|
Name |
Accession |
Description |
Interval |
E-value |
| Fdhalpha-like |
TIGR01701 |
oxidoreductase alpha (molybdopterin) subunit; This model represents a well-defined clade of ... |
16-766 |
0e+00 |
|
oxidoreductase alpha (molybdopterin) subunit; This model represents a well-defined clade of oxidoreductase alpha subunits most closely related to a group of formate dehydrogenases including the E. coli FdhH protein (TIGR01591). These alpha subunits contain a molybdopterin cofactor and generally associate with two other subunits which contain iron-sulfur clusters and cytochromes. The particular subunits with which this enzyme interacts and the substrate which is reduced is unknown at this time. In Ralstonia, the gene is associated with the cbb operon, but is not essential for CO2 fixation.
Pssm-ID: 273765 [Multi-domain] Cd Length: 743 Bit Score: 942.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 16 PAGGWGALKYVAINLFKEKVPGGNYRALLRQNQPDGFDCPGCAWPDR-EHASTFEFCENGVKAVAAEATAKRVTPAFFAE 94
Cdd:TIGR01701 1 DAGGWGAVKSVALGKVKPMHIRQTLKLLLTLNKPEGYDCPGCAWGVSpQTLAGLEFCENGAKAIAWETTPRTIDPEFFAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 95 HTVSALFDQSDYALEQHGRLTDPMVYDAATDRYVPIAWNAAFELIANHLRALgEPNRAAFYTSGRASNEAAFLYQLLVRY 174
Cdd:TIGR01701 81 HSVSELRTLDSHELEKLGRLTYPLSLRPGSDHYTPISWDDAYQEIAAKLNSL-DPKQVAFYTSGRTSNEAAYLYQLFARS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 175 YGTNNFPDCSNMCHEATSRGLPATVGVGKGTVTLDDFEQADTLLIFGQNPATNHPRMMGELRACAKRGATIVSINPLKER 254
Cdd:TIGR01701 160 LGSNNLPDCSNMCHEPSSVALKRSIGIGKGSVNLEDFEHTDCLVFIGSNAGTNHPRMLKYLYAAKKRGAKIIAINPLRER 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 255 GLERFASPQHPAEMLTMSSTPIASTFVQPRVGGDLALIKGVAKRVLELDDAARerggARVLDVDFIAAHTAGFDTFAADL 334
Cdd:TIGR01701 240 GLERFWIPQIPESMLTGGGTQISSEYYQVRIGGDIALFNGVMKLLIEAEDAQP----GSLIDHEFIANHTNGFDELRRHV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 335 RAQDWAALVGESGVPREQIDALARIYVRGERVIATWGMGLTQHKHSVATVHMLSNLMLMRGNIGRPGAGLCPVRGHSNVQ 414
Cdd:TIGR01701 316 LQLNWNDIERSSGLSQEEILEFAKLLANSRRVVFCWAMGLTQHAHGVDNISQVANLALLRGNIGKPGAGVCPIRGHSNVQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 415 GNRTVGIEEKPSDAFLERLGRVFDFAPPRGHGYDVVETIEAMLDGRIGVFIGLGGNFAMATPDTPRTWQGLRRCGLTVHI 494
Cdd:TIGR01701 396 GDRTMGITEKPEEEFLARLSQIYGFTPPDWPGDTTVAMIEAILTGKVRAFICLGGNFLEAMPDTAAIERALRQLDLRVHV 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 495 TTKLNRSHLVHGREALILPTLGRTEIDLQNGVAQGVSVEDSMCMVHASYGMNPPASPNLLSEVAIVARLGHALFGGDKID 574
Cdd:TIGR01701 476 ATKLNRSHVLAKEEALILPVLGRYEQDGQGTGKQAVSVESSMRMVHFSRGILKPRGAELRSEWAIIAEIAKALLPETPVA 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 575 WLGYMNDYAKIRDAIEASIEGFDDYNARIARPGGFHLRVASR-EREWLTPSGRANFIVHALPADTPIQRARARhgkrlMT 653
Cdd:TIGR01701 556 WEILVDTYDQIRDAIAATNPGYDDINHRKRRPDGFQLPGAALcERKFPTPDGKANFIVIPLPEFRVPTGHEFE-----LV 630
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 654 LMTTRSHDQYNTTIYALDDRYRGVFGERRVVFAHPDDLAMLGFEAGERVDLETVWDDGIERRVAGFLLVAYDIPRGCLGA 733
Cdd:TIGR01701 631 LVTLRSHDQFNTTIYGEDDRYRGVDGHRRVVFMNETDIKKLGLRNGERVDVYNQYGDGQKRKFDNLRIVFYDTPTGNAAA 710
|
730 740 750
....*....|....*....|....*....|...
