|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15102 |
PRK15102 |
trimethylamine-N-oxide reductase TorA; |
9-836 |
0e+00 |
|
trimethylamine-N-oxide reductase TorA;
Pssm-ID: 237909 [Multi-domain] Cd Length: 825 Bit Score: 1587.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 9 VSRRRFLAQLGGLTVAGMLGPSLLTPRSARAADAVAPGAaTKEGILTGSHWGAIRATVVDGRFVAAKPFEQDKYPSKMIA 88
Cdd:PRK15102 1 ASRRRFLKGLGGLSAAGMLGPSLLTPRSALAAQAAAAET-TKEWILTGSHWGAFRAKVKNGRFVEAKPFELDKYPTKMIN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 89 GLPDHVHNAARIRYPMVRVDWMRKGHQSDTSQRGDNRFVRVSWDEALDLFYQELERVQKTYGPSALLTA-SGWQSTGMFH 167
Cdd:PRK15102 80 GIKGHVYNPSRIRYPMVRLDWLRKRHKSDTSQRGDNRFVRVSWDEALDLFYEELERVQKTYGPSALHTGqTGWQSTGQFH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 168 NASGMLARAIALHGNSVSTGGDYSTGAAQVILPRVVGSMEVYEQQTSWPLVLQNSKTIVLWGSDMVKNQQANWWCPDHDV 247
Cdd:PRK15102 160 SATGHMQRAIGMHGNSVGTVGDYSTGAGQVILPYVLGSTEVYEQGTSWPLILENSKTIVLWGSDPVKNLQVGWNCETHES 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 248 YQYYEQLKEKVASGAISVISIDPVVTSTHDYLGRDkvkHIAINPQTDVPLQLALAHTLYSEKLYDKNFLDNYCVGFDQFL 327
Cdd:PRK15102 240 YAYLAQLKEKVAKGEINVISIDPVVTKTQNYLGCE---HLYVNPQTDVPLMLALAHTLYSENLYDKKFIDNYCLGFEQFL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 328 PYLLGEKDGQPKDAAWAEKLCGIDADTIRALARQMAGDRTQIIAGWCVQRMQHGEQWSWMVVVLAAMLGQIGLPGGGFGF 407
Cdd:PRK15102 317 PYLLGEKDGVPKTPEWAEKICGIDAETIRELARQMAKGRTQIIAGWCIQRQQHGEQPYWMGAVLAAMLGQIGLPGGGISY 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 408 GWHYNGAGTPGRKGIILSGFSGS--TTVPPVHDSTDYKGYSSTIPIARFMDAILEPGKVINWNGKSVKLPPLKMCVFAGT 485
Cdd:PRK15102 397 GHHYSGIGVPSSGGAIPGGFPGNldTGQKPKHDNSDYKGYSSTIPVARFIDAILEPGKTINWNGKKVTLPPLKMMIFSGT 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 486 NPFHRHQQINRIIEGWRKLETVIAIDNQWTSTCRFADIVLPATTQFERNDLDQFGNHSNRGIIAMKQVVSPQFEARNDFD 565
Cdd:PRK15102 477 NPWHRHQDRNRMKEAFRKLETVVAIDNQWTATCRFADIVLPACTQFERNDIDQYGSYSNRGIIAMKKVVEPLFESRSDFD 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 566 IFRDLCRRFNREAAFTEGLDEMGWLKRIWQEGSQQGKGRgIHLPTFEVFWnQQEYIEFDHPQMFVRHQAFREDPDLEPLG 645
Cdd:PRK15102 557 IFRELCRRFGREKEYTRGMDEMGWLKRLYQECKQQNKGK-FHMPEFDEFW-KKGYVEFGEGQPWVRHADFREDPELNPLG 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 646 TPSGLIEIYSKTIADMQYDDCQGHPMWFEKIERSHGGPGSQRWPLHLQSVHPDFRLHSQLCESETLRQQYAVGGKEPVFI 725
Cdd:PRK15102 635 TPSGLIEIYSRKIADMGYDDCQGHPMWFEKIERSHGGPGSDKYPLWLQSVHPDKRLHSQLCESEELRETYTVQGREPVYI 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 726 NPQDASARGIRNGDIVRVFNARGQVLAGAVVSDRYAPGVARIHEGAWYDPDKGGDINALCKYGNPNVLTLDIGTSQLAQA 805
Cdd:PRK15102 715 NPQDAKARGIKDGDVVRVFNDRGQVLAGAVVSDRYPPGVIRIHEGAWYGPDKGGEIGALCTYGDPNTLTLDIGTSQLAQA 794
|
810 820 830
....*....|....*....|....*....|.
gi 1385641982 806 TSAHTTLVEIEKYTGPIDNVTAFNGPVEMVA 836
Cdd:PRK15102 795 TSAHTCLVEIEKYQGKVPPVTSFNGPVEVVA 825
|
|
| torA |
TIGR02164 |
trimethylamine-N-oxide reductase TorA; This very narrowly defined family represents TorA, part ... |
9-836 |
0e+00 |
|
trimethylamine-N-oxide reductase TorA; This very narrowly defined family represents TorA, part of a family of related molybdoenzymes that include biotin sulfoxide reductases, dimethyl sulfoxide reductases, and at least two different subfamilies of trimethylamine-N-oxide reductases. A single enzyme from the larger family may have more than one activity. TorA typically is located in the periplasm, has a Tat (twin-arginine translocation)-dependent signal sequence, and is encoded in a torCAD operon.
Pssm-ID: 131219 [Multi-domain] Cd Length: 822 Bit Score: 1511.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 9 VSRRRFLAQLGGLTVAGMLGPSLLTPRSAraadAVAPGAATKEGILTGSHWGAIRATVVDGRFVAAKPFEQDKYPSKMIA 88
Cdd:TIGR02164 1 MSRRDFLKGIASSSAAVLGGPSLLTPLNA----LAAAAINEDEWKTTGSHWGAFRAKVKNGKVVEVKPFELDKYPTEMIN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 89 GLPDHVHNAARIRYPMVRVDWMRKGHQSDTSQRGDNRFVRVSWDEALDLFYQELERVQKTYGPSALLT-ASGWQSTGMFH 167
Cdd:TIGR02164 77 GIRGMVYNPSRVRYPMVRLDWLKKRHKSNTHQRGDNRFVRVTWDEALDLFYEELERVQKQYGPSALHAgQTGWRSTGQFH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 168 NASGMLARAIALHGNSVSTGGDYSTGAAQVILPRVVGSMEVYEQQTSWPLVLQNSKTIVLWGSDMVKNQQANWWCPDHDV 247
Cdd:TIGR02164 157 SCTSHMQRAVGMHGNYVKKIGDYSTGAGQTILPYVLGSTEVYAQGTSWPLILENSDTIVLWANDPVKNLQVGWNCETHES 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 248 YQYYEQLKEKVASGAISVISIDPVVTSTHDYLGRDkvkHIAINPQTDVPLQLALAHTLYSEKLYDKNFLDNYCVGFDQFL 327
Cdd:TIGR02164 237 FAYLAQLKEKVAAGEINVISIDPVVTKTQAYLGCE---HLYVNPQTDVALMLALAHTLYSENLYDKKFIEGYCLGFEEFL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 328 PYLLGEKDGQPKDAAWAEKLCGIDADTIRALARQMAGDRTQIIAGWCVQRMQHGEQWSWMVVVLAAMLGQIGLPGGGFGF 407
Cdd:TIGR02164 314 PYVLGSKDGVAKTPEWAAKICGVEAEVIRDLARMLVKGRTQLIFGWCIQRQQHGEQPYWMGAVLAAMIGQIGLPGGGISY 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 408 GWHYNGAGTPGRKGIILSGFSG--STTVPPVHDSTDYKGYSSTIPIARFMDAILEPGKVINWNGKSVKLPPLKMCVFAGT 485
Cdd:TIGR02164 394 GHHYSSIGVPSSGAAAPGAFPRnlDEGQKPKFDNSDFKGYSSTIPVARWIDAILEPGKTIDHNGSKVTYPPIKMMIFSGC 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 486 NPFHRHQQINRIIEGWRKLETVIAIDNQWTSTCRFADIVLPATTQFERNDLDQFGNHSNRGIIAMKQVVSPQFEARNDFD 565
Cdd:TIGR02164 474 NPWHHHQDRNRMKQAFQKLETVVTIDVSWTATCRFSDIVLPACTQFERNDIDVYGSYSNRGIIAMQKLVDPLFDSRSDFE 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 566 IFRDLCRRFNREAAFTEGLDEMGWLKRIWQEGSQQGKGRgIHLPTFEVFWNQQeYIEFDHPQMFVRHQAFREDPDLEPLG 645
Cdd:TIGR02164 554 IFTELCRRFGKEKEYTRNMDEMEWLKTLYNECKQANAGK-FEMPDFAEFWKKG-YVHFGDGEPWVRHADFREDPEINPLG 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 646 TPSGLIEIYSKTIADMQYDDCQGHPMWFEKIERSHGGPGSQRWPLHLQSVHPDFRLHSQLCESETLRQQYAVGGKEPVFI 725
Cdd:TIGR02164 632 TPSGLIEIFSRKIAQYGYDDCKGHPMWFEKTERSHGGPGSDKHPFWLQSCHPDKRLHSQMCESEALRETYAVQGREPVYI 711
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 726 NPQDASARGIRNGDIVRVFNARGQVLAGAVVSDRYAPGVARIHEGAWYDPDKGGDINALCKYGNPNVLTLDIGTSQLAQA 805
Cdd:TIGR02164 712 NPVDAKARGIKDGDLVRVFNDRGQLLAGAVVSDNFPKGVVRIHEGAWYGPLGGEEVGALCTYGDPNTLTLDIGTSKLAQA 791
|
810 820 830
....*....|....*....|....*....|.
