|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15102 |
PRK15102 |
trimethylamine-N-oxide reductase TorA; |
8-825 |
0e+00 |
|
trimethylamine-N-oxide reductase TorA;
Pssm-ID: 237909 [Multi-domain] Cd Length: 825 Bit Score: 1428.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 8 PSRRRFLSGMLAVGAASALAPNPLIS-----KVWAAGENPEQWIQSGSHYGAFEAKVVNGEWTETRPFKHDKYPCDMLNA 82
Cdd:PRK15102 1 ASRRRFLKGLGGLSAAGMLGPSLLTPrsalaAQAAAAETTKEWILTGSHWGAFRAKVKNGRFVEAKPFELDKYPTKMING 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 83 VREVVYNPSRVRYPMVRLDWLLKREKSDRSQRGDNRFVRVSWDQALDLFYEELERVQKTYGSSGVFTGLADWQMVGKYHK 162
Cdd:PRK15102 81 IKGHVYNPSRIRYPMVRLDWLRKRHKSDTSQRGDNRFVRVSWDEALDLFYEELERVQKTYGPSALHTGQTGWQSTGQFHS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 163 AGGAMDRGLGLHGSYVTTVGDYSAAAAQVILPHVIGSLEVYEQQTSLPLVIQNSNTIVLWGCDPIKNLQIEFLVPDHDAF 242
Cdd:PRK15102 161 ATGHMQRAIGMHGNSVGTVGDYSTGAGQVILPYVLGSTEVYEQGTSWPLILENSKTIVLWGSDPVKNLQVGWNCETHESY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 243 GYWQQIKEAVAQNKMRVISVDPVRSKSQNYLGCEQLALRPQTDVALMLALAHTLYEEKLYDTAFITDYTVGFEQFLPYLL 322
Cdd:PRK15102 241 AYLAQLKEKVAKGEINVISIDPVVTKTQNYLGCEHLYVNPQTDVPLMLALAHTLYSENLYDKKFIDNYCLGFEQFLPYLL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 323 GESDKQPKNAEWAAEICGLTAEQIRDFARLLVKGRTQFMGGWCVQRMHHGEQYPWMLVVLASMVGQIGLPGGGVGFGWHY 402
Cdd:PRK15102 321 GEKDGVPKTPEWAEKICGIDAETIRELARQMAKGRTQIIAGWCIQRQQHGEQPYWMGAVLAAMLGQIGLPGGGISYGHHY 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 403 NGGGTVTSTGPVLSGLGS--ITNPPQAKYKADFRGASEHIPTSRIVDCLLAPGNKIAFNGETLTYPDIKMAIYSAANPFH 480
Cdd:PRK15102 401 SGIGVPSSGGAIPGGFPGnlDTGQKPKHDNSDYKGYSSTIPVARFIDAILEPGKTINWNGKKVTLPPLKMMIFSGTNPWH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 481 AQQDRNRMIDAWKKLETVVVLDHQWTASCRFADIVLPVTTRFERNDIEQFGTHSNKGLMALHQIVKPQYEARHDFDIFAG 560
Cdd:PRK15102 481 RHQDRNRMKEAFRKLETVVAIDNQWTATCRFADIVLPACTQFERNDIDQYGSYSNRGIIAMKKVVEPLFESRSDFDIFRE 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 561 LCKRFDKEAVYRENRNEMQWIQALYDEGVKMGASLgVTLPDFTTFWQgDGYIEYPPGQPWVRHGEFREQPDLNPLGTPSG 640
Cdd:PRK15102 561 LCRRFGREKEYTRGMDEMGWLKRLYQECKQQNKGK-FHMPEFDEFWK-KGYVEFGEGQPWVRHADFREDPELNPLGTPSG 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 641 LIEIYSKTIAGFAYEDCPGHPVWMEPFERTHSGKK-DKYPLHLQSCHPDKRLHSQLCSSEAFRSTYAVAGREPLYISEQD 719
Cdd:PRK15102 639 LIEIYSRKIADMGYDDCQGHPMWFEKIERSHGGPGsDKYPLWLQSVHPDKRLHSQLCESEELRETYTVQGREPVYINPQD 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 720 ATTRGLKAGDIARVFNARGQVLAGVVISPDFTPGVVRIHEGAWYSPQEGGKAGTLCTYGDPNVLSADIGTSQLAQGPSAH 799
Cdd:PRK15102 719 AKARGIKDGDVVRVFNDRGQVLAGAVVSDRYPPGVIRIHEGAWYGPDKGGEIGALCTYGDPNTLTLDIGTSQLAQATSAH 798
|
810 820
....*....|....*....|....*.
gi 1995542531 800 TVLVEVERYQQKAPQVTAFGGPQIVK 825
Cdd:PRK15102 799 TCLVEIEKYQGKVPPVTSFNGPVEVV 824
|
|
| torA |
TIGR02164 |
trimethylamine-N-oxide reductase TorA; This very narrowly defined family represents TorA, part ... |
9-821 |
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: 1194.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 9 SRRRFLSGMLAVGAASALAPNPLISK--VWAAGENPEQWIQSGSHYGAFEAKVVNGEWTETRPFKHDKYPCDMLNAVREV 86
Cdd:TIGR02164 2 SRRDFLKGIASSSAAVLGGPSLLTPLnaLAAAAINEDEWKTTGSHWGAFRAKVKNGKVVEVKPFELDKYPTEMINGIRGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 87 VYNPSRVRYPMVRLDWLLKREKSDRSQRGDNRFVRVSWDQALDLFYEELERVQKTYGSSGVFTGLADWQMVGKYHKAGGA 166
Cdd:TIGR02164 82 VYNPSRVRYPMVRLDWLKKRHKSNTHQRGDNRFVRVTWDEALDLFYEELERVQKQYGPSALHAGQTGWRSTGQFHSCTSH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 167 MDRGLGLHGSYVTTVGDYSAAAAQVILPHVIGSLEVYEQQTSLPLVIQNSNTIVLWGCDPIKNLQIEFLVPDHDAFGYWQ 246
Cdd:TIGR02164 162 MQRAVGMHGNYVKKIGDYSTGAGQTILPYVLGSTEVYAQGTSWPLILENSDTIVLWANDPVKNLQVGWNCETHESFAYLA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 247 QIKEAVAQNKMRVISVDPVRSKSQNYLGCEQLALRPQTDVALMLALAHTLYEEKLYDTAFITDYTVGFEQFLPYLLGESD 326
Cdd:TIGR02164 242 QLKEKVAAGEINVISIDPVVTKTQAYLGCEHLYVNPQTDVALMLALAHTLYSENLYDKKFIEGYCLGFEEFLPYVLGSKD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 327 KQPKNAEWAAEICGLTAEQIRDFARLLVKGRTQFMGGWCVQRMHHGEQYPWMLVVLASMVGQIGLPGGGVGFGWHYNGGG 406
Cdd:TIGR02164 322 GVAKTPEWAAKICGVEAEVIRDLARMLVKGRTQLIFGWCIQRQQHGEQPYWMGAVLAAMIGQIGLPGGGISYGHHYSSIG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 407 TVTSTGPVLSGL-GSITNPPQAKY-KADFRGASEHIPTSRIVDCLLAPGNKIAFNGETLTYPDIKMAIYSAANPFHAQQD 484
Cdd:TIGR02164 402 VPSSGAAAPGAFpRNLDEGQKPKFdNSDFKGYSSTIPVARWIDAILEPGKTIDHNGSKVTYPPIKMMIFSGCNPWHHHQD 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 485 RNRMIDAWKKLETVVVLDHQWTASCRFADIVLPVTTRFERNDIEQFGTHSNKGLMALHQIVKPQYEARHDFDIFAGLCKR 564
Cdd:TIGR02164 482 RNRMKQAFQKLETVVTIDVSWTATCRFSDIVLPACTQFERNDIDVYGSYSNRGIIAMQKLVDPLFDSRSDFEIFTELCRR 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 565 FDKEAVYRENRNEMQWIQALYDEGVKMGASlGVTLPDFTTFWQgDGYIEYPPGQPWVRHGEFREQPDLNPLGTPSGLIEI 644
Cdd:TIGR02164 562 FGKEKEYTRNMDEMEWLKTLYNECKQANAG-KFEMPDFAEFWK-KGYVHFGDGEPWVRHADFREDPEINPLGTPSGLIEI 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 645 YSKTIAGFAYEDCPGHPVWMEPFERTHSG-KKDKYPLHLQSCHPDKRLHSQLCSSEAFRSTYAVAGREPLYISEQDATTR 723
Cdd:TIGR02164 640 FSRKIAQYGYDDCKGHPMWFEKTERSHGGpGSDKHPFWLQSCHPDKRLHSQMCESEALRETYAVQGREPVYINPVDAKAR 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 724 GLKAGDIARVFNARGQVLAGVVISPDFTPGVVRIHEGAWYSPQEGGKAGTLCTYGDPNVLSADIGTSQLAQGPSAHTVLV 803
Cdd:TIGR02164 720 GIKDGDLVRVFNDRGQLLAGAVVSDNFPKGVVRIHEGAWYGPLGGEEVGALCTYGDPNTLTLDIGTSKLAQATSANTCLV 799
|
810
....*....|....*...
gi 1995542531 804 EVERYQQKAPQVTAFGGP 821
Cdd:TIGR02164 800 EFEKYQGKVPKVTSFDGP 817
|
|
| bisC_fam |
TIGR00509 |
molybdopterin guanine dinucleotide-containing S/N-oxide reductases; This enzyme family shares ... |
49-824 |
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: 1061.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 49 GSHYGAFEAKVVNGEWTETRPFKHDKYPCDMLNAVREVVYNPSRVRYPMVRLDWLLKREKSDRSQRGDNRFVRVSWDQAL 128
Cdd:TIGR00509 1 ASHWGVFTATVQDGRIVAVTPFESDPNPTPMLEGVPDQVYSESRIKYPMVRKGFLENGVKSDRSGRGREEFVRVSWDEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 129 DLFYEELERVQKTYGSSGVFTGLADWQMVGKYHKAGGAMDRGLGLHGSYVTTVGDYSAAAAQVILPHVIGSLEVYEQQTS 208
Cdd:TIGR00509 81 DLVAEELKRVRKTHGPSAIFAGSYGWKSAGRLHNASTLLQRMLNLLGGYVGHAGDYSTGAAQVIMPHVVGDMEVYEQQTT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 209 LPLVIQNSNTIVLWGCDPIKNLQIEFLVPDHDAFGYWQQIKEAVAqnkmRVISVDPVRSKSQNYLGCEQLALRPQTDVAL 288
Cdd:TIGR00509 161 WPVILENSEVLVLWGADPLKTSQIAWGIPDHGGYEYLERLKAKGK----RVISIDPVRTETVEFFGAEWIPPNPQTDVAL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 289 MLALAHTLYEEKLYDTAFITDYTVGFEQFLPYLLGESDKQPKNAEWAAEICGLTAEQIRDFARLLVKGRTQFMGGWCVQR 368
Cdd:TIGR00509 237 MLGLAHTLVTEGLYDKDFLAKYTSGFEKFLPYLLGETDGTPKTAEWASKITGVPAETIKELARLFASKRTMLAAGWSMQR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 369 MHHGEQYPWMLVVLASMVGQIGLPGGGVGFGWHYNGGGTVTSTGPVLSGlgsITNPPQAKYK-ADFRGASEHIPTSRIVD 447
Cdd:TIGR00509 317 MQHGEQPHWMLVTLAAMLGQIGLPGGGFGFSYHYSGGGTPSASGPALSQ---GSNSVSSTAGpEWDDGSASVIPVARISD 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 448 CLLAPGNKIAFNGETLTYPDIKMAIYSAANPFHAQQDRNRMIDAWKKLETVVVLDHQWTASCRFADIVLPVTTRFERNDI 527
Cdd:TIGR00509 394 ALLNPGKEIDYNGKELKLPDIKMVYWAGGNPFHHHQDTNRLIKAWRKLETIIVHEPQWTPTAKHADIVLPATTSFERNDL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 528 EQFGTHSNKGLMALHQIVKPQYEARHDFDIFAGLCKRFDKEAVYRENRNEMQWIQALYDEGVKMGASLGVTLPDFTTFWQ 607
Cdd:TIGR00509 474 TMAGDYSNTGILAMKQVVPPQFEARNDYDIFAALAERLGVEEAFTEGKDEMGWLKHLYEKAAKQAKADGVEMPAFDAFWA 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 608 gDGYIEYPPGQP--WVRHGEFREQPDLNPLGTPSGLIEIYSKTIAGFAYEDCPGHPVWMEPFERTHSGKKDKYPLHLQSC 685
Cdd:TIGR00509 554 -EGIVEFPVPEGadFVRYAAFREDPLLNPLGTPSGLIEIYSKTIAKMGYDDCPGHPTWMEPAEWLGGPRGAKYPLHLISP 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 686 HPDKRLHSQLCSSEAfRSTYAVAGREPLYISEQDATTRGLKAGDIARVFNARGQVLAGVVISPDFTPGVVRIHEGAWYSP 765
Cdd:TIGR00509 633 HPKYRLHSQLDHTEL-RQAYKVQGREPVMIHPDDAAARGIADGDIVRVFNARGQILAGAVVTDGIRKGVVQIHEGAWYDP 711
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*....