gi 490663230 734 YYPETNPLVPLDSVGDVCNTPTSKSIPVLMHRS 766
Cdd:TIGR01701 711 YYPEANPLLPLDHHDPQSKTPEYKTIPVRLEAS 743
|
|
| MopB_ydeP |
cd02767 |
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
51-629 |
0e+00 |
|
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: 933.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 51 GFDCPGCAWPDREHA-STFEFCENGVKAVAAEATAKRVTPAFFAEHTVSALFDQSDYALEQHGRLTDPMVYDAATDRYVP 129
Cdd:cd02767 1 GFDCPGCAWGDPGQKlHGFEFCENGAKALAWETTPKRVTPEFFALHSVSELRTWSDYELEHLGRLTYPMRYDAGSDHYRP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 130 IAWNAAFELIANHLRALgEPNRAAFYTSGRASNEAAFLYQLLVRYYGTNNFPDCSNMCHEATSRGLPATVGVGKGTVTLD 209
Cdd:cd02767 81 ISWDEAFAEIAARLRAL-DPDRAAFYTSGRASNEAAYLYQLFARAYGTNNLPDCSNMCHEPSSVGLKKSIGVGKGTVSLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 210 DFEQADTLLIFGQNPATNHPRMMGELRACAKRGATIVSINPLKERGLERFASPQHPAEMLTmSSTPIASTFVQPRVGGDL 289
Cdd:cd02767 160 DFEHTDLIFFIGQNPGTNHPRMLHYLREAKKRGGKIIVINPLREPGLERFANPQNPESMLT-GGTKIADEYFQVRIGGDI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 290 ALIKGVAKRVLELDDAarergGARVLDVDFIAAHTAGFDTFAADLRAQDWAALVGESGVPREQIDALARIYVRGERVIAT 369
Cdd:cd02767 239 ALLNGMAKHLIERDDE-----PGNVLDHDFIAEHTSGFEEYVAALRALSWDEIERASGLSREEIEAFAAMYAKSERVVFV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 370 WGMGLTQHKHSVATVHMLSNLMLMRGNIGRPGAGLCPVRGHSNVQGNRTVGIEEKPSDAFLERLGRVFDFAPPRGHGYDV 449
Cdd:cd02767 314 WGMGITQHAHGVDNVRAIVNLALLRGNIGRPGAGLMPIRGHSNVQGDRTMGITEKPFPEFLDALEEVFGFTPPRDPGLDT 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 450 VETIEAMLDGRIGVFIGLGGNFAMATPDTPRTWQGLRRCGLTVHITTKLNRSHLVHGREALILPTLGRTEIDLQNGVAQG 529
Cdd:cd02767 394 VEAIEAALEGKVKAFISLGGNFAEAMPDPAATEEALRRLDLTVHVATKLNRSHLVHGEEALILPCLGRTEIDMQAGGAQA 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 530 VSVEDSMCMVHASYGMNPPASPNLLSEVAIVARLGHALFGGDKIDWLGYMNDYAKIRDAIEASI-EGFDDYNARIARPGG 608
Cdd:cd02767 474 VTVEDSMSMTHTSRGRLKPASRVLLSEEAIVAGIAGARLGEAKPEWEILVEDYDRIRDEIAAVIyEGFADFNQRGDQPGG 553
|
570 580
....*....|....*....|.
gi 490663230 609 FHLRVASREREWLTPSGRANF 629
Cdd:cd02767 554 FHLPNGARERKFNTPSGKAQF 574
|
|
| PRK09939 |
PRK09939 |
acid resistance putative oxidoreductase YdeP; |
9-766 |
0e+00 |
|
acid resistance putative oxidoreductase YdeP;
Pssm-ID: 182156 [Multi-domain] Cd Length: 759 Bit Score: 829.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 9 RIEPYAHPAGGWGALKYVAINLFKEKVPGGNYRALLRQNQPDGFDCPGCAWPDREHASTFEFCENGVKAVAAEATAKRVT 88
Cdd:PRK09939 4 KIESYQGAAGGWGAVKSVANAVRKQMDIRQDVIAMFDMNKPEGFDCPGCAWPDPKHSASFDICENGAKAIAWEVTDKQVN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 89 PAFFAEHTVSALFDQSDYALEQHGRLTDPMVYDAATDRYVPIAWNAAFELIANHLRALGEPNRAAFYTSGRASNEAAFLY 168
Cdd:PRK09939 84 ASFFAENTVQSLLTWGDHELEAAGRLTQPLKYDAVSDCYKPLSWQQAFDEIGARLQSYSDPNQVEFYTSGRTSNEAAFLY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 169 QLLVRYYGTNNFPDCSNMCHEATSRGLPATVGVGKGTVTLDDFEQADTLLIFGQNPATNHPRMMGELRACAKRGATIVSI 248
Cdd:PRK09939 164 QLFAREYGSNNFPDCSNMCHEPTSVGLAASIGVGKGTVLLEDFEKCDLVICIGHNPGTNHPRMLTSLRALVKRGAKMIAI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 249 NPLKERGLERFASPQHPAEMLTMSSTPIASTFVQPRVGGDLALIKGVAKRVLELDDAARERGGARVLDVDFIAAHTAGFD 328
Cdd:PRK09939 244 NPLQERGLERFTAPQNPFEMLTNSETQLASAYYNVRIGGDMALLKGMMRLLIERDDAASAAGRPSLLDDEFIQTHTVGFD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 329 TFAADLRAQDWAALVGESGVPREQIDALARIYVRGERVIATWGMGLTQHKHSVATVHMLSNLMLMRGNIGRPGAGLCPVR 408
Cdd:PRK09939 324 ELRRDVLNSEWKDIERISGLSQTQIAELADAYAAAERTIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGICPLR 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 409 GHSNVQGNRTVGIEEKPSDAFLERLGRVFDFAPPRGHGYDVVETIEAMLDGRIGVFIGLGGNFAMATPDTPRTWQGLRRC 488
