFSNGGNPTR 371
Cdd:cd02758 406 LMSGGGFADNSAGPR 420
|
|
| MopB_CT_Fdh-Nap-like |
cd00508 |
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and ... |
657-739 |
4.82e-13 |
|
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and other related proteins. Formate dehydrogenase H is a component of the anaerobic formate hydrogen lyase complex and catalyzes the reversible oxidation of formate to CO2 with the release of a proton and two electrons. Formate dehydrogenase N (alpha subunit) is the major electron donor to the bacterial nitrate respiratory chain and nitrate reductases, Nap and Nas, catalyze the reduction of nitrate to nitrite. This CD (MopB_CT_Fdh-Nap-like) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 238282 [Multi-domain] Cd Length: 120 Bit Score: 66.38 E-value: 4.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 657 RELYAVANREPVTIHPDDAQERGIQDGDTVRLWNARGQILAGAVISEGIKPGVICI--HEGAWPDLdltadgicknGAVN 734
Cdd:cd00508 26 PRLAALAPEPFVEIHPEDAARLGIKDGDLVRVSSRRGSVVVRARVTDRVRPGTVFMpfHWGGEVSG----------GAAN 95
|
....*
gi 2203217743 735 VLTKD 739
Cdd:cd00508 96 ALTND 100
|
|
| MopB_CT_Tetrathionate_Arsenate-R |
cd02780 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate ... |
645-760 |
6.57e-12 |
|
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate reductase, subunit A, (TtrA); respiratory arsenate As(V) reductase, catalytic subunit (ArrA); and other related proteins.
Pssm-ID: 239181 [Multi-domain] Cd Length: 143 Bit Score: 63.85 E-value: 6.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 645 HRLHSQ--LNYSSLRElyaVANREPVTIHPDDAQERGIQDGDTVRLWNARGQILAGAVISEGIKPGVI--CIHEGAW--- 717
Cdd:cd02780 10 SNLNSHrsANAPWLKE---IKPENPVWINPEDAAKLGIKTGDRVRVVTPGGSVVGKAKVTEGVRPGVVaiEHGYGHWayg 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2203217743 718 ----PDLDLTADGICKNGA-VNV---------LTKDLPSSRLGNGCAGNTALAWLEK 760
Cdd:cd02780 87 avasTIDGKDLPGDAWRGAgVNIndiglvdpsRGGWSLVDWVGGAAARYDTPVKIEK 143
|
|
| MopB_CT_Formate-Dh-Na-like |
cd02792 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
668-737 |
1.38e-11 |
|
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: 62.24 E-value: 1.38e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2203217743 668 VTIHPDDAQERGIQDGDTVRLWNARGQILAGAVISEGIKPGVICI--HEGAWpdldltadGICKNGAVNVLT 737
Cdd:cd02792 37 VEISPELAAERGIKNGDMVWVSSPRGKIKVKALVTDRVKPHEVGIpyHWGGM--------GLVIGDSANTLT 100
|
|
| MopB_Phenylacetyl-CoA-OR |
cd02760 |
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large ... |
56-517 |
2.04e-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: 67.69 E-value: 2.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 56 RVRFPMVRKgflaspeNPQGIRGQDE-FVRVSWDEALDLIHQQHKRIREA-YGPASIF---AGSYGwrsngvlhkASTLL 130
Cdd:cd02760 58 RVLQPMKRT-------NPKKGRNEDPgFVPISWDEALDLVAAKLRRVREKgLLDEKGLprlAATFG---------HGGTP 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 131 QRYMALAGGYTGHLG--DYSTGAAQAIMpyVVGGSEVYQQ--QTSWPLV--LEHSDVVVLWSAN------PLNtLKIAWN 198
