|
Name |
Accession |
Description |
Interval |
E-value |
| bisC_fam |
TIGR00509 |
molybdopterin guanine dinucleotide-containing S/N-oxide reductases; This enzyme family shares ... |
41-808 |
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: 1337.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 41 AGRWGAMNVEVKDGKIVSSTGALAKTIPNSLQSTAADQVHTTARIQHPMVRKSYLDNP-LQPAKGRGEDTYVQVSWEQAL 119
Cdd:TIGR00509 1 ASHWGVFTATVQDGRIVAVTPFESDPNPTPMLEGVPDQVYSESRIKYPMVRKGFLENGvKSDRSGRGREEFVRVSWDEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 120 KLIHEQHDRIRKANGPSAIFAGSYGWRSSGVLHKAQTLLQRYMNLAGGYSGHSGDYSTGAAQVIMPHVVGSVEVYEQQTS 199
Cdd:TIGR00509 81 DLVAEELKRVRKTHGPSAIFAGSYGWKSAGRLHNASTLLQRMLNLLGGYVGHAGDYSTGAAQVIMPHVVGDMEVYEQQTT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 200 WPLILENSQVVVLWGMNPLNTLKIAWSSTDEQGLEYFHQLKKSGKPVIAIDPIRSETIEFFGdnATWIAPNMGTDVALML 279
Cdd:TIGR00509 161 WPVILENSEVLVLWGADPLKTSQIAWGIPDHGGYEYLERLKAKGKRVISIDPVRTETVEFFG--AEWIPPNPQTDVALML 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 280 GIAHTLMTQGKHDKVFLEKYTTGYPQFEEYLTGKSNNTPKSAAWAAEITGVPEAQIVKLAELMAANRTMLMAGWGIQRQQ 359
Cdd:TIGR00509 239 GLAHTLVTEGLYDKDFLAKYTSGFEKFLPYLLGETDGTPKTAEWASKITGVPAETIKELARLFASKRTMLAAGWSMQRMQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 360 YGEQKHWMLVTLAAMLGQIGTPGGGFGFSYHYSNGGNPTRVGGVLPEMSAAIAGQASEAADDGGMTAIPVARIVDALENP 439
Cdd:TIGR00509 319 HGEQPHWMLVTLAAMLGQIGLPGGGFGFSYHYSGGGTPSASGPALSQGSNSVSSTAGPEWDDGSASVIPVARISDALLNP 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 440 GGKYQHNGKEQTYPNIKMIWWAGGGNFTHHQDTNRLIKAWQKPEMIVVSECYWTAAAKHADIVLPITTSFERNDLTMTGD 519
Cdd:TIGR00509 399 GKEIDYNGKELKLPDIKMVYWAGGNPFHHHQDTNRLIKAWRKLETIIVHEPQWTPTAKHADIVLPATTSFERNDLTMAGD 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 520 YSNQHIVPMKQAVAPQFEARNDFDVFADLAELLkpGGKEIYTEGKDEMAWLKFFYDAAQKGARAQRVTMPMFNAFWQQNk 599
Cdd:TIGR00509 479 YSNTGILAMKQVVPPQFEARNDYDIFAALAERL--GVEEAFTEGKDEMGWLKHLYEKAAKQAKADGVEMPAFDAFWAEG- 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 600 LIEMRRSEkNEQYVRYGDFRADPVKNALGTPSGKIEIYSKTLEKFGYKDCPAHPTWLAPDEWKGT--ADEKQLQLLTAHP 677
Cdd:TIGR00509 556 IVEFPVPE-GADFVRYAAFREDPLLNPLGTPSGLIEIYSKTIAKMGYDDCPGHPTWMEPAEWLGGprGAKYPLHLISPHP 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 678 AHRLHSQLNYAELRKKYAVADREPITIHTEDAARFGIANGDLVRVWNKRGQILTGAVVTDGIKKGVVCVHEGAWPDLE-- 755
Cdd:TIGR00509 635 KYRLHSQLDHTELRQAYKVQGREPVMIHPDDAAARGIADGDIVRVFNARGQILAGAVVTDGIRKGVVQIHEGAWYDPAdv 714
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*.
gi 446098945 756 ---NGLCKNGSANVLTADIPSSQLANACAGNSALVYIEKYTGNAPKLTAFDQPAVQ 808
Cdd:TIGR00509 715 repGGLCKYGNPNVLTADIGTSSLAQGNSGNTVLVEIEKYTGPAPPLTAFDQPAAA 770
|
|
| MopB_DMSOR-BSOR-TMAOR |
cd02769 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
39-661 |
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: 953.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 39 LTAGRWGAMNVEVKDGKIVSSTGALAKTIPNSLQSTAADQVHTTARIQHPMVRKSYLDNPLQPAKG-RGEDTYVQVSWEQ 117
Cdd:cd02769 1 PTASHWGAFRARVKDGRIVGVRPFEEDPDPSPLLDGVPDAVYSPTRIKYPMVRRGWLEKGPGSDRSlRGKEEFVRVSWDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 118 ALKLIHEQHDRIRKANGPSAIFAGSYGWRSSGVLHKAQTLLQRYMNLAGGYSGHSGDYSTGAAQVIMPHVVGSVEVY-EQ 196
Cdd:cd02769 81 ALDLVAAELKRVRKTYGNEAIFGGSYGWSSAGRFHHAQSLLHRFLNLAGGYVGSVGDYSTGAAQVILPHVVGSMEVYtEQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 197 QTSWPLILENSQVVVLWGMNPLNTLKIAW-SSTDEQGLEYFHQLKKSGKPVIAIDPIRSETIEFFgdNATWIAPNMGTDV 275
Cdd:cd02769 161 QTSWPVIAEHTELVVAFGADPLKNAQIAWgGIPDHQAYSYLKALKDRGIRFISISPLRDDTAAEL--GAEWIAIRPGTDV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 276 ALMLGIAHTLMTQGKHDKVFLEKYTTGYPQFEEYLTGKSNNTPKSAAWAAEITGVPEAQIVKLAELMAANRTMLMAGWGI 355
Cdd:cd02769 239 ALMLALAHTLVTEGLHDKAFLARYTVGFDKFLPYLLGESDGVPKTPEWAAAICGIPAETIRELARRFASKRTMIMAGWSL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 356 QRQQYGEQKHWMLVTLAAMLGQIGTPGGGFGFSYHYSNGGNPTRVGGVLPEMSaaiagQASEAADDggmtAIPVARIVDA 435
Cdd:cd02769 319 QRAHHGEQPHWMAVTLAAMLGQIGLPGGGFGFGYHYSNGGGPPRGAAPPPALP-----QGRNPVSS----FIPVARIADM 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 436 LENPGGKYQHNGKEQTYPNIKMIWWAGGGNFTHHQDTNRLIKAWQKPEMIVVSECYWTAAAKHADIVLPITTSFERNDLT 515
Cdd:cd02769 390 LLNPGKPFDYNGKKLTYPDIKLVYWAGGNPFHHHQDLNRLIRAWQKPETVIVHEPFWTATARHADIVLPATTSLERNDIG 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 516 MTGDysNQHIVPMKQAVAPQFEARNDFDVFADLAELLkpGGKEIYTEGKDEMAWLKFFYDAAQKGARAQRVTMPMFNAFW 595
Cdd:cd02769 470 GSGD--NRYIVAMKQVVEPVGEARDDYDIFADLAERL--GVEEQFTEGRDEMEWLRHLYEESRAQAAARGVEMPSFDEFW 545
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446098945 596 QQNKLIEMRRSEKneqYVRYGDFRADPVKNALGTPSGKIEIYSKTLEKFGYKDCPAHPTWLAPDEW 661
Cdd:cd02769 546 AQGYVELPIPEAD---FVRLADFREDPEANPLGTPSGRIEIFSETIAGFGYDDCPGHPTWLEPAEW 608
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
39-661 |
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: 875.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 39 LTAGRWGAMNVEVKDGKIV-SSTGALAKTIPNSLQSTAADQVHTTARIQHPMVRKSYLDNPLQPAKGRGEDTYVQVSWEQ 117
Cdd:cd02751 1 PTACHWGPFKAHVKDGVIVrVEPDDTDQPRPCPRGRSVRDRVYSPDRIKYPMKRVGWLGNGPGSRELRGEGEFVRISWDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 118 ALKLIHEQHDRIRKANGPSAIFAGSYGWRSSGVLHKAQTLLQRYMNLAGGYSGHSGDYSTGAAQVIMPHVVGSVEVYEQQ 197
Cdd:cd02751 81 ALDLVASELKRIREKYGNEAIFGGSYGWASAGRLHHAQSLLHRFLNLIGGYLGSYGTYSTGAAQVILPHVVGSDEVYEQG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 198 TSWPLILENSQVVVLWGMNPLNTLKIAWSSTDEQGLEYFHQLKKSGKPVIAIDPIRSETIEFFGDnaTWIAPNMGTDVAL 277
Cdd:cd02751 161 TSWDDIAEHSDLVVLFGANPLKTRQGGGGGPDHGSYYYLKQAKDAGVRFICIDPRYTDTAAVLAA--EWIPIRPGTDVAL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 278 MLGIAHTLMTQGKHDKVFLEKYTTGYPQFEEYLTGKSNNTPKSAAWAAEITGVPEAQIVKLAELMAANRTMLMAGWGIQR 357
Cdd:cd02751 239 MLAMAHTLITEDLHDQAFLARYTVGFDEFKDYLLGESDGVPKTPEWAAEITGVPAETIRALAREIASKRTMIAQGWGLQR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 358 QQYGEQKHWMLVTLAAMLGQIGTPGGGFGFSYHYSNGGNPTRVGGVLPEMSaaiagQASEAADDggmtAIPVARIVDALE 437
Cdd:cd02751 319 AHHGEQPAWMLVTLAAMLGQIGLPGGGFGFGYGYSNGGGPPRGGAGGPGLP-----QGKNPVKD----SIPVARIADALL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 438 NPGGKYQHNGKEQTYPNIKMIWWAGGGNFTHHQDTNRLIKAWQKPEMIVVSECYWTAAAKHADIVLPITTSFERNDLTMT 517
Cdd:cd02751 390 NPGKEFTANGKLKTYPDIKMIYWAGGNPLHHHQDLNRLIKALRKDETIVVHDIFWTASARYADIVLPATTSLERNDIGLT 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 518 GDYSNQHIVPMKQAVAPQFEARNDFDVFADLAELLkpGGKEIYTEGKDEMAWLKFFYDAAQKGARAQRVTMPMFNAFWQQ 597
Cdd:cd02751 470 GNYSNRYLIAMKQAVEPLGEARSDYEIFAELAKRL--GVEEEFTEGRDEMEWLEHLYEETRAKAAGPGPELPSFEEFWEK 547
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446098945 598 NKLIEMRRSEKneqYVRYGDFRADPVKNALGTPSGKIEIYSKTLEKFGYKDCPAHPTWLAPDEW 661
Cdd:cd02751 548 GIVRVPAAPKP---FVAFADFREDPEANPLGTPSGKIEIYSETLADFGYDDCPGHPTWIEPWEG 608
|
|
| PRK15102 |
PRK15102 |
trimethylamine-N-oxide reductase TorA; |
3-805 |
0e+00 |
|
trimethylamine-N-oxide reductase TorA;
Pssm-ID: 237909 [Multi-domain] Cd Length: 825 Bit Score: 832.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 3 LTRREFIKH-SGIAAGALVVTSA-APLPAWA------EEKGGKILTAGRWGAMNVEVKDGKIVSSTGALAKTIPNSLQST 74
Cdd:PRK15102 1 ASRRRFLKGlGGLSAAGMLGPSLlTPRSALAaqaaaaETTKEWILTGSHWGAFRAKVKNGRFVEAKPFELDKYPTKMING 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 75 AADQVHTTARIQHPMVRKSYLDNP-LQPAKGRGEDTYVQVSWEQALKLIHEQHDRIRKANGPSAIFAGSYGWRSSGVLHK 153
Cdd:PRK15102 81 IKGHVYNPSRIRYPMVRLDWLRKRhKSDTSQRGDNRFVRVSWDEALDLFYEELERVQKTYGPSALHTGQTGWQSTGQFHS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 154 AQTLLQRYMNLAGGYSGHSGDYSTGAAQVIMPHVVGSVEVYEQQTSWPLILENSQVVVLWGMNPLNTLKIAWSSTDEQGL 233
Cdd:PRK15102 161 ATGHMQRAIGMHGNSVGTVGDYSTGAGQVILPYVLGSTEVYEQGTSWPLILENSKTIVLWGSDPVKNLQVGWNCETHESY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 234 EYFHQLK---KSGK-PVIAIDPIRSETIEFFGDNATWIAPNmgTDVALMLGIAHTLMTQGKHDKVFLEKYTTGYPQFEEY 309
Cdd:PRK15102 241 AYLAQLKekvAKGEiNVISIDPVVTKTQNYLGCEHLYVNPQ--TDVPLMLALAHTLYSENLYDKKFIDNYCLGFEQFLPY 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 310 LTGKSNNTPKSAAWAAEITGVPEAQIVKLAELMAANRTMLMAGWGIQRQQYGEQKHWMLVTLAAMLGQIGTPGGGFGFSY 389
Cdd:PRK15102 319 LLGEKDGVPKTPEWAEKICGIDAETIRELARQMAKGRTQIIAGWCIQRQQHGEQPYWMGAVLAAMLGQIGLPGGGISYGH 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 390 HYSNGGNPTRvGGVLPemsAAIAGQASEAAD--------DGGMTAIPVARIVDALENPGGKYQHNGKEQTYPNIKMIWWA 461
Cdd:PRK15102 399 HYSGIGVPSS-GGAIP---GGFPGNLDTGQKpkhdnsdyKGYSSTIPVARFIDAILEPGKTINWNGKKVTLPPLKMMIFS 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 462 GGGNFTHHQDTNRLIKAWQKPEMIVVSECYWTAAAKHADIVLPITTSFERNDLTMTGDYSNQHIVPMKQAVAPQFEARND 541
Cdd:PRK15102 475 GTNPWHRHQDRNRMKEAFRKLETVVAIDNQWTATCRFADIVLPACTQFERNDIDQYGSYSNRGIIAMKKVVEPLFESRSD 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 542 FDVFADLAELLkpGGKEIYTEGKDEMAWLKFFYDAAQKgARAQRVTMPMFNAFWQQNkLIEMrrsEKNEQYVRYGDFRAD 621
Cdd:PRK15102 555 FDIFRELCRRF--GREKEYTRGMDEMGWLKRLYQECKQ-QNKGKFHMPEFDEFWKKG-YVEF---GEGQPWVRHADFRED 627
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 622 PVKNALGTPSGKIEIYSKTLEKFGYKDCPAHPTWLAPDEWK--GTADEK-QLQLLTAHPAHRLHSQL-NYAELRKKYAVA 697
Cdd:PRK15102 628 PELNPLGTPSGLIEIYSRKIADMGYDDCQGHPMWFEKIERShgGPGSDKyPLWLQSVHPDKRLHSQLcESEELRETYTVQ 707
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 698 DREPITIHTEDAARFGIANGDLVRVWNKRGQILTGAVVTDGIKKGVVCVHEGAW--PDLEN---GLCKNGSANVLTADIP 772
Cdd:PRK15102 708 GREPVYINPQDAKARGIKDGDVVRVFNDRGQVLAGAVVSDRYPPGVIRIHEGAWygPDKGGeigALCTYGDPNTLTLDIG 787
|
810 820 830
....*....|....*....|....*....|...