gi 1995542531 766 QEGGKAGTLCTYGDPNVLSADIGTSQLAQGPSAHTVLVEVERYQQKAPQVTAFGGPQIV 824
Cdd:TIGR00509 712 ADVREPGGLCKYGNPNVLTADIGTSSLAQGNSGNTVLVEIEKYTGPAPPLTAFDQPAAA 770
|
|
| MopB_DMSOR-BSOR-TMAOR |
cd02769 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
48-669 |
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: 891.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 48 SGSHYGAFEAKVVNGEWTETRPFKHDKYPCDMLNAVREVVYNPSRVRYPMVRLDWLLKREKSDRSQRGDNRFVRVSWDQA 127
Cdd:cd02769 2 TASHWGAFRARVKDGRIVGVRPFEEDPDPSPLLDGVPDAVYSPTRIKYPMVRRGWLEKGPGSDRSLRGKEEFVRVSWDEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 128 LDLFYEELERVQKTYGSSGVFTGLADWQMVGKYHKAGGAMDRGLGLHGSYVTTVGDYSAAAAQVILPHVIGSLEVY-EQQ 206
Cdd:cd02769 82 LDLVAAELKRVRKTYGNEAIFGGSYGWSSAGRFHHAQSLLHRFLNLAGGYVGSVGDYSTGAAQVILPHVVGSMEVYtEQQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 207 TSLPLVIQNSNTIVLWGCDPIKNLQIEFLV-PDHDAFGYWQQIKEAvaqnKMRVISVDPVRSKSQNYLGCEQLALRPQTD 285
Cdd:cd02769 162 TSWPVIAEHTELVVAFGADPLKNAQIAWGGiPDHQAYSYLKALKDR----GIRFISISPLRDDTAAELGAEWIAIRPGTD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 286 VALMLALAHTLYEEKLYDTAFITDYTVGFEQFLPYLLGESDKQPKNAEWAAEICGLTAEQIRDFARLLVKGRTQFMGGWC 365
Cdd:cd02769 238 VALMLALAHTLVTEGLHDKAFLARYTVGFDKFLPYLLGESDGVPKTPEWAAAICGIPAETIRELARRFASKRTMIMAGWS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 366 VQRMHHGEQYPWMLVVLASMVGQIGLPGGGVGFGWHYNGGGTVTSTGPVLSGLGSITNPpqakykadfrgASEHIPTSRI 445
Cdd:cd02769 318 LQRAHHGEQPHWMAVTLAAMLGQIGLPGGGFGFGYHYSNGGGPPRGAAPPPALPQGRNP-----------VSSFIPVARI 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 446 VDCLLAPGNKIAFNGETLTYPDIKMAIYSAANPFHAQQDRNRMIDAWKKLETVVVLDHQWTASCRFADIVLPVTTRFERN 525
Cdd:cd02769 387 ADMLLNPGKPFDYNGKKLTYPDIKLVYWAGGNPFHHHQDLNRLIRAWQKPETVIVHEPFWTATARHADIVLPATTSLERN 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 526 DIEqfGTHSNKGLMALHQIVKPQYEARHDFDIFAGLCKRFDKEAVYRENRNEMQWIQALYDEGVKMGASLGVTLPDFTTF 605
Cdd:cd02769 467 DIG--GSGDNRYIVAMKQVVEPVGEARDDYDIFADLAERLGVEEQFTEGRDEMEWLRHLYEESRAQAAARGVEMPSFDEF 544
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1995542531 606 WQgDGYIEYP-PGQPWVRHGEFREQPDLNPLGTPSGLIEIYSKTIAGFAYEDCPGHPVWMEPFER 669
Cdd:cd02769 545 WA-QGYVELPiPEADFVRLADFREDPEANPLGTPSGRIEIFSETIAGFGYDDCPGHPTWLEPAEW 608
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
48-669 |
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: 818.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 48 SGSHYGAFEAKVVNGEWTETRPFKHDK-YPCDMLNAVREVVYNPSRVRYPMVRLDWLLKREKSdRSQRGDNRFVRVSWDQ 126
Cdd:cd02751 2 TACHWGPFKAHVKDGVIVRVEPDDTDQpRPCPRGRSVRDRVYSPDRIKYPMKRVGWLGNGPGS-RELRGEGEFVRISWDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 127 ALDLFYEELERVQKTYGSSGVFTGLADWQMVGKYHKAGGAMDRGLGLHGSYVTTVGDYSAAAAQVILPHVIGSLEVYEQQ 206
Cdd:cd02751 81 ALDLVASELKRIREKYGNEAIFGGSYGWASAGRLHHAQSLLHRFLNLIGGYLGSYGTYSTGAAQVILPHVVGSDEVYEQG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 207 TSLPLVIQNSNTIVLWGCDPIKNLQIEFLVPDHDAFGYWQQIKEAvaqnKMRVISVDPVRSKSQNYLGCEQLALRPQTDV 286
Cdd:cd02751 161 TSWDDIAEHSDLVVLFGANPLKTRQGGGGGPDHGSYYYLKQAKDA----GVRFICIDPRYTDTAAVLAAEWIPIRPGTDV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 287 ALMLALAHTLYEEKLYDTAFITDYTVGFEQFLPYLLGESDKQPKNAEWAAEICGLTAEQIRDFARLLVKGRTQFMGGWCV 366
Cdd:cd02751 237 ALMLAMAHTLITEDLHDQAFLARYTVGFDEFKDYLLGESDGVPKTPEWAAEITGVPAETIRALAREIASKRTMIAQGWGL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 367 QRMHHGEQYPWMLVVLASMVGQIGLPGGGVGFGWHYNGGGTVTSTGPVLSGLGSITNPpqakykadfrgASEHIPTSRIV 446
Cdd:cd02751 317 QRAHHGEQPAWMLVTLAAMLGQIGLPGGGFGFGYGYSNGGGPPRGGAGGPGLPQGKNP-----------VKDSIPVARIA 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 447 DCLLAPGNKIAFNGETLTYPDIKMAIYSAANPFHAQQDRNRMIDAWKKLETVVVLDHQWTASCRFADIVLPVTTRFERND 526
Cdd:cd02751 386 DALLNPGKEFTANGKLKTYPDIKMIYWAGGNPLHHHQDLNRLIKALRKDETIVVHDIFWTASARYADIVLPATTSLERND 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 527 IEQFGTHSNKGLMALHQIVKPQYEARHDFDIFAGLCKRFDKEAVYRENRNEMQWIQALYDEGVKMGASLGVTLPDFTTFW 606
Cdd:cd02751 466 IGLTGNYSNRYLIAMKQAVEPLGEARSDYEIFAELAKRLGVEEEFTEGRDEMEWLEHLYEETRAKAAGPGPELPSFEEFW 545
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1995542531 607 QgDGYIEYP-PGQPWVRHGEFREQPDLNPLGTPSGLIEIYSKTIAGFAYEDCPGHPVWMEPFER 669
Cdd:cd02751 546 E-KGIVRVPaAPKPFVAFADFREDPEANPLGTPSGKIEIYSETLADFGYDDCPGHPTWIEPWEG 608
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
37-807 |
1.01e-180 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 534.81 E-value: 1.01e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 37 AAGENPEQWIQSGSHY----GAFEAKVVNGEWTETRPFKHDKYP----CDMLNAVREVVYNPSRVRYPMVRldwllkrek 108
Cdd:COG0243 15 ALEAAGTKTVKTTCPGcgvgCGLGVKVEDGRVVRVRGDPDHPVNrgrlCAKGAALDERLYSPDRLTYPMKR--------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 109 sdRSQRGDNRFVRVSWDQALDLFYEELERVQKTYGSSGVFTGlADWQMVGKYHKAGGAMDRGL-GLHGS-YVTTVGDYSA 186
Cdd:COG0243 86 --VGPRGSGKFERISWDEALDLIAEKLKAIIDEYGPEAVAFY-TSGGSAGRLSNEAAYLAQRFaRALGTnNLDDNSRLCH 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 187 AAAQVILPHVIGSLEVyeqQTSLPlVIQNSNTIVLWGCDPIKNlqieflvpdhdAFGYWQQIKEAVAQNKMRVISVDPVR 266
Cdd:COG0243 163 ESAVAGLPRTFGSDKG---TVSYE-DLEHADLIVLWGSNPAEN-----------HPRLLRRLREAAKKRGAKIVVIDPRR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 267 SKSQNYLGcEQLALRPQTDVALMLALAHTLYEEKLYDTAFITDYTVGFEQFLPYLlgesdkQPKNAEWAAEICGLTAEQI 346
Cdd:COG0243 228 TETAAIAD-EWLPIRPGTDAALLLALAHVLIEEGLYDRDFLARHTVGFDELAAYV------AAYTPEWAAEITGVPAEDI 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 347 RDFARLLVK-GRTQFMGGWCVQRMHHGEQYPWMLVVLASMVGQIGLPgggvgfgwhynGGGTVTSTGpvlsglgsitnpp 425
Cdd:COG0243 301 RELAREFATaKPAVILWGMGLQQHSNGTQTVRAIANLALLTGNIGKP-----------GGGPFSLTG------------- 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 426 qakykadfrgasehiptsrivDCLLapgnkiafNGETltyPDIKMAIYSAANPFHAQQDRNRMIDAWKKLETVVVLDHQW 505
Cdd:COG0243 357 ---------------------EAIL--------DGKP---YPIKALWVYGGNPAVSAPDTNRVREALRKLDFVVVIDTFL 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 506 TASCRFADIVLPVTTRFERNDIeqFGTHSNKGLMALHQIVKPQYEARHDFDIFAGLCKRFDKEAVYRENRNEMQWIQALY 585
Cdd:COG0243 405 TETARYADIVLPATTWLERDDI--VTNSEDRRVHLSRPAVEPPGEARSDWEIFAELAKRLGFEEAFPWGRTEEDYLRELL 482
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 586 DEGVKMGASlgvtlpdFTTFWQgDGYIEYP--PGQPWVRHGefreqpdlnPLGTPSGLIEIYSKTIAgfayedCPGHPVW 663
Cdd:COG0243 483 EATRGRGIT-------FEELRE-KGPVQLPvpPEPAFRNDG---------PFPTPSGKAEFYSETLA------LPPLPRY 539
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 664 MEPFERTHSgKKDKYPLHLQSCHPDKRLHSQLCSSEAFRstyAVAGREPLYISEQDATTRGLKAGDIARVFNARGQVLAG 743
Cdd:COG0243 540 APPYEGAEP-LDAEYPLRLITGRSRDQWHSTTYNNPRLR---EIGPRPVVEINPEDAAALGIKDGDLVRVESDRGEVLAR 615
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1995542531 744 VVISPDFTPGVVRIHEGAWYSPQEggkagtlCTYGDPNVLSADiGTSQLAQGPSAHTVLVEVER 807
Cdd:COG0243 616 AKVTEGIRPGVVFAPHGWWYEPAD-------DKGGNVNVLTPD-ATDPLSGTPAFKSVPVRVEK 671
|
|
| dmsA_ynfE |
TIGR02166 |
anaerobic dimethyl sulfoxide reductase, A subunit, DmsA/YnfE family; Members of this family ... |
9-807 |
4.77e-116 |
|
anaerobic dimethyl sulfoxide reductase, A subunit, DmsA/YnfE family; Members of this family include known and probable dimethyl sulfoxide reductase (DMSO reductase) A chains. In E. coli, dmsA encodes the canonical anaerobic DMSO reductase A chain. The paralog ynfE, as part of ynfFGH expressed from a multicopy plasmid, could complement a dmsABC deletion, suggesting a similar function and some overlap in specificity, although YnfE could not substitute for DmsA in a mixed complex.