gi 1385641982 806 TSAHTTLVEIEKYTGPIDNVTAFNGPVEMVA 836
Cdd:TIGR02164 792 TSANTCLVEFEKYQGKVPKVTSFDGPIEVEI 822
|
|
| bisC_fam |
TIGR00509 |
molybdopterin guanine dinucleotide-containing S/N-oxide reductases; This enzyme family shares ... |
56-834 |
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: 1284.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 56 GSHWGAIRATVVDGRFVAAKPFEQDKYPSKMIAGLPDHVHNAARIRYPMVRVDWMRKGHQSDTSQRGDNRFVRVSWDEAL 135
Cdd:TIGR00509 1 ASHWGVFTATVQDGRIVAVTPFESDPNPTPMLEGVPDQVYSESRIKYPMVRKGFLENGVKSDRSGRGREEFVRVSWDEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 136 DLFYQELERVQKTYGPSALLTAS-GWQSTGMFHNASGMLARAIALHGNSVSTGGDYSTGAAQVILPRVVGSMEVYEQQTS 214
Cdd:TIGR00509 81 DLVAEELKRVRKTHGPSAIFAGSyGWKSAGRLHNASTLLQRMLNLLGGYVGHAGDYSTGAAQVIMPHVVGDMEVYEQQTT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 215 WPLVLQNSKTIVLWGSDMVKNQQANWWCPDHDVYQYYEQLKEKVasgaISVISIDPVVTSTHDYLGrdkVKHIAINPQTD 294
Cdd:TIGR00509 161 WPVILENSEVLVLWGADPLKTSQIAWGIPDHGGYEYLERLKAKG----KRVISIDPVRTETVEFFG---AEWIPPNPQTD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 295 VPLQLALAHTLYSEKLYDKNFLDNYCVGFDQFLPYLLGEKDGQPKDAAWAEKLCGIDADTIRALARQMAGDRTQIIAGWC 374
Cdd:TIGR00509 234 VALMLGLAHTLVTEGLYDKDFLAKYTSGFEKFLPYLLGETDGTPKTAEWASKITGVPAETIKELARLFASKRTMLAAGWS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 375 VQRMQHGEQWSWMVVVLAAMLGQIGLPGGGFGFGWHYNGAGTPGRKGIILSGFSGSTTVPpvHDSTDYKGYSSTIPIARF 454
Cdd:TIGR00509 314 MQRMQHGEQPHWMLVTLAAMLGQIGLPGGGFGFSYHYSGGGTPSASGPALSQGSNSVSST--AGPEWDDGSASVIPVARI 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 455 MDAILEPGKVINWNGKSVKLPPLKMCVFAGTNPFHRHQQINRIIEGWRKLETVIAIDNQWTSTCRFADIVLPATTQFERN 534
Cdd:TIGR00509 392 SDALLNPGKEIDYNGKELKLPDIKMVYWAGGNPFHHHQDTNRLIKAWRKLETIIVHEPQWTPTAKHADIVLPATTSFERN 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 535 DLDQFGNHSNRGIIAMKQVVSPQFEARNDFDIFRDLCRRFNREAAFTEGLDEMGWLKRIWQEGSQQGKGRGIHLPTFEVF 614
Cdd:TIGR00509 472 DLTMAGDYSNTGILAMKQVVPPQFEARNDYDIFAALAERLGVEEAFTEGKDEMGWLKHLYEKAAKQAKADGVEMPAFDAF 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 615 WNQQeYIEFDHPQ--MFVRHQAFREDPDLEPLGTPSGLIEIYSKTIADMQYDDCQGHPMWFEKIERShGGPGSQRWPLHL 692
Cdd:TIGR00509 552 WAEG-IVEFPVPEgaDFVRYAAFREDPLLNPLGTPSGLIEIYSKTIAKMGYDDCPGHPTWMEPAEWL-GGPRGAKYPLHL 629
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 693 QSVHPDFRLHSQLcESETLRQQYAVGGKEPVFINPQDASARGIRNGDIVRVFNARGQVLAGAVVSDRYAPGVARIHEGAW 772
Cdd:TIGR00509 630 ISPHPKYRLHSQL-DHTELRQAYKVQGREPVMIHPDDAAARGIADGDIVRVFNARGQILAGAVVTDGIRKGVVQIHEGAW 708
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1385641982 773 YDPDKGGDINALCKYGNPNVLTLDIGTSQLAQATSAHTTLVEIEKYTGPIDNVTAFNGPVEM 834
Cdd:TIGR00509 709 YDPADVREPGGLCKYGNPNVLTADIGTSSLAQGNSGNTVLVEIEKYTGPAPPLTAFDQPAAA 770
|
|
| MopB_DMSOR-BSOR-TMAOR |
cd02769 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
54-679 |
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: 980.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 54 LTGSHWGAIRATVVDGRFVAAKPFEQDKYPSKMIAGLPDHVHNAARIRYPMVRVDWMRKGHQSDTSQRGDNRFVRVSWDE 133
Cdd:cd02769 1 PTASHWGAFRARVKDGRIVGVRPFEEDPDPSPLLDGVPDAVYSPTRIKYPMVRRGWLEKGPGSDRSLRGKEEFVRVSWDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 134 ALDLFYQELERVQKTYGPSALLTAS-GWQSTGMFHNASGMLARAIALHGNSVSTGGDYSTGAAQVILPRVVGSMEVY-EQ 211
Cdd:cd02769 81 ALDLVAAELKRVRKTYGNEAIFGGSyGWSSAGRFHHAQSLLHRFLNLAGGYVGSVGDYSTGAAQVILPHVVGSMEVYtEQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 212 QTSWPLVLQNSKTIVLWGSDMVKNQQANWWC-PDHDVYQYYEQLKEKvasgAISVISIDPVVTSTHDYLGrdkVKHIAIN 290
Cdd:cd02769 161 QTSWPVIAEHTELVVAFGADPLKNAQIAWGGiPDHQAYSYLKALKDR----GIRFISISPLRDDTAAELG---AEWIAIR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 291 PQTDVPLQLALAHTLYSEKLYDKNFLDNYCVGFDQFLPYLLGEKDGQPKDAAWAEKLCGIDADTIRALARQMAGDRTQII 370
Cdd:cd02769 234 PGTDVALMLALAHTLVTEGLHDKAFLARYTVGFDKFLPYLLGESDGVPKTPEWAAAICGIPAETIRELARRFASKRTMIM 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 371 AGWCVQRMQHGEQWSWMVVVLAAMLGQIGLPGGGFGFGWHYNGAGTPGRKGiilsgfsgsttVPPVHDSTDYKGYSSTIP 450
Cdd:cd02769 314 AGWSLQRAHHGEQPHWMAVTLAAMLGQIGLPGGGFGFGYHYSNGGGPPRGA-----------APPPALPQGRNPVSSFIP 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 451 IARFMDAILEPGKVINWNGKSVKLPPLKMCVFAGTNPFHRHQQINRIIEGWRKLETVIAIDNQWTSTCRFADIVLPATTQ 530
Cdd:cd02769 383 VARIADMLLNPGKPFDYNGKKLTYPDIKLVYWAGGNPFHHHQDLNRLIRAWQKPETVIVHEPFWTATARHADIVLPATTS 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 531 FERNDLDqfGNHSNRGIIAMKQVVSPQFEARNDFDIFRDLCRRFNREAAFTEGLDEMGWLKRIWQEGSQQGKGRGIHLPT 610
Cdd:cd02769 463 LERNDIG--GSGDNRYIVAMKQVVEPVGEARDDYDIFADLAERLGVEEQFTEGRDEMEWLRHLYEESRAQAAARGVEMPS 540
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1385641982 611 FEVFWNQQEYIEFDHPQMFVRHQAFREDPDLEPLGTPSGLIEIYSKTIADMQYDDCQGHPMWFEKIERS 679
Cdd:cd02769 541 FDEFWAQGYVELPIPEADFVRLADFREDPEANPLGTPSGRIEIFSETIAGFGYDDCPGHPTWLEPAEWL 609
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
54-678 |
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: 881.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 54 LTGSHWGAIRATVVDGRFVAAKPFEQDK-YPSKMIAGLPDHVHNAARIRYPMVRVDWMRKGHQSdTSQRGDNRFVRVSWD 132
Cdd:cd02751 1 PTACHWGPFKAHVKDGVIVRVEPDDTDQpRPCPRGRSVRDRVYSPDRIKYPMKRVGWLGNGPGS-RELRGEGEFVRISWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 133 EALDLFYQELERVQKTYGPSALLTAS-GWQSTGMFHNASGMLARAIALHGNSVSTGGDYSTGAAQVILPRVVGSMEVYEQ 211
Cdd:cd02751 80 EALDLVASELKRIREKYGNEAIFGGSyGWASAGRLHHAQSLLHRFLNLIGGYLGSYGTYSTGAAQVILPHVVGSDEVYEQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 212 QTSWPLVLQNSKTIVLWGSDMVKNQQANWWCPDHDVYQYYEQLKEKvasgAISVISIDPVVTSTHDYLGrdkVKHIAINP 291
Cdd:cd02751 160 GTSWDDIAEHSDLVVLFGANPLKTRQGGGGGPDHGSYYYLKQAKDA----GVRFICIDPRYTDTAAVLA---AEWIPIRP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 292 QTDVPLQLALAHTLYSEKLYDKNFLDNYCVGFDQFLPYLLGEKDGQPKDAAWAEKLCGIDADTIRALARQMAGDRTQIIA 371
Cdd:cd02751 233 GTDVALMLAMAHTLITEDLHDQAFLARYTVGFDEFKDYLLGESDGVPKTPEWAAEITGVPAETIRALAREIASKRTMIAQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 372 GWCVQRMQHGEQWSWMVVVLAAMLGQIGLPGGGFGFGWHYNGAGTPGRKGiilsgfsgsttVPPVHDSTDYKGYSSTIPI 451
Cdd:cd02751 313 GWGLQRAHHGEQPAWMLVTLAAMLGQIGLPGGGFGFGYGYSNGGGPPRGG-----------AGGPGLPQGKNPVKDSIPV 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 452 ARFMDAILEPGKVINWNGKSVKLPPLKMCVFAGTNPFHRHQQINRIIEGWRKLETVIAIDNQWTSTCRFADIVLPATTQF 531
Cdd:cd02751 382 ARIADALLNPGKEFTANGKLKTYPDIKMIYWAGGNPLHHHQDLNRLIKALRKDETIVVHDIFWTASARYADIVLPATTSL 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 532 ERNDLDQFGNHSNRGIIAMKQVVSPQFEARNDFDIFRDLCRRFNREAAFTEGLDEMGWLKRIWQEGSQQGKGRGIHLPTF 611
Cdd:cd02751 462 ERNDIGLTGNYSNRYLIAMKQAVEPLGEARSDYEIFAELAKRLGVEEEFTEGRDEMEWLEHLYEETRAKAAGPGPELPSF 541
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1385641982 612 EVFWNQQEYIEFDHPQMFVRHQAFREDPDLEPLGTPSGLIEIYSKTIADMQYDDCQGHPMWFEKIER 678
Cdd:cd02751 542 EEFWEKGIVRVPAAPKPFVAFADFREDPEANPLGTPSGKIEIYSETLADFGYDDCPGHPTWIEPWEG 608
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
61-817 |
0e+00 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 574.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 61 AIRATVVDGRFVAAKPFEQDKYPSKMI----AGLPDHVHNAARIRYPMVRVdwmrkghqsdtSQRGDNRFVRVSWDEALD 136
Cdd:COG0243 36 GLGVKVEDGRVVRVRGDPDHPVNRGRLcakgAALDERLYSPDRLTYPMKRV-----------GPRGSGKFERISWDEALD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 137 LFYQELERVQKTYGPSALLTASGWQSTGMFHNASGMLA-RAIALHG-NSVSTGGDYSTGAAQVILPRVVGSMEVyeqQTS 214
Cdd:COG0243 105 LIAEKLKAIIDEYGPEAVAFYTSGGSAGRLSNEAAYLAqRFARALGtNNLDDNSRLCHESAVAGLPRTFGSDKG---TVS 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 215 WPlVLQNSKTIVLWGSDMVKNQqanwwcpdHDVYQYYEQLKEKvaSGAIsVISIDPVVTSTHDYLGRdkvkHIAINPQTD 294
Cdd:COG0243 182 YE-DLEHADLIVLWGSNPAENH--------PRLLRRLREAAKK--RGAK-IVVIDPRRTETAAIADE----WLPIRPGTD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 295 VPLQLALAHTLYSEKLYDKNFLDNYCVGFDQFLPYLlgekdgQPKDAAWAEKLCGIDADTIRALARQMA-GDRTQIIAGW 373
Cdd:COG0243 246 AALLLALAHVLIEEGLYDRDFLARHTVGFDELAAYV------AAYTPEWAAEITGVPAEDIRELAREFAtAKPAVILWGM 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 374 CVQRMQHGEQWSWMVVVLAAMLGQIGLPgggfgfgwhynGAGTPGRKGiilsgfsgsttvppvhdstdykgysstipiar 453
Cdd:COG0243 320 GLQQHSNGTQTVRAIANLALLTGNIGKP-----------GGGPFSLTG-------------------------------- 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 454 fmDAILepgkvinwNGKSvklPPLKMCVFAGTNPFHRHQQINRIIEGWRKLETVIAIDNQWTSTCRFADIVLPATTQFER 533
Cdd:COG0243 357 --EAIL--------DGKP---YPIKALWVYGGNPAVSAPDTNRVREALRKLDFVVVIDTFLTETARYADIVLPATTWLER 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 534 NDLDqfGNHSNRGIIAMKQVVSPQFEARNDFDIFRDLCRRFNREAAFTEGLDEMGWLKRIWqegsQQGKGRGIhlpTFEV 613
Cdd:COG0243 424 DDIV--TNSEDRRVHLSRPAVEPPGEARSDWEIFAELAKRLGFEEAFPWGRTEEDYLRELL----EATRGRGI---TFEE 494
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 614 FWnQQEYIEFDHPQmfvrHQAFREDpdlEPLGTPSGLIEIYSKTIAdmqyddCQGHPMWFEKIERshGGPGSQRWPLHLQ 693
Cdd:COG0243 495 LR-EKGPVQLPVPP----EPAFRND---GPFPTPSGKAEFYSETLA------LPPLPRYAPPYEG--AEPLDAEYPLRLI 558
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 694 SVHPDFRLHSQLCESETLRQqyaVGGKEPVFINPQDASARGIRNGDIVRVFNARGQVLAGAVVSDRYAPGVARIHEGAWY 773
Cdd:COG0243 559 TGRSRDQWHSTTYNNPRLRE---IGPRPVVEINPEDAAALGIKDGDLVRVESDRGEVLARAKVTEGIRPGVVFAPHGWWY 635
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 1385641982 774 DPDKggdinalCKYGNPNVLTLDiGTSQLAQATSAHTTLVEIEK 817
Cdd:COG0243 636 EPAD-------DKGGNVNVLTPD-ATDPLSGTPAFKSVPVRVEK 671
|
|
| MopB_DmsA-EC |
cd02770 |