gi 446098945 773 SSQLANACAGNSALVYIEKYTGNAPKLTAFDQP 805
Cdd:PRK15102 788 TSQLAQATSAHTCLVEIEKYQGKVPPVTSFNGP 820
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
24-791 |
0e+00 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 580.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 24 AAPLPAWAEEKGGKILTA-----GRWGAMNVEVKDGKIVSSTGAlaKTIPNSLQ------STAADQVHTTARIQHPMVRK 92
Cdd:COG0243 9 AGAGAAALEAAGTKTVKTtcpgcGVGCGLGVKVEDGRVVRVRGD--PDHPVNRGrlcakgAALDERLYSPDRLTYPMKRV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 93 SyldnplqpakGRGEDTYVQVSWEQALKLIHEQHDRIRKANGPSAIFAGSYGWRSSGVLHKAQTLLQRYMNLAG--GYSG 170
Cdd:COG0243 87 G----------PRGSGKFERISWDEALDLIAEKLKAIIDEYGPEAVAFYTSGGSAGRLSNEAAYLAQRFARALGtnNLDD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 171 HSgDYSTGAAQVIMPHVVGSvevYEQQTSWPLIlENSQVVVLWGMNPLNTLKIAWSstdeqglEYFHQLKKSGKPVIAID 250
Cdd:COG0243 157 NS-RLCHESAVAGLPRTFGS---DKGTVSYEDL-EHADLIVLWGSNPAENHPRLLR-------RLREAAKKRGAKIVVID 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 251 PIRSETIEFFGDnatWIAPNMGTDVALMLGIAHTLMTQGKHDKVFLEKYTTGYPQFEEYLTgksnntPKSAAWAAEITGV 330
Cdd:COG0243 225 PRRTETAAIADE---WLPIRPGTDAALLLALAHVLIEEGLYDRDFLARHTVGFDELAAYVA------AYTPEWAAEITGV 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 331 PEAQIVKLAELMA-ANRTMLMAGWGIQRQQYGEQKHWMLVTLAAMLGQIGTPGGGFGFSYHysnggnptrvggvlpemsa 409
Cdd:COG0243 296 PAEDIRELAREFAtAKPAVILWGMGLQQHSNGTQTVRAIANLALLTGNIGKPGGGPFSLTG------------------- 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 410 aiagqaseaaddggmtaipvarivDALENpGGKYQhngkeqtypnIKMIWWAGGGNFTHHQDTNRLIKAWQKPEMIVVSE 489
Cdd:COG0243 357 ------------------------EAILD-GKPYP----------IKALWVYGGNPAVSAPDTNRVREALRKLDFVVVID 401
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 490 CYWTAAAKHADIVLPITTSFERNDLTMTgdYSNQHIVPMKQAVAPQFEARNDFDVFADLAELLkpGGKEIYTEGKDEMAW 569
Cdd:COG0243 402 TFLTETARYADIVLPATTWLERDDIVTN--SEDRRVHLSRPAVEPPGEARSDWEIFAELAKRL--GFEEAFPWGRTEEDY 477
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 570 LKFFYDAaqkgARAQRVTmpmFNAFWQQNKLIEMRRSEkneqyvryGDFRADpvkNALGTPSGKIEIYSKTLEkfgykdC 649
Cdd:COG0243 478 LRELLEA----TRGRGIT---FEELREKGPVQLPVPPE--------PAFRND---GPFPTPSGKAEFYSETLA------L 533
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 650 PAHPTWLAPDEWKGTADEK-QLQLLTAHPAHRLHSQL-NYAELRKkyaVADREPITIHTEDAARFGIANGDLVRVWNKRG 727
Cdd:COG0243 534 PPLPRYAPPYEGAEPLDAEyPLRLITGRSRDQWHSTTyNNPRLRE---IGPRPVVEINPEDAAALGIKDGDLVRVESDRG 610
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446098945 728 QILTGAVVTDGIKKGVVCVHEGAWPDLENglCKNGSANVLTADiPSSQLANACAGNSALVYIEK 791
Cdd:COG0243 611 EVLARAKVTEGIRPGVVFAPHGWWYEPAD--DKGGNVNVLTPD-ATDPLSGTPAFKSVPVRVEK 671
|
|
| MopB_DmsA-EC |
cd02770 |
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
49-660 |
1.49e-125 |
|
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: 389.76 E-value: 1.49e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 49 VEVKDGKIVS-STGALAKTIPNSLQSTAA-------DQVHTTARIQHPMVRKSyldnplqpakGRGEDTYVQVSWEQALK 120
Cdd:cd02770 16 AHVKDGVITRiETDDTGDDDPGFHQIRAClrgrsqrKRVYNPDRLKYPMKRVG----------KRGEGKFVRISWDEALD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 121 LIHEQHDRIRKANGPSAIFAGsYGWRSSGVLHKAQTLLQRYMNLAGGYSGHSGDYSTGAAQVIMPHVVGSVEvyeqQTSW 200
Cdd:cd02770 86 TIASELKRIIEKYGNEAIYVN-YGTGTYGGVPAGRGAIARLLNLTGGYLNYYGTYSWAQITTATPYTYGAAA----SGSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 201 PLILENSQVVVLWGMNPlntlkiAWSSTDEQG-LEYFHQLKKSGKPVIAIDPIRSETIEFFGDNatWIAPNMGTDVALML 279
Cdd:cd02770 161 LDDLKDSKLVVLFGHNP------AETRMGGGGsTYYYLQAKKAGAKFIVIDPRYTDTAVTLADE--WIPIRPGTDAALVA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 280 GIAHTLMTQGKHDKVFLEKYTTGY-----PQ-------FEEYLTGK-SNNTPKSAAWAAEITGVPEAQIVKLA-ELMAAN 345
Cdd:cd02770 233 AMAYVMITENLHDQAFLDRYCVGFdaehlPEgappnesYKDYVLGTgYDGTPKTPEWASEITGVPAETIRRLArEIATTK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 346 RTMLMAGWGIQRQQYGEQKHWMLVTLAAMLGQIGTPGGGFGfsyhySNGGNPTRVGGVLPEMSAAIAgqaseaaddggmT 425
Cdd:cd02770 313 PAAILQGWGPQRHANGEQAARAIMMLAAMTGNVGIPGGNTG-----ARPGGSAYNGAGLPAGKNPVK------------T 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 426 AIPVARIVDALENPG----GKYQHNGKEQTYPNIKMIwWAGGGNF---THHQDTNR---LIKAWQKPEMIVVSECYWTAA 495
Cdd:cd02770 376 SIPCFMWTDAIERGEemtaDDGGVKGADKLKSNIKMI-WNYAGNTlinQHSDDNNTtraLLDDESKCEFIVVIDNFMTPS 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 496 AKHADIVLPITTSFERNDLTMTGDYSNQHIV-PMKQAVAPQFEARNDFDVFADLAELLkpGGKEIYTEGKDEMAWLKFFY 574
Cdd:cd02770 455 ARYADILLPDTTELEREDIVLTSNAGMMEYLiYSQKAIEPLYECKSDYEICAELAKRL--GVEDQFTEGKTEQEWLEELY 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 575 DAaqkgARAQRVTMPMFNAFwqQNKLIEMRRSEKneQYVRYGDFRADPVKNALGTPSGKIEIYSKTL-----EKFGYKDC 649
Cdd:cd02770 533 GQ----TRAKEPGLPTYEEF--REKGIYRVPRAL--PFVAFEDFREDPENNPLKTPSGKIEIYSKALadmakTLPEGDEI 604
|
650
....*....|.
gi 446098945 650 PAHPTWLAPDE 660
Cdd:cd02770 605 PAIPKYVPAWE 615
|
|
| PRK14990 |
PRK14990 |
anaerobic dimethyl sulfoxide reductase subunit A; Provisional |
89-791 |
3.00e-96 |
|
anaerobic dimethyl sulfoxide reductase subunit A; Provisional
Pssm-ID: 184952 [Multi-domain] Cd Length: 814 Bit Score: 318.13 E-value: 3.00e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 89 MVRKSY----LDNPLQPAKGRGEDTYVQVSWEQALKLIHEQHDRIRKANGPSAIF----AGSYGWRSSGVLHKAQTLLQR 160
Cdd:PRK14990 110 MRRRVYnpdrLKYPMKRVGARGEGKFERISWEEAYDIIATNMQRLIKEYGNESIYlnygTGTLGGTMTRSWPPGNTLVAR 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 161 YMNLAGGYSGHSGDYSTGAAQVIMPHVVGSvevYEQQTSwPLILENSQVVVLWGMNPLNTlkiawsSTDEQGLEYF--HQ 238
Cdd:PRK14990 190 LMNCCGGYLNHYGDYSSAQIAEGLNYTYGG---WADGNS-PSDIENSKLVVLFGNNPGET------RMSGGGVTYYleQA 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 239 LKKSGKPVIAIDPIRSETIEffGDNATWIAPNMGTDVALMLGIAHTLMTQGKHDKVFLEKYTTGYPQ------------F 306
Cdd:PRK14990 260 RQKSNARMIIIDPRYTDTGA--GREDEWIPIRPGTDAALVNGLAYVMITENLVDQPFLDKYCVGYDEktlpasapknghY 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 307 EEYLTGK-SNNTPKSAAWAAEITGVPEAQIVKLA-ELMAANRTMLMAGWGIQRQQYGEQKHWMLVTLAAMLGQIGTPGGG 384
Cdd:PRK14990 338 KAYILGEgPDGVAKTPEWASQITGVPADKIIKLArEIGSTKPAFISQGWGPQRHANGEIATRAISMLAILTGNVGINGGN 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 385 FGF---SYHYSNGGNPTRVGGVLPEMSAAIAGQASEAADDggMTAIPvarivDALEnpggkyqhnGKEQTYPNIKMIW-W 460
Cdd:PRK14990 418 SGAregSYSLPFVRMPTLENPIQTSISMFMWTDAIERGPE--MTALR-----DGVR---------GKDKLDVPIKMIWnY 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 461 AGGGNFTHHQDTNR---LIKAWQKPEMIVVSECYWTAAAKHADIVLPITTSFERNDLTMTGDYSN-QHIVPMKQAVAPQF 536
Cdd:PRK14990 482 AGNCLINQHSEINRtheILQDDKKCELIVVIDCHMTSSAKYADILLPDCTASEQMDFALDASCGNmSYVIFNDQVIKPRF 561
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 537 EARNDFDVFADLAELLkpGGKEIYTEGKDEMAWLKFFYDAAQKGARaqrvTMPMFNAFWQQNKLiemRRSEKNEQYVRYG 616
Cdd:PRK14990 562 ECKTIYEMTSELAKRL--GVEQQFTEGRTQEEWMRHLYAQSREAIP----ELPTFEEFRKQGIF---KKRDPQGHHVAYK 632
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 617 DFRADPVKNALGTPSGKIEIYSKTLEKFGykdcpahPTWLAP---------------DEWKGTADEK-QLQLLTAHPAHR 680
Cdd:PRK14990 633 AFREDPQANPLTTPSGKIEIYSQALADIA-------ATWELPegdvidplpiytpgfESYQDPLNKQyPLQLTGFHYKSR 705
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 681 LHSQLNYAELRKkyaVADREPITIHTEDAARFGIANGDLVRVWNKRGQILTGAVVTDGIKKGVVCVHEGAW--PDlENGL 758
Cdd:PRK14990 706 VHSTYGNVDVLK---AACRQEMWINPLDAQKRGINNGDKVRIFNDRGEVHIEAKVTPRMMPGVVALGEGAWydPD-AKRV 781
|
730 740 750
....*....|....*....|....*....|...