Pssm-ID: 274006 [Multi-domain] Cd Length: 797 Bit Score: 371.03 E-value: 4.77e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 9 SRRRFLSGMLAVGAASALA-PNPLISKVWAAGENP-----EQWIQSGSHYG-----AFEAKVVNGE--WTETRPFKHDKY 75
Cdd:TIGR02166 2 SRRHFLKTSAALGGLAAASgALSLPFSVNAAAEATptgpdEKVVWSACTVNcgsrcPLRVHVKDGEitRIETDNTGDDEY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 76 P------CDMLNAVREVVYNPSRVRYPMVRLdwllkreksdrSQRGDNRFVRVSWDQALDLFYEELERVQKTYGSSGVF- 148
Cdd:TIGR02166 82 GnhqvraCLRGRSMRRRVYNPDRLKYPMKRV-----------GKRGEGKFERISWDEATDTIADNLKRIIEKYGNEAIYv 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 149 ---TGLADWQMVGKyhKAGGAMDRGLGLHGSYVTTVGDYSAAAAQVILPHVIGSlevyEQQTSLPLVIQNSNTIVLWGCD 225
Cdd:TIGR02166 151 nygTGTTGGTMSRS--WPPTAVARLLNLCGGYLNQYGSYSTAQINEAMPYTYGI----SADGSSLDDIENSKLVVMFGNN 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 226 PIKNLQieflvpdhDAFGYWQQIKEAVAQNKMRVISVDPVRSKSQNYLGCEQLALRPQTDVALMLALAHTLYEEKLYDTA 305
Cdd:TIGR02166 225 PAETRM--------SGGGQTYYFLQALEKSNARVIVIDPRYTDTVAGREDEWIPIRPGTDAALVAAIAYVMISENLHDQA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 306 FITDYTVGF-EQFLP-----------YLLGE-SDKQPKNAEWAAEICGLTAEQIRDFARLLVKGRTQFMG-GWCVQRMHH 371
Cdd:TIGR02166 297 FLDRYCVGFdEKTLPasapkngsykdYILGEgADGTPKTPEWASKITGIPADTIIKLAREIGNAKPAFISqGWGPQRHAN 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 372 GEQYPWMLVVLASMVGQIGLPGGgvgfgwhyNGGGTVTSTGPVLSGLGSITNPPQAKykadfrgasehIPTSRIVDClla 451
Cdd:TIGR02166 377 GEQAARAIMMLALLTGNVGIKGG--------NNGAREGNYSLPFARMPELPNPVKTS-----------ISCFLWTDA--- 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 452 pgnkiAFNGETLTYP------------DIKMAIYSAANPFHAQQ-DRNRMIDAW---KKLETVVVLDHQWTASCRFADIV 515
Cdd:TIGR02166 435 -----IDRGTEMTAIkdgvrgkdkldsNIKFLWNYAGNCLINQHsDINRTHKILqdeSKCEMIVVIDNHMTSSAKYADIL 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 516 LPVTTRFERNDIEQFGTHSNKG-LMALHQIVKPQYEARHDFDIFAGLCKRFDKEAVYRENRNEMQWIQALYDEGVKMGAS 594
Cdd:TIGR02166 510 LPDTTTLEQNDFIEDSYASNMSyLIFMQKAIEPLFECKPIYDMLSEVAKRLGVEAEFTEGRTQEEWLEHLYAQTRAADPA 589
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 595 lgvtLPDFTTFWQGDGYIEYPPGQPWVRHGEFREQPDLNPLGTPSGLIEIYSKTIAGFA--YEDCPGH-----PVWMEPF 667
Cdd:TIGR02166 590 ----LPSFAELRKQGIYKAKSAPGPFVAFEDFRRDPEANPLKTPSGKIEIYSERLAQIAhtWELPEGDvitplPEYVPTF 665
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 668 ERTHSGKKDKYPLHLQSCHPDKRLHSQLCSSEAFRStyavAGREPLYISEQDATTRGLKAGDIARVFNARGQVLAGVVIS 747
Cdd:TIGR02166 666 EGPDDPLRKDFPLQLTGFHYKGRTHSTYGNVDWLRE----AAPQELWINPIDAQKRGITNGDMVRIFNSRGEVEIPAKVT 741
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1995542531 748 PDFTPGVVRIHEGAWYSPQE-----GGKAGTLCTYgDPnvlsadigtSQLAQGPSAHTVLVEVER 807
Cdd:TIGR02166 742 PRIMPGVVALGQGAWYQPDKngidvGGCINTLTTQ-RP---------SPLAKGNPQHTNLVEVEK 796
|
|
| MopB_DmsA-EC |
cd02770 |
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
57-661 |
1.23e-104 |
|
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: 335.45 E-value: 1.23e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 57 AKVVNGE--WTETRPFKHDKY------PCDMLNAVREVVYNPSRVRYPMVRLDWllkreksdrsqRGDNRFVRVSWDQAL 128
Cdd:cd02770 16 AHVKDGVitRIETDDTGDDDPgfhqirACLRGRSQRKRVYNPDRLKYPMKRVGK-----------RGEGKFVRISWDEAL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 129 DLFYEELERVQKTYGSSGVF----TGLADWQMVGKyhkagGAMDRGLGLHGSYVTTVGDYSAAAAQVILPHVIGSLEvye 204
Cdd:cd02770 85 DTIASELKRIIEKYGNEAIYvnygTGTYGGVPAGR-----GAIARLLNLTGGYLNYYGTYSWAQITTATPYTYGAAA--- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 205 qQTSLPLVIQNSNTIVLWGCDPIKNLQIEFLVpdhdafGYW-QQIKEAVAqnkmRVISVDPVRSKSQNYLGCEQLALRPQ 283
Cdd:cd02770 157 -SGSSLDDLKDSKLVVLFGHNPAETRMGGGGS------TYYyLQAKKAGA----KFIVIDPRYTDTAVTLADEWIPIRPG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 284 TDVALMLALAHTLYEEKLYDTAFITDYTVGF-EQFLP-----------YLLGE-SDKQPKNAEWAAEICGLTAEQIRDFA 350
Cdd:cd02770 226 TDAALVAAMAYVMITENLHDQAFLDRYCVGFdAEHLPegappnesykdYVLGTgYDGTPKTPEWASEITGVPAETIRRLA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 351 RLLVKGRTQFM-GGWCVQRMHHGEQYPWMLVVLASMVGQIGLPGGgvgfgwhyNGGGTVTSTGPVLSGLGSITNPPQAKy 429
Cdd:cd02770 306 REIATTKPAAIlQGWGPQRHANGEQAARAIMMLAAMTGNVGIPGG--------NTGARPGGSAYNGAGLPAGKNPVKTS- 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 430 kadfrgasehIPTSRIVDCLLAPGNKIAFNGETLTY----PDIKMaIYSAANPFHAQQ--DRNRMIDA----WKKLETVV 499
Cdd:cd02770 377 ----------IPCFMWTDAIERGEEMTADDGGVKGAdklkSNIKM-IWNYAGNTLINQhsDDNNTTRAllddESKCEFIV 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 500 VLDHQWTASCRFADIVLPVTTRFERNDIEQFGTHSNKGLMALHQ-IVKPQYEARHDFDIFAGLCKRFDKEAVYRENRNEM 578
Cdd:cd02770 446 VIDNFMTPSARYADILLPDTTELEREDIVLTSNAGMMEYLIYSQkAIEPLYECKSDYEICAELAKRLGVEDQFTEGKTEQ 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 579 QWIQALYDEGVKmgaslgvTLPDFTTF--WQGDGYIEYPPGQPWVRHGEFREQPDLNPLGTPSGLIEIYSKTIAGFAyED 656
Cdd:cd02770 526 EWLEELYGQTRA-------KEPGLPTYeeFREKGIYRVPRALPFVAFEDFREDPENNPLKTPSGKIEIYSKALADMA-KT 597
|
....*
gi 1995542531 657 CPGHP 661
Cdd:cd02770 598 LPEGD 602
|
|
| PRK14990 |
PRK14990 |
anaerobic dimethyl sulfoxide reductase subunit A; Provisional |
22-807 |
7.68e-93 |
|
anaerobic dimethyl sulfoxide reductase subunit A; Provisional
Pssm-ID: 184952 [Multi-domain] Cd Length: 814 Bit Score: 309.65 E-value: 7.68e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 22 AASALAPNPLISKV-WAAGEnpeqwIQSGSHYgAFEAKVVNGE--WTETRPFKHDKY-------PCDMLNAVREVVYNPS 91
Cdd:PRK14990 45 AVDSAIPTKSDEKViWSACT-----VNCGSRC-PLRMHVVDGEikYVETDNTGDDNYdglhqvrACLRGRSMRRRVYNPD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 92 RVRYPMVRLdwllkreksdrSQRGDNRFVRVSWDQALDLFYEELERVQKTYGSSGVF----TGLADWQMVGKYHKAGGAM 167
Cdd:PRK14990 119 RLKYPMKRV-----------GARGEGKFERISWEEAYDIIATNMQRLIKEYGNESIYlnygTGTLGGTMTRSWPPGNTLV 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 168 DRGLGLHGSYVTTVGDYSAAAAQVILPHVIGSLevyeQQTSLPLVIQNSNTIVLWGCDPIKNLQieflvpdhDAFGYWQQ 247
Cdd:PRK14990 188 ARLMNCCGGYLNHYGDYSSAQIAEGLNYTYGGW----ADGNSPSDIENSKLVVLFGNNPGETRM--------SGGGVTYY 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 248 IKEAVAQNKMRVISVDPVRSKSQNYLGCEQLALRPQTDVALMLALAHTLYEEKLYDTAFITDYTVGF-EQFLP------- 319
Cdd:PRK14990 256 LEQARQKSNARMIIIDPRYTDTGAGREDEWIPIRPGTDAALVNGLAYVMITENLVDQPFLDKYCVGYdEKTLPasapkng 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 320 ----YLLGE-SDKQPKNAEWAAEICGLTAEQIRDFARLLVKGRTQFMG-GWCVQRMHHGEQYPWMLVVLASMVGQIGLpg 393
Cdd:PRK14990 336 hykaYILGEgPDGVAKTPEWASQITGVPADKIIKLAREIGSTKPAFISqGWGPQRHANGEIATRAISMLAILTGNVGI-- 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 394 ggvgfgwhyNGGGTVTSTGPV---LSGLGSITNPPQAKYKA-DFRGASEHIPTSrivdCLLAPGNKiafNGETLTYPdIK 469
Cdd:PRK14990 414 ---------NGGNSGAREGSYslpFVRMPTLENPIQTSISMfMWTDAIERGPEM----TALRDGVR---GKDKLDVP-IK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 470 MAIYSAANPF---HAQQDR-NRMIDAWKKLETVVVLDHQWTASCRFADIVLPVTTRFERNDieqFGTHSNKGLMAL---- 541
Cdd:PRK14990 477 MIWNYAGNCLinqHSEINRtHEILQDDKKCELIVVIDCHMTSSAKYADILLPDCTASEQMD---FALDASCGNMSYvifn 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 542 HQIVKPQYEARHDFDIFAGLCKRFDKEAVYRENRNEMQWIQALYDEGVKMGASLgvtlPDFTTFWQGDGYIEYPPGQPWV 621
Cdd:PRK14990 554 DQVIKPRFECKTIYEMTSELAKRLGVEQQFTEGRTQEEWMRHLYAQSREAIPEL----PTFEEFRKQGIFKKRDPQGHHV 629
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 622 RHGEFREQPDLNPLGTPSGLIEIYSKTIAGFA--YEDCPGH-----PVWMEPFERTHSGKKDKYPLHLQSCHPDKRLHSQ 694
Cdd:PRK14990 630 AYKAFREDPQANPLTTPSGKIEIYSQALADIAatWELPEGDvidplPIYTPGFESYQDPLNKQYPLQLTGFHYKSRVHST 709
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 695 LCSSEAFRStyavAGREPLYISEQDATTRGLKAGDIARVFNARGQVLAGVVISPDFTPGVVRIHEGAWYSPQeggkAGTL 774
Cdd:PRK14990 710 YGNVDVLKA----ACRQEMWINPLDAQKRGINNGDKVRIFNDRGEVHIEAKVTPRMMPGVVALGEGAWYDPD----AKRV 781
|
810 820 830
....*....|....*....|....*....|...