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
93-664 |
1.20e-114 |
|
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: 362.41 E-value: 1.20e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 93 HVHNAARIRYPMVRVDWmrkghqsdtsqRGDNRFVRVSWDEALDLFYQELERVQKTYGPSALLTASGWQSTGMFHNASGM 172
Cdd:cd02770 53 RVYNPDRLKYPMKRVGK-----------RGEGKFVRISWDEALDTIASELKRIIEKYGNEAIYVNYGTGTYGGVPAGRGA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 173 LARAIALHGNSVSTGGDYSTGAAQVILPRVVGSmevYEQQTSwPLVLQNSKTIVLWGSDMVKNQQANwwcpDHDVYqYYE 252
Cdd:cd02770 122 IARLLNLTGGYLNYYGTYSWAQITTATPYTYGA---AASGSS-LDDLKDSKLVVLFGHNPAETRMGG----GGSTY-YYL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 253 QLKEkvaSGAiSVISIDPVVTST----HDylgrdkvKHIAINPQTDVPLQLALAHTLYSEKLYDKNFLDNYCVGFD-QFL 327
Cdd:cd02770 193 QAKK---AGA-KFIVIDPRYTDTavtlAD-------EWIPIRPGTDAALVAAMAYVMITENLHDQAFLDRYCVGFDaEHL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 328 P-----------YLLGE-KDGQPKDAAWAEKLCGIDADTIRALARQMAGDRT-QIIAGWCVQRMQHGEQWSWMVVVLAAM 394
Cdd:cd02770 262 PegappnesykdYVLGTgYDGTPKTPEWASEITGVPAETIRRLAREIATTKPaAILQGWGPQRHANGEQAARAIMMLAAM 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 395 LGQIGLPGGgfgfgwhyNGAGTPGRKGIILSGFSGSTTvpPVHDStdykgysstIPIARFMDAILEPGKVINWNGK---S 471
Cdd:cd02770 342 TGNVGIPGG--------NTGARPGGSAYNGAGLPAGKN--PVKTS---------IPCFMWTDAIERGEEMTADDGGvkgA 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 472 VKL-PPLKMcVF--AGTNPFHRHQQINRIIEGWR----KLETVIAIDNQWTSTCRFADIVLPATTQFERNDLDQFGNHSN 544
Cdd:cd02770 403 DKLkSNIKM-IWnyAGNTLINQHSDDNNTTRALLddesKCEFIVVIDNFMTPSARYADILLPDTTELEREDIVLTSNAGM 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 545 RGI-IAMKQVVSPQFEARNDFDIFRDLCRRFNREAAFTEGLDEMGWLKRIWQEGSQQGKGrgihLPTFEVFWNQQEYiEF 623
Cdd:cd02770 482 MEYlIYSQKAIEPLYECKSDYEICAELAKRLGVEDQFTEGKTEQEWLEELYGQTRAKEPG----LPTYEEFREKGIY-RV 556
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1385641982 624 DHPQMFVRHQAFREDPDLEPLGTPSGLIEIYSKTIADMQYD 664
Cdd:cd02770 557 PRALPFVAFEDFREDPENNPLKTPSGKIEIYSKALADMAKT 597
|
|
| PRK14990 |
PRK14990 |
anaerobic dimethyl sulfoxide reductase subunit A; Provisional |
94-817 |
1.70e-105 |
|
anaerobic dimethyl sulfoxide reductase subunit A; Provisional
Pssm-ID: 184952 [Multi-domain] Cd Length: 814 Bit Score: 343.93 E-value: 1.70e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 94 VHNAARIRYPMVRVdwmrkghqsdtSQRGDNRFVRVSWDEALDLFYQELERVQKTYGPSALLTASGWQSTGMFHNAS--- 170
Cdd:PRK14990 114 VYNPDRLKYPMKRV-----------GARGEGKFERISWEEAYDIIATNMQRLIKEYGNESIYLNYGTGTLGGTMTRSwpp 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 171 --GMLARAIALHGNSVSTGGDYSTGAAQVILPRVVGSmevYEQQTSwPLVLQNSKTIVLWGSDMVKNQQANwwcpdHDVY 248
Cdd:PRK14990 183 gnTLVARLMNCCGGYLNHYGDYSSAQIAEGLNYTYGG---WADGNS-PSDIENSKLVVLFGNNPGETRMSG-----GGVT 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 249 QYYEQLKEKvaSGAISVIsIDPVVTSTHdyLGRDKvKHIAINPQTDVPLQLALAHTLYSEKLYDKNFLDNYCVGFDQ-FL 327
Cdd:PRK14990 254 YYLEQARQK--SNARMII-IDPRYTDTG--AGRED-EWIPIRPGTDAALVNGLAYVMITENLVDQPFLDKYCVGYDEkTL 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 328 P-----------YLLGE-KDGQPKDAAWAEKLCGIDADTIRALARQMAGDRTQIIA-GWCVQRMQHGEQWSWMVVVLAAM 394
Cdd:PRK14990 328 PasapknghykaYILGEgPDGVAKTPEWASQITGVPADKIIKLAREIGSTKPAFISqGWGPQRHANGEIATRAISMLAIL 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 395 LGQIGLpgggfgfgwhyNGAGTPGRKGiilsgfsgSTTVPPVHDSTDYKGYSSTIPIARFMDAIlEPGKVINW-----NG 469
Cdd:PRK14990 408 TGNVGI-----------NGGNSGAREG--------SYSLPFVRMPTLENPIQTSISMFMWTDAI-ERGPEMTAlrdgvRG 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 470 KSVKLPPLKMCV-FAGTNPFHRHQQINR---IIEGWRKLETVIAIDNQWTSTCRFADIVLPATTQFERND--LD-QFGNH 542
Cdd:PRK14990 468 KDKLDVPIKMIWnYAGNCLINQHSEINRtheILQDDKKCELIVVIDCHMTSSAKYADILLPDCTASEQMDfaLDaSCGNM 547
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 543 SNrgIIAMKQVVSPQFEARNDFDIFRDLCRRFNREAAFTEGLDEMGWLKRIWQegsqQGKGRGIHLPTFEVFWNQQEYIE 622
Cdd:PRK14990 548 SY--VIFNDQVIKPRFECKTIYEMTSELAKRLGVEQQFTEGRTQEEWMRHLYA----QSREAIPELPTFEEFRKQGIFKK 621
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 623 FDHPQMFVRHQAFREDPDLEPLGTPSGLIEIYSKTIADM-------QYDDCQGHPMWFEKIErSHGGPGSQRWPLHLQSV 695
Cdd:PRK14990 622 RDPQGHHVAYKAFREDPQANPLTTPSGKIEIYSQALADIaatwelpEGDVIDPLPIYTPGFE-SYQDPLNKQYPLQLTGF 700
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 696 HPDFRLHSQLCESETLRqqyaVGGKEPVFINPQDASARGIRNGDIVRVFNARGQVLAGAVVSDRYAPGVARIHEGAWYDP 775
Cdd:PRK14990 701 HYKSRVHSTYGNVDVLK----AACRQEMWINPLDAQKRGINNGDKVRIFNDRGEVHIEAKVTPRMMPGVVALGEGAWYDP 776
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 1385641982 776 DKggdiNALCKYGNPNVLTLDiGTSQLAQATSAHTTLVEIEK 817
Cdd:PRK14990 777 DA----KRVDKGGCINVLTTQ-RPSPLAKGNPSHTNLVQVEK 813
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
99-573 |
3.49e-84 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 273.51 E-value: 3.49e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 99 RIRYPMVRvdwmrkghqsdtsqRGDNRFVRVSWDEALDLFYQELERVQKTYGPSALLT---ASGWQSTGMFHNASGMLAR 175
Cdd:pfam00384 1 RLKYPMVR--------------RGDGKFVRVSWDEALDLIAKKLKRIIKKYGPDAIAInggSGGLTDVESLYALKKLLNR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 176 AIALHGNSVSTGGDYSTGAAQvilprVVGSMEVYEQQ-TSWPLVLQNSKTIVLWGSDMVKNQQANWWCpdhdvyQYYEQL 254
Cdd:pfam00384 67 LGSKNGNTEDHNGDLCTAAAA-----AFGSDLRSNYLfNSSIADIENADLILLIGTNPREEAPILNAR------IRKAAL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 255 KekvasGAISVISIDPVVTSTHDYlgrdkvKHIAINPQTDVPLQLALAHTLYSEKLYDKNFldnycvgfdqflpyllgek 334
Cdd:pfam00384 136 K-----GKAKVIVIGPRLDLTYAD------EHLGIKPGTDLALALAGAHVFIKELKKDKDF------------------- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 335 dgqpkdaawaeklcgidadTIRALarqmagdrtqIIAGWCVQRMQHGEQWSWMVVVLAAMLGQIGLPGGGFGFGWHYNGA 414
Cdd:pfam00384 186 -------------------APKPI----------IIVGAGVLQRQDGEAIFRAIANLADLTGNIGRPGGGWNGLNILQGA 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 415 GTPGRKgiilsgfsgsttvppvhdstdykgysstipiarfMDAILEPGKVINWNGKSVKLPPLKMCVFAGTNPFHRHQQI 494
Cdd:pfam00384 237 ASPVGA----------------------------------LDLGLVPGIKSVEMINAIKKGGIKVLYLLGNNPFVTHADE 282
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 495 NRIIEGWRKLETVIAIDNQW-TSTCRFADIVLPATTQFERNDLDQFGNHSNrgiIAMKQVVSPQFEARNDFDIFRDLCRR 573
Cdd:pfam00384 283 NRVVKALQKLDLFVVYDGHHgDKTAKYADVILPAAAYTEKNGTYVNTEGRV---QSTKQAVPPPGEAREDWKILRALSEV 359
|
|
| MopB_CT_DMSOR-BSOR-TMAOR |
cd02793 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
688-817 |
5.54e-75 |
|
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: 240.23 E-value: 5.54e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 688 WPLHLQSVHPDFRLHSQLCESEtLRQQYAVGGKEPVFINPQDASARGIRNGDIVRVFNARGQVLAGAVVSDRYAPGVARI 767
Cdd:cd02793 1 YPLHLLSNQPATRLHSQLDHGS-LSRAYKVQGREPIRINPADAAARGIADGDIVRVFNDRGACLAGAVVTDGIMPGVVQL 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1385641982 768 HEGAWYDPDKGGDINALCKYGNPNVLTLDIGTSQLAQATSAHTTLVEIEK 817
Cdd:cd02793 80 PTGAWYDPDDPGEPGPLCKHGNPNVLTLDIGTSSLAQGCSAQTCLVQIEK 129
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
59-574 |
1.86e-73 |
|
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: 245.32 E-value: 1.86e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 59 WGAIRATVVDGRFVAAKPFEQDKY----PSKMIAGLPDHVHNAARIRYPMVRVDwmrkghqsdtsqrGDNRFVRVSWDEA 134
Cdd:cd00368 10 GCGILVYVKDGKVVRIEGDPNHPVnegrLCDKGRAGLDGLYSPDRLKYPLIRVG-------------GRGKFVPISWDEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 135 LDLFYQELERVQKTYGPSALLTASGWQSTGMFHNASGMLARAIAlhGNSVSTGGDYSTGAAQVILPRvvgsMEVYEQQTS 214
Cdd:cd00368 77 LDEIAEKLKEIREKYGPDAIAFYGGGGASNEEAYLLQKLLRALG--SNNVDSHARLCHASAVAALKA----FGGGAPTNT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 215 WPlVLQNSKTIVLWGSDMVKNQQanwwcpdhdvyQYYEQLKEKVASGAiSVISIDPVVTSThdylGRDKVKHIAINPQTD 294
Cdd:cd00368 151 LA-DIENADLILLWGSNPAETHP-----------VLAARLRRAKKRGA-KLIVIDPRRTET----AAKADEWLPIRPGTD 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 295 VplqlALAhtlyseklydknfldnycvgfdqflpyllgekdgqpkDAAWAEKLCGIDADTIRALARQMA-GDRTQIIAGW 373
Cdd:cd00368 214 A----ALA-------------------------------------LAEWAAEITGVPAETIRALAREFAaAKRAVILWGM 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 374 CVQRMQHGEQWSWMVVVLAAMLGQIGLPgggfgfgwhynGAGtpgrkgiilsgfsgsttvppvhdstdykgysstipiar 453
Cdd:cd00368 253 GLTQHTNGTQNVRAIANLAALTGNIGRP-----------GGG-------------------------------------- 283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 454 fmdailepgkvinwngksvklpplkmcVFAGTNPFHRHQQINRIIEGWRKLETVIAIDNQWTSTCRFADIVLPATTQFER 533
Cdd:cd00368 284 ---------------------------LGPGGNPLVSAPDANRVRAALKKLDFVVVIDIFMTETAAYADVVLPAATYLEK 336
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1385641982 534 NDLdqFGNhSNRGIIAMKQVVSPQFEARNDFDIFRDLCRRF 574
Cdd:cd00368 337 EGT--YTN-TEGRVQLFRQAVEPPGEARSDWEILRELAKRL 374
|
|
| MopB_CT_DMSOR-like |
cd02777 |
The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
688-817 |
2.43e-66 |
|
The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide reductase (BSOR), trimethylamine N-oxide reductase (TMAOR) and other related proteins. DMSOR always catalyzes the reduction of DMSO to dimethylsulfide, but its cellular location and oligomerization state are organism-dependent. For example, in Rhodobacter sphaeriodes and Rhodobacter capsulatus, it is an 82-kDa monomeric soluble protein found in the periplasmic space; in E. coli, it is membrane-bound and exists as a heterotrimer. BSOR catalyzes the reduction of biotin sulfixode to biotin, and is unique among Mo enzymes because no additional auxiliary proteins or cofactors are required. TMAOR is similar to DMSOR, but its only natural substrate is TMAO. Also included in this group is the pyrogallol-phloroglucinol transhydroxylase from Pelobacter acidigallici. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239178 [Multi-domain] Cd Length: 127 Bit Score: 216.68 E-value: 2.43e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 688 WPLHLQSVHPDFRLHSQLCESETLRQQYAVGGKEPVFINPQDASARGIRNGDIVRVFNARGQVLAGAVVSDRYAPGVARI 767