Cdd:PRK09939 404 GHSNVQGDRTVGITEKPSAEFLARLGERYGFTPPHAPGHAAIASMQAICTGQARALICMGGNFALAMPDREASAVPLTQL 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 489 GLTVHITTKLNRSHLVHGREALILPTLGRTEIDLQNGVAQGVSVEDSMCMVHASYGMNPPASPNLLSEVAIVARLGHALF 568
Cdd:PRK09939 484 DLAVHVATKLNRSHLLTARHSYILPVLGRSEIDMQKSGAQAVTVEDSMSMIHASRGVLKPAGVMLKSECAVVAGIAQAAL 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 569 GGDKIDWLGYMNDYAKIRDAIEASIEGFDDYNARIARPGGFHLRVASREREWLTPSGRANFIVHALPADTPIQRARARhg 648
Cdd:PRK09939 564 PQSVVAWEYLVEDYDRIRNDIEAVLPEFADYNQRIRHPGGFHLINAAAERRWMTPSGKANFITSKGLLEDPSSAFNSK-- 641
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 649 krlMTLMTTRSHDQYNTTIYALDDRYRGVFGERRVVFAHPDDLAMLGFEAGERVDLETVWDDGIE--RRVAGFLLVAYDI 726
Cdd:PRK09939 642 ---LVMATVRSHDQYNTTIYGMDDRYRGVFGQRDVVFMSAKQAKICRVKNGERVNLIALTPDGKRssRRMDRLKVVIYPM 718
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 490663230 727 PRGCLGAYYPETNPLVPLDSVGDVCNTPTSKSIPVLMHRS 766
Cdd:PRK09939 719 ADRSLVTYFPESNHMLTLDNHDPLSGIPGYKSIPVELEPS 758
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
54-761 |
1.39e-170 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 506.69 E-value: 1.39e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 54 CPGCAwpdrehastfEFCENGVKAvaAEATAKRVTPAffAEHTVSALFD-----QSDYALEQHGRLTDPMVYD--AATDR 126
Cdd:COG0243 28 CPGCG----------VGCGLGVKV--EDGRVVRVRGD--PDHPVNRGRLcakgaALDERLYSPDRLTYPMKRVgpRGSGK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 127 YVPIAWNAAFELIANHLRALGE---PNRAAFYTSG----RASNEAAFLYQLLVRYYGTNNFPDCSNMCHEATSRGLPATV 199
Cdd:COG0243 94 FERISWDEALDLIAEKLKAIIDeygPEAVAFYTSGgsagRLSNEAAYLAQRFARALGTNNLDDNSRLCHESAVAGLPRTF 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 200 GVGKGTVTLDDFEQADTLLIFGQNPATNHPRMMGELR-ACAKRGATIVSINPLKERglerfaspqhpaemltmsSTPIAS 278
Cdd:COG0243 174 GSDKGTVSYEDLEHADLIVLWGSNPAENHPRLLRRLReAAKKRGAKIVVIDPRRTE------------------TAAIAD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 279 TFVQPRVGGDLALIKGVAKRVLELDdaarerggarVLDVDFIAAHTAGFDTFAADLRAQDWAALVGESGVPREQIDALAR 358
Cdd:COG0243 236 EWLPIRPGTDAALLLALAHVLIEEG----------LYDRDFLARHTVGFDELAAYVAAYTPEWAAEITGVPAEDIRELAR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 359 IYVRGERVIATWGMGLTQHKHSVATVHMLSNLMLMRGNIGRPGAGLCPVRGhsnvqgnrtvgieekpsdaflerlgrvfd 438
Cdd:COG0243 306 EFATAKPAVILWGMGLQQHSNGTQTVRAIANLALLTGNIGKPGGGPFSLTG----------------------------- 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 439 fapprghgydvvetiEAMLDG---RIGVFIGLGGNFAMATPDTPRTWQGLRRCGLTVHITTKLNRSHLVhgrEALILPTL 515
Cdd:COG0243 357 ---------------EAILDGkpyPIKALWVYGGNPAVSAPDTNRVREALRKLDFVVVIDTFLTETARY---ADIVLPAT 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 516 GRTEidlQNGVAqgVSVEDSmcMVHASYGMNPPASpNLLSEVAIVARLGHALFGGDKIDWLGYMNDYakIRDAIEASIEG 595
Cdd:COG0243 419 TWLE---RDDIV--TNSEDR--RVHLSRPAVEPPG-EARSDWEIFAELAKRLGFEEAFPWGRTEEDY--LRELLEATRGR 488
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 596 ---FDDYNARiarpGGFHLRVAS-----REREWLTPSGRANFIVHALPAD------TPIQRARARHGKRLMTLMTTRSHD 661
Cdd:COG0243 489 gitFEELREK----GPVQLPVPPepafrNDGPFPTPSGKAEFYSETLALPplpryaPPYEGAEPLDAEYPLRLITGRSRD 564
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 662 QYNTTIYALdDRYRGVFGeRRVVFAHPDDLAMLGFEAGERVDLETVWDdgierRVAGFLLVAYDIPRGCLGAYY------ 735
Cdd:COG0243 565 QWHSTTYNN-PRLREIGP-RPVVEINPEDAAALGIKDGDLVRVESDRG-----EVLARAKVTEGIRPGVVFAPHgwwyep 637
|
730 740 750
....*....|....*....|....*....|.