gi 446098945 759 CKNGSANVLTADIPSSqLANACAGNSALVYIEK 791
Cdd:PRK14990 782 DKGGCINVLTTQRPSP-LAKGNPSHTNLVQVEK 813
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
84-550 |
4.45e-86 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 277.36 E-value: 4.45e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 84 RIQHPMVRksyldnplqpakgRGEDTYVQVSWEQALKLIHEQHDRIRKANGPSAIF--AGSYGWRSSGVLHKAQTLLQRY 161
Cdd:pfam00384 1 RLKYPMVR-------------RGDGKFVRVSWDEALDLIAKKLKRIIKKYGPDAIAinGGSGGLTDVESLYALKKLLNRL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 162 MNLAGGYSGHSGDYSTGAAQvimphVVGSVEVYEQQ-TSWPLILENSQVVVLWGMNPLNTLKIAWSSTDEqgleyfhQLK 240
Cdd:pfam00384 68 GSKNGNTEDHNGDLCTAAAA-----AFGSDLRSNYLfNSSIADIENADLILLIGTNPREEAPILNARIRK-------AAL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 241 KSGKPVIAIDPIRSETIEFFgdnatWIAPNMGTDVALMLGIAHTLMTQGKHDKVFlekyttgypqfeeyltgksnntpks 320
Cdd:pfam00384 136 KGKAKVIVIGPRLDLTYADE-----HLGIKPGTDLALALAGAHVFIKELKKDKDF------------------------- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 321 aawaaeitgvpeaqivklaelmaANRTMLMAGWGIQRQQYGEQKHWMLVTLAAMLGQIGTPGGGFGFSYHYSNGGNPTrv 400
Cdd:pfam00384 186 -----------------------APKPIIIVGAGVLQRQDGEAIFRAIANLADLTGNIGRPGGGWNGLNILQGAASPV-- 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 401 ggvlpemsaaiagqaseAADDGGmtAIPVARIVDALENPGgkyqhngkeqtYPNIKMIWWAGGGNFTHHQDTNRLIKAWQ 480
Cdd:pfam00384 241 -----------------GALDLG--LVPGIKSVEMINAIK-----------KGGIKVLYLLGNNPFVTHADENRVVKALQ 290
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446098945 481 KPEMIVVSECYW-TAAAKHADIVLPITTSFERNDLTMTGDYSNQHivpMKQAVAPQFEARNDFDVFADLAE 550
Cdd:pfam00384 291 KLDLFVVYDGHHgDKTAKYADVILPAAAYTEKNGTYVNTEGRVQS---TKQAVPPPGEAREDWKILRALSE 358
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
44-552 |
1.29e-80 |
|
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: 263.42 E-value: 1.29e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 44 WGAMNVEVKDGKIVSSTGALAKTIPNSLQS----TAADQVHTTARIQHPMVRKSyldnplqpakgrGEDTYVQVSWEQAL 119
Cdd:cd00368 10 GCGILVYVKDGKVVRIEGDPNHPVNEGRLCdkgrAGLDGLYSPDRLKYPLIRVG------------GRGKFVPISWDEAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 120 KLIHEQHDRIRKANGPSAIFAGSYGWRSSGVLHKAQTLLqryMNLAGGYSGHSGDYSTGAAQVIMPHvvgsVEVYEQQTS 199
Cdd:cd00368 78 DEIAEKLKEIREKYGPDAIAFYGGGGASNEEAYLLQKLL---RALGSNNVDSHARLCHASAVAALKA----FGGGAPTNT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 200 WPLIlENSQVVVLWGMNPLNTLKIAWSstdeqgleYFHQLKKSGKPVIAIDPIRSETIEffgDNATWIAPNMGTDVALML 279
Cdd:cd00368 151 LADI-ENADLILLWGSNPAETHPVLAA--------RLRRAKKRGAKLIVIDPRRTETAA---KADEWLPIRPGTDAALAL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 280 giahtlmtqgkhdkvflekyttgypqfeeyltgksnntpksAAWAAEITGVPEAQIVKLAELMA-ANRTMLMAGWGIQRQ 358
Cdd:cd00368 219 -----------------------------------------AEWAAEITGVPAETIRALAREFAaAKRAVILWGMGLTQH 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 359 QYGEQKHWMLVTLAAMLGQIGTPGGGFGFsyhysnGGNPtrvggvlpemsaaiagqaseaaddggmtaipvarivdalen 438
Cdd:cd00368 258 TNGTQNVRAIANLAALTGNIGRPGGGLGP------GGNP----------------------------------------- 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 439 pggkyqhngkeqtypnikmiwwagggnFTHHQDTNRLIKAWQKPEMIVVSECYWTAAAKHADIVLPITTSFERNDLTMTG 518
Cdd:cd00368 291 ---------------------------LVSAPDANRVRAALKKLDFVVVIDIFMTETAAYADVVLPAATYLEKEGTYTNT 343
|
490 500 510
....*....|....*....|....*....|....
gi 446098945 519 DYsnqHIVPMKQAVAPQFEARNDFDVFADLAELL 552
Cdd:cd00368 344 EG---RVQLFRQAVEPPGEARSDWEILRELAKRL 374
|
|
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
46-654 |
6.51e-70 |
|
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: 238.69 E-value: 6.51e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 46 AMNVEVKDGKIVSSTGALAKTIPNSL--QSTAAD--QVHTTARIQHPMVRKsyldnplqpakGRGEDTYVQVSWEQALKL 121
Cdd:cd02766 13 SLLVTVEDGRIVRVEGDPAHPYTRGFicAKGARYveRVYSPDRLLTPLKRV-----------GRKGGQWERISWDEALDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 122 IHEQHDRIRKANGPSAI----FAGSYGWrssgvLHKAQtllQRYMNLAGGYSGHSGDYSTGAAQVIMPHVVGsvevyeqq 197
Cdd:cd02766 82 IAAKLKEIKAEYGPESIlpysYAGTMGL-----LQRAA---RGRFFHALGASELRGTICSGAGIEAQKYDFG-------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 198 TSW---PLILENSQVVVLWGMNPlntlkiawSSTDEQGLEYFHQLKKSGKPVIAIDPIRSETIEFfgdnATW-IAPNMGT 273
Cdd:cd02766 146 ASLgndPEDMVNADLIVIWGINP--------AATNIHLMRIIQEARKRGAKVVVIDPYRTATAAR----ADLhIQIRPGT 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 274 DVALMLGIAHTLMTQGKHDKVFLEKYTTGYPQFEEYLtgkSNNTPksaAWAAEITGVPEAQIVKLAELMA-ANRTMLMAG 352
Cdd:cd02766 214 DGALALGVAKVLFREGLYDRDFLARHTEGFEELKAHL---ETYTP---EWAAEITGVSAEEIEELARLYGeAKPPSIRLG 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 353 WGIQRQQYGEQK-HWmLVTLAAMLGQIGTPGGGFgfsyHYSNGGnptrvggvlpemsaaiagqaseaaddggmtaipvar 431
Cdd:cd02766 288 YGMQRYRNGGQNvRA-IDALPALTGNIGVPGGGA----FYSNSG------------------------------------ 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 432 ivdalenpggkyqhngkeqtyPNIKMIWWAGGGNFTHHQDTNRLIKAWQKP-EMIVVSECYWTAAAKHADIVLPITTSFE 510
Cdd:cd02766 327 ---------------------PPVKALWVYNSNPVAQAPDSNKVRKGLAREdLFVVVHDQFMTDTARYADIVLPATTFLE 385
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 511 RNDLtmTGDYSNQHIVPMKQAVAPQFEARNDFDVFADLAELLkpGGKEIYTEGkDEMAWLkffydaaqkgARAQRVTMPM 590
Cdd:cd02766 386 HEDV--YASYWHYYLQYNEPAIPPPGEARSNTEIFRELAKRL--GFGEPPFEE-SDEEWL----------DQALDGTGLP 450
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446098945 591 FnafwqqnkLIEMRRSEKNeqyVRYGDFRADPVK-NALGTPSGKIEIYSKTLEKFGykdCPAHPT 654
Cdd:cd02766 451 L--------EGIDLERLLG---PRKAGFPLVAWEdRGFPTPSGKFEFYSERAAKRG---LPPLPE 501
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
47-770 |
8.73e-67 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 234.78 E-value: 8.73e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 47 MNVEVKDGKIVSSTGALAKTIPNSLQ----STAADQVHTTARIQHPMVRKsyldnplqpakgrgEDTYVQVSWEQALKLI 122
Cdd:COG3383 20 IDLEVKDGKIVKVEGDPDHPVNRGRLcvkgRFGFEFVNSPDRLTTPLIRR--------------GGEFREVSWDEALDLV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 123 HEQHDRIRKANGPSAIfaGSYGwrSSGVLHKAQTLLQRYMNLAGG-----YSGHSGDYSTGAAqviMPHVVGSVEV---Y 194
Cdd:COG3383 86 AERLREIQAEHGPDAV--AFYG--SGQLTNEENYLLQKLARGVLGtnnidNNARLCMASAVAG---LKQSFGSDAPpnsY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 195 EQqtswpliLENSQVVVLWGMNPLNTLKIAWSstdeqgleYFHQLKKSGKPVIAIDPIRSETIEFfgdnAT-WIAPNMGT 273
Cdd:COG3383 159 DD-------IEEADVILVIGSNPAEAHPVLAR--------RIKKAKKNGAKLIVVDPRRTETARL----ADlHLQIKPGT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 274 DVALMLGIAHTLMTQGKHDKVFLEKYTTGypqFEEYLTGKSNNTPksaAWAAEITGVPEAQIVKLAELMA-ANRTMLMAG 352
Cdd:COG3383 220 DLALLNGLLHVIIEEGLVDEDFIAERTEG---FEELKASVAKYTP---ERVAEITGVPAEDIREAARLIAeAKRAMILWG 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 353 WGIQRQQYGEQKHWMLVTLAAMLGQIGTPGGGFGFSYHYSN-------GGNPTRVGGVLPEMSAAIAGQASEA------A 419
Cdd:COG3383 294 MGVNQHTQGTDNVNAIINLALATGNIGRPGTGPFPLTGQNNvqggrdmGALPNVLPGYRDVTDPEHRAKVADAwgvpplP 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 420 DDGGMTAIpvaRIVDALenpggkyqHNGKeqtypnIKMIWWAGGGNFTHHQDTNRLIKAWQKPEMIVVSECYWTAAAKHA 499
Cdd:COG3383 374 DKPGLTAV---EMFDAI--------ADGE------IKALWIIGENPAVSDPDANHVREALEKLEFLVVQDIFLTETAEYA 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 500 DIVLPITTSFERnDLTMTGdySNQHIVPMKQAVAPQFEARNDFDVFADLAELL-----KPGGKEIYtegkDEMAWLKFFY 574
Cdd:COG3383 437 DVVLPAASWAEK-DGTFTN--TERRVQRVRKAVEPPGEARPDWEIIAELARRLgygfdYDSPEEVF----DEIARLTPDY 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 575 daaqKGARAQRVtmpmfnafwqqnkliemrrseKNEQYVRYgdfradPV--KNALGTPsgkieIYSKtlEKFGYKDCPAH 652
Cdd:COG3383 510 ----SGISYERL---------------------EALGGVQW------PCpsEDHPGTP-----RLFT--GRFPTPDGKAR 551
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 653 ptwLAPDEWKGTA----DEKQLQLLTAHPAHRLHSQlnyAELRKKYAVADREP---ITIHTEDAARFGIANGDLVRVWNK 725
Cdd:COG3383 552 ---FVPVEYRPPAelpdEEYPLVLTTGRLLDQWHTG---TRTRRSPRLNKHAPepfVEIHPEDAARLGIKDGDLVRVSSR 625
|
730 740 750 760
....*....|....*....|....*....|....*....|....*..