Cdd:cd02777 1 YPLQLISPHPKRRLHSQLDNVPWLREAYKVKGREPVWINPLDAAARGIKDGDIVRVFNDRGAVLAGARVTDRIMPGVVAL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1385641982 768 HEGAWYDPDKGGDInalCKYGNPNVLTLDIGTSQLAQATSAHTTLVEIEK 817
Cdd:cd02777 81 PEGAWYDPDDNGGL---DKGGNPNVLTSDIPTSKLAQGNPANTCLVEIEK 127
|
|
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
61-664 |
4.80e-60 |
|
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: 212.49 E-value: 4.80e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 61 AIRATVVDGRFV-----AAKPFEQDKYPSKMIAgLPDHVHNAARIRYPMVRVDwmrkghqsdtsqRGDNRFVRVSWDEAL 135
Cdd:cd02766 13 SLLVTVEDGRIVrvegdPAHPYTRGFICAKGAR-YVERVYSPDRLLTPLKRVG------------RKGGQWERISWDEAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 136 DLFYQELERVQKTYGPSALLTASGWQSTGMFHNAS-GMLARAI---ALHGNSVSTGGdystGAAQVIlprVVGsmevyeq 211
Cdd:cd02766 80 DTIAAKLKEIKAEYGPESILPYSYAGTMGLLQRAArGRFFHALgasELRGTICSGAG----IEAQKY---DFG------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 212 qTSW---PLVLQNSKTIVLWGSDMVknqqanwWCPDHdvyqYYEQLKEKVASGAIsVISIDPVVTSThdylGRDKVKHIA 288
Cdd:cd02766 146 -ASLgndPEDMVNADLIVIWGINPA-------ATNIH----LMRIIQEARKRGAK-VVVIDPYRTAT----AARADLHIQ 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 289 INPQTDVPLQLALAHTLYSEKLYDKNFLDNYCVGFDQFLPYLlgekdgQPKDAAWAEKLCGIDADTIRALARQMA-GDRT 367
Cdd:cd02766 209 IRPGTDGALALGVAKVLFREGLYDRDFLARHTEGFEELKAHL------ETYTPEWAAEITGVSAEEIEELARLYGeAKPP 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 368 QIIAGWCVQRMQHGEQWSWMVVVLAAMLGQIGlpgggfgfgwhYNGAGtpgrkgiILSGFSGsttvppvhdstdykgyss 447
Cdd:cd02766 283 SIRLGYGMQRYRNGGQNVRAIDALPALTGNIG-----------VPGGG-------AFYSNSG------------------ 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 448 tipiarfmdailepgkvinwngksvklPPLKMCVFAGTNPFHRHQQINRIIEG-WRKLETVIAIDNQWTSTCRFADIVLP 526
Cdd:cd02766 327 ---------------------------PPVKALWVYNSNPVAQAPDSNKVRKGlAREDLFVVVHDQFMTDTARYADIVLP 379
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 527 ATTQFERNDLDQFGNHSNrgIIAMKQVVSPQFEARNDFDIFRDLCRRFNREAAFTEGlDEMGWLKRIWqegsqqgkgRGI 606
Cdd:cd02766 380 ATTFLEHEDVYASYWHYY--LQYNEPAIPPPGEARSNTEIFRELAKRLGFGEPPFEE-SDEEWLDQAL---------DGT 447
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1385641982 607 HLPTFEvfwnqQEYIEFDHPQMfvrhQAFREDP-DLEPLGTPSGLIEIYSKTIADMQYD 664
Cdd:cd02766 448 GLPLEG-----IDLERLLGPRK----AGFPLVAwEDRGFPTPSGKFEFYSERAAKRGLP 497
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
62-765 |
2.71e-53 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 197.41 E-value: 2.71e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 62 IRATVVDGRFVAAKPFEQdkYP-------SKMIAGLpDHVHNAARIRYPMVRvdwmrkghqsdtsqrGDNRFVRVSWDEA 134
Cdd:COG3383 20 IDLEVKDGKIVKVEGDPD--HPvnrgrlcVKGRFGF-EFVNSPDRLTTPLIR---------------RGGEFREVSWDEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 135 LDLFYQELERVQKTYGPSAL-LTASGWQSTGMFHNAsGMLARAiALHGNSVSTGGDY---STGAAqviLPRVVGSMEV-- 208
Cdd:COG3383 82 LDLVAERLREIQAEHGPDAVaFYGSGQLTNEENYLL-QKLARG-VLGTNNIDNNARLcmaSAVAG---LKQSFGSDAPpn 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 209 -YEQqtswplvLQNSKTIVLWGSDMVknqqanwWCpdHDVYqyYEQLKEKVASGAiSVISIDPVVTSTHDYLGRdkvkHI 287
Cdd:COG3383 157 sYDD-------IEEADVILVIGSNPA-------EA--HPVL--ARRIKKAKKNGA-KLIVVDPRRTETARLADL----HL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 288 AINPQTDVPLQLALAHTLYSEKLYDKNFLDNYCVGFDQFLPYLLGEkdgqpkDAAWAEKLCGIDADTIRALARQMA-GDR 366
Cdd:COG3383 214 QIKPGTDLALLNGLLHVIIEEGLVDEDFIAERTEGFEELKASVAKY------TPERVAEITGVPAEDIREAARLIAeAKR 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 367 TQIIagWCVQRMQHgEQWSWMVVV---LAAMLGQIGLPGGGFGFGWHYN---GAGTPGRKGIILSGFSgsttvpPVHDST 440
Cdd:COG3383 288 AMIL--WGMGVNQH-TQGTDNVNAiinLALATGNIGRPGTGPFPLTGQNnvqGGRDMGALPNVLPGYR------DVTDPE 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 441 DYKGYSS-----TIP------IARFMDAILEpGKVinwngksvklpplKMCVFAGTNPFHRHQQINRIIEGWRKLETVIA 509
Cdd:COG3383 359 HRAKVADawgvpPLPdkpgltAVEMFDAIAD-GEI-------------KALWIIGENPAVSDPDANHVREALEKLEFLVV 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 510 IDNQWTSTCRFADIVLPATTQFERNdldqfGNHSN--RGIIAMKQVVSPQFEARNDFDIFRDLCRRFNREAAFT---EGL 584
Cdd:COG3383 425 QDIFLTETAEYADVVLPAASWAEKD-----GTFTNteRRVQRVRKAVEPPGEARPDWEIIAELARRLGYGFDYDspeEVF 499
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 585 DEMGWL---------KRIWQEGSQQgkgrgihlptfevfWnqqEYIEFDHPQMFVRHqafredpdLEPLGTPSGLieiys 655
Cdd:COG3383 500 DEIARLtpdysgisyERLEALGGVQ--------------W---PCPSEDHPGTPRLF--------TGRFPTPDGK----- 549
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 656 ktiADMQYDDcqghpmWFEKIERShggpgSQRWPLHLQSVHPDFRLHS--QLCESETLRQQYAvggkEP-VFINPQDASA 732
Cdd:COG3383 550 ---ARFVPVE------YRPPAELP-----DEEYPLVLTTGRLLDQWHTgtRTRRSPRLNKHAP----EPfVEIHPEDAAR 611
|
730 740 750
....*....|....*....|....*....|...
gi 1385641982 733 RGIRNGDIVRVFNARGQVLAGAVVSDRYAPGVA 765
Cdd:COG3383 612 LGIKDGDLVRVSSRRGEVVLRARVTDRVRPGTV 644
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
62-664 |
1.32e-50 |
|
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: 185.20 E-value: 1.32e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 62 IRATVVDGRFVAAKPFEQDKYPSKMIA----GLPDHVHNAARIRYPMVRVdwmrkghqsdtSQRGDNRFVRVSWDEALDL 137
Cdd:cd02759 13 VLVYVKDGKLVKVEGDPNHPTNKGRLCmrglAAPEIVYHPDRLLYPLKRV-----------GERGENKWERISWDEALDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 138 FYQELERVQKTYGPSALLTASGwqsTGMFHNASGML--ARAIALHGNSVSTGGDYSTGAAQVILPRVVGSMEVYEQQTSW 215
Cdd:cd02759 82 IAEKLAEIKAEYGPESIATAVG---TGRGTMWQDSLfwIRFVRLFGSPNLFLSGESCYWPRDMAHALTTGFGLGYDEPDW 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 216 PlvlqNSKTIVLWGsdmvKNQQANWWCPdhdvyqYYEQLKEKVASGAiSVISIDPVVTsthdYLGRDKVKHIAINPQTDV 295
Cdd:cd02759 159 E----NPECIVLWG----KNPLNSNLDL------QGHWLVAAMKRGA-KLIVVDPRLT----WLAARADLWLPIRPGTDA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 296 PLQLALAHTLYSEKLYDKNFLDNYCVGFDQFLPYLlgekdgQPKDAAWAEKLCGIDADTIRALARQMAGDRtqiiaGWCV 375
Cdd:cd02759 220 ALALGMLNVIINEGLYDKDFVENWCYGFEELAERV------QEYTPEKVAEITGVPAEKIRKAARLYATAK-----PACI 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 376 qrmqhgeqwswmvvvlaamlgQIGLPGGgfgfgwHYNGAGTPGRKGIILSGFSGSTTVPpvhdstdykgysstipiarfm 455
Cdd:cd02759 289 ---------------------QWGLAID------QQKNGTQTSRAIAILRAITGNLDVP--------------------- 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 456 dailepgkvinwnGKSVKLP-PLKMCVFAGTNPFHRHQQINRIIEGWRKLETVIAIDNQWTSTCRFADIVLPATTQFERN 534
Cdd:cd02759 321 -------------GGNLLIPyPVKMLIVFGTNPLASYADTAPVLEALKALDFIVVVDLFMTPTAMLADIVLPVAMSLERP 387
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 535 DLDqfGNHSNRGIIAMKQ-VVSPQFEARNDFDIFRDLCRRFNREAAfteglDEMGWLKRIWQEGSQQGkgrgihlptfev 613
Cdd:cd02759 388 GLR--GGFEAENFVQLRQkAVEPYGEAKSDYEIVLELGKRLGPEEA-----EYYKYEKGLLRPDGQPG------------ 448
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1385641982 614 fwnqqeyiefdhpqmfvrhqafredpdlepLGTPSGLIEIYSKTIADMQYD 664
Cdd:cd02759 449 ------------------------------FNTPTGKVELYSTMLEELGYD 469
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
94-581 |
2.38e-47 |
|
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and other related proteins. Thiosulfate reductase catalyzes the cleavage of sulfur-sulfur bonds in thiosulfate. Polysulfide reductase is a membrane-bound enzyme that catalyzes the reduction of polysulfide using either hydrogen or formate as the electron donor. Members of the MopB_Thiosulfate-R-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239156 [Multi-domain] Cd Length: 454 Bit Score: 175.18 E-value: 2.38e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 94 VHNAARIRYPMVRVdwmrkghqsdtSQRGDNRFVRVSWDEALDLFYQELERVQKTYGPSALL--TASGWQSTGMFHNASG 171
Cdd:cd02755 50 LYDPDRLKKPLIRV-----------GERGEGKFREASWDEALQYIASKLKEIKEQHGPESVLfgGHGGCYSPFFKHFAAA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 172 MLARAIALHGNSVSTGgdYSTGAAQVILPrvVGSMEVYEqqtswplvLQNSKTIVLWGsdmvknqqanwwcpdHDVYQ-- 249
Cdd:cd02755 119 FGSPNIFSHESTCLAS--KNLAWKLVIDS--FGGEVNPD--------FENARYIILFG---------------RNLAEai 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 250 ---YYEQLKEKVASGAiSVISIDP----VVTSTHDYlgrdkvkhIAINPQTDVPLQLALAHTLYSEKLYDKNFLDNYCVG 322
Cdd:cd02755 172 ivvDARRLMKALENGA-KVVVVDPrfseLASKADEW--------IPIKPGTDLAFVLALIHVLISENLYDAAFVEKYTNG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 323 FDQFlpyllgEKDGQPKDAAWAEKLCGIDADTIRALARQMAGDRTQIIA--GWCVQRMQHGEQWSWMVVVLAAMLGQIgl 400
Cdd:cd02755 243 FELL------KAHVKPYTPEWAAQITDIPADTIRRIAREFAAAAPHAVVdpGWRGTFYSNSFQTRRAIAIINALLGNI-- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 401 pgggfgfgwhyngagtpGRKGiilsGFSGSTTVPPvhdstdYkgysstipiarfmdailepgkvinwngksvklpPLKMC 480
Cdd:cd02755 315 -----------------DKRG----GLYYAGSAKP------Y---------------------------------PIKAL 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 481 VFAGTNPFHRHQQINRIIEGWRKLETVIAIDNQWTSTCRFADIVLPATTQFERNDLDQFGNHSNRGIIAMKQVVSPQFEA 560
Cdd:cd02755 335 FIYRTNPFHSMPDRARLIKALKNLDLVVAIDILPSDTALYADVILPEATYLERDEPFSDKGGPAPAVATRQRAIEPLYDT 414
|
490 500
....*....|....*....|.