Cdd:cd02760 122 AMYMGTFPAFLAAWGpiDFSFGSGQGVK--CVHSEHLYGEfwHRAFTVAadTPLANYVISFGSNveasggPCA-VTRHAD 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 199 AsdeqglsyfsalRDSGKKLICIDPMRSETVdffGDKMEWVAPHMGTDVALMLGIAHTLVEN---GWHDEAFLARCT--- 272
Cdd:cd02760 199 A------------RVRGYKRVQVEPHLSVTG---ACSAEWVPIRPKTDPAFMFAMIHVMVHEqglGKLDVPFLRDRTssp 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 273 --------------TG---------------------------------YAVFASYLLGESDGI--------------AK 291
Cdd:cd02760 264 ylvgpdglylrdaaTGkplvwdersgravpfdtrgavpavagdfavdgaVSVDADDETAIHQGVegttaftmlvehmrKY 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 292 TAEWAAEICGVGAAKIRELAAIFHQNTTM-----------------LMAGWGMQRQQFGEQKHWMIVTLAAMLGQIGTPG 354
Cdd:cd02760 344 TPEWAESICDVPAATIRRIAREFLENASIgstievdgvtlpyrpvaVTLGKSVNNGWGAFECCWARTLLATLVGALEVPG 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 355 GGFGLSYHfSNGGNPTRRSAVLSSMQGSLPGGCDAVDKIPVA----------RIVEALENPGGAyQHNGMNRHF------ 418
Cdd:cd02760 424 GTLGTTVR-LNRPHDDRLASVKPGEDGFMAQGFNPTDKEHWVvkptgrnahrTLVPIVGNSAWS-QALGPTQLAwmflre 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 419 ------------PDIRFIWWAGGAnfTHHQDTNRLIRAWQKPELVVISECFWTAAAKHADIVLPATTSFERNDLTMTG-- 484
Cdd:cd02760 502 vpldwkfelptlPDVWFNYRTNPA--ISFWDTATLVDNIAKFPFTVSFAYTEDETNWMADVLLPEATDLESLQMIKVGgt 579
|
570 580 590
....*....|....*....|....*....|....*...
gi 2203217743 485 DYSNQHL----VPMKQ-VVPPRYEARNDFDVFAELSER 517
Cdd:cd02760 580 KFVEQFWehrgVVLRQpAVEPQGEARDFTWISTELAKR 617
|
|
| MopB_CT_Nitrate-R-NapA-like |
cd02791 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
658-744 |
2.18e-10 |
|
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to nitrite. Monomeric Nas is located in the cytoplasm and participates in nitrogen assimilation. Dimeric Nap is located in the periplasm and is coupled to quinol oxidation via a membrane-anchored tetraheme cytochrome. This CD (MopB_CT_Nitrate-R-Nap) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs
Pssm-ID: 239192 [Multi-domain] Cd Length: 122 Bit Score: 58.74 E-value: 2.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 658 ELYAvANREP-VTIHPDDAQERGIQDGDTVRLWNARGQILAGAVISEGIKPGV--ICIHegaWPDLDLTAdgicknGAVN 734
Cdd:cd02791 27 RLNA-HVPEPyVEIHPEDAARLGLKEGDLVRVTSRRGEVVLRVRVTDRVRPGEvfVPMH---WGDQFGRS------GRVN 96
|
90
....*....|..
gi 2203217743 735 VLTKDL--PSSR 744
Cdd:cd02791 97 ALTLDAtdPVSG 108
|
|
| MopB_CT_Acetylene-hydratase |
cd02781 |
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related ... |
648-739 |
2.66e-10 |
|
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: 58.86 E-value: 2.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 648 HSQL-NYSSLRELyavaNREP-VTIHPDDAQERGIQDGDTVRLWNARGQILAGAVISEGIKPGVICIHEGAW---PDLDL 722
Cdd:cd02781 17 HSEHrQLPSLREL----HPDPvAEINPETAAKLGIADGDWVWVETPRGRARQKARLTPGIRPGVVRAEHGWWypeREAGE 92
|
90
....*....|....*..