gi 1995542531 775 CTYGDPNVLSADiGTSQLAQGPSAHTVLVEVER 807
Cdd:PRK14990 782 DKGGCINVLTTQ-RPSPLAKGNPSHTNLVQVEK 813
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
54-565 |
7.32e-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: 243.39 E-value: 7.32e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 54 AFEAKVVNGEWTETRPFKHDKY----PCDMLNAVREVVYNPSRVRYPMVRldwllkreksdrsQRGDNRFVRVSWDQALD 129
Cdd:cd00368 12 GILVYVKDGKVVRIEGDPNHPVnegrLCDKGRAGLDGLYSPDRLKYPLIR-------------VGGRGKFVPISWDEALD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 130 LFYEELERVQKTYGSSGVFTGLADWQMVGKYHKAGGAMdRGLGlhGSYVTTVGDYSAAAAQVILPHvigsLEVYEQQTSL 209
Cdd:cd00368 79 EIAEKLKEIREKYGPDAIAFYGGGGASNEEAYLLQKLL-RALG--SNNVDSHARLCHASAVAALKA----FGGGAPTNTL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 210 PlVIQNSNTIVLWGCDPIKNLQIEFlvpdhdafgywQQIKEAVaQNKMRVISVDPVRSKSqNYLGCEQLALRPQTDVALM 289
Cdd:cd00368 152 A-DIENADLILLWGSNPAETHPVLA-----------ARLRRAK-KRGAKLIVIDPRRTET-AAKADEWLPIRPGTDAALA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 290 lalahtlyeeklydtafitdytvgfeqflpyllgesdkqpkNAEWAAEICGLTAEQIRDFARLLVK-GRTQFMGGWCVQR 368
Cdd:cd00368 218 -----------------------------------------LAEWAAEITGVPAETIRALAREFAAaKRAVILWGMGLTQ 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 369 MHHGEQYPWMLVVLASMVGQIglpgggvgfgwHYNGGGtvtstgpvlsglgsitnppqakykadfrgasehiptsrivdc 448
Cdd:cd00368 257 HTNGTQNVRAIANLAALTGNI-----------GRPGGG------------------------------------------ 283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 449 llapgnkiafngetltypdikmaIYSAANPFHAQQDRNRMIDAWKKLETVVVLDHQWTASCRFADIVLPVTTRFERNDIe 528
Cdd:cd00368 284 -----------------------LGPGGNPLVSAPDANRVRAALKKLDFVVVIDIFMTETAAYADVVLPAATYLEKEGT- 339
|
490 500 510
....*....|....*....|....*....|....*..
gi 1995542531 529 qfGTHSNKGLMALHQIVKPQYEARHDFDIFAGLCKRF 565
Cdd:cd00368 340 --YTNTEGRVQLFRQAVEPPGEARSDWEILRELAKRL 374
|
|
| MopB_CT_DMSOR-BSOR-TMAOR |
cd02793 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
678-807 |
1.04e-67 |
|
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: 220.20 E-value: 1.04e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 678 YPLHLQSCHPDKRLHSQLCSSEAfRSTYAVAGREPLYISEQDATTRGLKAGDIARVFNARGQVLAGVVISPDFTPGVVRI 757
Cdd:cd02793 1 YPLHLLSNQPATRLHSQLDHGSL-SRAYKVQGREPIRINPADAAARGIADGDIVRVFNDRGACLAGAVVTDGIMPGVVQL 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1995542531 758 HEGAWYSPQEGGKAGTLCTYGDPNVLSADIGTSQLAQGPSAHTVLVEVER 807
Cdd:cd02793 80 PTGAWYDPDDPGEPGPLCKHGNPNVLTLDIGTSSLAQGCSAQTCLVQIEK 129
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
92-564 |
6.13e-59 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 204.94 E-value: 6.13e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 92 RVRYPMVRldwllkreksdrsqRGDNRFVRVSWDQALDLFYEELERVQKTYGSSGVF--TGLADWQMVGKYHKAGGAMDR 169
Cdd:pfam00384 1 RLKYPMVR--------------RGDGKFVRVSWDEALDLIAKKLKRIIKKYGPDAIAinGGSGGLTDVESLYALKKLLNR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 170 GLGLHGSYVTTVGDYSAAAAQvilphVIGSLEVYEQQ-TSLPLVIQNSNTIVLWGCDPIKNLQIeflvpdhdafgYWQQI 248
Cdd:pfam00384 67 LGSKNGNTEDHNGDLCTAAAA-----AFGSDLRSNYLfNSSIADIENADLILLIGTNPREEAPI-----------LNARI 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 249 KEAVAQNKMRVISVDPVRSKSQNYlgcEQLALRPQTDVALMLALAHTLYEEKLYDTAFITDytvgfeqflpyllgesdkq 328
Cdd:pfam00384 131 RKAALKGKAKVIVIGPRLDLTYAD---EHLGIKPGTDLALALAGAHVFIKELKKDKDFAPK------------------- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 329 pknaewaaeicgltaeqirdfARLLVkgrtqfmgGWCVQRMHHGEQYPWMLVVLASMVGQIGLpgggvgfgwhyNGGGTv 408
Cdd:pfam00384 189 ---------------------PIIIV--------GAGVLQRQDGEAIFRAIANLADLTGNIGR-----------PGGGW- 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 409 tstgpvlSGLGSITNppqakykadfrGASEHiPTSRIVdclLAPGNKIAFNGETLTYPDIKMAIYSAANPFHAQQDRNRM 488
Cdd:pfam00384 228 -------NGLNILQG-----------AASPV-GALDLG---LVPGIKSVEMINAIKKGGIKVLYLLGNNPFVTHADENRV 285
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1995542531 489 IDAWKKLETVVVLD-HQWTASCRFADIVLPVTTRFERNDIEQFGTHSNkglMALHQIVKPQYEARHDFDIFAGLCKR 564
Cdd:pfam00384 286 VKALQKLDLFVVYDgHHGDKTAKYADVILPAAAYTEKNGTYVNTEGRV---QSTKQAVPPPGEAREDWKILRALSEV 359
|
|
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
85-658 |
2.91e-58 |
|
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: 207.10 E-value: 2.91e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 85 EVVYNPSRVRYPMVRldwllkreksdrSQRGDNRFVRVSWDQALDLFYEELERVQKTYGSSGV-------FTGLADWQMV 157
Cdd:cd02766 48 ERVYSPDRLLTPLKR------------VGRKGGQWERISWDEALDTIAAKLKEIKAEYGPESIlpysyagTMGLLQRAAR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 158 GKYHKAGGAMDrglgLHGSYVTTVGDysaaAAQVIlphVIGSLevyeqQTSLPLVIQNSNTIVLWGCDPIKNlQIEFlvp 237
Cdd:cd02766 116 GRFFHALGASE----LRGTICSGAGI----EAQKY---DFGAS-----LGNDPEDMVNADLIVIWGINPAAT-NIHL--- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 238 dhdafgyWQQIKEAVAQNkMRVISVDPVRSKSQNYlgCEQ-LALRPQTDVALMLALAHTLYEEKLYDTAFITDYTVGFEQ 316
Cdd:cd02766 176 -------MRIIQEARKRG-AKVVVIDPYRTATAAR--ADLhIQIRPGTDGALALGVAKVLFREGLYDRDFLARHTEGFEE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 317 FLPYLlgesdkQPKNAEWAAEICGLTAEQIRDFARLLVK-GRTQFMGGWCVQRmhhgeqypwmlvvlasmvgqiglpggg 395
Cdd:cd02766 246 LKAHL------ETYTPEWAAEITGVSAEEIEELARLYGEaKPPSIRLGYGMQR--------------------------- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 396 vgfgwHYNGGGTVtstgpvlsglgsitnppqakykadfrgasehiptsRIVDCLLAPGNKIAFNGETLTY----PDIKMA 471
Cdd:cd02766 293 -----YRNGGQNV-----------------------------------RAIDALPALTGNIGVPGGGAFYsnsgPPVKAL 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 472 IYSAANPFHAQQDRNRMI-DAWKKLETVVVLDHQWTASCRFADIVLPVTTRFERNDIEQFGTHSNKGLMalHQIVKPQYE 550
Cdd:cd02766 333 WVYNSNPVAQAPDSNKVRkGLAREDLFVVVHDQFMTDTARYADIVLPATTFLEHEDVYASYWHYYLQYN--EPAIPPPGE 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 551 ARHDFDIFAGLCKRFDKEAVYREnRNEMQWI-QALYDEGVKMgasLGVTLPDFTTFWQGDgyieyPPGQPWVRHGefreq 629
Cdd:cd02766 411 ARSNTEIFRELAKRLGFGEPPFE-ESDEEWLdQALDGTGLPL---EGIDLERLLGPRKAG-----FPLVAWEDRG----- 476
|
570 580
....*....|....*....|....*....
gi 1995542531 630 pdlnpLGTPSGLIEIYSKTIAGFAYEDCP 658
Cdd:cd02766 477 -----FPTPSGKFEFYSERAAKRGLPPLP 500
|
|
| MopB_CT_DMSOR-like |
cd02777 |
The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
678-807 |
4.55e-57 |
|
The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide reductase (BSOR), trimethylamine N-oxide reductase (TMAOR) and other related proteins. DMSOR always catalyzes the reduction of DMSO to dimethylsulfide, but its cellular location and oligomerization state are organism-dependent. For example, in Rhodobacter sphaeriodes and Rhodobacter capsulatus, it is an 82-kDa monomeric soluble protein found in the periplasmic space; in E. coli, it is membrane-bound and exists as a heterotrimer. BSOR catalyzes the reduction of biotin sulfixode to biotin, and is unique among Mo enzymes because no additional auxiliary proteins or cofactors are required. TMAOR is similar to DMSOR, but its only natural substrate is TMAO. Also included in this group is the pyrogallol-phloroglucinol transhydroxylase from Pelobacter acidigallici. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239178 [Multi-domain] Cd Length: 127 Bit Score: 191.26 E-value: 4.55e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 678 YPLHLQSCHPDKRLHSQLCSSEAFRSTYAVAGREPLYISEQDATTRGLKAGDIARVFNARGQVLAGVVISPDFTPGVVRI 757
Cdd:cd02777 1 YPLQLISPHPKRRLHSQLDNVPWLREAYKVKGREPVWINPLDAAARGIKDGDIVRVFNDRGAVLAGARVTDRIMPGVVAL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1995542531 758 HEGAWYSPQEGgkaGTLCTYGDPNVLSADIGTSQLAQGPSAHTVLVEVER 807
Cdd:cd02777 81 PEGAWYDPDDN---GGLDKGGNPNVLTSDIPTSKLAQGNPANTCLVEIEK 127
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
85-755 |
2.27e-55 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 203.19 E-value: 2.27e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 85 EVVYNPSRVRYPMVRldwllkreksdrsqrGDNRFVRVSWDQALDLFYEELERVQKTYGSSGVFtGLADWQM-------V 157
Cdd:COG3383 54 EFVNSPDRLTTPLIR---------------RGGEFREVSWDEALDLVAERLREIQAEHGPDAVA-FYGSGQLtneenylL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 158 GKYHKAGgamdrgLG-LHGSYVTTVGDYSAAAAqviLPHVIGSLEV---YEQqtslplvIQNSNTIVLWGCDPIKNlqie 233
Cdd:COG3383 118 QKLARGV------LGtNNIDNNARLCMASAVAG---LKQSFGSDAPpnsYDD-------IEEADVILVIGSNPAEA---- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 234 flvpdHDAFgyWQQIKEAVaQNKMRVISVDPVRSKSqnylgCEQ----LALRPQTDVALMLALAHTLYEEKLYDTAFITD 309
Cdd:COG3383 178 -----HPVL--ARRIKKAK-KNGAKLIVVDPRRTET-----ARLadlhLQIKPGTDLALLNGLLHVIIEEGLVDEDFIAE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 310 YTVGFEQFLPYLLGESdkqpknAEWAAEICGLTAEQIRDFARLLVKG-RTQFMGGWCVQRMHHGEQYPWMLVVLASMVGQ 388
Cdd:COG3383 245 RTEGFEELKASVAKYT------PERVAEITGVPAEDIREAARLIAEAkRAMILWGMGVNQHTQGTDNVNAIINLALATGN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 389 IGLPGGGVGFGWHYN---GGGTVTSTGPVLSGLGSITNPPQAKYKADFRGAsEHIPTsrivdcllAPGnkiafngetLTY 465
Cdd:COG3383 319 IGRPGTGPFPLTGQNnvqGGRDMGALPNVLPGYRDVTDPEHRAKVADAWGV-PPLPD--------KPG---------LTA 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 466 PDIKMAIYS---------AANPFHAQQDRNRMIDAWKKLETVVVLDHQWTASCRFADIVLPVTTRFERNdieqfGTHSN- 535
Cdd:COG3383 381 VEMFDAIADgeikalwiiGENPAVSDPDANHVREALEKLEFLVVQDIFLTETAEYADVVLPAASWAEKD-----GTFTNt 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 536 -KGLMALHQIVKPQYEARHDFDIFAGLCKRF-------DKEAVYRENRNEMQWIQAL-YDegvKMGASLGVTLPDFTtfw 606
Cdd:COG3383 456 eRRVQRVRKAVEPPGEARPDWEIIAELARRLgygfdydSPEEVFDEIARLTPDYSGIsYE---RLEALGGVQWPCPS--- 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 607 qgdgyiEYPPGQPWVRHGEFReqpdlnplgTPSGLieiysktiAGFAYEDcpghpvWMEPFERThsgkKDKYPLHLQSch 686
Cdd:COG3383 530 ------EDHPGTPRLFTGRFP---------TPDGK--------ARFVPVE------YRPPAELP----DEEYPLVLTT-- 574
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1995542531 687 pdKRLHSQLCSSEAFRSTYAVAGREP---LYISEQDATTRGLKAGDIARVFNARGQVLAGVVISPDFTPGVV 755
Cdd:COG3383 575 --GRLLDQWHTGTRTRRSPRLNKHAPepfVEIHPEDAARLGIKDGDLVRVSSRRGEVVLRARVTDRVRPGTV 644
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
81-666 |
2.55e-54 |
|
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: 195.60 E-value: 2.55e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 81 NAVREVVYNPSRVRYPMVRLdwllkreksdrSQRGDNRFVRVSWDQALDLFYEELERVQKTYGSSGVftglADWQMVGKY 160