gi 490663230 736 -----PETNPLVPlDSVGDVCNTPTSKSIPV 761
Cdd:COG0243 638 addkgGNVNVLTP-DATDPLSGTPAFKSVPV 667
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
60-761 |
4.52e-92 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 302.57 E-value: 4.52e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 60 PDREHASTFEFCENG--VKAVAAEATAKRVTPAffAEHTVS---------ALFDQsdyaLEQHGRLTDPMVYDaaTDRYV 128
Cdd:COG3383 3 PMKKVKTVCPYCGVGcgIDLEVKDGKIVKVEGD--PDHPVNrgrlcvkgrFGFEF----VNSPDRLTTPLIRR--GGEFR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 129 PIAWNAAFELIANHLRALGE---PNRAAFYTSGRASNEAAFLYQLLVR-YYGTNNFPDCSNMCHEATSRGLPATVGVGKG 204
Cdd:COG3383 75 EVSWDEALDLVAERLREIQAehgPDAVAFYGSGQLTNEENYLLQKLARgVLGTNNIDNNARLCMASAVAGLKQSFGSDAP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 205 TVTLDDFEQADTLLIFGQNPATNHPRMMGELRACAKRGATIVSINPlKERGLERFASpqhpaemltmsstpiasTFVQPR 284
Cdd:COG3383 155 PNSYDDIEEADVILVIGSNPAEAHPVLARRIKKAKKNGAKLIVVDP-RRTETARLAD-----------------LHLQIK 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 285 VGGDLALIKGVAKRVLELDDAarerggarvlDVDFIAAHTAGFDTFAADLRAQDWAALVGESGVPREQIDALARIYVRGE 364
Cdd:COG3383 217 PGTDLALLNGLLHVIIEEGLV----------DEDFIAERTEGFEELKASVAKYTPERVAEITGVPAEDIREAARLIAEAK 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 365 RVIATWGMGLTQHKHSVATVHMLSNLMLMRGNIGRPGAGLCPVRGHSNVQGNRTVGIeeKP----------SDAFLERLG 434
Cdd:COG3383 287 RAMILWGMGVNQHTQGTDNVNAIINLALATGNIGRPGTGPFPLTGQNNVQGGRDMGA--LPnvlpgyrdvtDPEHRAKVA 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 435 RVFDFAP-PRGHGYDVVETIEAMLDGRIGVFIGLGGNFAMATPDTPRTWQGLRRCGLTVHI------TTKLnrSHLVhgr 507
Cdd:COG3383 365 DAWGVPPlPDKPGLTAVEMFDAIADGEIKALWIIGENPAVSDPDANHVREALEKLEFLVVQdiflteTAEY--ADVV--- 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 508 ealiLPTLGRTEIDlqnGVAqgVSVEDSMCMVHASygMNPPasPNLLSEVAIVARLGHALfgGDKIDWlgymNDYAKIRD 587
Cdd:COG3383 440 ----LPAASWAEKD---GTF--TNTERRVQRVRKA--VEPP--GEARPDWEIIAELARRL--GYGFDY----DSPEEVFD 500
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 588 AIEASIEGFD--DYnARIARPGGFHLRVASRERE---------WLTPSGRANFIV--HALPADTPIQRARarhgkrlMTL 654
Cdd:COG3383 501 EIARLTPDYSgiSY-ERLEALGGVQWPCPSEDHPgtprlftgrFPTPDGKARFVPveYRPPAELPDEEYP-------LVL 572
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 655 MTTRSHDQYNTT-----IYALDDRYRGVFgerrvVFAHPDDLAMLGFEAGERVDLETvwddgieRR--VAGFLLVAYDIP 727
Cdd:COG3383 573 TTGRLLDQWHTGtrtrrSPRLNKHAPEPF-----VEIHPEDAARLGIKDGDLVRVSS-------RRgeVVLRARVTDRVR 640
|
730 740 750
....*....|....*....|....*....|....*...