gi 2203217743 723 TADGICKNGAVNVLTKD 739
Cdd:cd02781 93 PALGGVWESNANALTSD 109
|
|
| PRK13532 |
PRK13532 |
nitrate reductase catalytic subunit NapA; |
81-697 |
2.70e-10 |
|
nitrate reductase catalytic subunit NapA;
Pssm-ID: 237416 [Multi-domain] Cd Length: 830 Bit Score: 64.15 E-value: 2.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 81 EFVRVSWDEALDLIHQQHKRIREAYGPASI--FA-GSY--------------GWRSNGVLHKAstllqRY-MALA-GGYT 141
Cdd:PRK13532 115 EFTPVSWDQAFDVMAEKFKKALKEKGPTAVgmFGsGQWtiwegyaasklmkaGFRSNNIDPNA-----RHcMASAvVGFM 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 142 GHLG-DYSTGAAQAImpyvvggsevyqqqtswplvlEHSDVVVLWSANPLNTLKIAWNASDEQGLSyfsalrDSGKKLIC 220
Cdd:PRK13532 190 RTFGiDEPMGCYDDI---------------------EAADAFVLWGSNMAEMHPILWSRVTDRRLS------NPDVKVAV 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 221 IDPMRSETVDFfGDKMEWVAPHmgTDVALMLGIAHTLVENGWHDEAFLARCTT--------GYAVFASYLL--------- 283
Cdd:PRK13532 243 LSTFEHRSFEL-ADNGIIFTPQ--TDLAILNYIANYIIQNNAVNWDFVNKHTNfrkgatdiGYGLRPTHPLekaaknpgt 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 284 -GESDGI-----AK-----TAEWAAEICGVGAAKIRELAAIFHQNTTMLMAGWGMqrqqfGEQKH----W---MIVTLAA 345
Cdd:PRK13532 320 aGKSEPIsfeefKKfvapyTLEKTAKMSGVPKEQLEQLAKLYADPNRKVVSFWTM-----GFNQHtrgvWannLVYNIHL 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 346 MLGQIGTPGGGfglsyHFSNGGNP----TRRSavLSSMQGSLPGgcDAVDKIPVAR--------IVEALENPGGAYQHNG 413
Cdd:PRK13532 395 LTGKISTPGNG-----PFSLTGQPsacgTARE--VGTFSHRLPA--DMVVTNPKHReiaekiwkLPEGTIPPKPGYHAVA 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 414 MNRHFPD--IRFIW------WAGGANFTHhqdtnRLIRAWQKPE-LVVISECFWTAAAKHADIVLPATTSFERNdltmtG 484
Cdd:PRK13532 466 QDRMLKDgkLNAYWvmcnnnMQAGPNINE-----ERLPGWRNPDnFIVVSDPYPTVSALAADLILPTAMWVEKE-----G 535
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 485 DYSN-----QHlvpMKQVVPPRYEARNDFDVFAELSER------W-----EKGGYARfteGKselqwleTFYNVARqrgA 548
Cdd:PRK13532 536 AYGNaerrtQF---WRQQVKAPGEAKSDLWQLVEFSKRfkteevWpeellAKKPEYR---GK-------TLYDVLF---A 599
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 549 NQQVELPPfaefwqANQLIEMPENPDSER---------FIRFADFCR--------------------------------- 586
Cdd:PRK13532 600 NGQVDKFP------LSELAEGYLNDEAKHfgfyvqkglFEEYASFGRghghdlapfdtyhkvrglrwpvvdgketlwryr 673
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 587 ---DPLAhplKTASGkieifsqrIADYGYPD-------CPGHPMWLEPDE----W--QGnaepeqlQVLSaHpahrLHSQ 650
Cdd:PRK13532 674 egyDPYV---KAGEG--------FKFYGKPDgkavifaLPYEPPAESPDEeydlWlsTG-------RVLE-H----WHTG 730
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 2203217743 651 LNYSSLRELY-AVANREpVTIHPDDAQERGIQDGDTVRLWNARGQILA 697
Cdd:PRK13532 731 SMTRRVPELYrAFPEAV-CFMHPEDAKARGLRRGDEVKVVSRRGEVKS 777
|
|
| MopB_CT_Formate-Dh_H |
cd02790 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
657-716 |
2.75e-09 |
|
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 with the release of a proton and two electrons. It is a component of the anaerobic formate hydrogen lyase complex. The E. coli formate dehydrogenase H (Fdh-H) is a monomer composed of a single polypeptide chain with a Mo active site region and a [4Fe-4S] center. This CD (MopB_CT_Formate-Dh_H) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239191 [Multi-domain] Cd Length: 116 Bit Score: 55.32 E-value: 2.75e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2203217743 657 RELYAVANREPVTIHPDDAQERGIQDGDTVRLWNARGQILAGAVISEGIKPGVI----CIHEGA 716
Cdd:cd02790 26 EGLDAIAPEEYVEINPEDAKRLGIEDGEKVRVSSRRGSVEVRARVTDRVPEGVVfmpfHFAEAA 89
|
|
| MopB_CT_Nitrate-R-NarG-like |
cd02776 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
636-717 |
3.87e-09 |
|
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: 55.85 E-value: 3.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 636 LQVLSAHPAHRLHSqlNYS-SLRELYAVANREPVTIHPDDAQERGIQDGDTVRLWNARGQILAGAVISEGIKPGViCIHE 714
Cdd:cd02776 2 LNYLTPHGKWSIHS--TYRdNLLMLRLQRGGPVVWMNPKDAAELGIKDNDWVEVFNDNGVVVARAKVSPRIPRGT-VFMY 78
|
...