gi 1385641982 561 RNDFDIFRDLCRRFNREAAFT 581
Cdd:cd02755 415 RPGWDILKELARRLGLFGTPS 435
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
62-605 |
5.25e-43 |
|
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: 165.09 E-value: 5.25e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 62 IRATVVDGRFVAAKPFEQdkYPSKM----IAG--LPDHVHNAARIRYPMVRvdwmrkghqsdtsqRGDNRFVRVSWDEAL 135
Cdd:cd02754 13 VEIGVKDGKVVAVRGDPE--HPVNRgrlcIKGlnLHKTLNGPERLTRPLLR--------------RNGGELVPVSWDEAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 136 DLFYQELERVQKTYGPSALltasGWQSTGMFHN----ASGMLARAiALHGNSVSTGGDYSTGAAQVILPRVVGSMEV--- 208
Cdd:cd02754 77 DLIAERFKAIQAEYGPDSV----AFYGSGQLLTeeyyAANKLAKG-GLGTNNIDTNSRLCMASAVAGYKRSFGADGPpgs 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 209 YEQqtswplvLQNSKTIVLWGSDMVknqqanwWCpdHDV-YQYYEQLKEKvASGAIsVISIDPVVTSTHDYLGRdkvkHI 287
Cdd:cd02754 152 YDD-------IEHADCFFLIGSNMA-------EC--HPIlFRRLLDRKKA-NPGAK-IIVVDPRRTRTADIADL----HL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 288 AINPQTDVPLQLALAHTLYSEKLYDKNFLDNYCVGFDQFLPYLlgekdgQPKDAAWAEKLCGIDADTIRALARQMaGDRT 367
Cdd:cd02754 210 PIRPGTDLALLNGLLHVLIEEGLIDRDFIDAHTEGFEELKAFV------ADYTPEKVAEITGVPEADIREAARLF-GEAR 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 368 QIIAGWCVQRMQHgEQWSW---MVVVLAAMLGQIGLPgggfgfgwhYNGA----GTP----GRKgiilsgFSGSTTVPPV 436
Cdd:cd02754 283 KVMSLWTMGVNQS-TQGTAannAIINLHLATGKIGRP---------GSGPfsltGQPnamgGRE------VGGLANLLPG 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 437 HDSTDYKgySSTIPIARFMDaiLEPGKVINWNG-KSVKLPP------LKMCVFAGTNPFHRHQQINRIIEGWRKLETVIA 509
Cdd:cd02754 347 HRSVNNP--EHRAEVAKFWG--VPEGTIPPKPGlHAVEMFEaiedgeIKALWVMCTNPAVSLPNANRVREALERLEFVVV 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 510 IDNQWTS-TCRFADIVLPATTQFERNDLdqFGNhSNRGIIAMKQVVSPQFEARNDFDIFRDLCRRFNREAAFTEGLDEmg 588
Cdd:cd02754 423 QDAFADTeTAEYADLVLPAASWGEKEGT--MTN-SERRVSLLRAAVEPPGEARPDWWILADVARRLGFGELFPYTSPE-- 497
|
570
....*....|....*..
gi 1385641982 589 wlkRIWQEGSQQGKGRG 605
Cdd:cd02754 498 ---EVFEEYRRLSRGRG 511
|
|
| MopB_Nitrate-R-NarG-like |
cd02750 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
61-574 |
1.10e-42 |
|
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under anaerobic conditions in the presence of nitrate, E. coli synthesizes the cytoplasmic membrane-bound quinol-nitrate oxidoreductase (NarGHI), which reduces nitrate to nitrite and forms part of a redox loop generating a proton-motive force. Found in prokaryotes and some archaea, NarGHI usually functions as a heterotrimer. The alpha chain contains the molybdenum cofactor-containing Mo-bisMGD catalytic subunit. Members of the MopB_Nitrate-R-NarG-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239151 [Multi-domain] Cd Length: 461 Bit Score: 162.10 E-value: 1.10e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 61 AIRATVVDGRFVAAKPfeQDKYPSkMIAGLPDH--------------VHNAARIRYPMVRVdwmrkghqsdtSQRGDNRF 126
Cdd:cd02750 17 SWNVYVKNGIVTREEQ--ATDYPE-TPPDLPDYnprgcqrgasfswyLYSPDRVKYPLKRV-----------GARGEGKW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 127 VRVSWDEALDLFYQELERVQKTYGPSALLTASGWQSTGMFHNASGM----LARAIALHGNSVStgGDYSTGAaqvilPRV 202
Cdd:cd02750 83 KRISWDEALELIADAIIDTIKKYGPDRVIGFSPIPAMSMVSYAAGSrfasLIGGVSLSFYDWY--GDLPPGS-----PQT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 203 VGSM-EVYEqqtswPLVLQNSKTIVLWGSDMVKNQqanwwCPDhdvYQYYEQLKEKvasGAiSVISIDPvvtsthDYLGR 281
Cdd:cd02750 156 WGEQtDVPE-----SADWYNADYIIMWGSNVPVTR-----TPD---AHFLTEARYN---GA-KVVVVSP------DYSPS 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 282 DKV--KHIAINPQTDVPLQLALAHTLYSEKLYDKNFLDNYCvgfDqfLPYLLgekdgqpKDAAWAEKLCGIDADTIRALA 359
Cdd:cd02750 213 AKHadLWVPIKPGTDAALALAMAHVIIKEKLYDEDYLKEYT---D--LPFLV-------YTPAWQEAITGVPRETVIRLA 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 360 RQMA-GDRTQIIAGWCVQRMQHGEQWSWMVVVLAAMLGQIGLpgggfgfgwhyNGAGtpgrkgiilsgfsgsttvppvhD 438
Cdd:cd02750 281 REFAtNGRSMIIVGAGINHWYHGDLCYRALILLLALTGNEGK-----------NGGG----------------------W 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 439 STdYKGysstipiarfmdailEPGKVINWNGksvklpplkmcvfagtNPFHRHQQINRIIEG--WRKLETVIAIDNQWTS 516
Cdd:cd02750 328 AH-YVG---------------QPRVLFVWRG----------------NLFGSSGKGHEYFEDapEGKLDLIVDLDFRMDS 375
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1385641982 517 TCRFADIVLPATTQFERNDLDQFGNHsnRGIIAMKQVVSPQFEARNDFDIFRDLCRRF 574
Cdd:cd02750 376 TALYSDIVLPAATWYEKHDLSTTDMH--PFIHPFSPAVDPLWEAKSDWEIFKALAKKV 431
|
|
| Fdh-alpha |
TIGR01591 |
formate dehydrogenase, alpha subunit, archaeal-type; This model describes a subset of formate ... |
92-773 |
1.31e-42 |
|
formate dehydrogenase, alpha subunit, archaeal-type; This model describes a subset of formate dehydrogenase alpha chains found mainly archaea but also in alpha and gamma proteobacteria and a small number of gram positive bacteria. The alpha chain contains domains for molybdopterin dinucleotide binding and molybdopterin oxidoreductase (pfam01568 and pfam00384, respectively). The holo-enzyme also contains beta and gamma subunits. The enzyme catalyzes the oxidation of formate (produced from pyruvate during anaerobic growth) to carbon dioxide with the concomitant release of two electrons and two protons. The enzyme's purpose is to allow growth on formate in some circumstances and, in the case of FdhH in gamma proteobacteria, to pass electrons to hydrogenase (by which process acid is neutralized). This model is well-defined, with only a single fragmentary sequence falling between trusted and noise. The alpha subunit of a version of nitrate reductase is closely related.
Pssm-ID: 130652 [Multi-domain] Cd Length: 671 Bit Score: 165.72 E-value: 1.31e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 92 DHVHNAARIRYPMVRvdwmrkghqsdtsqRGDnRFVRVSWDEALDLFYQELERVQKTYGPSALLTASGWQSTGMFHNASG 171
Cdd:TIGR01591 46 EFINSKDRLTTPLIR--------------EGD-KFREVSWDEAISYIAEKLKEIKEKYGPDSIGFIGSSRGTNEENYLLQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 172 MLARAIaLHGNSVSTGGDYSTGAAQVILPRVVGSmevyEQQTSWPLVLQNSKTIVLWGSDMVKNqqanwwcpdHDVYQYY 251
Cdd:TIGR01591 111 KLARAV-IGTNNVDNCARVCHGPSVAGLKQTVGI----GAMSNTISEIENADLIVIIGYNPAES---------HPVVAQY 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 252 eqLKEKVASGAiSVISIDPVVTST---HDYlgrdkvkHIAINPQTDVPLQLALAHTLYSEKLYDKNFLDNYCVGFDQFLP 328
Cdd:TIGR01591 177 --LKNAKRNGA-KIIVIDPRKTETakiADL-------HIPLKPGTDIALLNAMANVIIEEGLYDKAFIEKRTEGFEEFRE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 329 YLlgeKDGQPKdaaWAEKLCGIDADTIRALARQMA-GDRTQIIAGWCVQRMQHGEQWSWMVVVLAAMLGQIGLPGGGFGF 407
Cdd:TIGR01591 247 IV---KGYTPE---YVEDITGVPADLIREAARMYAkAGSAAILWGMGVTQHSQGVETVMALINLAMLTGNIGKPGGGVNP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 408 GWHYN---GAGTPGRKGIILSGFSgsttvpPVHDSTDYKGYSStipIARFMDAILEPGKVINWNGKSVKLPPLKMCVFAG 484
Cdd:TIGR01591 321 LRGQNnvqGACDMGALPDFLPGYQ------PVSDEEVREKFAK---AWGVVKLPAEPGLRIPEMIDAAADGDVKALYIMG 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 485 TNPFHRHQQINRIIEGWRKLETVIAIDNQWTSTCRFADIVLPATTQFERNdlDQFGNhSNRGIIAMKQVVSPQFEARNDF 564
Cdd:TIGR01591 392 EDPLQSDPNTSKVRKALEKLELLVVQDIFMTETAKYADVVLPAAAWLEKE--GTFTN-AERRIQRFFKAVEPKGESKPDW 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 565 DIFRDLCRR----FNREAAftegldemgwlKRIWQEGSQQGkgrgihlPTF-EVfwNQQEYIEFDHPQMFVRHQAFREDP 639
Cdd:TIGR01591 469 EIIQELANAlgldWNYNHP-----------QEIMDEIRELT-------PLFaGL--TYERLDELGSLQWPCNDSDASPTS 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 640 DL--EPLGTPSGLIEIYSKTiadmqyddcqghpmWFEKIERSHGgpgsqRWPLHLQSVHPDFRLH--SQLCESETLRqqy 715
Cdd:TIGR01591 529 YLykDKFATPDGKAKFIPLE--------------WVAPIEEPDD-----EYPLILTTGRVLTHYNvgEMTRRVAGLR--- 586
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 1385641982 716 AVGGKEPVFINPQDASARGIRNGDIVRVFNARGQVLAGAVVSDRYAPGVARIHEGAWY 773
Cdd:TIGR01591 587 RLSPEPYVEINTEDAKKLGIKDGDLVKVKSRRGEITLRAKVSDRVNKGAIYITMHFWD 644
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
61-764 |
7.51e-42 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 164.46 E-value: 7.51e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 61 AIRATVVDGRFV------AAKPFEqDKYPSKMIAGLpDHVHNAARIRYPMVRVdwmrkghqsdtSQRGDNRFVRVSWDEA 134
Cdd:PRK15488 56 PIEARVVNGKNVfiqgnpKAKSFG-TKVCARGGSGH-SLLYDPQRIVKPLKRV-----------GERGEGKWQEISWDEA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 135 LDLFYQELERVQKTYGPSALL--TASGWQSTGMFHnasgmLARAIAlhgnSVSTGGDYST-GAAQVILPRVV--GSMEvy 209
Cdd:PRK15488 123 YQEIAAKLNAIKQQHGPESVAfsSKSGSLSSHLFH-----LATAFG----SPNTFTHASTcPAGYAIAAKVMfgGKLK-- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 210 eqqtswpLVLQNSKTIVLWGsdmvknqqanwwcpdHDVYQ-----YYEQLKEKVASGAISVISIDP---VVTSTHDylgr 281
Cdd:PRK15488 192 -------RDLANSKYIINFG---------------HNLYEginmsDTRGLMTAQMEKGAKLVVFEPrfsVVASKAD---- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 282 dkvKHIAINPQTDVPLQLALAHTLYSEKLYDKNFLDNYCVGFDQFlpyllgEKDGQPKDAAWAEKLCGIDADTIRALARQ 361
Cdd:PRK15488 246 ---EWHAIRPGTDLAVVLALCHVLIEENLYDKAFVERYTSGFEEL------AASVKEYTPEWAEAISDVPADDIRRIARE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 362 MAGDRTQIIAGWCVQRMQHGEQW--SWMVVVLAAMLGQIglpgggfgfgwhyngagtpGRKGIILSGFSGST-------T 432
Cdd:PRK15488 317 LAAAAPHAIVDFGHRATFTPEEFdmRRAIFAANVLLGNI-------------------ERKGGLYFGKNASVynklageK 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 433 VPPVHDSTDYKGYSStiPIARFMDAILEPGKVINWNGKSVK---------LP-PLKMCVFAGTNPFHRHQQINRIIEGWR 502
Cdd:PRK15488 378 VAPTLAKPGVKGMPK--PTAKRIDLVGEQFKYIAAGGGVVQsiidatltqKPyQIKGWVMSRHNPMQTVTDRADVVKALK 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 503 KLETVIAIDNQWTSTCRFADIVLPATTQFERND--LDQFGNHSNRGIiaMKQVVSPQFEARNDFDIFRDLCRRFnreaaf 580
Cdd:PRK15488 456 KLDLVVVCDVYLSESAAYADVVLPESTYLERDEeiSDKSGKNPAYAL--RQRVVEPIGDTKPSWQIFKELGEKM------ 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 581 teGLDEMGWLKRIWQEGSQQGKGRGIHLPTFEvfwnQQEYIEFDHPQM---------FVRH----QAFREDPDLE---PL 644
Cdd:PRK15488 528 --GLGQYYPWQDMETLQLYQVNGDHALLKELK----KKGYVSFGVPLLlrepkmvakFVARypnaKAVDEDGTYGsqlKF 601
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 645 GTPSGLIEIYSKTIADM-------QYDDC---QGHPMWFEKIERS-HGGPGSQRWPLhlqsvhpdfrLHSQLCESetlrq 713
Cdd:PRK15488 602 KTPSGKIELFSAKLEALapgygvpRYRDValkKEDELYFIQGKVAvHTNGATQNVPL----------LANLMSDN----- 666
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|.