gi 490663230 728 RGCLGAYY----PETNPLVPlDSVGDVCNTPTSKSIPV 761
Cdd:COG3383 641 PGTVFMPFhwgeGAANALTN-DALDPVSKQPEYKACAV 677
|
|
| Fdh-alpha |
TIGR01591 |
formate dehydrogenase, alpha subunit, archaeal-type; This model describes a subset of formate ... |
113-761 |
2.18e-70 |
|
formate dehydrogenase, alpha subunit, archaeal-type; This model describes a subset of formate dehydrogenase alpha chains found mainly archaea but also in alpha and gamma proteobacteria and a small number of gram positive bacteria. The alpha chain contains domains for molybdopterin dinucleotide binding and molybdopterin oxidoreductase (pfam01568 and pfam00384, respectively). The holo-enzyme also contains beta and gamma subunits. The enzyme catalyzes the oxidation of formate (produced from pyruvate during anaerobic growth) to carbon dioxide with the concomitant release of two electrons and two protons. The enzyme's purpose is to allow growth on formate in some circumstances and, in the case of FdhH in gamma proteobacteria, to pass electrons to hydrogenase (by which process acid is neutralized). This model is well-defined, with only a single fragmentary sequence falling between trusted and noise. The alpha subunit of a version of nitrate reductase is closely related.
Pssm-ID: 130652 [Multi-domain] Cd Length: 671 Bit Score: 243.91 E-value: 2.18e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 113 RLTDPMVYDAatDRYVPIAWNAAFELIANHLRALGE---PNRAAFYTSGRASNEAAFLYQLLVR-YYGTNNFPDCSNMCH 188
Cdd:TIGR01591 53 RLTTPLIREG--DKFREVSWDEAISYIAEKLKEIKEkygPDSIGFIGSSRGTNEENYLLQKLARaVIGTNNVDNCARVCH 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 189 EATSRGLPATVGVGKGTVTLDDFEQADTLLIFGQNPATNHPRMMGELRACAKRGATIVSINPLKERGLErfaspqhpaem 268
Cdd:TIGR01591 131 GPSVAGLKQTVGIGAMSNTISEIENADLIVIIGYNPAESHPVVAQYLKNAKRNGAKIIVIDPRKTETAK----------- 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 269 ltmsstpIASTFVQPRVGGDLALIKGVAKRVLElddaarerggARVLDVDFIAAHTAGFDTFAADLRAQDWAALVGESGV 348
Cdd:TIGR01591 200 -------IADLHIPLKPGTDIALLNAMANVIIE----------EGLYDKAFIEKRTEGFEEFREIVKGYTPEYVEDITGV 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 349 PREQIDALARIYVRGERVIATWGMGLTQHKHSVATVHMLSNLMLMRGNIGRPGAGLCPVRGHSNVQGNRTVGI--EEKP- 425
Cdd:TIGR01591 263 PADLIREAARMYAKAGSAAILWGMGVTQHSQGVETVMALINLAMLTGNIGKPGGGVNPLRGQNNVQGACDMGAlpDFLPg 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 426 -----SDAFLERLGRVFDFAP-PRGHGYDVVETIEAMLDGRIGVFIGLGGNFAMATPDTPRTWQGLRRCGLTV----HIT 495
Cdd:TIGR01591 343 yqpvsDEEVREKFAKAWGVVKlPAEPGLRIPEMIDAAADGDVKALYIMGEDPLQSDPNTSKVRKALEKLELLVvqdiFMT 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 496 TKLNRSHLVhgrealiLPTLGRTEidlQNGVAqgVSVEDSMCMVHASygMNPPAspNLLSEVAIVARLGHALfggdKIDW 575
Cdd:TIGR01591 423 ETAKYADVV-------LPAAAWLE---KEGTF--TNAERRIQRFFKA--VEPKG--ESKPDWEIIQELANAL----GLDW 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 576 lgYMNDYAKIRDAIE--------ASIEGFDDYNA--RIARPGGFHLRVASREREWLTPSGRANFIvhALPADTPIQRARA 645
Cdd:TIGR01591 483 --NYNHPQEIMDEIReltplfagLTYERLDELGSlqWPCNDSDASPTSYLYKDKFATPDGKAKFI--PLEWVAPIEEPDD 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 646 RHGkrlMTLMTTRSHDQYNTTiyALDDRYRGV--FGERRVVFAHPDDLAMLGFEAGERVDL-----ETVWDDGIERRVAG 718
Cdd:TIGR01591 559 EYP---LILTTGRVLTHYNVG--EMTRRVAGLrrLSPEPYVEINTEDAKKLGIKDGDLVKVksrrgEITLRAKVSDRVNK 633