Cdd:cd02759 43 LAAPEIVYHPDRLLYPLKRV-----------GERGENKWERISWDEALDEIAEKLAEIKAEYGPESI----ATAVGTGRG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 161 HKAGGAMD--RGLGLHGSYVTTVGDYS-----AAAAQVILPHVIGSLEV-YEqqtslplviqNSNTIVLWGCDPIK-NLq 231
Cdd:cd02759 108 TMWQDSLFwiRFVRLFGSPNLFLSGEScywprDMAHALTTGFGLGYDEPdWE----------NPECIVLWGKNPLNsNL- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 232 ieflvpdhDAFGYWQQikeAVAQNKMRVISVDPVRS----KSQNYLgceqlALRPQTDVALMLALAHTLYEEKLYDTAFI 307
Cdd:cd02759 177 --------DLQGHWLV---AAMKRGAKLIVVDPRLTwlaaRADLWL-----PIRPGTDAALALGMLNVIINEGLYDKDFV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 308 TDYTVGFEQFLPYLlgesdkQPKNAEWAAEICGLTAEQIRDFARLLVKGRtqfmgGWCVQrmhhgeqypWMLVVLASMvg 387
Cdd:cd02759 241 ENWCYGFEELAERV------QEYTPEKVAEITGVPAEKIRKAARLYATAK-----PACIQ---------WGLAIDQQK-- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 388 qiglpgggvgfgwhyNGggtvTSTGPVLSGLGSITNppqakyKADFRGASehiptsrivdcLLAPgnkiafngetltYPd 467
Cdd:cd02759 299 ---------------NG----TQTSRAIAILRAITG------NLDVPGGN-----------LLIP------------YP- 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 468 IKMAIYSAANPFHAQQDRNRMIDAWKKLETVVVLDHQWTASCRFADIVLPVTTRFERNDIeQFGTHSNKGLMALHQIVKP 547
Cdd:cd02759 330 VKMLIVFGTNPLASYADTAPVLEALKALDFIVVVDLFMTPTAMLADIVLPVAMSLERPGL-RGGFEAENFVQLRQKAVEP 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 548 QYEARHDFDIFAGLCKRFD-KEAVYREnrnemqwiqalYDEGvkmgaslgvtlpdfttFWQGDGyieyPPGqpwvrhgef 626
Cdd:cd02759 409 YGEAKSDYEIVLELGKRLGpEEAEYYK-----------YEKG----------------LLRPDG----QPG--------- 448
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1995542531 627 reqpdlnpLGTPSGLIEIYSKTIAGFAYedcPGHPVWMEP 666
Cdd:cd02759 449 --------FNTPTGKVELYSTMLEELGY---DPLPYYREP 477
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
85-573 |
3.37e-44 |
|
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: 168.56 E-value: 3.37e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 85 EVVYNPSRVRYPMVRldwllkreksdrsqRGDNRFVRVSWDQALDLFYEELERVQKTYG-------SSGVFTgLADWQMV 157
Cdd:cd02754 47 KTLNGPERLTRPLLR--------------RNGGELVPVSWDEALDLIAERFKAIQAEYGpdsvafyGSGQLL-TEEYYAA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 158 GKYHKAGgamdrgLGlhgsyvTTVGDY-------SAAAAqvilpHV--IGSLEV---YEQqtslplvIQNSNTIVLWG-- 223
Cdd:cd02754 112 NKLAKGG------LG------TNNIDTnsrlcmaSAVAG-----YKrsFGADGPpgsYDD-------IEHADCFFLIGsn 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 224 ---CDPIknlqieflvpdhdafgYWQQIKEAVAQN-KMRVISVDPVRSKSqnylgCEQ----LALRPQTDVALMLALAHT 295
Cdd:cd02754 168 maeCHPI----------------LFRRLLDRKKANpGAKIIVVDPRRTRT-----ADIadlhLPIRPGTDLALLNGLLHV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 296 LYEEKLYDTAFITDYTVGFEQFLPYLlgesdkQPKNAEWAAEICGLTAEQIRDFARLLVKGRTqFMGGWC--VQRMHHG- 372
Cdd:cd02754 227 LIEEGLIDRDFIDAHTEGFEELKAFV------ADYTPEKVAEITGVPEADIREAARLFGEARK-VMSLWTmgVNQSTQGt 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 373 ---EQypWMLVVLA------------SMVGQIglpgggvgfgwhyNGGGT--VTSTGPVLSGLGSITNPPQAKYKADFRG 435
Cdd:cd02754 300 aanNA--IINLHLAtgkigrpgsgpfSLTGQP-------------NAMGGreVGGLANLLPGHRSVNNPEHRAEVAKFWG 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 436 asehIPTSRIVDcllAPGNKI--AFNGetLTYPDIKMAIYSAANPFHAQQDRNRMIDAWKKLETVVVLDHQW-TASCRFA 512
Cdd:cd02754 365 ----VPEGTIPP---KPGLHAveMFEA--IEDGEIKALWVMCTNPAVSLPNANRVREALERLEFVVVQDAFAdTETAEYA 435
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 513 DIVLPVTTRFERndiEQFGTHSNKGLMALHQIVKPQYEARHDFDIFAGLCKRFDK---------EAVYRE 573
Cdd:cd02754 436 DLVLPAASWGEK---EGTMTNSERRVSLLRAAVEPPGEARPDWWILADVARRLGFgelfpytspEEVFEE 502
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
87-564 |
2.56e-43 |
|
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: 163.62 E-value: 2.56e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 87 VYNPSRVRYPMVRLdwllkreksdrSQRGDNRFVRVSWDQALDLFYEELERVQKTYG-SSGVFTGLADWQMvgKYHKAgg 165
Cdd:cd02755 50 LYDPDRLKKPLIRV-----------GERGEGKFREASWDEALQYIASKLKEIKEQHGpESVLFGGHGGCYS--PFFKH-- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 166 aMDRGLGL-----HGSyvTTVGDYSAAAAQVILPHvigslevyeqQTSLPLVIQNSNTIVLWGcdpiKNLqIEFLVpdhd 240
Cdd:cd02755 115 -FAAAFGSpnifsHES--TCLASKNLAWKLVIDSF----------GGEVNPDFENARYIILFG----RNL-AEAII---- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 241 aFGYWQQIKEAVAqNKMRVISVDPVRSKSQnYLGCEQLALRPQTDVALMLALAHTLYEEKLYDTAFITDYTVGFEQFLPy 320
Cdd:cd02755 173 -VVDARRLMKALE-NGAKVVVVDPRFSELA-SKADEWIPIKPGTDLAFVLALIHVLISENLYDAAFVEKYTNGFELLKA- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 321 llgesDKQPKNAEWAAEICGLTAEQIRDFARLLVKG--RTQFMGGWCVQRMHHGEQYPWMLVVLASMVGQIglpgggvgf 398
Cdd:cd02755 249 -----HVKPYTPEWAAQITDIPADTIRRIAREFAAAapHAVVDPGWRGTFYSNSFQTRRAIAIINALLGNI--------- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 399 gwhyngggtvtstgpvlsglgsitnppqakykaDFRGAsehiptsrivdcllapgnkIAFNGETLTYPdIKMAIYSAANP 478
Cdd:cd02755 315 ---------------------------------DKRGG-------------------LYYAGSAKPYP-IKALFIYRTNP 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 479 FHAQQDRNRMIDAWKKLETVVVLDHQWTASCRFADIVLPVTTRFERNDieqFGTHSNKGLMALHQ---IVKPQYEARHDF 555
Cdd:cd02755 342 FHSMPDRARLIKALKNLDLVVAIDILPSDTALYADVILPEATYLERDE---PFSDKGGPAPAVATrqrAIEPLYDTRPGW 418
|
....*....
gi 1995542531 556 DIFAGLCKR 564
Cdd:cd02755 419 DILKELARR 427
|
|
| MopB_4 |
cd02765 |
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
58-666 |
4.49e-39 |
|
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: 153.40 E-value: 4.49e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 58 KVVNGEWtetrPFKHDKYPCdmLNAVREV--VYNPSRVRYPMVRLdwllkreksdrSQRGDNRFVRVSWDQALDLFYEEL 135
Cdd:cd02765 25 KVEPNEW----PDKTYKRGC--TRGLSHLqrVYSPDRLKYPMKRV-----------GERGEGKFERITWDEALDTIADKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 136 ERVQKTYG--SSGVFTgladwqMVGKYHKAGGAMDR--GLGLHGSyVTTVGDYSAAAAQVIlphVIGSLEVYEQQTSLPL 211
Cdd:cd02765 88 TEAKREYGgkSILWMS------SSGDGAILSYLRLAllGGGLQDA-LTYGIDTGVGQGFNR---VTGGGFMPPTNEITDW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 212 ViqNSNTIVLWGCDPIKNLQ--IEFLVpdhDAfgywqqiKEAVAqnkmRVISVDPVRSKSQNYlgCEQ-LALRPQTDVAL 288
Cdd:cd02765 158 V--NAKTIIIWGSNILETQFqdAEFFL---DA-------RENGA----KIVVIDPVYSTTAAK--ADQwVPIRPGTDPAL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 289 MLALAHTLYEEKLYDTAFITDYTVGfeqflPYLLGESDKQ-----------PKN-------------------------- 331
Cdd:cd02765 220 ALGMINYILEHNWYDEAFLKSNTSA-----PFLVREDNGTllrqadvtatpAEDgyvvwdtnsdspepvaatninpaleg 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 332 ------------------------AEWAAEICGLTAEQIRDFARLLVKGR-TQFMGGWCVQRMHHGEQYPWMLVVLASMV 386
Cdd:cd02765 295 eytingvkvhtvltalreqaasypPKAAAEICGLEEAIIETLAEWYATGKpSGIWGFGGVDRYYHSHVFGRTAAILAALT 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 387 GQIglpgggvgfgwhyngggtvtstGPVLSGLGSITnppqakykadfrgasehiptsrivdcllapgnkiafngetltyp 466
Cdd:cd02765 375 GNI----------------------GRVGGGVGQIK-------------------------------------------- 388
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 467 dikmAIYSAANPFHAQQ-DRNRMIDAWKKLETVVVLDHQWTASCRFADIVLPVTTRFERND-IEQFGTHSNkgLMALHQI 544
Cdd:cd02765 389 ----FMYFMGSNFLGNQpDRDRWLKVMKNLDFIVVVDIFHTPTVRYADIVLPAAHWFEVEDlLVRYTTHPH--VLLQQKA 462
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 545 VKPQYEARHDFDIFAGLCKRFDKEAVYreNRNEMQWIQALYDEgvKMGASLGVTLPDFttfwQGDGYIEYP--PGQPWVR 622
Cdd:cd02765 463 IEPLFESKSDFEIEKGLAERLGLGDYF--PKTPEDYVRAFMNS--DDPALDGITWEAL----KEEGIIMRLatPEDPYVA 534
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1995542531 623 HGEfreqpdlNPLGTPSGLIEIYSKTIAgfayEDCPGHPVWMEP 666
Cdd:cd02765 535 YLD-------QKFGTPSGKLEFYNEAAP----ELEEALPLPEEP 567
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
9-773 |
5.61e-36 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 145.97 E-value: 5.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 9 SRRRFLSGMLAVGAASALA---PNPLISKVWAAGENPEQWIQS----GSHYGAFEAKVVNGEWTETRPFKHDKYP----C 77
Cdd:PRK15488 4 SRRDFLKGAGAGCAACALGsllPGALAANEIAQLKGKTKLTPSicemCSTRCPIEARVVNGKNVFIQGNPKAKSFgtkvC 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 78 DMLNAVREVVYNPSRVRYPMVRldwllkreksdRSQRGDNRFVRVSWDQALDLFYEELERVQKTYGS-SGVFTGLADWQM 156
Cdd:PRK15488 84 ARGGSGHSLLYDPQRIVKPLKR-----------VGERGEGKWQEISWDEAYQEIAAKLNAIKQQHGPeSVAFSSKSGSLS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 157 VGKYHKAGGAMDRGLGLHGSyvTTVGDYSAAAAqvilpHVIGslevyeqqTSLPLVIQNSNTIVLWGcdpiknlqieflv 236
Cdd:PRK15488 153 SHLFHLATAFGSPNTFTHAS--TCPAGYAIAAK-----VMFG--------GKLKRDLANSKYIINFG------------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 237 pdHDAF-----GYWQQIKEAVAQNKMRVISVDP----VRSKSQnylgcEQLALRPQTDVALMLALAHTLYEEKLYDTAFI 307
Cdd:PRK15488 205 --HNLYeginmSDTRGLMTAQMEKGAKLVVFEPrfsvVASKAD-----EWHAIRPGTDLAVVLALCHVLIEENLYDKAFV 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 308 TDYTVGFEQFLPYLlgesdkQPKNAEWAAEICGLTAEQIRDFARLLVKGRTQFMGGWCVQRMHHGEQYPW--MLVVLASM 385
Cdd:PRK15488 278 ERYTSGFEELAASV------KEYTPEWAEAISDVPADDIRRIARELAAAAPHAIVDFGHRATFTPEEFDMrrAIFAANVL 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 386 VGQIGLP--GGGVGFGWHYN--GGGTVTST--GPVLSGLGSITNP------PQAKYKadfrgASEHIPTSRIVDCLLapg 453
Cdd:PRK15488 352 LGNIERKggLYFGKNASVYNklAGEKVAPTlaKPGVKGMPKPTAKridlvgEQFKYI-----AAGGGVVQSIIDATL--- 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 454 nkiafngETLTYPdIKMAIYSAANPFHAQQDRNRMIDAWKKLETVVVLDHQWTASCRFADIVLPVTTRFERNdiEQFGTH 533
Cdd:PRK15488 424 -------TQKPYQ-IKGWVMSRHNPMQTVTDRADVVKALKKLDLVVVCDVYLSESAAYADVVLPESTYLERD--EEISDK 493
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 534 SNK--GLMALHQIVKPQYEARHDFDIFAGLCKRFDKEAVYR-ENRNEMQWIQ-----ALYDEGVKMG-ASLGVTL----P 600
Cdd:PRK15488 494 SGKnpAYALRQRVVEPIGDTKPSWQIFKELGEKMGLGQYYPwQDMETLQLYQvngdhALLKELKKKGyVSFGVPLllreP 573
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 601 DFTtfwqgDGYIE-YPPGQPWVRHGEFREQPDLNplgTPSGLIEIYSKTIAGFAyedcPGHPVW-MEPFERTHSGK---- 674
Cdd:PRK15488 574 KMV-----AKFVArYPNAKAVDEDGTYGSQLKFK---TPSGKIELFSAKLEALA----PGYGVPrYRDVALKKEDElyfi 641
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 675 KDKYPLHLQSCHPDKRLHSQLCSSeafrstyavagrEPLYISEQDATTRGLKAGDIARVFNA----RGQVLAGVVISPD- 749
Cdd:PRK15488 642 QGKVAVHTNGATQNVPLLANLMSD------------NAVWIHPQTAGKLGIKNGDEIRLENSvgkeKGKALVTPGIRPDt 709
|
810 820 830
....*....|....*....|....*....|....*...