gi 446098945 726 RGQILTGAVVTDGIKKGVVCV--HegaWPDlenglcknGSANVLTAD 770
Cdd:COG3383 626 RGEVVLRARVTDRVRPGTVFMpfH---WGE--------GAANALTND 661
|
|
| MopB_CT_DMSOR-BSOR-TMAOR |
cd02793 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
669-791 |
1.86e-66 |
|
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: 216.73 E-value: 1.86e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 669 QLQLLTAHPAHRLHSQLNYAELRKKYAVADREPITIHTEDAARFGIANGDLVRVWNKRGQILTGAVVTDGIKKGVVCVHE 748
Cdd:cd02793 2 PLHLLSNQPATRLHSQLDHGSLSRAYKVQGREPIRINPADAAARGIADGDIVRVFNDRGACLAGAVVTDGIMPGVVQLPT 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 446098945 749 GAWPDLE-----NGLCKNGSANVLTADIPSSQLANACAGNSALVYIEK 791
Cdd:cd02793 82 GAWYDPDdpgepGPLCKHGNPNVLTLDIGTSSLAQGCSAQTCLVQIEK 129
|
|
| MopB_CT_DMSOR-like |
cd02777 |
The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
670-791 |
2.67e-57 |
|
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: 191.64 E-value: 2.67e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 670 LQLLTAHPAHRLHSQL-NYAELRKKYAVADREPITIHTEDAARFGIANGDLVRVWNKRGQILTGAVVTDGIKKGVVCVHE 748
Cdd:cd02777 3 LQLISPHPKRRLHSQLdNVPWLREAYKVKGREPVWINPLDAAARGIKDGDIVRVFNDRGAVLAGARVTDRIMPGVVALPE 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 446098945 749 GAW--PDLENGLCKNGSANVLTADIPSSQLANACAGNSALVYIEK 791
Cdd:cd02777 83 GAWydPDDNGGLDKGGNPNVLTSDIPTSKLAQGNPANTCLVEIEK 127
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
49-658 |
2.74e-56 |
|
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: 200.61 E-value: 2.74e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 49 VEVKDGKIVSSTGALAKTIPNS---LQSTAAD-QVHTTARIQHPMVRKsyldNPlqpakgRGEDTYVQVSWEQALKLIHE 124
Cdd:cd02759 15 VYVKDGKLVKVEGDPNHPTNKGrlcMRGLAAPeIVYHPDRLLYPLKRV----GE------RGENKWERISWDEALDEIAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 125 QHDRIRKANGPSAIfaGSYGWRSSGVLHKAQTLLQRYMNLAGG----YSGHSGDYSTGAAqviMPHVVGSVEVYEQqTSW 200
Cdd:cd02759 85 KLAEIKAEYGPESI--ATAVGTGRGTMWQDSLFWIRFVRLFGSpnlfLSGESCYWPRDMA---HALTTGFGLGYDE-PDW 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 201 plilENSQVVVLWGMNPLNTlkiawsSTDEQGlEYFHQLKKSGKPVIAIDPIRSETIEffgDNATWIAPNMGTDVALMLG 280
Cdd:cd02759 159 ----ENPECIVLWGKNPLNS------NLDLQG-HWLVAAMKRGAKLIVVDPRLTWLAA---RADLWLPIRPGTDAALALG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 281 IAHTLMTQGKHDKVFLEKYTTGypqFEEYLTGKSNNTPksaAWAAEITGVPEAQIVKLAELMAANRTMLMAgWG--IQRQ 358
Cdd:cd02759 225 MLNVIINEGLYDKDFVENWCYG---FEELAERVQEYTP---EKVAEITGVPAEKIRKAARLYATAKPACIQ-WGlaIDQQ 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 359 QYGEQKHWMLVTLAAMLGQIGTPGGGFGFSYhysnggnptrvggvlpemsaaiagqaseaaddggmtaipvarivdalen 438
Cdd:cd02759 298 KNGTQTSRAIAILRAITGNLDVPGGNLLIPY------------------------------------------------- 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 439 pggkyqhngkeqtypNIKMIWWAGGGNFTHHQDTNRLIKAWQKPEMIVVSECYWTAAAKHADIVLPITTSFERNDLtMTG 518
Cdd:cd02759 329 ---------------PVKMLIVFGTNPLASYADTAPVLEALKALDFIVVVDLFMTPTAMLADIVLPVAMSLERPGL-RGG 392
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 519 DYSNQHIVPMKQAVAPQFEARNDFDVFADLAELLkpggkeiyteGKDEMAWLKFfydaaqKGARAQRVTMPMFNafwqqn 598
Cdd:cd02759 393 FEAENFVQLRQKAVEPYGEAKSDYEIVLELGKRL----------GPEEAEYYKY------EKGLLRPDGQPGFN------ 450
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 599 kliemrrsekneqyvrygdfradpvknalgTPSGKIEIYSKTLEKFGYkdcPAHPTWLAP 658
Cdd:cd02759 451 ------------------------------TPTGKVELYSTMLEELGY---DPLPYYREP 477
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
1-749 |
1.22e-41 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 163.30 E-value: 1.22e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 1 MTLTRREFIKHSGIAAGALVVTSAAP--LPAW--AEEKGGKILTAG-------RWgAMNVEVKDGKIVSSTG-ALAKTIP 68
Cdd:PRK15488 1 MSLSRRDFLKGAGAGCAACALGSLLPgaLAANeiAQLKGKTKLTPSicemcstRC-PIEARVVNGKNVFIQGnPKAKSFG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 69 NSL---QSTAADQVHTTARIQHPMVRksyldnplqpAKGRGEDTYVQVSWEQALKLIHEQHDRIRKANGPSAI-FAGSYG 144
Cdd:PRK15488 80 TKVcarGGSGHSLLYDPQRIVKPLKR----------VGERGEGKWQEISWDEAYQEIAAKLNAIKQQHGPESVaFSSKSG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 145 WRSSGVLHKAQtllqrymnlAGGYSGHSGDYST--GAAQVIMPHVVGsvevyeqqTSWPLILENSQVVVLWGMNPLNTLK 222
Cdd:PRK15488 150 SLSSHLFHLAT---------AFGSPNTFTHASTcpAGYAIAAKVMFG--------GKLKRDLANSKYIINFGHNLYEGIN 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 223 IAwsstDEQGLEYFhQLKKSGKpVIAIDPIRSetieFFGDNAT-WIAPNMGTDVALMLGIAHTLMTQGKHDKVFLEKYTT 301
Cdd:PRK15488 213 MS----DTRGLMTA-QMEKGAK-LVVFEPRFS----VVASKADeWHAIRPGTDLAVVLALCHVLIEENLYDKAFVERYTS 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 302 GYPQFEEYLTGKsnnTPKsaaWAAEITGVPEAQIVKLAELMAANRTMLMAGWG----IQRQQYGEQKhwMLVTLAAMLGQ 377
Cdd:PRK15488 283 GFEELAASVKEY---TPE---WAEAISDVPADDIRRIARELAAAAPHAIVDFGhratFTPEEFDMRR--AIFAANVLLGN 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 378 IGTPGGGFGfsyhysnGGNPTRVGGVLPEMSAAIAGQaseaADDGGMTAIPVARIvdalenpggkyqhngkEQTYPNIKM 457
Cdd:PRK15488 355 IERKGGLYF-------GKNASVYNKLAGEKVAPTLAK----PGVKGMPKPTAKRI----------------DLVGEQFKY 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 458 IWWAGG----------------------GNFTHHQ---DTNRLIKAWQKPEMIVVSECYWTAAAKHADIVLPITTSFERN 512
Cdd:PRK15488 408 IAAGGGvvqsiidatltqkpyqikgwvmSRHNPMQtvtDRADVVKALKKLDLVVVCDVYLSESAAYADVVLPESTYLERD 487
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 513 DltMTGDYSNQHIVPM--KQAVAPQFEARNDFDVFADLAELLKPGgkEIYTEgkDEMAWLKFFydaaqkgaraqrvtmpm 590
Cdd:PRK15488 488 E--EISDKSGKNPAYAlrQRVVEPIGDTKPSWQIFKELGEKMGLG--QYYPW--QDMETLQLY----------------- 544
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 591 fnafwQQNKLIEMRRSEKNEQYVRYG------------DFRAD-PVKNALG------------TPSGKIEIYSKTLEKF- 644
Cdd:PRK15488 545 -----QVNGDHALLKELKKKGYVSFGvplllrepkmvaKFVARyPNAKAVDedgtygsqlkfkTPSGKIELFSAKLEALa 619
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 645 ------GYKDCPahptwlapdewkgTADEKQLQLLTAHPAHRLHSQLNY----AELRKKyavadrEPITIHTEDAARFGI 714
Cdd:PRK15488 620 pgygvpRYRDVA-------------LKKEDELYFIQGKVAVHTNGATQNvpllANLMSD------NAVWIHPQTAGKLGI 680
|
810 820 830
....*....|....*....|....*....|....*
gi 446098945 715 ANGDLVRVWNKRGQILTGAVVTDGIKKGVVCVHEG 749
Cdd:PRK15488 681 KNGDEIRLENSVGKEKGKALVTPGIRPDTLFAYMG 715
|
|
| MopB_4 |
cd02765 |
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
46-653 |
1.25e-41 |
|
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: 160.72 E-value: 1.25e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 46 AMNVEVKDGKIVSSTGAL--AKTIPN--SLQSTAADQVHTTARIQHPMVRKSYldnplqpakgRGEDTYVQVSWEQALKL 121
Cdd:cd02765 13 PLKCHVRDGKIVKVEPNEwpDKTYKRgcTRGLSHLQRVYSPDRLKYPMKRVGE----------RGEGKFERITWDEALDT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 122 IHEQHDRIRKANGPSAIfagsyGWR-SSGVLHKAQTLLQRYMNlAGGYSGHSGDYSTGAAQVIMPhVVGSVEVYEQQTsw 200
Cdd:cd02765 83 IADKLTEAKREYGGKSI-----LWMsSSGDGAILSYLRLALLG-GGLQDALTYGIDTGVGQGFNR-VTGGGFMPPTNE-- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 201 PLILENSQVVVLWGMNPLntlkiawsSTDEQGLEYFHQLKKSGKPVIAIDPIRSETIEffgDNATWIAPNMGTDVALMLG 280
Cdd:cd02765 154 ITDWVNAKTIIIWGSNIL--------ETQFQDAEFFLDARENGAKIVVIDPVYSTTAA---KADQWVPIRPGTDPALALG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 281 IAHTLMTQGKHDKVFLEKYT-------------------TGYPQFEEYLTGKSN-NTPKSAA------------------ 322
Cdd:cd02765 223 MINYILEHNWYDEAFLKSNTsapflvredngtllrqadvTATPAEDGYVVWDTNsDSPEPVAatninpalegeytingvk 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 323 ------------------WAAEITGVPEAQIVKLAELMAANR-TMLMAGWGIQRQQYGEQKHWMLVTLAAMLGQIGTPGG 383
Cdd:cd02765 303 vhtvltalreqaasyppkAAAEICGLEEAIIETLAEWYATGKpSGIWGFGGVDRYYHSHVFGRTAAILAALTGNIGRVGG 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 384 GFGfsyhysnggnptrvggvlpemsaaiagqaseaaddggmtaipvarivdalenpggkyqhngkeqtypNIKMIWWaGG 463
Cdd:cd02765 383 GVG-------------------------------------------------------------------QIKFMYF-MG 394
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 464 GNFTHHQDTNRLIKAWQKP-EMIVVSECYWTAAAKHADIVLPITTSFERNDLTMTgdYSNQ-HIVPMKQAVAPQFEARND 541
Cdd:cd02765 395 SNFLGNQPDRDRWLKVMKNlDFIVVVDIFHTPTVRYADIVLPAAHWFEVEDLLVR--YTTHpHVLLQQKAIEPLFESKSD 472
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 542 FDVFADLAELLKPGGKeiytEGKDEMAWLKFFYDAaqKGARAQRVTMPMFNAfwqqNKLIeMRRSEKNEQYVRYGDfrad 621
Cdd:cd02765 473 FEIEKGLAERLGLGDY----FPKTPEDYVRAFMNS--DDPALDGITWEALKE----EGII-MRLATPEDPYVAYLD---- 537
|
650 660 670
....*....|....*....|....*....|..