gi 2203217743 715 GAW 717
Cdd:cd02776 79 HAQ 81
|
|
| MopB_CT_1 |
cd02782 |
The MopB_CT_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
664-755 |
3.12e-08 |
|
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: 52.78 E-value: 3.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 664 NREPVTIHPDDAQERGIQDGDTVRLWNARGQILAGAVISEGIKPGVICIHEGaWPDLDLTADGICKNGAVNVltKDLPSS 743
Cdd:cd02782 31 NRCTLRIHPDDAAALGLADGDKVRVTSAAGSVEAEVEVTDDMMPGVVSLPHG-WGHDYPGVSGAGSRPGVNV--NDLTDD 107
|
90
....*....|..
gi 2203217743 744 RLGNGCAGNTAL 755
Cdd:cd02782 108 TQRDPLSGNAAH 119
|
|
| PRK09939 |
PRK09939 |
acid resistance putative oxidoreductase YdeP; |
176-356 |
4.51e-08 |
|
acid resistance putative oxidoreductase YdeP;
Pssm-ID: 182156 [Multi-domain] Cd Length: 759 Bit Score: 56.59 E-value: 4.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 176 LEHSDVVVLWSANPlntlkiawNASDEQGLSYFSALRDSGKKLICIDPMRSETVDFFG---DKMEWVAPH---------- 242
Cdd:PRK09939 206 FEKCDLVICIGHNP--------GTNHPRMLTSLRALVKRGAKMIAINPLQERGLERFTapqNPFEMLTNSetqlasayyn 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 243 --MGTDVALMLGIAHTLVEN----------GWHDEAFLARCTTGYAVFASYLLgesdgiakTAEWA--AEICGVGAAKIR 308
Cdd:PRK09939 278 vrIGGDMALLKGMMRLLIERddaasaagrpSLLDDEFIQTHTVGFDELRRDVL--------NSEWKdiERISGLSQTQIA 349
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2203217743 309 ELA-AIFHQNTTMLMAGWGMQRQQFGEQKHWMIVTLAAMLGQIGTPGGG 356
Cdd:PRK09939 350 ELAdAYAAAERTIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAG 398
|
|
| PRK14991 |
PRK14991 |
tetrathionate reductase subunit TtrA; |
647-715 |
5.24e-08 |
|
tetrathionate reductase subunit TtrA;
Pssm-ID: 237883 [Multi-domain] Cd Length: 1031 Bit Score: 56.54 E-value: 5.24e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2203217743 647 LHSQLNYSSLReLYAVANREPVTIHPDDAQERGIQDGDTVRLWNARGQILAGAVISEGIKPGVICIHEG 715
Cdd:PRK14991 898 LMSSMSIASPR-LRQVKPANPVALNPQDAARLGIQHGDRVRISTPGGSVVAQASVLNGVMPGVIAIEHG 965
|
|
| MopB_CT_Thiosulfate-R-like |
cd02778 |
The MopB_CT_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, ... |
670-751 |
6.80e-07 |
|
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: 48.81 E-value: 6.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 670 IHPDDAQERGIQDGDTVRLWNARGQILAGAVISEGIKPGVICIHE--GAW-PDLDLtADGicKNGAVNVLTK---DLPSS 743
Cdd:cd02778 34 INPETAARLGIKDGDRVEVSSARGKVTGKARLTEGIRPDTVFMPHgfGHWaPALSR-AYG--GGVNDNNLLPgstEPVSG 110
|
....*...