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 490663230 719 FLLVAYdiprgcLGAYYPETNPLVPLDSvGDVCNTPTSKSIPV 761
Cdd:TIGR01591 634 GAIYIT------MHFWDGAVNNLTTDDL-DPISGTPEYKYTAV 669
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
113-415 |
4.12e-66 |
|
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: 228.25 E-value: 4.12e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 113 RLTDPMVydAATDRYVPIAWNAAFELIANHLRALGE---PNRAAFYTSGRASNEAAFLYQLLVR-YYGTNNFPDCSNMCH 188
Cdd:cd02753 54 RLTKPLI--RKNGKFVEASWDEALSLVASRLKEIKDkygPDAIAFFGSAKCTNEENYLFQKLARaVGGTNNVDHCARLCH 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 189 EATSRGLPATVGVGKGTVTLDDFEQADTLLIFGQNPATNHPRMMGELRACAKRGATIVSINPlKERGLERFASpqhpaem 268
Cdd:cd02753 132 SPTVAGLAETLGSGAMTNSIADIEEADVILVIGSNTTEAHPVIARRIKRAKRNGAKLIVADP-RRTELARFAD------- 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 269 ltmsstpiasTFVQPRVGGDLALIKGVAKRVLElddaarerggARVLDVDFIAAHTAGFDTFAADLRA--QDWAALVgeS 346
Cdd:cd02753 204 ----------LHLQLRPGTDVALLNAMAHVIIE----------EGLYDEEFIEERTEGFEELKEIVEKytPEYAERI--T 261
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490663230 347 GVPREQIDALARIYVRGERVIATWGMGLTQHKHSVATVHMLSNLMLMRGNIGRPGAGLCPVRGHSNVQG 415
Cdd:cd02753 262 GVPAEDIREAARMYATAKSAAILWGMGVTQHSHGTDNVMALSNLALLTGNIGRPGTGVNPLRGQNNVQG 330
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
112-567 |
3.98e-64 |
|
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: 218.74 E-value: 3.98e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 112 GRLTDPMVYDAATDRYVPIAWNAAFELIANHLRALGE---PNRAAFYTSGRASNEAAFLYQLLVRYYGTNNFPDCSNMCH 188
Cdd:cd00368 53 DRLKYPLIRVGGRGKFVPISWDEALDEIAEKLKEIREkygPDAIAFYGGGGASNEEAYLLQKLLRALGSNNVDSHARLCH 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 189 EATSRGLPAtVGVGKGTVTLDDFEQADTLLIFGQNPATNHPRMMGELRACAKRGATIVSINPLKERglerfaspqhpaem 268
Cdd:cd00368 133 ASAVAALKA-FGGGAPTNTLADIENADLILLWGSNPAETHPVLAARLRRAKKRGAKLIVIDPRRTE-------------- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 269 ltmsSTPIASTFVQPRVGGDLALIKGvakrvlelddaarerggarvldvdfiaahtagfdtfaadlraqDWAALVgeSGV 348
Cdd:cd00368 198 ----TAAKADEWLPIRPGTDAALALA-------------------------------------------EWAAEI--TGV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 349 PREQIDALARIYVRGERVIATWGMGLTQHKHSVATVHMLSNLMLMRGNIGRPGAGLCPvrghsnvqgnrtvgieekpsda 428
Cdd:cd00368 229 PAETIRALAREFAAAKRAVILWGMGLTQHTNGTQNVRAIANLAALTGNIGRPGGGLGP---------------------- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 429 flerlgrvfdfapprghgydvvetieamldgrigvfiglGGNFAMATPDTPRTWQGLRRCGLTVHITTKLNRSHLVhgrE 508
Cdd:cd00368 287 ---------------------------------------GGNPLVSAPDANRVRAALKKLDFVVVIDIFMTETAAY---A 324
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490663230 509 ALILPTLGRTEidlqngvaqgvsVEDSMCMVHASYG-MNPPASP--NLLSEVAIVARLGHAL 567
Cdd:cd00368 325 DVVLPAATYLE------------KEGTYTNTEGRVQlFRQAVEPpgEARSDWEILRELAKRL 374
|
|
| MopB_CT_ydeP |
cd02787 |
The MopB_CT_ydeP CD includes a group of related uncharacterized bacterial ... |
652-761 |
3.88e-60 |
|
The MopB_CT_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative molybdopterin cofactor binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239188 [Multi-domain] Cd Length: 112 Bit Score: 198.27 E-value: 3.88e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 652 MTLMTTRSHDQYNTTIYALDDRYRGVFGERRVVFAHPDDLAMLGFEAGERVDLETVWDDGIERRVAGFLLVAYDIPRGCL 731