gi 1385641982 714 qyavggkePVFINPQDASARGIRNGDIVRVFNARGQVLAGAVVSdryaPGV 764
Cdd:PRK15488 667 --------AVWIHPQTAGKLGIKNGDEIRLENSVGKEKGKALVT----PGI 705
|
|
| MopB_4 |
cd02765 |
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
61-672 |
2.94e-38 |
|
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: 151.09 E-value: 2.94e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 61 AIRATVVDGRFVAAKPFE--QDKYPSKMIAGLP--DHVHNAARIRYPMVRVdwmrkghqsdtSQRGDNRFVRVSWDEALD 136
Cdd:cd02765 13 PLKCHVRDGKIVKVEPNEwpDKTYKRGCTRGLShlQRVYSPDRLKYPMKRV-----------GERGEGKFERITWDEALD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 137 LFYQELERVQKTYGPSALLtasgwqstgmFHNASGMLArAIALHGNSVSTGGDYSTGAAQVILPRVVGSMEV----YEQQ 212
Cdd:cd02765 82 TIADKLTEAKREYGGKSIL----------WMSSSGDGA-ILSYLRLALLGGGLQDALTYGIDTGVGQGFNRVtgggFMPP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 213 TSWPLVLQNSKTIVLWGSDMVKNQQANwwcpdhdvYQYYEQLKEKvasGAiSVISIDPVVTSThdylGRDKVKHIAINPQ 292
Cdd:cd02765 151 TNEITDWVNAKTIIIWGSNILETQFQD--------AEFFLDAREN---GA-KIVVIDPVYSTT----AAKADQWVPIRPG 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 293 TDVPLQLALAHTLYSEKLYDKNFLDNYCVGfdqflPYLLGEKDGQ---PKDAAWAEKLCGI-----DADTIR-------- 356
Cdd:cd02765 215 TDPALALGMINYILEHNWYDEAFLKSNTSA-----PFLVREDNGTllrQADVTATPAEDGYvvwdtNSDSPEpvaatnin 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 357 -ALARQMAGDRTQIIAGWCVQRMQHGEQWSWMVVVLAamlgqiGLPGGGFGFGWHYNGAGTPGrkgiILSGFSGSTTVpp 435
Cdd:cd02765 290 pALEGEYTINGVKVHTVLTALREQAASYPPKAAAEIC------GLEEAIIETLAEWYATGKPS----GIWGFGGVDRY-- 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 436 VHDSTDYKGYSSTIPIARFMdailepGKVINWNGKsvklppLKMCVFAGTNpFHRHQQINRIIEGW-RKLETVIAIDNQW 514
Cdd:cd02765 358 YHSHVFGRTAAILAALTGNI------GRVGGGVGQ------IKFMYFMGSN-FLGNQPDRDRWLKVmKNLDFIVVVDIFH 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 515 TSTCRFADIVLPATTQFERNDLdqFGNHSNRGIIAMKQ-VVSPQFEARNDFDIFRDLCRRFNREAAFTEglDEMGWLKRi 593
Cdd:cd02765 425 TPTVRYADIVLPAAHWFEVEDL--LVRYTTHPHVLLQQkAIEPLFESKSDFEIEKGLAERLGLGDYFPK--TPEDYVRA- 499
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 594 wQEGSQQGKGRGIhlpTFEVFWNQQEYIEFDHPqmfvrhqafrEDPDL----EPLGTPSGLIEIYSKTIAdmqyDDCQGH 669
Cdd:cd02765 500 -FMNSDDPALDGI---TWEALKEEGIIMRLATP----------EDPYVayldQKFGTPSGKLEFYNEAAP----ELEEAL 561
|
...
gi 1385641982 670 PMW 672
Cdd:cd02765 562 PLP 564
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
65-541 |
2.68e-35 |
|
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: 141.77 E-value: 2.68e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 65 TVVDGRFVAAK-----PFEQDKYPSKMIAgLPDHVHNAARIRYPMVRVDwmrkghqsdtsqrgdNRFVRVSWDEALDLFY 139
Cdd:cd02762 16 TVEDGRVASIRgdpddPLSKGYICPKAAA-LGDYQNDPDRLRTPMRRRG---------------GSFEEIDWDEAFDEIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 140 QELERVQKTYGPSALL----TASGWQSTGMFHnaSGMLARAIALHGNSVSTGGDYSTG-AAQVILPRVVGSMEVYEqqts 214
Cdd:cd02762 80 ERLRAIRARHGGDAVGvyggNPQAHTHAGGAY--SPALLKALGTSNYFSAATADQKPGhFWSGLMFGHPGLHPVPD---- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 215 wplvLQNSKTIVLWGSDMVKNQQANWWCPDHDVyqyyeQLKEKVASGAiSVISIDPVVTSTHDYLGRdkvkHIAINPQTD 294
Cdd:cd02762 154 ----IDRTDYLLILGANPLQSNGSLRTAPDRVL-----RLKAAKDRGG-SLVVIDPRRTETAKLADE----HLFVRPGTD 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 295 VPLQLALAHTLYSEKLYDKNFLDNYCVGFDQFLPYLlgekdgQPKDAAWAEKLCGIDADTIRALARQMA-GDRTQIIAGW 373
Cdd:cd02762 220 AWLLAAMLAVLLAEGLTDRRFLAEHCDGLDEVRAAL------AEFTPEAYAPRCGVPAETIRRLAREFAaAPSAAVYGRL 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 374 CVQRMQHGEQWSWMVVVLAAMLGQIGLPGGGFGFGWHYNGAGTPGRKGIilsGFSGSTTvpPVHDSTDYKGyssTIPIAR 453
Cdd:cd02762 294 GVQTQLFGTLCSWLVKLLNLLTGNLDRPGGAMFTTPALDLVGQTSGRTI---GRGEWRS--RVSGLPEIAG---ELPVNV 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 454 FMDAILEPGkvinwnGKSVKlpplKMCVFAGtNPFHRHQQINRIIEGWRKLETVIAIDNQWTSTCRFADIVLPATTQFER 533
Cdd:cd02762 366 LAEEILTDG------PGRIR----AMIVVAG-NPVLSAPDGARLEAALGGLEFMVSVDVYMTETTRHADYILPPASQLEK 434
|
....*...
gi 1385641982 534 NDLDQFGN 541
Cdd:cd02762 435 PHATFFNL 442
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
92-573 |
1.71e-32 |
|
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: 132.72 E-value: 1.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 92 DHVHNAARIRYPMVRVDwmrkghqsdtsqrgdNRFVRVSWDEALDLFYQELERVQKTYGPSALLTASGWQSTgmfhNASG 171
Cdd:cd02753 47 DFVNSKDRLTKPLIRKN---------------GKFVEASWDEALSLVASRLKEIKDKYGPDAIAFFGSAKCT----NEEN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 172 ML----ARAIaLHGNSVSTGGDY---STGAAqviLPRVVGSmevyEQQTSWPLVLQNSKTIVLWGSDMVKNqqanwwcpd 244
Cdd:cd02753 108 YLfqklARAV-GGTNNVDHCARLchsPTVAG---LAETLGS----GAMTNSIADIEEADVILVIGSNTTEA--------- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 245 HDVyqYYEQLKEKVASGAiSVISIDPVVTSTHdylgRDKVKHIAINPQTDVPLQLALAHTLYSEKLYDKNFLDNYCVGFD 324
Cdd:cd02753 171 HPV--IARRIKRAKRNGA-KLIVADPRRTELA----RFADLHLQLRPGTDVALLNAMAHVIIEEGLYDEEFIEERTEGFE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 325 QFL----PYLLGEkdgqpkdaawAEKLCGIDADTIRALARQMA-GDRTQIIAGWCVQRMQHGEQWSWMVVVLAAMLGQIG 399
Cdd:cd02753 244 ELKeiveKYTPEY----------AERITGVPAEDIREAARMYAtAKSAAILWGMGVTQHSHGTDNVMALSNLALLTGNIG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 400 LPgggfgfgwhynGAGtpgrkgiiLSGFSGSTTVPPVHD----STDYKGYsstipiarfmdailepgkvinwngksvklp 475
Cdd:cd02753 314 RP-----------GTG--------VNPLRGQNNVQGACDmgalPNVLPGY------------------------------ 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 476 pLKMCVFAGTNPFHRHQQINRIIEGWRKLETVIAIDNQWTSTCRFADIVLPATTQFERNdldqfGNHSN--RGIIAMKQV 553
Cdd:cd02753 345 -VKALYIMGENPALSDPNTNHVRKALESLEFLVVQDIFLTETAELADVVLPAASFAEKD-----GTFTNteRRVQRVRKA 418
|
490 500
....*....|....*....|
gi 1385641982 554 VSPQFEARNDFDIFRDLCRR 573
Cdd:cd02753 419 VEPPGEARPDWEIIQELANR 438
|
|
| MopB_CT_DmsA-EC |
cd02794 |
The MopB_CT_DmsA-EC CD includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
688-817 |
4.13e-29 |
|
The MopB_CT_DmsA-EC CD includes the DmsA enzyme of the dmsABC operon encoding the anaerobic dimethylsulfoxide reductase (DMSOR) of Escherichia coli and other related DMSOR-like enzymes. Unlike other DMSOR-like enzymes, this group has a predicted N-terminal iron-sulfur [4Fe-4S] cluster binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239195 [Multi-domain] Cd Length: 121 Bit Score: 112.38 E-value: 4.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 688 WPLHLQSVHPDFRLHSQLCESETLRQQYavggKEPVFINPQDASARGIRNGDIVRVFNARGQVLAGAVVSDRYAPGVARI 767
Cdd:cd02794 1 YPLQLIGWHYKRRTHSTFDNVPWLREAF----PQEVWINPLDAAARGIKDGDRVLVFNDRGKVIRPVKVTERIMPGVVAL 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1385641982 768 HEGAWYDPDKGGdinaLCKYGNPNVLTLDIgTSQLAQATSAHTTLVEIEK 817
Cdd:cd02794 77 PQGAWYEPDANG----IDKGGCINTLTGLR-PSPLAKGNPQHTNLVQVEK 121
|
|
| Molydop_binding |
pfam01568 |
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
690-812 |
1.30e-25 |
|
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: 101.97 E-value: 1.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 690 LHLQSVHPDFRLHSQLcesETLR-QQYAVGGKEPVFINPQDASARGIRNGDIVRVFNARGQVLAGAVVSDRYAPGVARIH 768
Cdd:pfam01568 1 LYLITGRVLGQYHSQT---RTRRvLRLAKPEPEVVEIHPEDAAALGIKDGDLVEVTSRRGSVVVRAKVTDRVRPGVVFMP 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1385641982 769 EGAWYDPdkggdinalcKYGNPNVLTLDiGTSQLAQATSAHTTL 812
Cdd:pfam01568 78 FGWWYEP----------RGGNANALTDD-ATDPLSGGPEFKTCA 110
|
|
| MopB_CT |
cd02775 |
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a ... |
699-784 |
6.89e-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: 88.15 E-value: 6.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 699 FRLHSQLCE-SETLRQQYavgGKEPVFINPQDASARGIRNGDIVRVFNARGQVLAGAVVSDRYAPGVARIHEGAWYDPDK 777
Cdd:cd02775 3 DHFHSGTRTrNPWLRELA---PEPVVEINPEDAAALGIKDGDLVRVESRRGSVVLRAKVTDGVPPGVVFLPHGWGHRGGR 79
|
....*..