gi 2203217743 744 RLGNGCAG 751
Cdd:cd02778 111 GAGLQEFT 118
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
437-517 |
7.80e-07 |
|
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production and conversion]; NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) is part of the Pathway/BioSystem: NADH dehydrogenase
Pssm-ID: 440657 [Multi-domain] Cd Length: 453 Bit Score: 52.15 E-value: 7.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 437 DTNRLIRAWQKPELVVISECFWTAAAKHADIVLPATTSFERNdltmtGDYSNQ--HLVPMKQVVPPRYEARNDFDVFAEL 514
Cdd:COG1034 347 DPAAALAALAKADFVVVLDHFGSATAERADVVLPAAAFAEKS-----GTFVNLegRVQRFNAAVPPPGEARPDWRVLRAL 421
|
...
gi 2203217743 515 SER 517
Cdd:COG1034 422 ANA 424
|
|
| NarG |
COG5013 |
Nitrate reductase alpha subunit [Energy production and conversion, Inorganic ion transport and ... |
51-255 |
1.93e-05 |
|
Nitrate reductase alpha subunit [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 444037 [Multi-domain] Cd Length: 1231 Bit Score: 48.28 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 51 VHSNTRVRFPMVR----------KGFLASP--------ENP------QGIRGQDEFVRVSWDEALDLIHQQHKRIREAYG 106
Cdd:COG5013 106 TYSPTRVKYPYVRgvllelwreaRARHGDPveawasivEDPekrrryKSARGKGGFVRATWDEANEIIAAANVYTIKKYG 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 107 PASIF------AGSYgwrsngVLHKASTllqRYMALAGGYTGHLGD-YstgaaqAIMPyvVGGSEVYQQQTSWPlvlEHS 179
Cdd:COG5013 186 PDRVAgfspipAMSM------VSYAAGA---RFLSLIGGVMLSFYDwY------ADLP--PASPQVWGEQTDVP---ESA 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 180 DvvvLWSANPLntlkIAWNAS-------DEQglsYFSALRDSGKKLICIDPMRSETVDfFGDkmEWVAPHMGTDVALMLG 252
Cdd:COG5013 246 D---WYNSGYL----IMWGSNvpqtrtpDAH---FMTEARYKGTKVVVVSPDYAENTK-FAD--EWLPPKQGTDAALAMA 312
|
...
gi 2203217743 253 IAH 255
Cdd:COG5013 313 MGH 315
|
|
| MopB_CT_Arsenite-Ox |
cd02779 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of Arsenite oxidase ... |
657-710 |
1.95e-05 |
|
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of Arsenite oxidase (Arsenite-Ox) and related proteins. Arsenite oxidase oxidizes arsenite to the less toxic arsenate; it transfers the electrons obtained from the oxidation of arsenite towards the soluble periplasmic electron carriers cytochrome c and/or amicyanin.
Pssm-ID: 239180 [Multi-domain] Cd Length: 115 Bit Score: 44.37 E-value: 1.95e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2203217743 657 RELYAVANREP---VTIHPDDAQERGIQDGDTVRLWNARGQILAGAVISEGIKPGVI 710
Cdd:cd02779 21 QNNSEIAERVPlpyIEVNPEDAKREGLKNGDLVEVYNDYGSTTAMAYVTNTVKPGQT 77
|
|
| MopB_CT_ydeP |
cd02787 |
The MopB_CT_ydeP CD includes a group of related uncharacterized bacterial ... |
646-718 |
2.54e-05 |
|
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: 44.19 E-value: 2.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203217743 646 RLHSQLN---YSsLRELY--AVANREPVTIHPDDAQERGIQDGDTVRLWNARGQ-----ILAGAVISEGIKPGVICIHeg 715
Cdd:cd02787 7 RSHDQFNttiYG-LDDRYrgVFGRRDVVFMNPDDIARLGLKAGDRVDLESAFGDgqgriVRGFRVVEYDIPRGCLAAY-- 83
|
...