Cdd:cd02787 1 LFLVTTRSHDQFNTTIYGLDDRYRGVFGRRDVVFMNPDDIARLGLKAGDRVDLESAFGDGQGRIVRGFRVVEYDIPRGCL 80
|
90 100 110
....*....|....*....|....*....|
gi 490663230 732 GAYYPETNPLVPLDSVGDVCNTPTSKSIPV 761
Cdd:cd02787 81 AAYYPEGNVLVPLDHRDPQSKTPAYKSVPV 110
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
112-636 |
5.82e-57 |
|
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: 204.38 E-value: 5.82e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 112 GRLTDPMVyDAATDRYVPIAWNAAFELIANHLRALGE---PNRAAFYTSGRASNEAAFLYQLLVR-YYGTNNFPDCSNMC 187
Cdd:cd02754 53 ERLTRPLL-RRNGGELVPVSWDEALDLIAERFKAIQAeygPDSVAFYGSGQLLTEEYYAANKLAKgGLGTNNIDTNSRLC 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 188 HEATSRGLPATVGVGKGTVTLDDFEQADTLLIFGQNPATNHPRMMGEL--RACAKRGATIVSINPLKERglerfaspqhp 265
Cdd:cd02754 132 MASAVAGYKRSFGADGPPGSYDDIEHADCFFLIGSNMAECHPILFRRLldRKKANPGAKIIVVDPRRTR----------- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 266 aemltmsSTPIASTFVQPRVGGDLALIKGVAKRVLElddaareRGGArvlDVDFIAAHTAGFDTFAADLRAQDWAALVGE 345
Cdd:cd02754 201 -------TADIADLHLPIRPGTDLALLNGLLHVLIE-------EGLI---DRDFIDAHTEGFEELKAFVADYTPEKVAEI 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 346 SGVPREQIDALARIYVRGERVIATWGMGLTQHKHSVATVHMLSNLMLMRGNIGRPGAGLCPVRGHSNVQGNRTVG----- 420
Cdd:cd02754 264 TGVPEADIREAARLFGEARKVMSLWTMGVNQSTQGTAANNAIINLHLATGKIGRPGSGPFSLTGQPNAMGGREVGglanl 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 421 ------IEEKPSDAFLERLGRVFDFAPPRGHGYDVVETIEAMLDGRIGVFIGLGGNFAMATPDTPRTWQGLRRCGLTV-- 492
Cdd:cd02754 344 lpghrsVNNPEHRAEVAKFWGVPEGTIPPKPGLHAVEMFEAIEDGEIKALWVMCTNPAVSLPNANRVREALERLEFVVvq 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 493 ---HITtklnrshlVHGREA-LILPTLGRTEidlQNGVAqgVSVEDSMCMVHASygMNPPasPNLLSEVAIVARLGHALF 568
Cdd:cd02754 424 dafADT--------ETAEYAdLVLPAASWGE---KEGTM--TNSERRVSLLRAA--VEPP--GEARPDWWILADVARRLG 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 569 GGDKIDWLG---YMNDYAKIRDAIEASIEGFdDYnARIaRPGGFHLRVASRERE----------WLTPSGRANFI-VHAL 634
Cdd:cd02754 487 FGELFPYTSpeeVFEEYRRLSRGRGADLSGL-SY-ERL-RDGGVQWPCPDGPPEgtrrlfedgrFPTPDGRARFVaVPYR 563
|
..
gi 490663230 635 PA 636
Cdd:cd02754 564 PP 565
|
|
| MopB_Formate-Dh-Na-like |
cd02752 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
107-415 |
1.63e-31 |
|
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: 130.98 E-value: 1.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 107 ALEQHG----RLTDPMVYDAATDRYVPIAWNAAFELIANHLRALGE---------------PNRAAFYTSGRASNEAAFL 167
Cdd:cd02752 44 ALRDFVhspkRLKYPMYRAPGSGKWEEISWDEALDEIARKMKDIRDasfveknaagvvvnrPDSIAFLGSAKLSNEECYL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 168 YQLLVRYYGTNNFPDCSNMCHEATSRGLPATVGVGKGTVTLDDFEQADTLLIFGQNPATNHP-RMMGELRACAKRGATIV 246
Cdd:cd02752 124 IRKFARALGTNNLDHQARIUHSPTVAGLANTFGRGAMTNSWNDIKNADVILVMGGNPAEAHPvSFKWILEAKEKNGAKLI 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 247 SINPlkergleRFaspqhpaemlTMSSTpIASTFVQPRVGGDLALIKGVAKRVLElddaarerggarvLDVDFIAAHTag 326
Cdd:cd02752 204 VVDP-------RF----------TRTAA-KADLYVPIRSGTDIAFLGGMINYIIR-------------YTPEEVEDIC-- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 327 fdtfaadlraqdwaalvgesGVPREQI----DALARIYVRGERVIATWGMGLTQHKHSVATVHMLSNLMLMRGNIGRPGA 402
Cdd:cd02752 251 --------------------GVPKEDFlkvaEMFAATGRPDKPGTILYAMGWTQHTVGSQNIRAMCILQLLLGNIGVAGG 310
|
330
....*....|...