gi 446098945 622 pvkNALGTPSGKIEIYSKTLEKFgyKDCPAHP 653
Cdd:cd02765 538 ---QKFGTPSGKLEFYNEAAPEL--EEALPLP 564
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
47-568 |
1.92e-41 |
|
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: 159.30 E-value: 1.92e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 47 MNVEVKDGKIVSSTGAlaKTIPNSLQST------AADQVHTTARIQHPMVRKsyldnplqpakgrgEDTYVQVSWEQALK 120
Cdd:cd02753 13 LELWVKDNKIVGVEPV--KGHPVNRGKLcvkgrfGFDFVNSKDRLTKPLIRK--------------NGKFVEASWDEALS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 121 LIHEQHDRIRKANGPSAIfaGSYGwrSSGVLHKAQTLLQRYMNLAGGYSG--------HSgdySTGAAqviMPHVVGS-- 190
Cdd:cd02753 77 LVASRLKEIKDKYGPDAI--AFFG--SAKCTNEENYLFQKLARAVGGTNNvdhcarlcHS---PTVAG---LAETLGSga 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 191 --VEVYEqqtswpliLENSQVVVLWGMNPLNTLKIAWSstdeqgleYFHQLKKSGKPVIAIDPIRSETIEFfgdNATWIA 268
Cdd:cd02753 147 mtNSIAD--------IEEADVILVIGSNTTEAHPVIAR--------RIKRAKRNGAKLIVADPRRTELARF---ADLHLQ 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 269 PNMGTDVALMLGIAHTLMTQGKHDKVFLEKYTTGYPQFEEYLtgkSNNTPKSaawAAEITGVPEAQIVKLAELMA-ANRT 347
Cdd:cd02753 208 LRPGTDVALLNAMAHVIIEEGLYDEEFIEERTEGFEELKEIV---EKYTPEY---AERITGVPAEDIREAARMYAtAKSA 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 348 MLMAGWGIQRQQYGEQKHWMLVTLAAMLGQIGTPGGgfgfsyhysnGGNPTRvggvlpemsaaiaGQA-SEAADDggMTA 426
Cdd:cd02753 282 AILWGMGVTQHSHGTDNVMALSNLALLTGNIGRPGT----------GVNPLR-------------GQNnVQGACD--MGA 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 427 IPVarivdalenpggkyqhngkeqTYPN-IKMIWWAGGGNFTHHQDTNRLIKAWQKPEMIVVSECYWTAAAKHADIVLPI 505
Cdd:cd02753 337 LPN---------------------VLPGyVKALYIMGENPALSDPNTNHVRKALESLEFLVVQDIFLTETAELADVVLPA 395
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446098945 506 TTSFERNdltmtGDYSN--QHIVPMKQAVAPQFEARNDFDVFADLAELLkpGGKEIYTEGK---DEMA 568
Cdd:cd02753 396 ASFAEKD-----GTFTNteRRVQRVRKAVEPPGEARPDWEIIQELANRL--GYPGFYSHPEeifDEIA 456
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
73-570 |
2.62e-39 |
|
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: 153.92 E-value: 2.62e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 73 STAADQVHTTARIQHPMVRksyldnplqpakgRGEDTYVQVSWEQALKLIHEQHDRIRKANGPSAIfagsyGWRSSGvlh 152
Cdd:cd02754 43 LNLHKTLNGPERLTRPLLR-------------RNGGELVPVSWDEALDLIAERFKAIQAEYGPDSV-----AFYGSG--- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 153 kaQTLLQRYM---NLAGGYSGHSG-DYST----GAAQVIMPHVVGSVEV---YEQqtswpliLENSQVVVLWGMNPLNTL 221
Cdd:cd02754 102 --QLLTEEYYaanKLAKGGLGTNNiDTNSrlcmASAVAGYKRSFGADGPpgsYDD-------IEHADCFFLIGSNMAECH 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 222 KIAWSstdeqgleYFHQLKKSGKP--VIAIDPIRSETieffGDNAT-WIAPNMGTDVALMLGIAHTLMTQGKHDKVFLEK 298
Cdd:cd02754 173 PILFR--------RLLDRKKANPGakIIVVDPRRTRT----ADIADlHLPIRPGTDLALLNGLLHVLIEEGLIDRDFIDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 299 YTTGYPQFEEYLtgkSNNTPksaAWAAEITGVPEAQIVKLAELMA-ANRTMLMAGWGIQRQQYGEQKHWMLVTLAAMLGQ 377
Cdd:cd02754 241 HTEGFEELKAFV---ADYTP---EKVAEITGVPEADIREAARLFGeARKVMSLWTMGVNQSTQGTAANNAIINLHLATGK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 378 IGTPGGGFGfsyhySNGGNP----TRVGGVLPEMSAAIAGQAS-----EAADDGGM--TAIPVARIVDALENPggKYQHN 446
Cdd:cd02754 315 IGRPGSGPF-----SLTGQPnamgGREVGGLANLLPGHRSVNNpehraEVAKFWGVpeGTIPPKPGLHAVEMF--EAIED 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 447 GKeqtypnIKMIWWAGGGNFTHHQDTNRLIKAWQKPEMIVVSECYW-TAAAKHADIVLPITTSFERnDLTMTGdySNQHI 525
Cdd:cd02754 388 GE------IKALWVMCTNPAVSLPNANRVREALERLEFVVVQDAFAdTETAEYADLVLPAASWGEK-EGTMTN--SERRV 458
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 446098945 526 VPMKQAVAPQFEARNDFDVFADLAELLKPGG-------KEIYtegkDEMAWL 570
Cdd:cd02754 459 SLLRAAVEPPGEARPDWWILADVARRLGFGElfpytspEEVF----EEYRRL 506
|
|
| MopB_Nitrate-R-NarG-like |
cd02750 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
84-549 |
2.12e-38 |
|
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: 149.39 E-value: 2.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 84 RIQHPMVRKSyldnplqpakGRGEDTYVQVSWEQALKLIHEQHDRIRKANGPSAIFAGSygwRSSGVLHKAQTLLQRYMN 163
Cdd:cd02750 66 RVKYPLKRVG----------ARGEGKWKRISWDEALELIADAIIDTIKKYGPDRVIGFS---PIPAMSMVSYAAGSRFAS 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 164 LAGGYSGH----SGDYSTGAAQVIMPhvvgSVEVYEqqtswPLILENSQVVVLWGMNPLNTlkiawSSTDEQgleYFHQL 239
Cdd:cd02750 133 LIGGVSLSfydwYGDLPPGSPQTWGE----QTDVPE-----SADWYNADYIIMWGSNVPVT-----RTPDAH---FLTEA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 240 KKSGKPVIAIDPIRSETIEFfGDnaTWIAPNMGTDVALMLGIAHTLMTQGKHDKVFLEKYTTgYPqfeeYLTgksnNTPk 319
Cdd:cd02750 196 RYNGAKVVVVSPDYSPSAKH-AD--LWVPIKPGTDAALALAMAHVIIKEKLYDEDYLKEYTD-LP----FLV----YTP- 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 320 saAWAAEITGVPEAQIVKLAELMAAN-RTMLMAGWGIQRQQYGEQKHWMLVTLAAMLGQIGTPGGGFGfsyHYsnggnpt 398
Cdd:cd02750 263 --AWQEAITGVPRETVIRLAREFATNgRSMIIVGAGINHWYHGDLCYRALILLLALTGNEGKNGGGWA---HY------- 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 399 rvggvlpemsaaiAGQaseaaddggmtaipvarivdalenpggkyqhngkeqtyPNIKMIWWaggGN-FTHHQDTNRLIK 477
Cdd:cd02750 331 -------------VGQ--------------------------------------PRVLFVWR---GNlFGSSGKGHEYFE 356
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446098945 478 A--WQKPEMIVVSECYWTAAAKHADIVLPITTSFERNDLTMTGdySNQHIVPMKQAVAPQFEARNDFDVFADLA 549
Cdd:cd02750 357 DapEGKLDLIVDLDFRMDSTALYSDIVLPAATWYEKHDLSTTD--MHPFIHPFSPAVDPLWEAKSDWEIFKALA 428
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
49-655 |
7.64e-35 |
|
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: 138.58 E-value: 7.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 49 VEVKDGKIVSSTGAlaktiPNSLQS---------TAADQVHTTARIQHPMVRksyldnplqpAKGRGEDTYVQVSWEQAL 119
Cdd:cd02755 16 ARVEDGRVVKIDGN-----PLSPLSrgklcargnAGIQLLYDPDRLKKPLIR----------VGERGEGKFREASWDEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 120 KLIHEQHDRIRKANGP-SAIFAGSYGWRSSGVLHKAQTLlQRYmNLAGGYSGHSGDYSTGAAQVIMPHvvGSVEVYEqqt 198
Cdd:cd02755 81 QYIASKLKEIKEQHGPeSVLFGGHGGCYSPFFKHFAAAF-GSP-NIFSHESTCLASKNLAWKLVIDSF--GGEVNPD--- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 199 swpliLENSQVVVLWGMNplntLKIAWSSTDEQGleyFHQLKKSGKPVIAIDPIRSETIEFFGDnatWIAPNMGTDVALM 278
Cdd:cd02755 154 -----FENARYIILFGRN----LAEAIIVVDARR---LMKALENGAKVVVVDPRFSELASKADE---WIPIKPGTDLAFV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 279 LGIAHTLMTQGKHDKVFLEKYTTGypqFEEYLTGKSNNTPksaAWAAEITGVPEAQIVKLA-ELMA-ANRTMLMAGWgiq 356
Cdd:cd02755 219 LALIHVLISENLYDAAFVEKYTNG---FELLKAHVKPYTP---EWAAQITDIPADTIRRIArEFAAaAPHAVVDPGW--- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 357 rqqygeqkhwmlvtlaamlgqigtpgggFGFSYHYSNggnptrvggvlpEMSAAIAgqaseaaddggmtaipvarIVDAL 436
Cdd:cd02755 290 ----------------------------RGTFYSNSF------------QTRRAIA-------------------IINAL 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 437 ----ENPGGKYQhNGKEQTYPnIKMIWWAGGGNFTHHQDTNRLIKAWQKPEMIVVSECYWTAAAKHADIVLPITTSFERN 512
Cdd:cd02755 311 lgniDKRGGLYY-AGSAKPYP-IKALFIYRTNPFHSMPDRARLIKALKNLDLVVAIDILPSDTALYADVILPEATYLERD 388
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 513 DLTMTGDYSNQHIVPMKQAVAPQFEARNDFDVFADLAEllkpggkeiytegkdemawlkffydaaqkgaraqrvtmpmfn 592
Cdd:cd02755 389 EPFSDKGGPAPAVATRQRAIEPLYDTRPGWDILKELAR------------------------------------------ 426
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446098945 593 afwqqnkliemrrsekneqyvRYGDFradpvknalGTPSGKIEIYSKTLEKFGYKdcpahPTW 655
Cdd:cd02755 427 ---------------------RLGLF---------GTPSGKIELYSPILAKAGYD-----PLP 454
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
49-553 |
1.86e-34 |
|
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: 139.07 E-value: 1.86e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 49 VEVKDGKIVSSTG----ALAK--TIPNSLQSTAADqvHTTARIQHPMVRKSyldnplqpakgrgeDTYVQVSWEQALKLI 122
Cdd:cd02762 15 VTVEDGRVASIRGdpddPLSKgyICPKAAALGDYQ--NDPDRLRTPMRRRG--------------GSFEEIDWDEAFDEI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 123 HEQHDRIRKANGPSAIF---AGSYGWRSSGVLHKAQtlLQRYMNLAGGYSGHSGDYstgaaqviMPHVVGSVEVYEQQTS 199
Cdd:cd02762 79 AERLRAIRARHGGDAVGvygGNPQAHTHAGGAYSPA--LLKALGTSNYFSAATADQ--------KPGHFWSGLMFGHPGL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 200 WPLI-LENSQVVVLWGMNPLNTLKIAWSSTDEQGLeyFHQLKKSGKPVIAIDPIRSETIEFfGDNATWIAPnmGTDVALM 278
Cdd:cd02762 149 HPVPdIDRTDYLLILGANPLQSNGSLRTAPDRVLR--LKAAKDRGGSLVVIDPRRTETAKL-ADEHLFVRP--GTDAWLL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 279 LGIAHTLMTQGKHDKVFLEKYTTGYPQFEEYLTgksnntPKSAAWAAEITGVPEAQIVKLA-ELMAANRTMLMAGWGIQR 357
Cdd:cd02762 224 AAMLAVLLAEGLTDRRFLAEHCDGLDEVRAALA------EFTPEAYAPRCGVPAETIRRLArEFAAAPSAAVYGRLGVQT 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 358 QQYGEQKHWMLVTLAAMLGQIGTPGG---------GFGFS--YHYSNGGNPTRVGGvLPEmsaaIAGQaseaaddggmta 426
Cdd:cd02762 298 QLFGTLCSWLVKLLNLLTGNLDRPGGamfttpaldLVGQTsgRTIGRGEWRSRVSG-LPE----IAGE------------ 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 427 IPVARIVDALENPGGKyqhngkeqtypNIK-MIWWAGggNFTHHQ-DTNRLIKAWQKPEMIVVSECYWTAAAKHADIVLP 504
Cdd:cd02762 361 LPVNVLAEEILTDGPG-----------RIRaMIVVAG--NPVLSApDGARLEAALGGLEFMVSVDVYMTETTRHADYILP 427
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 446098945 505 ITTSFERNDLTMTGDYSNQHIVPMKQAVAPQFEAR-NDFDVFADLAELLK 553
Cdd:cd02762 428 PASQLEKPHATFFNLEFPRNAFRYRRPLFPPPPGTlPEWEILARLVEALD 477
|
|
| MopB_Arsenate-R |
cd02757 |
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ... |
44-645 |
1.04e-25 |
|
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: 112.15 E-value: 1.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 44 WGAMNVEVKDGKIV---------SSTGALAKTIPNSLQstaadQVHTTARIQHPMVRKSyldnplqPAKGRGED-TYVQV 113
Cdd:cd02757 12 WCGLQAYVEDGRVTkvegnplhpGSRGRLCAKGHLGLQ-----QVYDPDRILYPMKRTN-------PRKGRDVDpKFVPI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 114 SWEQALKLIHEQHDRIRKANGPS--AIFAGSYGwrssgvlHKAQTLLQRYMNLAG--GYSGHSGdystgaaqvimphVVG 189
Cdd:cd02757 80 SWDEALDTIADKIRALRKENEPHkiMLHRGRYG-------HNNSILYGRFTKMIGspNNISHSS-------------VCA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 190 SVEVYEQQTSWPLI------LENSQVVVLWGMNPL-------NTLKIaWSSTDEQGleyfhqlkksgkPVIAIDPiRSET 256
Cdd:cd02757 140 ESEKFGRYYTEGGWdynsydYANAKYILFFGADPLesnrqnpHAQRI-WGGKMDQA------------KVVVVDP-RLSN 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 257 IEFFGDNatWIAPNMGTDVALMLGIAHTLMTQGKHDKVFL-------EKYTTGYPQFEEYLTGKSNN------------- 316
Cdd:cd02757 206 TAAKADE--WLPIKPGEDGALALAIAHVILTEGLWDKDFVgdfvdgkNYFKAGETVDEESFKEKSTEglvkwwnlelkdy 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 317 TPKsaaWAAEITGVPEAQIVKLAELMA--ANRTMLMAGWGIQRQQYGEQKHWMLVTLAAMLGQIGTPGGGFgfsyhySNG 394
Cdd:cd02757 284 TPE---WAAKISGIPAETIERVAREFAtaAPAAAAFTWRGATMQNRGSYNSMACHALNGLVGSIDSKGGLC------PNM 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 395 GNptrvggvlPEMSAAIAgqaseaaddggmtaipvarivdalenpggkYQHNgkeqtyPNikmiwWAGGGNFthhqdtnR 474
Cdd:cd02757 355 GV--------PKIKVYFT------------------------------YLDN------PV-----FSNPDGM-------S 378
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 475 LIKAWQKPEMIVVSECYWTAAAKHADIVLPITTSFERNDLTMTGDYSNQHIVPMKQAVAPQFEARNDFDVFADLAELLKP 554
Cdd:cd02757 379 WEEALAKIPFHVHLSPFMSETTYFADIVLPDGHHFERWDVMSQENNLHPWLSIRQPVVKSLGEVREETEILIELAKKLDP 458
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 555 GGKEiytegkdemawlkffydaaqkgaraqrvtmpmfnafwqqnkliEMRRSEkNEQYVRYGDFRADP--VKNALGTPSG 632
Cdd:cd02757 459 KGSD-------------------------------------------GMKRYA-PGQFKDPETGKNNRweFENVFPTETG 494
|
650
....*....|...