gi 1995542531 750 -F--------TPGVVR-----IHEGAWYSPQEGGKAGT 773
Cdd:PRK15488 710 lFaymgfgskNKELTRatgkgIHCGNLLPHVTSPVSGT 747
|
|
| MopB_Nitrate-R-NarG-like |
cd02750 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
87-565 |
2.51e-35 |
|
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: 140.15 E-value: 2.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 87 VYNPSRVRYPMVRldwllkreksdRSQRGDNRFVRVSWDQALDLFYEELERVQKTYGSSGVFTglaDWQMVGKYHKAGGA 166
Cdd:cd02750 61 LYSPDRVKYPLKR-----------VGARGEGKWKRISWDEALELIADAIIDTIKKYGPDRVIG---FSPIPAMSMVSYAA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 167 MDRGLGLHG----SYVTTVGDYSAAAaqvilPHVIG-SLEVYEqqtslPLVIQNSNTIVLWGCDPIKNLQIeflvpdhDA 241
Cdd:cd02750 127 GSRFASLIGgvslSFYDWYGDLPPGS-----PQTWGeQTDVPE-----SADWYNADYIIMWGSNVPVTRTP-------DA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 242 FGYWQqikeaVAQNKMRVISVDPVRSKSQNYLGcEQLALRPQTDVALMLALAHTLYEEKLYDTAFITDYTVgfeqfLPYL 321
Cdd:cd02750 190 HFLTE-----ARYNGAKVVVVSPDYSPSAKHAD-LWVPIKPGTDAALALAMAHVIIKEKLYDEDYLKEYTD-----LPFL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 322 LgesdkqpKNAEWAAEICGLTAEQIRDFARLLVK-GRTQFMGGWCVQRMHHGEQYPWMLVVLASMVGqiglpgggvgfGW 400
Cdd:cd02750 259 V-------YTPAWQEAITGVPRETVIRLAREFATnGRSMIIVGAGINHWYHGDLCYRALILLLALTG-----------NE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 401 HYNGGGTVTSTGPVlsglgsitnppqakykadfrgasehiptsrivdcllapgnkiafngetltypdiKMAIYSAANPF- 479
Cdd:cd02750 321 GKNGGGWAHYVGQP------------------------------------------------------RVLFVWRGNLFg 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 480 -HAQQDRNRMIDAWKKLETVVVLDHQWTASCRFADIVLPVTTRFERNDIEQfgTHSNKGLMALHQIVKPQYEARHDFDIF 558
Cdd:cd02750 347 sSGKGHEYFEDAPEGKLDLIVDLDFRMDSTALYSDIVLPAATWYEKHDLST--TDMHPFIHPFSPAVDPLWEAKSDWEIF 424
|
....*..
gi 1995542531 559 AGLCKRF 565
Cdd:cd02750 425 KALAKKV 431
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
89-566 |
1.43e-33 |
|
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: 136.37 E-value: 1.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 89 NPSRVRYPMVRldwllkreksdrsqRGDnRFVRVSWDQALDLFYEELERVQKTYGSSGVftgladwqmvGKYHKAGGAMD 168
Cdd:cd02762 51 DPDRLRTPMRR--------------RGG-SFEEIDWDEAFDEIAERLRAIRARHGGDAV----------GVYGGNPQAHT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 169 RGLGLHGSY----VTTVGDYSAAAAQVIlPHVIGSLEVYEQQTSLPLV-IQNSNTIVLWGCDPIKNLQIEFLVPDHDAfg 243
Cdd:cd02762 106 HAGGAYSPAllkaLGTSNYFSAATADQK-PGHFWSGLMFGHPGLHPVPdIDRTDYLLILGANPLQSNGSLRTAPDRVL-- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 244 ywqQIKEAVAQNKmRVISVDPVRSKSQNyLGCEQLALRPQTDVALMLALAHTLYEEKLYDTAFITDYTVGFEQFLPYLlg 323
Cdd:cd02762 183 ---RLKAAKDRGG-SLVVIDPRRTETAK-LADEHLFVRPGTDAWLLAAMLAVLLAEGLTDRRFLAEHCDGLDEVRAAL-- 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 324 esdkQPKNAEWAAEICGLTAEQIRDFARLLVKGRTQF----MGgwcVQRMHHGEQYPWMLVVLASMVGqiglpgggvgfg 399
Cdd:cd02762 256 ----AEFTPEAYAPRCGVPAETIRRLAREFAAAPSAAvygrLG---VQTQLFGTLCSWLVKLLNLLTG------------ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 400 wHYNGGGTVTSTGPVLSGLGSiTNPPQAKYKADFRGASEH------IPTSRIVDCLLAPGNKiafngetltypDIKMAIY 473
Cdd:cd02762 317 -NLDRPGGAMFTTPALDLVGQ-TSGRTIGRGEWRSRVSGLpeiageLPVNVLAEEILTDGPG-----------RIRAMIV 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 474 SAANPFHAQQDRNRMIDAWKKLETVVVLDHQWTASCRFADIVLPVTTRFERNDIEQFGTHSNKGLMAL-HQIVKPQYEAR 552
Cdd:cd02762 384 VAGNPVLSAPDGARLEAALGGLEFMVSVDVYMTETTRHADYILPPASQLEKPHATFFNLEFPRNAFRYrRPLFPPPPGTL 463
|
490
....*....|....
gi 1995542531 553 HDFDIFAGLCKRFD 566
Cdd:cd02762 464 PEWEILARLVEALD 477
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
85-573 |
6.52e-29 |
|
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: 121.94 E-value: 6.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 85 EVVYNPSRVRYPMVRLDwllkreksdrsqrgdNRFVRVSWDQALDLFYEELERVQKTYGSSGV-FTGLA-----DWQMVG 158
Cdd:cd02753 47 DFVNSKDRLTKPLIRKN---------------GKFVEASWDEALSLVASRLKEIKDKYGPDAIaFFGSAkctneENYLFQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 159 KYHKAGGA---MDRGLGL-HGSYV----TTVGdySAAAAQVILPhvigslevyeqqtslplvIQNSNTIVLWGCDPIKNl 230
Cdd:cd02753 112 KLARAVGGtnnVDHCARLcHSPTVaglaETLG--SGAMTNSIAD------------------IEEADVILVIGSNTTEA- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 231 qieflvpdHDAFGywQQIKEAVaQNKMRVISVDPVRSKSqnylgCEQ----LALRPQTDVALMLALAHTLYEEKLYDTAF 306
Cdd:cd02753 171 --------HPVIA--RRIKRAK-RNGAKLIVADPRRTEL-----ARFadlhLQLRPGTDVALLNAMAHVIIEEGLYDEEF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 307 ITDYTVGFEQFLpyllgesDKQPKNA-EWAAEICGLTAEQIRDFARLLVKGRTQfMGGWC--VQRMHHGEQYPWMLVVLA 383
Cdd:cd02753 235 IEERTEGFEELK-------EIVEKYTpEYAERITGVPAEDIREAARMYATAKSA-AILWGmgVTQHSHGTDNVMALSNLA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 384 SMVGQIGLpgggvgfgwhyNGGGtvtstgpvlsglgsiTNPpqakykadFR------GASEH--IPTsrivdcllapgnk 455
Cdd:cd02753 307 LLTGNIGR-----------PGTG---------------VNP--------LRgqnnvqGACDMgaLPN------------- 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 456 iafngetlTYPDIKMAIY-SAANPFHAQQDRNRMIDAWKKLETVVVLDHQWTASCRFADIVLPVTTRFERNdieqfGTHS 534
Cdd:cd02753 340 --------VLPGYVKALYiMGENPALSDPNTNHVRKALESLEFLVVQDIFLTETAELADVVLPAASFAEKD-----GTFT 406
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1995542531 535 N--KGLMALHQIVKPQYEARHDFDIFAGLCKR-------FDKEAVYRE 573
Cdd:cd02753 407 NteRRVQRVRKAVEPPGEARPDWEIIQELANRlgypgfySHPEEIFDE 454
|
|
| MopB_Arsenate-R |
cd02757 |
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ... |
87-650 |
3.18e-26 |
|
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other related proteins. These members belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239158 [Multi-domain] Cd Length: 523 Bit Score: 113.69 E-value: 3.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 87 VYNPSRVRYPMvrldwllKREKSDRSQRGDNRFVRVSWDQALDLFYEELERVQKTyGSSGVFTgladwQMVGKY-HKAGG 165
Cdd:cd02757 51 VYDPDRILYPM-------KRTNPRKGRDVDPKFVPISWDEALDTIADKIRALRKE-NEPHKIM-----LHRGRYgHNNSI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 166 AMDRGLGLHGSyvTTVGDYSAAAAQVilpHVIGS--LEVYEQQTSLPLviQNSNTIVLWGCDPIK-NLQIEFlvpdhdaf 242
Cdd:cd02757 118 LYGRFTKMIGS--PNNISHSSVCAES---EKFGRyyTEGGWDYNSYDY--ANAKYILFFGADPLEsNRQNPH-------- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 243 gyWQQIKEAVAqNKMRVISVDPVRSKSQNyLGCEQLALRPQTDVALMLALAHTLYEEKLYDTAFITDYTVGFEQFLP-YL 321
Cdd:cd02757 183 --AQRIWGGKM-DQAKVVVVDPRLSNTAA-KADEWLPIKPGEDGALALAIAHVILTEGLWDKDFVGDFVDGKNYFKAgET 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 322 LGESDKQPK---------NA-------EWAAEICGLTAEQI----RDFARLLVKGRTQFMGGWCvqrMHHGEQYPWM-LV 380
Cdd:cd02757 259 VDEESFKEKsteglvkwwNLelkdytpEWAAKISGIPAETIervaREFATAAPAAAAFTWRGAT---MQNRGSYNSMaCH 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 381 VLASMVGQIglpgggvgfgwhYNGGGTVTSTGpvlsglgsitnppqakykadfrgasehiptsrivdcllapgnkiafng 460
Cdd:cd02757 336 ALNGLVGSI------------DSKGGLCPNMG------------------------------------------------ 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 461 etltYPDIKMAIYSAANPFHAQQDRNRMIDAWKKLETVVVLDHQWTASCRFADIVLPVTTRFERNDIEQFGTHSNkGLMA 540
Cdd:cd02757 356 ----VPKIKVYFTYLDNPVFSNPDGMSWEEALAKIPFHVHLSPFMSETTYFADIVLPDGHHFERWDVMSQENNLH-PWLS 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 541 LHQ-IVKPQYEARHDFDIFAGLCKRFDKEAvyreNRNEMQWIqalydegvkmgaslgvtlpdfttFWQgdgYIEYPPGQP 619
Cdd:cd02757 431 IRQpVVKSLGEVREETEILIELAKKLDPKG----SDGMKRYA-----------------------PGQ---FKDPETGKN 480
|
570 580 590
....*....|....*....|....*....|.