gi 1385641982 778 GGDINAL 784
Cdd:cd02775 80 GGNANVL 86
|
|
| MopB_CT_4 |
cd02785 |
The MopB_CT_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
687-817 |
7.31e-20 |
|
The MopB_CT_4 CD includes a group of related uncharacterized bacterial and archaeal molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239186 [Multi-domain] Cd Length: 124 Bit Score: 85.88 E-value: 7.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 687 RWPLHLQSVHPDFRLHSQLCESETLRQQyavgGKEP-VFINPQDASARGIRNGDIVRVFNARGQVLAGAVVSDRYAPGVA 765
Cdd:cd02785 1 KYPLACIQRHSRFRVHSQFSNVPWLLEL----QPEPrVKINPIDAAARGIAHGDLVEVYNDRGSVVCKAKVDDGIQPGVV 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1385641982 766 RIHEGAWYDPDKGGDINALCkygNPNVLTLDIGtsqLAQATSA-HTTLVEIEK 817
Cdd:cd02785 77 TAEQGWWSRYFQEGSLQDLT---SPFVNPVHEY---IYGPNSAfYDTLVEVRK 123
|
|
| MopB_Arsenate-R |
cd02757 |
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ... |
59-669 |
1.74e-19 |
|
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: 92.89 E-value: 1.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 59 WGAIRATVVDGRFVAakpfeqdkypskmIAGLPDH-----------------VHNAARIRYPMVRVDwMRKGHQSDtsqr 121
Cdd:cd02757 12 WCGLQAYVEDGRVTK-------------VEGNPLHpgsrgrlcakghlglqqVYDPDRILYPMKRTN-PRKGRDVD---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 122 gdNRFVRVSWDEALDLFYQELERVQKTYGPSALLTASGWQStgmfHNASGMLARAIALHG--NSVStggdYSTgaaqvil 199
Cdd:cd02757 74 --PKFVPISWDEALDTIADKIRALRKENEPHKIMLHRGRYG----HNNSILYGRFTKMIGspNNIS----HSS------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 200 prVVGSMEVYEQQTSWPLV------LQNSKTIVLWGSDMVknqQANWWCPdhdvyqYYEQLKEKVASGAiSVISIDPVVT 273
Cdd:cd02757 137 --VCAESEKFGRYYTEGGWdynsydYANAKYILFFGADPL---ESNRQNP------HAQRIWGGKMDQA-KVVVVDPRLS 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 274 ST---HDYLgrdkvkhIAINPQTDVPLQLALAHTLYSEKLYDKNFLDNYCVGFDQFLP-YLLGEKDGQPKDA-------- 341
Cdd:cd02757 205 NTaakADEW-------LPIKPGEDGALALAIAHVILTEGLWDKDFVGDFVDGKNYFKAgETVDEESFKEKSTeglvkwwn 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 342 --------AWAEKLCGIDADTIRALARQMAGDRTQIIA-GWCVQRMQHGeqwSWMVVVLAAMLGqiGLpgggfgfgwhyn 412
Cdd:cd02757 278 lelkdytpEWAAKISGIPAETIERVAREFATAAPAAAAfTWRGATMQNR---GSYNSMACHALN--GL------------ 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 413 gAGTPGRKGIILSGfsgsttvppvhdstdykgysstipiarfmdailepgkviNWNGKsvklppLKMCVFAGTNPFHRHQ 492
Cdd:cd02757 341 -VGSIDSKGGLCPN---------------------------------------MGVPK------IKVYFTYLDNPVFSNP 374
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 493 QINRIIEGWRKLETVIAIDNQWTSTCRFADIVLPATTQFERNDLDQFGNHSNRGIIAMKQVVSPQFEARNDFDIFRDLCR 572
Cdd:cd02757 375 DGMSWEEALAKIPFHVHLSPFMSETTYFADIVLPDGHHFERWDVMSQENNLHPWLSIRQPVVKSLGEVREETEILIELAK 454
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 573 RFNReaaftEGLDEMgwlKRIWQEgsqQGKgrgihlpTFEVFWNQQEyiEFDhpqmfvrhqafredpdlEPLGTPSGLIE 652
Cdd:cd02757 455 KLDP-----KGSDGM---KRYAPG---QFK-------DPETGKNNRW--EFE-----------------NVFPTETGKFE 497
|
650
....*....|....*..
gi 1385641982 653 IYSKTIADMQYDDCQGH 669
Cdd:cd02757 498 FYSETLKKYLQNHADKK 514
|
|
| MopB_CT_3 |
cd02786 |
The MopB_CT_3 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
689-815 |
5.49e-17 |
|
The MopB_CT_3 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239187 [Multi-domain] Cd Length: 116 Bit Score: 77.71 E-value: 5.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 689 PLHLQSVHPDFRLHSQLCESETLRQQyavGGKEPVFINPQDASARGIRNGDIVRVFNARGQVLAGAVVSDRYAPGVArIH 768
Cdd:cd02786 2 PLRLITPPAHNFLNSTFANLPELRAK---EGEPTLLIHPADAAARGIADGDLVVVFNDRGSVTLRAKVTDDVPPGVV-VA 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1385641982 769 EGAWYD---PDkGGDINALckygNPNVLTlDIGtsqlaQATSAHTTLVEI 815
Cdd:cd02786 78 EGGWWRehsPD-GRGVNAL----TSARLT-DLG-----GGSTFHDTRVEV 116
|
|
| Molybdopterin_N |
pfam18364 |
Molybdopterin oxidoreductase N-terminal domain; This is the N-terminal domain of pfam00384 ... |
55-95 |
2.32e-15 |
|
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: 70.50 E-value: 2.32e-15
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1385641982 55 TGSHWGAIRATVVDGRFVAAKPFEQDKYPSKMIAGLPDHVH 95
Cdd:pfam18364 1 TASHWGAFRAVVKDGRIVGVEPFEGDPDPSPLLQGVPDAVY 41
|
|
| MopB_Formate-Dh-Na-like |
cd02752 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
88-574 |
9.97e-13 |
|
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: 71.66 E-value: 9.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 88 AGLPDHVHNAARIRYPMVRVDwmrkghqsdtsqrGDNRFVRVSWDEALDLFyqeLERVQKT------YGPSALLTASGWQ 161
Cdd:cd02752 43 AALRDFVHSPKRLKYPMYRAP-------------GSGKWEEISWDEALDEI---ARKMKDIrdasfvEKNAAGVVVNRPD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 162 STGM-----FHNASGMLARAIA--------------LHGNSV-STGGDYSTGAaqvilprvvgsmevyeQQTSWpLVLQN 221
Cdd:cd02752 107 SIAFlgsakLSNEECYLIRKFAralgtnnldhqariUHSPTVaGLANTFGRGA----------------MTNSW-NDIKN 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 222 SKTIVLWGSDMVKNqqanwwcpdHDV-YQYYEQLKEKvaSGAiSVISIDPVVTSTH---DYlgrdkvkHIAINPQTDVPL 297
Cdd:cd02752 170 ADVILVMGGNPAEA---------HPVsFKWILEAKEK--NGA-KLIVVDPRFTRTAakaDL-------YVPIRSGTDIAF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 298 qlalahtLYSeklydknfLDNYCVGFDqflpyllgekdgqPKDAawaEKLCGIDADTIRALARQMA----GDRTQIIAgW 373
Cdd:cd02752 231 -------LGG--------MINYIIRYT-------------PEEV---EDICGVPKEDFLKVAEMFAatgrPDKPGTIL-Y 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 374 CVQRMQH--GEQWSWMVVVLAAMLGQIGLPgggfgfgwhynGAGTPgrkgiILSGFSGsttvppVHDSTDYkgysstipi 451
Cdd:cd02752 279 AMGWTQHtvGSQNIRAMCILQLLLGNIGVA-----------GGGVN-----ALRGHSN------VQGATDL--------- 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 452 arfmdAILepgkvinwngkSVKLPPLkmcvFAGTNPFHRHQQINRIIEGWRKLETVIAIDNQWTSTCRFAD--------- 522
Cdd:cd02752 328 -----GLL-----------SHNLPGY----LGGQNPNSSFPNANKVRRALDKLDWLVVIDPFPTETAAFWKnpgmdpksi 387
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1385641982 523 ----IVLPATTQFERNDldQFGNhSNRGIIAMKQVVSPQFEARNDFDIFRDLCRRF 574
Cdd:cd02752 388 qtevFLLPAACQYEKEG--SITN-SGRWLQWRYKVVEPPGEAKSDGDILVELAKRL 440
|
|
| MopB_CT_Fdh-Nap-like |
cd00508 |
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and ... |
723-784 |
2.71e-12 |
|
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: 64.07 E-value: 2.71e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1385641982 723 VFINPQDASARGIRNGDIVRVFNARGQVLAGAVVSDRYAPGV--ARIHegaWYDPDKGGDINAL 784
Cdd:cd00508 37 VEIHPEDAARLGIKDGDLVRVSSRRGSVVVRARVTDRVRPGTvfMPFH---WGGEVSGGAANAL 97
|
|
| MopB_CT_Nitrate-R-NapA-like |
cd02791 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
721-785 |
5.33e-12 |
|
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to nitrite. Monomeric Nas is located in the cytoplasm and participates in nitrogen assimilation. Dimeric Nap is located in the periplasm and is coupled to quinol oxidation via a membrane-anchored tetraheme cytochrome. This CD (MopB_CT_Nitrate-R-Nap) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs
Pssm-ID: 239192 [Multi-domain] Cd Length: 122 Bit Score: 63.36 E-value: 5.33e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1385641982 721 EP-VFINPQDASARGIRNGDIVRVFNARGQVLAGAVVSDRYAPGV--ARIHEGAWYDPDKGgdINALC 785
Cdd:cd02791 34 EPyVEIHPEDAARLGLKEGDLVRVTSRRGEVVLRVRVTDRVRPGEvfVPMHWGDQFGRSGR--VNALT 99
|
|
| MopB_CT_Formate-Dh-Na-like |
cd02792 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
689-817 |
3.07e-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: 61.47 E-value: 3.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 689 PLHLQSvhpdFRLHSQLCESETLRQQYAVGGKEP---VFINPQDASARGIRNGDIVRVFNARGQVLAGAVVSDRYAPGVA 765
Cdd:cd02792 4 PLVLTT----GRLTEHFHGGNMTRNSPYLAELQPemfVEISPELAAERGIKNGDMVWVSSPRGKIKVKALVTDRVKPHEV 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1385641982 766 RI--HEGAWYdPDKGGDINALCKYGnpnvltLDIGTSqlAQATSAhtTLVEIEK 817
Cdd:cd02792 80 GIpyHWGGMG-LVIGDSANTLTPYV------GDPNTQ--TPEYKA--FLVNIEK 122
|
|
| MopB_2 |
cd02763 |
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
98-561 |
3.69e-11 |
|
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: 66.78 E-value: 3.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 98 ARIRYPMvrvdwMRKGhqsdtsQRGDNRFVRVSWDEALDLFYQELERVQKTyGPSALLTASG---WQS-TGMFHNASGML 173
Cdd:cd02763 53 ARLTKPL-----LRKG------PRGSGQFEEIEWEEAFSIATKRLKAARAT-DPKKFAFFTGrdqMQAlTGWFAGQFGTP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 174 AraIALHGN----SVSTGGDYSTGaaqvilprvvGSMevyeqqtsWPLV---LQNSKTIVLWGSdmvknqqanwwCPDHD 246
Cdd:cd02763 121 N--YAAHGGfcsvNMAAGGLYSIG----------GSF--------WEFGgpdLEHTKYFMMIGV-----------AEDHH 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 247 VYQYYEQLKEKVASGAiSVISIDPVVTSthdyLGRDKVKHIAINPQTDVPLQLALAHTLYSEKLYDKNFLDNYCVGfdqf 326
Cdd:cd02763 170 SNPFKIGIQKLKRRGG-KFVAVNPVRTG----YAAIADEWVPIKPGTDGAFILALAHELLKAGLIDWEFLKRYTNA---- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 327 lPYLLgekDGQPKdaaWAEKLCGIDADTIRALARQMA------------------GDRTQIIAGWCV--QRMQ------H 380
Cdd:cd02763 241 -AELV---DYTPE---WVEKITGIPADTIRRIAKELGvtardqpielpiawtdvwGRKHEKITGRPVsfHAMRgiaahsN 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 381 GEQWSWMVVVLAAMLGQIGLPGGGFGFGwHYNGAGTPG---RKGIILSGFSGSTTVPP---VHDSTDY------------ 442
Cdd:cd02763 314 GFQTIRALFVLMMLLGTIDRPGGFRHKP-PYPRHIPPLpkpPKIPSADKPFTPLYGPPlgwPASPDDLlvdedgnplrid 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 443 KGYSSTIPIAR--FMDAILEPGkvinWNGKSVKLPPLKMcvFAGTNPFHRHQQINRIIE--------GWRKLETVIAIDN 512
Cdd:cd02763 393 KAYSWEYPLAAhgCMQNVITNA----WRGDPYPIDTLMI--YMANMAWNSSMNTPEVREmltdkdasGNYKIPFIIVCDA 466
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1385641982 513 QWTSTCRFADIVLPATTQFERND----LDQFGNHSNRGIIAMKQ-VVSPQFEAR 561
Cdd:cd02763 467 FYSEMVAFADLVLPDTTYLERHDamslLDRPISEADGPVDAIRVpIVEPKGDVK 520
|
|
| MopB_CT_Acetylene-hydratase |
cd02781 |
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related ... |
702-794 |
1.15e-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: 60.01 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 702 HSQLCESETLRQqyavggKEP---VFINPQDASARGIRNGDIVRVFNARGQVLAGAVVSDRYAPGVARIHEGAWYDPDKG 778
Cdd:cd02781 17 HSEHRQLPSLRE------LHPdpvAEINPETAAKLGIADGDWVWVETPRGRARQKARLTPGIRPGVVRAEHGWWYPEREA 90
|
90
....*....|....*..