gi 446098945 633 KIEIYSKTLEKFG 645
Cdd:cd02757 495 KFEFYSETLKKYL 507
|
|
| MopB_CT_DmsA-EC |
cd02794 |
The MopB_CT_DmsA-EC CD includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
670-791 |
3.50e-24 |
|
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: 98.13 E-value: 3.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 670 LQLLTAHPAHRLHSQL-NYAELRKkyavADREPITIHTEDAARFGIANGDLVRVWNKRGQILTGAVVTDGIKKGVVCVHE 748
Cdd:cd02794 3 LQLIGWHYKRRTHSTFdNVPWLRE----AFPQEVWINPLDAAARGIKDGDRVLVFNDRGKVIRPVKVTERIMPGVVALPQ 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 446098945 749 GAW--PDlENGLCKNGSANVLTADIPSSqLANACAGNSALVYIEK 791
Cdd:cd02794 79 GAWyePD-ANGIDKGGCINTLTGLRPSP-LAKGNPQHTNLVQVEK 121
|
|
| Molydop_binding |
pfam01568 |
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
670-775 |
1.54e-22 |
|
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: 93.11 E-value: 1.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 670 LQLLTAHPAHRLHSQLNYAELRKKYAVAdREPITIHTEDAARFGIANGDLVRVWNKRGQILTGAVVTDGIKKGVVCVHEG 749
Cdd:pfam01568 1 LYLITGRVLGQYHSQTRTRRVLRLAKPE-PEVVEIHPEDAAALGIKDGDLVEVTSRRGSVVVRAKVTDRVRPGVVFMPFG 79
|
90 100
....*....|....*....|....*...
gi 446098945 750 AWPDlenglCKNGSANVLTADI--PSSQ 775
Cdd:pfam01568 80 WWYE-----PRGGNANALTDDAtdPLSG 102
|
|
| MopB_CT |
cd02775 |
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a ... |
677-774 |
3.79e-21 |
|
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: 88.92 E-value: 3.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 677 PAHRLHSQL--NYAELRkkyAVADREPITIHTEDAARFGIANGDLVRVWNKRGQILTGAVVTDGIKKGVVCVHEGAWPDL 754
Cdd:cd02775 1 LRDHFHSGTrtRNPWLR---ELAPEPVVEINPEDAAALGIKDGDLVRVESRRGSVVLRAKVTDGVPPGVVFLPHGWGHRG 77
|
90 100
....*....|....*....|
gi 446098945 755 ENGlcknGSANVLTADIPSS 774
Cdd:cd02775 78 GRG----GNANVLTPDALDP 93
|
|
| MopB_ydeP |
cd02767 |
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
84-563 |
1.13e-20 |
|
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: 96.99 E-value: 1.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 84 RIQHPMVRKsyldnplqpakgRGEDTYVQVSWEQALKLIHEqhdRIRKANGPSAIFAGSyGwRSSgvlHKAQTLLQRYMN 163
Cdd:cd02767 64 RLTYPMRYD------------AGSDHYRPISWDEAFAEIAA---RLRALDPDRAAFYTS-G-RAS---NEAAYLYQLFAR 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 164 LAG-------GYSGHSgdySTGAAqviMPHVVGSVE---VYEQqtswpliLENSQVVVLWGMNPlntlkiawSSTDEQGL 233
Cdd:cd02767 124 AYGtnnlpdcSNMCHE---PSSVG---LKKSIGVGKgtvSLED-------FEHTDLIFFIGQNP--------GTNHPRML 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 234 EYFHQLKKSGKPVIAIDPIRSETIEFFGD---------NATWIA-----PNMGTDVALMLGIAHTLMTQGKH-----DKV 294
Cdd:cd02767 183 HYLREAKKRGGKIIVINPLREPGLERFANpqnpesmltGGTKIAdeyfqVRIGGDIALLNGMAKHLIERDDEpgnvlDHD 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 295 FLEKYTTGYPQFEEYLtgksnntpKSAAWaAEI---TGVPEAQIVKLAEL-MAANRTMLMAGWGIQRQQYGEQKHWMLVT 370
Cdd:cd02767 263 FIAEHTSGFEEYVAAL--------RALSW-DEIeraSGLSREEIEAFAAMyAKSERVVFVWGMGITQHAHGVDNVRAIVN 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 371 LAAMLGQIGTPGGGFGFSYHYSN--GGnptRVGGVLPEMSAAIAGQASE-----AADDGGMTAipvariVDALENpggky 443
Cdd:cd02767 334 LALLRGNIGRPGAGLMPIRGHSNvqGD---RTMGITEKPFPEFLDALEEvfgftPPRDPGLDT------VEAIEA----- 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 444 QHNGKeqtypnIKmIWWAGGGNF-THHQDTNRLIKAWQKPEMIV-VSECYWTAAAKHAD--IVLPITTSFERnDLTMTGD 519
Cdd:cd02767 400 ALEGK------VK-AFISLGGNFaEAMPDPAATEEALRRLDLTVhVATKLNRSHLVHGEeaLILPCLGRTEI-DMQAGGA 471
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446098945 520 YSNQHIVPMKQAVAPQF-------------------------EARNDFDVFADLAELLKPGGKEIYTEG 563
Cdd:cd02767 472 QAVTVEDSMSMTHTSRGrlkpasrvllseeaivagiagarlgEAKPEWEILVEDYDRIRDEIAAVIYEG 540
|
|
| PRK13532 |
PRK13532 |
nitrate reductase catalytic subunit NapA; |
1-541 |
3.52e-17 |
|
nitrate reductase catalytic subunit NapA;
Pssm-ID: 237416 [Multi-domain] Cd Length: 830 Bit Score: 86.49 E-value: 3.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 1 MTLTRREFIKHSGIAAGALVVtsAAPLPAWAEEKGGKILTAGRW------------GAMnVEVKDGKIVSSTGA------ 62
Cdd:PRK13532 1 MKLSRRDFMKANAAAAAAAAA--GLSLPAVANAVVGSAQTAIKWdkapcrfcgtgcGVL-VGTKDGRVVATQGDpdapvn 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 63 ----------LAKTIpnslqsTAADqvhttaRIQHPMVRKSyldnplqpaKGR----GEdtYVQVSWEQALKLIHEQHDR 128
Cdd:PRK13532 78 rglncikgyfLSKIM------YGKD------RLTQPLLRMK---------DGKydkeGE--FTPVSWDQAFDVMAEKFKK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 129 IRKANGPSAIfaGSYGwrsSGvlhkaQTLLQRymnlagGYsghsgdystgAAQVIM----------P---HVVGSVEVYE 195
Cdd:PRK13532 135 ALKEKGPTAV--GMFG---SG-----QWTIWE------GY----------AASKLMkagfrsnnidPnarHCMASAVVGF 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 196 QQT---SWPL----ILENSQVVVLWG-----MNPlntlkIAWSS-TDEQgleyfhqLKKSGKPVIAIDPIRSETIEFfGD 262
Cdd:PRK13532 189 MRTfgiDEPMgcydDIEAADAFVLWGsnmaeMHP-----ILWSRvTDRR-------LSNPDVKVAVLSTFEHRSFEL-AD 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 263 NATWIAPNmgTDVALMLGIAHTLMTQGKHDKVFLEKYTT--------GY---PQ--------------------FEEYlt 311
Cdd:PRK13532 256 NGIIFTPQ--TDLAILNYIANYIIQNNAVNWDFVNKHTNfrkgatdiGYglrPThplekaaknpgtagksepisFEEF-- 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 312 gKSNNTPKSAAWAAEITGVPEAQIVKLAELMAANRTMLMAGW--GIQRQQYGEQKHWMLVTLAAMLGQIGTPGGG-FGFS 388
Cdd:PRK13532 332 -KKFVAPYTLEKTAKMSGVPKEQLEQLAKLYADPNRKVVSFWtmGFNQHTRGVWANNLVYNIHLLTGKISTPGNGpFSLT 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 389 YHYSNGGNPTRVG-----------------------------GVLPEMSAAIAGQASEAADDGGMTAIPVarivdalenp 439
Cdd:PRK13532 411 GQPSACGTAREVGtfshrlpadmvvtnpkhreiaekiwklpeGTIPPKPGYHAVAQDRMLKDGKLNAYWV---------- 480
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 440 ggkyQHNGKEQTYPNIKMIWWagggnfthhqdtnrliKAWQKPE-MIVVSECYWTAAAKHADIVLPITTSFERNdltmtG 518
Cdd:PRK13532 481 ----MCNNNMQAGPNINEERL----------------PGWRNPDnFIVVSDPYPTVSALAADLILPTAMWVEKE-----G 535
|
650 660
....*....|....*....|....*...
gi 446098945 519 DYSN-----QHivpMKQAVAPQFEARND 541
Cdd:PRK13532 536 AYGNaerrtQF---WRQQVKAPGEAKSD 560
|
|
| MopB_CT_3 |
cd02786 |
The MopB_CT_3 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
670-770 |
1.77e-16 |
|
The MopB_CT_3 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239187 [Multi-domain] Cd Length: 116 Bit Score: 76.17 E-value: 1.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 670 LQLLTAhPAH-RLHSQL-NYAELRKKyavaDREP-ITIHTEDAARFGIANGDLVRVWNKRGQILTGAVVTDGIKKGVVcV 746
Cdd:cd02786 3 LRLITP-PAHnFLNSTFaNLPELRAK----EGEPtLLIHPADAAARGIADGDLVVVFNDRGSVTLRAKVTDDVPPGVV-V 76
|
90 100
....*....|....*....|....