gi 1995542531 620 WVRHGEfreqpdlNPLGTPSGLIEIYSKTIA 650
Cdd:cd02757 481 NRWEFE-------NVFPTETGKFEFYSETLK 504
|
|
| MopB_CT_DmsA-EC |
cd02794 |
The MopB_CT_DmsA-EC CD includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
678-807 |
5.50e-22 |
|
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: 91.97 E-value: 5.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 678 YPLHLQSCHPDKRLHSQLCSSEAFRStyavAGREPLYISEQDATTRGLKAGDIARVFNARGQVLAGVVISPDFTPGVVRI 757
Cdd:cd02794 1 YPLQLIGWHYKRRTHSTFDNVPWLRE----AFPQEVWINPLDAAARGIKDGDRVLVFNDRGKVIRPVKVTERIMPGVVAL 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1995542531 758 HEGAWYSPQEGGkagtLCTYGDPNVLSADIgTSQLAQGPSAHTVLVEVER 807
Cdd:cd02794 77 PQGAWYEPDANG----IDKGGCINTLTGLR-PSPLAKGNPQHTNLVQVEK 121
|
|
| Molydop_binding |
pfam01568 |
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
680-802 |
1.00e-18 |
|
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: 82.32 E-value: 1.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 680 LHLQSCHPDKRLHSQLCSSEAFRstYAVAGREPLYISEQDATTRGLKAGDIARVFNARGQVLAGVVISPDFTPGVVRIHE 759
Cdd:pfam01568 1 LYLITGRVLGQYHSQTRTRRVLR--LAKPEPEVVEIHPEDAAALGIKDGDLVEVTSRRGSVVVRAKVTDRVRPGVVFMPF 78
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1995542531 760 GAWYSPqeggkagtlcTYGDPNVLSADiGTSQLAQGPSAHTVL 802
Cdd:pfam01568 79 GWWYEP----------RGGNANALTDD-ATDPLSGGPEFKTCA 110
|
|
| MopB_Formate-Dh-Na-like |
cd02752 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
54-565 |
2.89e-16 |
|
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: 83.22 E-value: 2.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 54 AFEAKVVNGEWTETRP-FKHdkyP------CDMLNAVREVVYNPSRVRYPMVRLDwllkreksdrsqrGDNRFVRVSWDQ 126
Cdd:cd02752 12 GLIAYVQNGVWVHQEGdPDH---PvnrgslCPKGAALRDFVHSPKRLKYPMYRAP-------------GSGKWEEISWDE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 127 ALDlfyEELERVQKTYGSSGVFTGLADWQMVGK---YHKAGGAMD-----------RGLGL----------HGSYVTTVG 182
Cdd:cd02752 76 ALD---EIARKMKDIRDASFVEKNAAGVVVNRPdsiAFLGSAKLSneecylirkfaRALGTnnldhqariuHSPTVAGLA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 183 D---YSAaaaqvilphvigslevyeqQTSLPLVIQNSNTIVLWGCDPIKNLQIEFlvpdhdafgywQQIKEAVAQNKMRV 259
Cdd:cd02752 153 NtfgRGA-------------------MTNSWNDIKNADVILVMGGNPAEAHPVSF-----------KWILEAKEKNGAKL 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 260 ISVDPVR----SKSQNYLgceqlALRPQTDVALMLALAHtlyeeklydtaFITDYTvgfeqflpyllgesdkqPKNAEwa 335
Cdd:cd02752 203 IVVDPRFtrtaAKADLYV-----PIRSGTDIAFLGGMIN-----------YIIRYT-----------------PEEVE-- 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 336 aEICGLTAEQIRDFARLLVKGRTQFMGG---WCVQRMHH--GEQYPWMLVVLASMVGQIGLPgggvgfgwhynGGGTvts 410
Cdd:cd02752 248 -DICGVPKEDFLKVAEMFAATGRPDKPGtilYAMGWTQHtvGSQNIRAMCILQLLLGNIGVA-----------GGGV--- 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 411 tgPVLSGlgsitnppqakyKADFRGASEHIPTSRIVdcllaPGnkiafngetltYpdikmaiYSAANPFHAQQDRNRMID 490
Cdd:cd02752 313 --NALRG------------HSNVQGATDLGLLSHNL-----PG-----------Y-------LGGQNPNSSFPNANKVRR 355
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 491 AWKKLETVVVLD---HQWTASCRFAD----------IVLPVTTRFERNdieqfGTHSNKG--LMALHQIVKPQYEARHDF 555
Cdd:cd02752 356 ALDKLDWLVVIDpfpTETAAFWKNPGmdpksiqtevFLLPAACQYEKE-----GSITNSGrwLQWRYKVVEPPGEAKSDG 430
|
570
....*....|
gi 1995542531 556 DIFAGLCKRF 565
Cdd:cd02752 431 DILVELAKRL 440
|
|
| MopB_CT |
cd02775 |
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a ... |
690-774 |
7.53e-15 |
|
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: 70.81 E-value: 7.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 690 RLHSQLCS-SEAFRstyAVAGREPLYISEQDATTRGLKAGDIARVFNARGQVLAGVVISPDFTPGVVRIHEGAWYSPQEG 768
Cdd:cd02775 4 HFHSGTRTrNPWLR---ELAPEPVVEINPEDAAALGIKDGDLVRVESRRGSVVLRAKVTDGVPPGVVFLPHGWGHRGGRG 80
|
....*.
gi 1995542531 769 GKAGTL 774
Cdd:cd02775 81 GNANVL 86
|
|
| Molybdopterin_N |
pfam18364 |
Molybdopterin oxidoreductase N-terminal domain; This is the N-terminal domain of pfam00384 ... |
48-88 |
4.74e-12 |
|
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: 60.87 E-value: 4.74e-12
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1995542531 48 SGSHYGAFEAKVVNGEWTETRPFKHDKYPCDMLNAVREVVY 88
Cdd:pfam18364 1 TASHWGAFRAVVKDGRIVGVEPFEGDPDPSPLLQGVPDAVY 41
|
|
| MopB_CT_4 |
cd02785 |
The MopB_CT_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
677-762 |
1.08e-11 |
|
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: 62.77 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 677 KYPLHLQSCHPDKRLHSQLCSSEAFRStyavAGREP-LYISEQDATTRGLKAGDIARVFNARGQVLAGVVISPDFTPGVV 755
Cdd:cd02785 1 KYPLACIQRHSRFRVHSQFSNVPWLLE----LQPEPrVKINPIDAAARGIAHGDLVEVYNDRGSVVCKAKVDDGIQPGVV 76
|
....*..
gi 1995542531 756 RIHEGAW 762
Cdd:cd02785 77 TAEQGWW 83
|
|
| MopB_2 |
cd02763 |
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
88-350 |
1.78e-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: 67.93 E-value: 1.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 88 YNPSRVRYPMVRldwllkreksdRSQRGDNRFVRVSWDQALDLFYEELERVQKTYGSS-GVFTGLADWQ-MVGKYHKAGG 165
Cdd:cd02763 50 YSPARLTKPLLR-----------KGPRGSGQFEEIEWEEAFSIATKRLKAARATDPKKfAFFTGRDQMQaLTGWFAGQFG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 166 AMDrgLGLHGSYVttvgdySAAAAQVILPHVIGSLEVYEQQTslplvIQNSNTIVLWGcdpiknlqiefLVPDHDAfgyw 245
Cdd:cd02763 119 TPN--YAAHGGFC------SVNMAAGGLYSIGGSFWEFGGPD-----LEHTKYFMMIG-----------VAEDHHS---- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 246 QQIKEAVAQNKM---RVISVDPVRSkSQNYLGCEQLALRPQTDVALMLALAHTLYEEKLYDTAFITDYTVGfeqflPYLL 322
Cdd:cd02763 171 NPFKIGIQKLKRrggKFVAVNPVRT-GYAAIADEWVPIKPGTDGAFILALAHELLKAGLIDWEFLKRYTNA-----AELV 244
|
250 260
....*....|....*....|....*...
gi 1995542531 323 gesDKQPknaEWAAEICGLTAEQIRDFA 350
Cdd:cd02763 245 ---DYTP---EWVEKITGIPADTIRRIA 266
|
|
| MopB_CT_3 |
cd02786 |
The MopB_CT_3 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
678-805 |
2.72e-10 |
|
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: 58.45 E-value: 2.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 678 YPLHLQSCHPDKRLHSQLCSSEAFRSTyavAGREPLYISEQDATTRGLKAGDIARVFNARGQVLAGVVISPDFTPGVVRI 757
Cdd:cd02786 1 YPLRLITPPAHNFLNSTFANLPELRAK---EGEPTLLIHPADAAARGIADGDLVVVFNDRGSVTLRAKVTDDVPPGVVVA 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1995542531 758 HEGAWYSPQEGGKAgtlctygdPNVLSADIGTSqLAQGPSAHTVLVEV 805
Cdd:cd02786 78 EGGWWREHSPDGRG--------VNALTSARLTD-LGGGSTFHDTRVEV 116
|
|
| MopB_Phenylacetyl-CoA-OR |
cd02760 |
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large ... |
88-564 |
1.01e-09 |
|
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: 62.29 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 88 YNPSRVRYPMvrldwllKREKSDRSQRGDNRFVRVSWDQALDLFYEELERVQKtygssgvfTGLADWQMVGKYHKAGGAM 167
Cdd:cd02760 54 YNPNRVLQPM-------KRTNPKKGRNEDPGFVPISWDEALDLVAAKLRRVRE--------KGLLDEKGLPRLAATFGHG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 168 DRGLGLHGSYVTTVG-----DYSAAAAQVIlpHVIGSLEVYEQqtslplVIQNSNTIVlwGCDPIKNLQIEFLVPDHDAF 242
Cdd:cd02760 119 GTPAMYMGTFPAFLAawgpiDFSFGSGQGV--KCVHSEHLYGE------FWHRAFTVA--ADTPLANYVISFGSNVEASG 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 243 GYWQQIKEAVAQNK-MRVISVDPVRSKSqNYLGCEQLALRPQTDVALMLALAHTLYEEK---LYDTAFITD-----YTVG 313
Cdd:cd02760 189 GPCAVTRHADARVRgYKRVQVEPHLSVT-GACSAEWVPIRPKTDPAFMFAMIHVMVHEQglgKLDVPFLRDrtsspYLVG 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 314 ----------------------------FEQFLPY------LLGESDKQPKNA-------------------------EW 334
Cdd:cd02760 268 pdglylrdaatgkplvwdersgravpfdTRGAVPAvagdfaVDGAVSVDADDEtaihqgvegttaftmlvehmrkytpEW 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 335 AAEICGLTAEQIRDFAR-----------LLVKGRT------QFMGGWCVQRMHHGEQYPWMLVVLASMVGQIGLPGGGVg 397
Cdd:cd02760 348 AESICDVPAATIRRIAReflenasigstIEVDGVTlpyrpvAVTLGKSVNNGWGAFECCWARTLLATLVGALEVPGGTL- 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 398 fgwhyngGGTVTSTGPVLSGLGSItNPPQAKYKADFRGASEHI-----PTSRIVDCLLAP--GNK--------------- 455
Cdd:cd02760 427 -------GTTVRLNRPHDDRLASV-KPGEDGFMAQGFNPTDKEhwvvkPTGRNAHRTLVPivGNSawsqalgptqlawmf 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 456 -----IAFNGETLTYPDIkMAIYSaANPFHAQQDRNRMIDAWKKLETVVVLDHQWTASCRFADIVLPVTTRFERND---- 526
Cdd:cd02760 499 lrevpLDWKFELPTLPDV-WFNYR-TNPAISFWDTATLVDNIAKFPFTVSFAYTEDETNWMADVLLPEATDLESLQmikv 576
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1995542531 527 -----IEQFGTHsnKGLMALHQIVKPQYEARHDFDIFAGLCKR 564
Cdd:cd02760 577 ggtkfVEQFWEH--RGVVLRQPAVEPQGEARDFTWISTELAKR 617
|
|
| MopB_ydeP |
cd02767 |
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
92-389 |
3.04e-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: 60.40 E-value: 3.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 92 RVRYPMVRldwllkreksdrsQRGDNRFVRVSWDQALDLFYEELErvqktygssgvftGLADWQMV----GK-------- 159
Cdd:cd02767 64 RLTYPMRY-------------DAGSDHYRPISWDEAFAEIAARLR-------------ALDPDRAAfytsGRasneaayl 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 160 YHKAGgamdRGLGLHGsyVTTVGDYSAAAAQVILPHVIG------SLEVYEqqtslplviqNSNTIVLWGCDPIKNlQIE 233
Cdd:cd02767 118 YQLFA----RAYGTNN--LPDCSNMCHEPSSVGLKKSIGvgkgtvSLEDFE----------HTDLIFFIGQNPGTN-HPR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 234 FLVPDHDAfgywqqikeavAQNKMRVISVDPVR-----------SKSQNYLGCEQLA-----LRPQTDVALMLALAHTLY 297
Cdd:cd02767 181 MLHYLREA-----------KKRGGKIIVINPLRepglerfanpqNPESMLTGGTKIAdeyfqVRIGGDIALLNGMAKHLI 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 298 EEK-----LYDTAFITDYTVGFEQFLPYLlgesdkqpKNAEWaAEI---CGLTAEQIRDFARLLVKG-RTQFMGGWCVQR 368
Cdd:cd02767 250 ERDdepgnVLDHDFIAEHTSGFEEYVAAL--------RALSW-DEIeraSGLSREEIEAFAAMYAKSeRVVFVWGMGITQ 320
|
330 340
....*....|....*....|.