gi 1385641982 779 GDINAL-CKYGNPNVLT 794
Cdd:cd02781 91 GEPALGgVWESNANALT 107
|
|
| MopB_Phenylacetyl-CoA-OR |
cd02760 |
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large ... |
65-573 |
1.25e-10 |
|
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large subunit (PadB2), and other related proteins. The phenylacetyl-CoA:acceptor oxidoreductase has been characterized as a membrane-bound molybdenum-iron-sulfur enzyme involved in anaerobic metabolism of phenylalanine in the denitrifying bacterium Thauera aromatica. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239161 [Multi-domain] Cd Length: 760 Bit Score: 65.38 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 65 TVVDGRFVAAKP-FE-QDKYPSK-----MIAGLPDHVHNAARIRYPMVRVDwMRKGHQSDTSqrgdnrFVRVSWDEALDL 137
Cdd:cd02760 17 KVVDGVATEIEPnFAaEDIHPARgrvcvKAYGLVQKTYNPNRVLQPMKRTN-PKKGRNEDPG------FVPISWDEALDL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 138 FYQELERV-QKTYGPSALLT--ASGWQSTGMFHNASGMLARAIALHGNSvstggDYSTGAAQVIlpRVVGSMEVYEQqts 214
Cdd:cd02760 90 VAAKLRRVrEKGLLDEKGLPrlAATFGHGGTPAMYMGTFPAFLAAWGPI-----DFSFGSGQGV--KCVHSEHLYGE--- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 215 wplVLQNSKTIVlwgsdmvknqqanwwcPDHDVYQYYEQLKEKV-ASGA--------------ISVISIDPVVTSThdyl 279
Cdd:cd02760 160 ---FWHRAFTVA----------------ADTPLANYVISFGSNVeASGGpcavtrhadarvrgYKRVQVEPHLSVT---- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 280 GRDKVKHIAINPQTDVPLQLALAHTLYSEK---LYDKNFLDN-----YCVGFDQFL--------PYLLGEKDGQ--PKDA 341
Cdd:cd02760 217 GACSAEWVPIRPKTDPAFMFAMIHVMVHEQglgKLDVPFLRDrtsspYLVGPDGLYlrdaatgkPLVWDERSGRavPFDT 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 342 A-------------------------------------------------WAEKLCGIDADTIRALARQMA-----GDRT 367
Cdd:cd02760 297 RgavpavagdfavdgavsvdaddetaihqgvegttaftmlvehmrkytpeWAESICDVPAATIRRIAREFLenasiGSTI 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 368 QI------------IAGWCVQRMQHGEQWSWMVVVLAAMLGQIGLPGGGFGFGWHYNG-------AGTPGRKGIILSGFS 428
Cdd:cd02760 377 EVdgvtlpyrpvavTLGKSVNNGWGAFECCWARTLLATLVGALEVPGGTLGTTVRLNRphddrlaSVKPGEDGFMAQGFN 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 429 GSTTVPPVHDSTDYKGYSSTIPIARFMD----------AILEPGKVINWNGKSVKLPPLKMCVFAgTNPFHRHQQINRII 498
Cdd:cd02760 457 PTDKEHWVVKPTGRNAHRTLVPIVGNSAwsqalgptqlAWMFLREVPLDWKFELPTLPDVWFNYR-TNPAISFWDTATLV 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 499 EGWRKLETVIAIDNQWTSTCRFADIVLPATTQFERNDL---------DQFGNHsnRGIIAMKQVVSPQFEARNDFDIFRD 569
Cdd:cd02760 536 DNIAKFPFTVSFAYTEDETNWMADVLLPEATDLESLQMikvggtkfvEQFWEH--RGVVLRQPAVEPQGEARDFTWISTE 613
|
....
gi 1385641982 570 LCRR 573
Cdd:cd02760 614 LAKR 617
|
|
| MopB_CT_Tetrathionate_Arsenate-R |
cd02780 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate ... |
688-817 |
8.69e-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: 57.69 E-value: 8.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 688 WPLHLQSVHPDFRLHSqlceSETLRQQYAVGGKEPVFINPQDASARGIRNGDIVRVFNARGQVLAGAVVSDRYAPGVARI 767
Cdd:cd02780 1 YPFILVTFKSNLNSHR----SANAPWLKEIKPENPVWINPEDAAKLGIKTGDRVRVVTPGGSVVGKAKVTEGVRPGVVAI 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1385641982 768 --HEGAW---------YDPDKGGDInALCKYGNPNVL-----TLDIGTSQLAQATSAH--TTLVEIEK 817
Cdd:cd02780 77 ehGYGHWaygavastiDGKDLPGDA-WRGAGVNINDIglvdpSRGGWSLVDWVGGAAAryDTPVKIEK 143
|
|
| MopB_ydeP |
cd02767 |
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
99-401 |
1.04e-09 |
|
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239168 [Multi-domain] Cd Length: 574 Bit Score: 61.94 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 99 RIRYPMVRvdwmrkghqsdtsQRGDNRFVRVSWDEALDLFYQELERVQK------TYGPSALLTASGWQstgmfhnasgM 172
Cdd:cd02767 64 RLTYPMRY-------------DAGSDHYRPISWDEAFAEIAARLRALDPdraafyTSGRASNEAAYLYQ----------L 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 173 LARAiaLHGNSVSTGGDYSTGAAQVILPRVVGS---MEVYEQqtswplvLQNSKTIVLWGSDMVKNQqanwwcPdhdvyQ 249
Cdd:cd02767 121 FARA--YGTNNLPDCSNMCHEPSSVGLKKSIGVgkgTVSLED-------FEHTDLIFFIGQNPGTNH------P-----R 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 250 YYEQLKEKVASGAiSVISIDPVV-----------TSTHDYLGRDKV--KHIAINPQTDVPLQLALA-HTLYSEK----LY 311
Cdd:cd02767 181 MLHYLREAKKRGG-KIIVINPLRepglerfanpqNPESMLTGGTKIadEYFQVRIGGDIALLNGMAkHLIERDDepgnVL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 312 DKNFLDNYCVGFDQFLPYLlgekdgqpKDAAWA--EKLCGIDADTIRALARQ-MAGDRTQIIAGWCVQRMQHGEQWSWMV 388
Cdd:cd02767 260 DHDFIAEHTSGFEEYVAAL--------RALSWDeiERASGLSREEIEAFAAMyAKSERVVFVWGMGITQHAHGVDNVRAI 331
|
330
....*....|...
gi 1385641982 389 VVLAAMLGQIGLP 401
Cdd:cd02767 332 VNLALLRGNIGRP 344
|
|
| MopB_CT_Nitrate-R-NarG-like |
cd02776 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
689-770 |
2.16e-09 |
|
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under anaerobic conditions in the presence of nitrate, E. coli synthesizes the cytoplasmic membrane-bound quinol-nitrate oxidoreductase (NarGHI), which reduces nitrate to nitrite and forms part of a redox loop generating a proton-motive force. Found in prokaryotes and some archaea, NarGHI usually functions as a heterotrimer. The alpha chain contains the molybdenum cofactor-containing Mo-bisMGD catalytic subunit. This CD (MopB_CT_Nitrate-R-NarG-like) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239177 [Multi-domain] Cd Length: 141 Bit Score: 56.62 E-value: 2.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 689 PLHLQSVHPDFRLHSQLCESE-TLRQQYavgGKEPVFINPQDASARGIRNGDIVRVFNARGQVLAGAVVSDRYAPGVARI 767
Cdd:cd02776 1 PLNYLTPHGKWSIHSTYRDNLlMLRLQR---GGPVVWMNPKDAAELGIKDNDWVEVFNDNGVVVARAKVSPRIPRGTVFM 77
|
...
gi 1385641982 768 HEG 770
Cdd:cd02776 78 YHA 80
|
|
| MopB_CT_1 |
cd02782 |
The MopB_CT_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
725-809 |
3.25e-09 |
|
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: 55.86 E-value: 3.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 725 INPQDASARGIRNGDIVRVFNARGQVLAGAVVSDRYAPGVARIHEGawYDPDKGGDINALCKYG-NPNVLTLDIGTSQLA 803
Cdd:cd02782 37 IHPDDAAALGLADGDKVRVTSAAGSVEAEVEVTDDMMPGVVSLPHG--WGHDYPGVSGAGSRPGvNVNDLTDDTQRDPLS 114
|
....*.
gi 1385641982 804 qATSAH 809
Cdd:cd02782 115 -GNAAH 119
|
|
| MopB_CT_Formate-Dh_H |
cd02790 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
723-764 |
3.08e-07 |
|
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 with the release of a proton and two electrons. It is a component of the anaerobic formate hydrogen lyase complex. The E. coli formate dehydrogenase H (Fdh-H) is a monomer composed of a single polypeptide chain with a Mo active site region and a [4Fe-4S] center. This CD (MopB_CT_Formate-Dh_H) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239191 [Multi-domain] Cd Length: 116 Bit Score: 49.54 E-value: 3.08e-07
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1385641982 723 VFINPQDASARGIRNGDIVRVFNARGQVLAGAVVSDRYAPGV 764
Cdd:cd02790 37 VEINPEDAKRLGIEDGEKVRVSSRRGSVEVRARVTDRVPEGV 78
|
|
| PRK14991 |
PRK14991 |
tetrathionate reductase subunit TtrA; |
685-770 |
5.86e-07 |
|
tetrathionate reductase subunit TtrA;
Pssm-ID: 237883 [Multi-domain] Cd Length: 1031 Bit Score: 53.46 E-value: 5.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 685 SQRWPLHLQSvhpdFR--LHSQLC-ESETLRQqyaVGGKEPVFINPQDASARGIRNGDIVRVFNARGQVLAGAVVSDRYA 761
Cdd:PRK14991 884 ESQWPLLLIS----FKsnLMSSMSiASPRLRQ---VKPANPVALNPQDAARLGIQHGDRVRISTPGGSVVAQASVLNGVM 956
|
....*....
gi 1385641982 762 PGVARIHEG 770
Cdd:PRK14991 957 PGVIAIEHG 965
|
|
| MopB_CT_Thiosulfate-R-like |
cd02778 |
The MopB_CT_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, ... |
723-817 |
6.74e-07 |
|
The MopB_CT_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and other related proteins. Thiosulfate reductase catalyzes the cleavage of sulfur-sulfur bonds in thiosulfate. Polysulfide reductase is a membrane-bound enzyme that catalyzes the reduction of polysulfide using either hydrogen or formate as the electron donor. Also included in this CD is the phenylacetyl-CoA:acceptor oxidoreductase, large subunit (PadB2), which has been characterized as a membrane-bound molybdenum-iron-sulfur enzyme involved in anaerobic metabolism of phenylalanine in the denitrifying bacterium Thauera aromatica. The MopB_CT_Thiosulfate-R-like CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239179 [Multi-domain] Cd Length: 123 Bit Score: 48.81 E-value: 6.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 723 VFINPQDASARGIRNGDIVRVFNARGQVLAGAVVSDRYAPG-VARIHE-GAWYDP-----DKGGDINALckygnpnvltL 795
Cdd:cd02778 32 LWINPETAARLGIKDGDRVEVSSARGKVTGKARLTEGIRPDtVFMPHGfGHWAPAlsrayGGGVNDNNL----------L 101
|
90 100
....*....|....*....|..
gi 1385641982 796 DIGTSQLAQATSAHTTLVEIEK 817
Cdd:cd02778 102 PGSTEPVSGGAGLQEFTVTVRK 123
|
|
| MopB_CT_Arsenite-Ox |
cd02779 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of Arsenite oxidase ... |
725-763 |
9.79e-06 |
|
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: 45.53 E-value: 9.79e-06
10 20 30
....*....|....*....|....*....|....*....
gi 1385641982 725 INPQDASARGIRNGDIVRVFNARGQVLAGAVVSDRYAPG 763
Cdd:cd02779 37 VNPEDAKREGLKNGDLVEVYNDYGSTTAMAYVTNTVKPG 75
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
502-581 |
3.20e-04 |
|
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: 44.06 E-value: 3.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1385641982 502 RKLETVIAIDNQWTSTCRFADIVLPATTQFERNDLdqFGNHSNRgIIAMKQVVSPQFEARNDFDIFRDLCRRFNREAAFT 581
Cdd:COG1034 356 AKADFVVVLDHFGSATAERADVVLPAAAFAEKSGT--FVNLEGR-VQRFNAAVPPPGEARPDWRVLRALANALGAGLPYD 432
|
|
| FwdD |
COG1153 |
Formylmethanofuran dehydrogenase subunit D [Energy production and conversion]; |
724-772 |
7.50e-04 |
|
Formylmethanofuran dehydrogenase subunit D [Energy production and conversion];
Pssm-ID: 440767 [Multi-domain] Cd Length: 127 Bit Score: 40.22 E-value: 7.50e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1385641982 724 FINPQDASARGIRNGDIVRVFNARGQVLAGAVVSDRYAPGVARIHEGAW 772
Cdd:COG1153 34 ELNPEDMKKLGIKEGDKVKVTSEYGEVVVKAKESEDLHPGLVFIPMGPW 82
|
|
| MopB_CT_ydeP |
cd02787 |
The MopB_CT_ydeP CD includes a group of related uncharacterized bacterial ... |
716-768 |
1.06e-03 |
|
The MopB_CT_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative molybdopterin cofactor binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239188 [Multi-domain] Cd Length: 112 Bit Score: 39.57 E-value: 1.06e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1385641982 716 AVGGKEPVFINPQDASARGIRNGDIVRVFNARGQ-----VLAGAVVSDRYAPGVARIH 768
Cdd:cd02787 26 VFGRRDVVFMNPDDIARLGLKAGDRVDLESAFGDgqgriVRGFRVVEYDIPRGCLAAY 83
|
|
| PRK13532 |
PRK13532 |
nitrate reductase catalytic subunit NapA; |
723-752 |
1.21e-03 |
|
nitrate reductase catalytic subunit NapA;
Pssm-ID: 237416 [Multi-domain] Cd Length: 830 Bit Score: 42.58 E-value: 1.21e-03
10 20 30
....*....|....*....|....*....|
gi 1385641982 723 VFINPQDASARGIRNGDIVRVFNARGQVLA 752
Cdd:PRK13532 748 CFMHPEDAKARGLRRGDEVKVVSRRGEVKS 777
|
|
| |