gi 446098945 747 HEGAWPDLENGlcKNGSANVLTAD 770
Cdd:cd02786 77 AEGGWWREHSP--DGRGVNALTSA 98
|
|
| MopB_CT_4 |
cd02785 |
The MopB_CT_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
669-791 |
7.39e-16 |
|
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: 74.71 E-value: 7.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 669 QLQLLTAHPAHRLHSQ-LNYAELRKkyavADREP-ITIHTEDAARFGIANGDLVRVWNKRGQILTGAVVTDGIKKGVVCV 746
Cdd:cd02785 3 PLACIQRHSRFRVHSQfSNVPWLLE----LQPEPrVKINPIDAAARGIAHGDLVEVYNDRGSVVCKAKVDDGIQPGVVTA 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 446098945 747 HEGAWPDLENGlcknGSANVLTADIPSSQLANACAGNSA----LVYIEK 791
Cdd:cd02785 79 EQGWWSRYFQE----GSLQDLTSPFVNPVHEYIYGPNSAfydtLVEVRK 123
|
|
| MopB_CT_Fdh-Nap-like |
cd00508 |
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and ... |
704-775 |
1.04e-14 |
|
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: 71.00 E-value: 1.04e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446098945 704 IHTEDAARFGIANGDLVRVWNKRGQILTGAVVTDGIKKGVVCV--HegaWPDLENGlcknGSANVLT---ADIPSSQ 775
Cdd:cd00508 39 IHPEDAARLGIKDGDLVRVSSRRGSVVVRARVTDRVRPGTVFMpfH---WGGEVSG----GAANALTndaLDPVSGQ 108
|
|
| MopB_2 |
cd02763 |
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
39-555 |
2.21e-12 |
|
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: 70.63 E-value: 2.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 39 LTAGRWGaMNVEVKDGKIVSSTG----ALAKTIPNSLQSTAADQVHTTARIQHPMVRKSyldnplqpakGRGEDTYVQVS 114
Cdd:cd02763 6 MCACRCG-IRVHLRDGKVRYIKGnpdhPLNKGVICAKGSSGIMKQYSPARLTKPLLRKG----------PRGSGQFEEIE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 115 WEQALKLIHEQHDRIRKANgPS--AIFAGSygwrssgvlHKAQTLLQRYMNLAG--GYSGHSGDYSTGAAQVIMPHVVGS 190
Cdd:cd02763 75 WEEAFSIATKRLKAARATD-PKkfAFFTGR---------DQMQALTGWFAGQFGtpNYAAHGGFCSVNMAAGGLYSIGGS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 191 VevyeqqtsWPL---ILENSQVVVLWGM---NPLNTLKIAWSstdeqgleyfhQLKKSGKPVIAIDPIRSetieffGDNA 264
Cdd:cd02763 145 F--------WEFggpDLEHTKYFMMIGVaedHHSNPFKIGIQ-----------KLKRRGGKFVAVNPVRT------GYAA 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 265 T---WIAPNMGTDVALMLGIAHTLMTQGKHDKVFLEKYTTGyPQFEEYltgksnnTPKsaaWAAEITGVPEAQIVKLAEL 341
Cdd:cd02763 200 IadeWVPIKPGTDGAFILALAHELLKAGLIDWEFLKRYTNA-AELVDY-------TPE---WVEKITGIPADTIRRIAKE 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 342 MAA----NRTMLMAGW----------------------GIQRQQYGEQKHWMLVTLAAMLGQIGTPGGGFG---FSYHYS 392
Cdd:cd02763 269 LGVtardQPIELPIAWtdvwgrkhekitgrpvsfhamrGIAAHSNGFQTIRALFVLMMLLGTIDRPGGFRHkppYPRHIP 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 393 NGGNPTRVGGVLPEMSAAIAGQASEAA--------DDGGMTAIPVARIVDALENPGGKYQH---NG-KEQTYP-NIKMIW 459
Cdd:cd02763 349 PLPKPPKIPSADKPFTPLYGPPLGWPAspddllvdEDGNPLRIDKAYSWEYPLAAHGCMQNvitNAwRGDPYPiDTLMIY 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 460 WAGGGnFTHHQDTNRLIKAWQ--------KPEMIVVSECYWTAAAKHADIVLPITTSFERND-LTM----------TGDY 520
Cdd:cd02763 429 MANMA-WNSSMNTPEVREMLTdkdasgnyKIPFIIVCDAFYSEMVAFADLVLPDTTYLERHDaMSLldrpiseadgPVDA 507
|
570 580 590
....*....|....*....|....*....|....*.
gi 446098945 521 SNQHIVPMKQAVAPqFEarndfDVFADLAELLK-PG 555
Cdd:cd02763 508 IRVPIVEPKGDVKP-FQ-----EVLIELGTRLGlPG 537
|
|
| MopB_CT_Formate-Dh_H |
cd02790 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
695-768 |
3.91e-12 |
|
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: 63.80 E-value: 3.91e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446098945 695 AVADREPITIHTEDAARFGIANGDLVRVWNKRGQILTGAVVTDGIKKGVV----CVHEGAwpdlenglckngsANVLT 768
Cdd:cd02790 30 AIAPEEYVEINPEDAKRLGIEDGEKVRVSSRRGSVEVRARVTDRVPEGVVfmpfHFAEAA-------------ANLLT 94
|
|
| MopB_Arsenite-Ox |
cd02756 |
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the ... |
84-663 |
1.75e-11 |
|
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the electrons obtained from the oxidation of arsenite towards the soluble periplasmic electron carriers cytochrome c and/or amicyanin. Arsenite oxidase is a heterodimeric enzyme containing a large and a small subunit. The large catalytic subunit harbors the molybdopterin cofactor and the [3Fe-4S] cluster; and the small subunit belongs to the structural class of the Rieske proteins. The small subunit is not included in this alignment. Members of MopB_Arsenite-Ox CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239157 [Multi-domain] Cd Length: 676 Bit Score: 67.89 E-value: 1.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 84 RIQHPMVRKSyldnplqpakgrgeDTYVQVSWEQALKLIHEQHDRIRKANGPS-AIFAgsygwrssgvlhkaqtllqRYM 162
Cdd:cd02756 117 RLTTPLVRRG--------------GQLQPTTWDDAIDLVARVIKGILDKDGNDdAVFA-------------------SRF 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 163 NLAGGYSGHSGDYSTG-----AAQVIM----------PHVVGSVE--VYEQQTSWpLILENSQVVVLWGMNPLNT----- 220
Cdd:cd02756 164 DHGGGGGGFENNWGVGkfffmALQTPFvrihnrpaynSEVHATREmgVGELNNSY-EDARLADTIVLWGNNPYETqtvyf 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 221 -------LKIAWSSTDEQGLEyfhqlkkSGKPV-----IAIDPIRSETIEFFG-----DNATWIAPNMGTDVALMLGIAh 283
Cdd:cd02756 243 lnhwlpnLRGATVSEKQQWFP-------PGEPVppgriIVVDPRRTETVHAAEaaagkDRVLHLQVNPGTDTALANAIA- 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 284 tlmtqgkhdkvflekyTTGYPQFEEYLtgksnntpksaAWAAEITGVPEAQIVKLAELMA-------ANRTMLM--AG-- 352
Cdd:cd02756 315 ----------------RYIYESLDEVL-----------AEAEQITGVPRAQIEKAADWIAkpkeggyRKRVMFEyeKGii 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 353 WGIQ--RQQYGeqkhwmLVTLAAMLGQIGTPGGG----FGFSYHYSNGGNPTrVGGVLPEMSAAIAGQASEAADDGGMTA 426
Cdd:cd02756 368 WGNDnyRPIYS------LVNLAIITGNIGRPGTGcvrqGGHQEGYVRPPPPP-PPWYPQYQYAPYIDQLLISGKGKVLWV 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 427 IPVARIVdaLENPGGKYQHNGKEQTYPNIKMIWWAGGGNFTHHQDTNRLIKAWQKPE--MIVVSECYWTAAAKHADIVLP 504
Cdd:cd02756 441 IGCDPYK--TTPNAQRLRETINHRSKLVTDAVEAALYAGTYDREAMVCLIGDAIQPGglFIVVQDIYPTKLAEDAHVILP 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 505 ITTSFERNDLTMTGDysNQHIVPMKQAVAPQFEARNDFDVFADLAELLkpggKEIYT-EGKDEMAWLKFF---YDAAQKG 580
Cdd:cd02756 519 AAANGEMNETSMNGH--ERRLRLYEKFMDPPGEAMPDWWIAAMIANRI----YELYQeEGKGGSAQYQFFgfiWKTEEDN 592
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 581 AR--AQRVTMPMFNAFWQQNKLIEmrrsekNEQYVRYGDFRADPVKN----ALGTPSGKIEI--YSKTLEKFGYKDCPAH 652
Cdd:cd02756 593 FMdgSQEFADGGEFSEDYYVLGQE------RYEGVTYNRLKAVGVNGiqlpVTTDTVTKILVtnVLRTEGVFDTEDGKAY 666
|
650
....*....|.
gi 446098945 653 ptWLAPDEWKG 663
Cdd:cd02756 667 --VIDLAPWPG 675
|
|
| MopB_CT_Formate-Dh-Na-like |
cd02792 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
704-770 |
7.74e-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: 59.93 E-value: 7.74e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446098945 704 IHTEDAARFGIANGDLVRVWNKRGQILTGAVVTDGIKKGVVCV--HEGAWpdlenGLCKNGSANVLTAD 770
Cdd:cd02792 39 ISPELAAERGIKNGDMVWVSSPRGKIKVKALVTDRVKPHEVGIpyHWGGM-----GLVIGDSANTLTPY 102
|
|
| MopB_CT_Tetrathionate_Arsenate-R |
cd02780 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate ... |
679-751 |
2.91e-10 |
|
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate reductase, subunit A, (TtrA); respiratory arsenate As(V) reductase, catalytic subunit (ArrA); and other related proteins.
Pssm-ID: 239181 [Multi-domain] Cd Length: 143 Bit Score: 59.23 E-value: 2.91e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446098945 679 HRLHSQ--LNYAELrkkYAVADREPITIHTEDAARFGIANGDLVRVWNKRGQILTGAVVTDGIKKGVV--CVHEGAW 751
Cdd:cd02780 10 SNLNSHrsANAPWL---KEIKPENPVWINPEDAAKLGIKTGDRVRVVTPGGSVVGKAKVTEGVRPGVVaiEHGYGHW 83
|
|
| MopB_Formate-Dh-Na-like |
cd02752 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
49-553 |
4.66e-10 |
|
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate respiration in bacteria such as in the E. coli formate dehydrogenase N (Fdh-N). Fdh-N is a membrane protein that is a complex of three different subunits and is the major electron donor to the nitrate respiratory chain. Also included in this CD is the Desulfovibrio gigas tungsten formate dehydrogenase, DgW-FDH. In contrast to Fdh-N, which is a functional heterotrimer, DgW-FDH is a heterodimer. The DgW-FDH complex is composed of a large subunit carrying the W active site and one [4Fe-4S] center, and a small subunit that harbors a series of three [4Fe-4S] clusters as well as a putative vacant binding site for a fourth cluster. The smaller subunit is not included in this alignment. 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: 63.19 E-value: 4.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 49 VEVKDGKIVSSTGALAKTIP-NSLQSTAA---DQVHTTARIQHPMVRKSyldnplqpakgrGEDTYVQVSWEQALKLIHE 124
Cdd:cd02752 15 AYVQNGVWVHQEGDPDHPVNrGSLCPKGAalrDFVHSPKRLKYPMYRAP------------GSGKWEEISWDEALDEIAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 125 QHDRIRKANGPSAIFAGSY--GWRSSGVLHKAQT------LLQRYMNLAG-GYSGHSGDYSTGaaqvimPHVVGSVEVY- 194
Cdd:cd02752 83 KMKDIRDASFVEKNAAGVVvnRPDSIAFLGSAKLsneecyLIRKFARALGtNNLDHQARIUHS------PTVAGLANTFg 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 195 --EQQTSWPLIlENSQVVVLWGMNPLNTLKIAWSstdeqglEYFHQLKKSGKPVIAIDPIRSETieffGDNATWIAP-NM 271
Cdd:cd02752 157 rgAMTNSWNDI-KNADVILVMGGNPAEAHPVSFK-------WILEAKEKNGAKLIVVDPRFTRT----AAKADLYVPiRS 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 272 GTDVALMLGIAHTLMtqgkhdkvfleKYTtgypqfeeyltgksnntPKSAAwaaEITGVPEAQIVKLAELMAANRTMLMA 351
Cdd:cd02752 225 GTDIAFLGGMINYII-----------RYT-----------------PEEVE---DICGVPKEDFLKVAEMFAATGRPDKP 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 352 G---W--GIQRQQYGEQkhwmLVTLAAM----LGQIGTPGGG-FGFSYHySNggnptrVGGvlpemsaaiagqaseAADD 421
Cdd:cd02752 274 GtilYamGWTQHTVGSQ----NIRAMCIlqllLGNIGVAGGGvNALRGH-SN------VQG---------------ATDL 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 422 GGMtaipvariVDALenPGgkyqhngkeqtypnikmiwWAGGGNF-THHQDTNRLIKAWQKPEMIVVSECYWTAAA---- 496
Cdd:cd02752 328 GLL--------SHNL--PG-------------------YLGGQNPnSSFPNANKVRRALDKLDWLVVIDPFPTETAafwk 378
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446098945 497 KHAD---------IVLPITTSFERNdltmtGDYSNQH--IVPMKQAVAPQFEARNDFDVFADLAELLK 553
Cdd:cd02752 379 NPGMdpksiqtevFLLPAACQYEKE-----GSITNSGrwLQWRYKVVEPPGEAKSDGDILVELAKRLG 441
|
|
| MopB_CT_Acetylene-hydratase |
cd02781 |
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related ... |
682-770 |
5.12e-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: 58.09 E-value: 5.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 682 HSQL-NYAELRKKyavaDREP-ITIHTEDAARFGIANGDLVRVWNKRGQILTGAVVTDGIKKGVVCVHEGAW----PDLE 755
Cdd:cd02781 17 HSEHrQLPSLREL----HPDPvAEINPETAAKLGIADGDWVWVETPRGRARQKARLTPGIRPGVVRAEHGWWyperEAGE 92
|
90
....*....|....*..