gi 2203217743 716 aWP 718
Cdd:cd02787 84 -YP 85
|
|
| Molybdopterin_N |
pfam18364 |
Molybdopterin oxidoreductase N-terminal domain; This is the N-terminal domain of pfam00384 ... |
12-52 |
1.92e-04 |
|
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: 39.30 E-value: 1.92e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2203217743 12 TAAHWGPMLVETDGETVFSSRGALATGMENSLQSAVRDQVH 52
Cdd:pfam18364 1 TASHWGAFRAVVKDGRIVGVEPFEGDPDPSPLLQGVPDAVY 41
|
|
| MopB_NADH-Q-OR-NuoG2 |
cd02768 |
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone ... |
440-516 |
2.81e-03 |
|
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone oxidoreductase (NADH-Q-OR)/respiratory complex I/NADH dehydrogenase-1 (NDH-1). The NADH-Q-OR is the first energy-transducting complex in the respiratory chains of many prokaryotes and eukaryotes. Mitochondrial complex I and its bacterial counterpart, NDH-1, function as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. The atomic structure of complex I is not known and the mechanisms of electron transfer and proton pumping are not established. The nad11 gene codes for the largest (75-kDa) subunit of the mitochondrial NADH:ubiquinone oxidoreductase, it constitutes the electron input part of the enzyme, or the so-called NADH dehydrogenase fragment. In Escherichia coli, this subunit is encoded by the nuoG gene, and is part of the 14 distinct subunits constituting the 'minimal' functional enzyme. The nad11 gene is nuclear-encoded in animals, plants, and fungi, but is still encoded in the mitochondrial genome of some protists. The Nad11/NuoG subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain family belongs to the molybdopterin_binding (MopB) superfamily of proteins. Bacterial type II NADH-quinone oxidoreductases and NQR-type sodium-motive NADH-quinone oxidoreductases are not homologs of this domain family.
Pssm-ID: 239169 [Multi-domain] Cd Length: 386 Bit Score: 40.73 E-value: 2.81e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2203217743 440 RLIRAWQKPELVVISECFWTAAAKHADIVLPATTSFERNdltmtGDYSNQ-HLVPM-KQVVPPRYEARNDFDVFAELSE 516
Cdd:cd02768 311 PAAVALAAADAFVVYQGHHGDTGAQADVILPAAAFTEKS-----GTYVNTeGRVQRfKKAVSPPGDAREDWKILRALSN 384
|
|
| MopB_CT_FmdC-FwdD |
cd02789 |
The MopB_FmdC-FwdD CD includes the C-terminus of subunit C of molybdenum formylmethanofuran ... |
670-735 |
7.57e-03 |
|
The MopB_FmdC-FwdD CD includes the C-terminus of subunit C of molybdenum formylmethanofuran dehydrogenase (FmdC) and subunit D of tungsten formylmethanofuran dehydrogenase (FwdD), and other related proteins. Formylmethanofuran dehydrogenase catalyzes the first step in methane formation from CO2 in methanogenic archaea and some eubacteria. Members of this CD belong to the molybdopterin_binding superfamily of proteins. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239190 [Multi-domain] Cd Length: 106 Bit Score: 36.63 E-value: 7.57e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2203217743 670 IHPDDAQERGIQDGDTVRLWNARGQILAGAVISEGIKPGVICIHEGAW------PDLDLTADGICKNGAVNV 735
Cdd:cd02789 35 INPEDYKLLGKPEGDKVKVTSEFGEVVVFAKENEGVPEGMVFIPMGPWanvvvdPYTDSTGSPIFKGVPVYI 106
|
|
| |