gi 1995542531 369 MHHGEQYPWMLVVLASMVGQI 389
Cdd:cd02767 321 HAHGVDNVRAIVNLALLRGNI 341
|
|
| MopB_CT_1 |
cd02782 |
The MopB_CT_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
690-807 |
1.24e-07 |
|
The MopB_CT_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239183 [Multi-domain] Cd Length: 129 Bit Score: 51.24 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 690 RLHSQLCSSEAFRSTYAVAGRE--PLYISEQDATTRGLKAGDIARVFNARGQVLAGVVISPDFTPGVVRIHEGawYSPQE 767
Cdd:cd02782 10 RRHLRSNNSWLHNDPRLVKGRNrcTLRIHPDDAAALGLADGDKVRVTSAAGSVEAEVEVTDDMMPGVVSLPHG--WGHDY 87
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1995542531 768 GGKAGTLCTYG-DPNVLSADIGTSQLAQGPSAHTVLVEVER 807
Cdd:cd02782 88 PGVSGAGSRPGvNVNDLTDDTQRDPLSGNAAHNGVPVRLAR 128
|
|
| MopB_CT_Nitrate-R-NapA-like |
cd02791 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
711-768 |
1.60e-07 |
|
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: 50.65 E-value: 1.60e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1995542531 711 EP-LYISEQDATTRGLKAGDIARVFNARGQVLAGVVISPDFTPGVV--RIHEGAWYSPQEG 768
Cdd:cd02791 34 EPyVEIHPEDAARLGLKEGDLVRVTSRRGEVVLRVRVTDRVRPGEVfvPMHWGDQFGRSGR 94
|
|
| MopB_CT_Fdh-Nap-like |
cd00508 |
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and ... |
676-781 |
2.14e-07 |
|
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: 50.20 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 676 DKYPLHLQSchpdKRLHSQLCSSEAFRSTYAVAGREP---LYISEQDATTRGLKAGDIARVFNARGQVLAGVVISPDFTP 752
Cdd:cd00508 1 EEYPLVLTT----GRLLEHWHTGTMTRRSPRLAALAPepfVEIHPEDAARLGIKDGDLVRVSSRRGSVVVRARVTDRVRP 76
|
90 100 110
....*....|....*....|....*....|..
gi 1995542531 753 GVVRI--HegaWYSPQEGGKAGTLCTY-GDPN 781
Cdd:cd00508 77 GTVFMpfH---WGGEVSGGAANALTNDaLDPV 105
|
|
| MopB_CT_Nitrate-R-NarG-like |
cd02776 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
709-760 |
1.26e-06 |
|
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under anaerobic conditions in the presence of nitrate, E. coli synthesizes the cytoplasmic membrane-bound quinol-nitrate oxidoreductase (NarGHI), which reduces nitrate to nitrite and forms part of a redox loop generating a proton-motive force. Found in prokaryotes and some archaea, NarGHI usually functions as a heterotrimer. The alpha chain contains the molybdenum cofactor-containing Mo-bisMGD catalytic subunit. This CD (MopB_CT_Nitrate-R-NarG-like) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239177 [Multi-domain] Cd Length: 141 Bit Score: 48.53 E-value: 1.26e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1995542531 709 GREPLYISEQDATTRGLKAGDIARVFNARGQVLAGVVISPDFTPGVVRIHEG 760
Cdd:cd02776 29 GGPVVWMNPKDAAELGIKDNDWVEVFNDNGVVVARAKVSPRIPRGTVFMYHA 80
|
|
| MopB_CT_Formate-Dh-Na-like |
cd02792 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
676-782 |
1.99e-05 |
|
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: 44.52 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 676 DKYPLHLQSchpdKRLHSQLCSSEAFRSTYAVAGREP---LYISEQDATTRGLKAGDIARVFNARGQVLAGVVISPDFTP 752
Cdd:cd02792 1 EEFPLVLTT----GRLTEHFHGGNMTRNSPYLAELQPemfVEISPELAAERGIKNGDMVWVSSPRGKIKVKALVTDRVKP 76
|
90 100 110
....*....|....*....|....*....|...
gi 1995542531 753 GVVRI--HEGAWySPQEGGKAGTLCTY-GDPNV 782
Cdd:cd02792 77 HEVGIpyHWGGM-GLVIGDSANTLTPYvGDPNT 108
|
|
| MopB_CT_Acetylene-hydratase |
cd02781 |
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related ... |
678-786 |
3.38e-05 |
|
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: 44.22 E-value: 3.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 678 YPLHLQSCHpdKRL---HSQLCSSEAFRStyavagREPLY---ISEQDATTRGLKAGDIARVFNARGQVLAGVVISPDFT 751
Cdd:cd02781 2 YPLILTTGA--RSYyyfHSEHRQLPSLRE------LHPDPvaeINPETAAKLGIADGDWVWVETPRGRARQKARLTPGIR 73
|
90 100 110
....*....|....*....|....*....|....*.
gi 1995542531 752 PGVVRIHEGAWYSPQEGGKAGTLCTYG-DPNVLSAD 786
Cdd:cd02781 74 PGVVRAEHGWWYPEREAGEPALGGVWEsNANALTSD 109
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
484-593 |
3.75e-05 |
|
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: 47.14 E-value: 3.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 484 DRNRMIDAWKKLETVVVLDHQWTASCRFADIVLPVTTRFERNdieqfGTHSN-KG-LMALHQIVKPQYEARHDFDIFAGL 561
Cdd:COG1034 347 DPAAALAALAKADFVVVLDHFGSATAERADVVLPAAAFAEKS-----GTFVNlEGrVQRFNAAVPPPGEARPDWRVLRAL 421
|
90 100 110
....*....|....*....|....*....|..
gi 1995542531 562 CKRFDKEAVYRENRNEMQWIQALYDEGVKMGA 593
Cdd:COG1034 422 ANALGAGLPYDSLEEVRAELAAEAPATVSAEG 453
|
|
| MopB_CT_Tetrathionate_Arsenate-R |
cd02780 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate ... |
678-773 |
1.05e-04 |
|
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: 43.05 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 678 YPLHLQSCHPdkRLHSQlcSSEAFRSTYAVAGREPLYISEQDATTRGLKAGDIARVFNARGQVLAGVVISPDFTPGVVRI 757
Cdd:cd02780 1 YPFILVTFKS--NLNSH--RSANAPWLKEIKPENPVWINPEDAAKLGIKTGDRVRVVTPGGSVVGKAKVTEGVRPGVVAI 76
|
90
....*....|....*...
gi 1995542531 758 --HEGAWyspQEGGKAGT 773
Cdd:cd02780 77 ehGYGHW---AYGAVAST 91
|
|
| MopB_NDH-1_NuoG2-N7 |
cd02771 |
MopB_NDH-1_NuoG2-N7: The second domain of the NuoG subunit (with a [4Fe-4S] cluster, N7) of ... |
471-571 |
5.91e-04 |
|
MopB_NDH-1_NuoG2-N7: The second domain of the NuoG subunit (with a [4Fe-4S] cluster, N7) of the NADH-quinone oxidoreductase/NADH dehydrogenase-1 (NDH-1) found in various bacteria. The NDH-1 is the first energy-transducting complex in the respiratory chain and functions as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. In Escherichia coli NDH-1, the largest subunit is encoded by the nuoG gene, and is part of the 14 distinct subunits constituting the functional enzyme. The NuoG subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Unique to this group, compared to the other prokaryotic and eukaryotic groups in this domain protein family (NADH-Q-OR-NuoG2), is an N-terminal [4Fe-4S] cluster (N7/N1c) present in the second domain. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain belongs to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239172 [Multi-domain] Cd Length: 472 Bit Score: 43.15 E-value: 5.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 471 AIYSAANPFHAQQDRNRMIDAWKKLETVVVLDHQWTASCRFADIVLPVTTRFERNdieqfGTHSNKGLMAlhQ-----IV 545
Cdd:cd02771 341 ALIVLGNDLYRSAPERRVEAALDAAEFVVVLDHFLTETAERADVVLPAASFAEKS-----GTFVNYEGRA--QrffkaYD 413
|
90 100
....*....|....*....|....*.
gi 1995542531 546 KPQYEARHDFDIFAGLCKRFDKEAVY 571
Cdd:cd02771 414 DPAGDARSDWRWLHALAAKLGGKLVP 439
|
|
| MopB_CT_Arsenite-Ox |
cd02779 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of Arsenite oxidase ... |
707-780 |
1.20e-03 |
|
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: 39.36 E-value: 1.20e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1995542531 707 VAGREPL-YI--SEQDATTRGLKAGDIARVFNARGQVLAGVVISPDFTPGVVRIHEGAWyspqEGGKAGTLCTYGDP 780
Cdd:cd02779 26 IAERVPLpYIevNPEDAKREGLKNGDLVEVYNDYGSTTAMAYVTNTVKPGQTFMLMAHP----RPGANGLVTPYVDP 98
|
|
| PRK14991 |
PRK14991 |
tetrathionate reductase subunit TtrA; |
659-760 |
7.15e-03 |
|
tetrathionate reductase subunit TtrA;
Pssm-ID: 237883 [Multi-domain] Cd Length: 1031 Bit Score: 39.98 E-value: 7.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995542531 659 GHPVWMEP-FE-----RTHSGKKDkYPLHLQSchpdkrLHSQLCSSEAFRST--YAVAGREPLYISEQDATTRGLKAGDI 730
Cdd:PRK14991 863 GCPTWYPPrLAdgtplREQFPESQ-WPLLLIS------FKSNLMSSMSIASPrlRQVKPANPVALNPQDAARLGIQHGDR 935
|
90 100 110
....*....|....*....|....*....|
gi 1995542531 731 ARVFNARGQVLAGVVISPDFTPGVVRIHEG 760
Cdd:PRK14991 936 VRISTPGGSVVAQASVLNGVMPGVIAIEHG 965
|
|
| TAT_signal |
pfam10518 |
TAT (twin-arginine translocation) pathway signal sequence; |
7-27 |
8.31e-03 |
|
TAT (twin-arginine translocation) pathway signal sequence;
Pssm-ID: 463131 [Multi-domain] Cd Length: 26 Bit Score: 34.66 E-value: 8.31e-03
|
| |