gi 446098945 756 NGL--CKNGSANVLTAD 770
Cdd:cd02781 93 PALggVWESNANALTSD 109
|
|
| PRK09939 |
PRK09939 |
acid resistance putative oxidoreductase YdeP; |
204-384 |
5.63e-10 |
|
acid resistance putative oxidoreductase YdeP;
Pssm-ID: 182156 [Multi-domain] Cd Length: 759 Bit Score: 63.14 E-value: 5.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 204 LENSQVVVLWGMNPlntlkiawSSTDEQGLEYFHQLKKSGKPVIAIDPIRSETIEFFG----------DNATWIAP---- 269
Cdd:PRK09939 206 FEKCDLVICIGHNP--------GTNHPRMLTSLRALVKRGAKMIAINPLQERGLERFTapqnpfemltNSETQLASayyn 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 270 -NMGTDVALMLGIAHTLMTQGKH----------DKVFLEKYTTGYPQFE-EYLTGKSNNTPKsaawaaeITGVPEAQIVK 337
Cdd:PRK09939 278 vRIGGDMALLKGMMRLLIERDDAasaagrpsllDDEFIQTHTVGFDELRrDVLNSEWKDIER-------ISGLSQTQIAE 350
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446098945 338 LAE-LMAANRTMLMAGWGIQRQQYGEQKHWMLVTLAAMLGQIGTPGGG 384
Cdd:PRK09939 351 LADaYAAAERTIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAG 398
|
|
| MopB_CT_Nitrate-R-NapA-like |
cd02791 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
704-770 |
1.26e-09 |
|
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to nitrite. Monomeric Nas is located in the cytoplasm and participates in nitrogen assimilation. Dimeric Nap is located in the periplasm and is coupled to quinol oxidation via a membrane-anchored tetraheme cytochrome. This CD (MopB_CT_Nitrate-R-Nap) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs
Pssm-ID: 239192 [Multi-domain] Cd Length: 122 Bit Score: 56.81 E-value: 1.26e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446098945 704 IHTEDAARFGIANGDLVRVWNKRGQILTGAVVTDGIKKGVVCV--HegaWPDLENGLcknGSANVLTAD 770
Cdd:cd02791 39 IHPEDAARLGLKEGDLVRVTSRRGEVVLRVRVTDRVRPGEVFVpmH---WGDQFGRS---GRVNALTLD 101
|
|
| Molybdopterin_N |
pfam18364 |
Molybdopterin oxidoreductase N-terminal domain; This is the N-terminal domain of pfam00384 ... |
40-80 |
2.65e-09 |
|
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: 53.17 E-value: 2.65e-09
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 446098945 40 TAGRWGAMNVEVKDGKIVSSTGALAKTIPNSLQSTAADQVH 80
Cdd:pfam18364 1 TASHWGAFRAVVKDGRIVGVEPFEGDPDPSPLLQGVPDAVY 41
|
|
| MopB_Tetrathionate-Ra |
cd02758 |
The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other ... |
98-555 |
5.18e-09 |
|
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: 59.66 E-value: 5.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 98 PLQPAKGRGEDTYVQVSWEQAL-------------------------KLIHEQH-DRIRKANGPSAIFAGSYGwrssgvl 151
Cdd:cd02758 87 PLKRVGPRGSGKWKPISWEQLIeevveggdlfgeghveglkairdldTPIDPDHpDLGPKANQLLYTFGRDEG------- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 152 hkAQTLLQRYMNLA---------GGYSGHSGDYSTGAA---QVIMPHVvgsvevyeqQTSWplilENSQVVVLWGM---- 215
Cdd:cd02758 160 --RTPFIKRFANQAfgtvnfgghGSYCGLSYRAGNGALmndLDGYPHV---------KPDF----DNAEFALFIGTspaq 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 216 --NPLNTL--KIAwSSTDEQGLEYfhqlkksgkpvIAIDPIRSETIEFFGDNATWIAPNMGTDVALMLGIAHTLMTQGKH 291
Cdd:cd02758 225 agNPFKRQarRLA-EARTEGNFKY-----------VVVDPVLPNTTSAAGENIRWVPIKPGGDGALAMAMIRWIIENERY 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 292 DKVFLE------KYTTGYPQFeeyltgkSNNT-------PKSA-------------AWAAEITGVPEAQIVKLAE----- 340
Cdd:cd02758 293 NAEYLSipskeaAKAAGEPSW-------TNAThlvitvrVKSAlqllkeeafsyslEEYAEICGVPEAKIIELAKeftsh 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 341 LMAA---NRTMLMAGwgiqrqqYGEQKHWMLVTLAAMLGQIGTPGGGFGFSYHYSNGGNPTRVGGVLPEMSAAIAGqase 417
Cdd:cd02758 366 GRAAavvHHGGTMHS-------NGFYNAYAIRMLNALIGNLNWKGGLLMSGGGFADNSAGPRYDFKKFFGEVKPWG---- 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 418 aaddggmtaIPVARIVDALE-NPGGKYQHNGKEQTYPNiKMIWWAGGGNFTHHQDTNRL------IKAW----------- 479
Cdd:cd02758 435 ---------VPIDRSKKAYEkTSEYKRKVAAGENPYPA-KRPWYPLTPELYTEVIASAAegypykLKALilwmanpvyga 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 480 --------------QKPEMIVVSECYWTAAAKHADIVLPITTSFERNDLTMTGDYS---NQH----IVPMKQAVAPQFEA 538
Cdd:cd02758 505 pglvkqveeklkdpKKLPLFIAIDAFINETSAYADYIVPDTTYYESWGFSTPWGGVptkASTarwpVIAPLTEKTANGHP 584
|
570
....*....|....*...
gi 446098945 539 RNDFDVFADLAELLK-PG 555
Cdd:cd02758 585 VSMESFLIDLAKALGlPG 602
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
471-555 |
5.21e-08 |
|
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: 56.00 E-value: 5.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 471 DTNRLIKAWQKPEMIVVSECYWTAAAKHADIVLPITTSFERNdltmtGDYSNQ--HIVPMKQAVAPQFEARNDFDVFADL 548
Cdd:COG1034 347 DPAAALAALAKADFVVVLDHFGSATAERADVVLPAAAFAEKS-----GTFVNLegRVQRFNAAVPPPGEARPDWRVLRAL 421
|
....*..
gi 446098945 549 AELLKPG 555
Cdd:COG1034 422 ANALGAG 428
|
|
| PRK14991 |
PRK14991 |
tetrathionate reductase subunit TtrA; |
653-749 |
3.97e-07 |
|
tetrathionate reductase subunit TtrA;
Pssm-ID: 237883 [Multi-domain] Cd Length: 1031 Bit Score: 53.85 E-value: 3.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 653 PTWLAPDEWKGTADEKQLQ------LLTAHPAHrLHSQLNYAELRKKyAVADREPITIHTEDAARFGIANGDLVRVWNKR 726
Cdd:PRK14991 865 PTWYPPRLADGTPLREQFPesqwplLLISFKSN-LMSSMSIASPRLR-QVKPANPVALNPQDAARLGIQHGDRVRISTPG 942
|
90 100
....*....|....*....|...
gi 446098945 727 GQILTGAVVTDGIKKGVVCVHEG 749
Cdd:PRK14991 943 GSVVAQASVLNGVMPGVIAIEHG 965
|
|
| MopB_CT_1 |
cd02782 |
The MopB_CT_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
686-790 |
9.68e-07 |
|
The MopB_CT_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239183 [Multi-domain] Cd Length: 129 Bit Score: 48.54 E-value: 9.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 686 NYAELRKkyaVADREPITIHTEDAARFGIANGDLVRVWNKRGQILTGAVVTDGIKKGVVCVHEGAWPDLENGLCKNGSAN 765
Cdd:cd02782 22 NDPRLVK---GRNRCTLRIHPDDAAALGLADGDKVRVTSAAGSVEAEVEVTDDMMPGVVSLPHGWGHDYPGVSGAGSRPG 98
|
90 100
....*....|....*....|....*
gi 446098945 766 VLTADIPSSQLANACAGNSALVYIE 790
Cdd:cd02782 99 VNVNDLTDDTQRDPLSGNAAHNGVP 123
|
|
| MopB_CT_Thiosulfate-R-like |
cd02778 |
The MopB_CT_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, ... |
704-770 |
2.38e-06 |
|
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: 47.27 E-value: 2.38e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 704 IHTEDAARFGIANGDLVRVWNKRGQILTGAVVTDGIKKGVVCVHE--GAW-PDLENGLCKNGSANVLTAD 770
Cdd:cd02778 34 INPETAARLGIKDGDRVEVSSARGKVTGKARLTEGIRPDTVFMPHgfGHWaPALSRAYGGGVNDNNLLPG 103
|
|
| MopB_CT_Arsenite-Ox |
cd02779 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of Arsenite oxidase ... |
696-758 |
1.57e-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: 44.76 E-value: 1.57e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446098945 696 VADREP---ITIHTEDAARFGIANGDLVRVWNKRGQILTGAVVTDGIKKGVVCVHEGAWPDLENGL 758
Cdd:cd02779 26 IAERVPlpyIEVNPEDAKREGLKNGDLVEVYNDYGSTTAMAYVTNTVKPGQTFMLMAHPRPGANGL 91
|
|
| MopB_NADH-Q-OR-NuoG2 |
cd02768 |
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone ... |
84-552 |
1.99e-05 |
|
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: 47.66 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 84 RIQHPMVRKSyldnplqpakgrgeDTYVQVSWEQALKLIHEqhdRIRKANGPSAI-FAGSYgwrssgVLHKAQTLLQRYM 162
Cdd:cd02768 54 RLTQPLIKKG--------------GKLVPVSWEEALKTVAE---GLKAVKGDKIGgIAGPR------ADLESLFLLKKLL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 163 NLAGgysghSGDYSTGAAQVIMPHVVGSVEVYEQQTSwplI--LENSQVVVLWGMNP------LNT-LKIAWsstdeqgl 233
Cdd:cd02768 111 NKLG-----SNNIDHRLRQSDLPADNRLRGNYLFNTS---IaeIEEADAVLLIGSNLrkeaplLNArLRKAV-------- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 234 eyfhqlKKSGKPVIAIDPirseTIEFFGDNATWIAPNMGTDVALMLGIAHtlmtqGKHDKVFLEKyttgypqfeeyltgk 313
Cdd:cd02768 175 ------KKKGAKIAVIGP----KDTDLIADLTYPVSPLGASLATLLDIAE-----GKHLKPFAKS--------------- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 314 snntpksaawaaeitgvpeaqivklaeLMAANRTMLMAGWGIQRQQYGEQkhwmLVTLAAMLGQIGTPGGGFGFsyhySN 393
Cdd:cd02768 225 ---------------------------LKKAKKPLIILGSSALRKDGAAI----LKALANLAAKLGTGAGLWNG----LN 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 394 GGNptrvggvlpemsaaiagqaSEAADDGGmtaipvaRIVDALENPGgkyqHNGKEQTYPNikmiwwaGGGNFthHQDTN 473
Cdd:cd02768 270 VLN-------------------SVGARLGG-------AGLDAGLALL----EPGKAKLLLL-------GEDEL--DRSNP 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446098945 474 RLIKAWQKPEMIVVSECYWTAAAKHADIVLPITTSFERNdltmtGDYSNQ-HIVPM-KQAVAPQFEARNDFDVFADLAEL 551
Cdd:cd02768 311 PAAVALAAADAFVVYQGHHGDTGAQADVILPAAAFTEKS-----GTYVNTeGRVQRfKKAVSPPGDAREDWKILRALSNL 385
|
.
gi 446098945 552 L 552
Cdd:cd02768 386 L 386
|
|
| MopB_CT_Nitrate-R-NarG-like |
cd02776 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
701-749 |
3.44e-05 |
|
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: 44.29 E-value: 3.44e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 446098945 701 PITIHTEDAARFGIANGDLVRVWNKRGQILTGAVVTDGIKKGVVCVHEG 749
Cdd:cd02776 32 VVWMNPKDAAELGIKDNDWVEVFNDNGVVVARAKVSPRIPRGTVFMYHA 80
|
|
| TAT_signal_seq |
TIGR01409 |
Tat (twin-arginine translocation) pathway signal sequence; Proteins assembled with various ... |
3-31 |
2.85e-04 |
|
Tat (twin-arginine translocation) pathway signal sequence; Proteins assembled with various cofactors or by means of cytosolic molecular chaperones are poor candidates for translocation across the bacterial inner membrane by the standard general secretory (Sec) pathway. This model describes a family of predicted long, non-Sec signal sequences and signal-anchor sequences (uncleaved signal sequences). All contain an absolutely conserved pair of arginine residues, in a motif approximated by (S/T)-R-R-X-F-L-K, followed by a membrane-spanning hydrophobic region. Members with small amino acid side chains at the -1 and -3 positions from the C-terminus of the model should be predicted to be cleaved as are Sec pathway signal sequences. Members are almost exclusively bacterial, although archaeal sequences are also found. A large fraction of the members of this family may have bound redox-active cofactors. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273604 Cd Length: 29 Bit Score: 38.65 E-value: 2.85e-04
10 20
....*....|....*....|....*....
gi 446098945 3 LTRREFIKHSGIAAGALVVTSAAPLPAWA 31
Cdd:TIGR01409 1 LSRRDFLKGAAAAGAAAGLGALLPSPARA 29
|
|
| |