gi 490663230 403 GLCPVRGHSNVQG 415
Cdd:cd02752 311 GVNALRGHSNVQG 323
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
113-567 |
1.95e-26 |
|
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: 114.42 E-value: 1.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 113 RLTDPMVYDAatDRYVPIAWNAAFELIANHLRALGE---PNRAAFYTSGRASNEAAFLYQL--LVRYYGTNNFPDCS--- 184
Cdd:cd02762 54 RLRTPMRRRG--GSFEEIDWDEAFDEIAERLRAIRArhgGDAVGVYGGNPQAHTHAGGAYSpaLLKALGTSNYFSAAtad 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 185 NMCHEATSRGLPATVGvgkgTVTLDDFEQADTLLIFGQNPATNHPRMM------GELRACAKRGATIVSINPLKERGLER 258
Cdd:cd02762 132 QKPGHFWSGLMFGHPG----LHPVPDIDRTDYLLILGANPLQSNGSLRtapdrvLRLKAAKDRGGSLVVIDPRRTETAKL 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 259 faSPQHpaemltmsstpiasTFVQPrvGGDLALIKGVAKRVLElddaarerggARVLDVDFIAAHTAGFDTFAADLRAQD 338
Cdd:cd02762 208 --ADEH--------------LFVRP--GTDAWLLAAMLAVLLA----------EGLTDRRFLAEHCDGLDEVRAALAEFT 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 339 WAALVGESGVPREQIDALARIYVRGERVIATWGMGLTQHKHSVATvHMLSNLM-LMRGNIGRPGAGLC-----PVRGHSn 412
Cdd:cd02762 260 PEAYAPRCGVPAETIRRLAREFAAAPSAAVYGRLGVQTQLFGTLC-SWLVKLLnLLTGNLDRPGGAMFttpalDLVGQT- 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 413 vqGNRTVGIEEKPSdafleRLGRVFDFA---PPRGhgydVVETIEAMLDGRIGVFIGLGGNFAMATPDTPRTWQGLRRCG 489
Cdd:cd02762 338 --SGRTIGRGEWRS-----RVSGLPEIAgelPVNV----LAEEILTDGPGRIRAMIVVAGNPVLSAPDGARLEAALGGLE 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490663230 490 LTVHITTKLNRShlvhGREA-LILPTLGRteidLQNGVAQGVSVEDSMCMVHASYGMNPPaSPNLLSEVAIVARLGHAL 567
Cdd:cd02762 407 FMVSVDVYMTET----TRHAdYILPPASQ----LEKPHATFFNLEFPRNAFRYRRPLFPP-PPGTLPEWEILARLVEAL 476
|
|
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
113-629 |
2.27e-23 |
|
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: 104.64 E-value: 2.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 113 RLTDPMVYD-AATDRYVPIAWNAAFELIANHLRALGEpnraafytsgRASNEAAFLY-----QLLVRYYGTNNFpdcSNM 186
Cdd:cd02766 55 RLLTPLKRVgRKGGQWERISWDEALDTIAAKLKEIKA----------EYGPESILPYsyagtMGLLQRAARGRF---FHA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 187 ----------CHEATSRGLPATVGVGKGtVTLDDFEQADTLLIFGQNPATNHPRMMGELRACAKRGATIVSINPLKERGL 256
Cdd:cd02766 122 lgaselrgtiCSGAGIEAQKYDFGASLG-NDPEDMVNADLIVIWGINPAATNIHLMRIIQEARKRGAKVVVIDPYRTATA 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 257 ERfaspqhpaemltmsstpiASTFVQPRVGGDLALIKGVAKRVLELDDAarerggarvlDVDFIAAHTAGFDTFAADLRA 336
Cdd:cd02766 201 AR------------------ADLHIQIRPGTDGALALGVAKVLFREGLY----------DRDFLARHTEGFEELKAHLET 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 337 QDWAALVGESGVPREQIDALARIYVRGERVIATWGMGLTQHKHSVATVHMLSNLMLMRGNIGRPGAGlcpvrghsnvqgn 416
Cdd:cd02766 253 YTPEWAAEITGVSAEEIEELARLYGEAKPPSIRLGYGMQRYRNGGQNVRAIDALPALTGNIGVPGGG------------- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 417 rtvgieekpsdAFLERLGrvfdfaPPrghgydvvetIEAMLdgrigVFiglGGNFAMATPDTPRTWQGL-RRCGLTVHIT 495
Cdd:cd02766 320 -----------AFYSNSG------PP----------VKALW-----VY---NSNPVAQAPDSNKVRKGLaREDLFVVVHD 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 496 TKLNRShlvhGREA-LILPtlgrteidlqngVAQGVSVEDsmcmVHASYG-----MNPPASPNL---LSEVAIVARLGHA 566
Cdd:cd02766 365 QFMTDT----ARYAdIVLP------------ATTFLEHED----VYASYWhyylqYNEPAIPPPgeaRSNTEIFRELAKR 424
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490663230 567 L------FGGDKIDWLgymndyAKIRDAIEASIEGFDDYNARIARPGGFHLrVASREREWLTPSGRANF 629
Cdd:cd02766 425 LgfgeppFEESDEEWL------DQALDGTGLPLEGIDLERLLGPRKAGFPL-VAWEDRGFPTPSGKFEF 486
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
125-417 |
4.27e-23 |
|
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: 104.62 E-value: 4.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 125 DRYVPIAWNAAFELIANHLR----ALGepNRAAFYTSG---------RASNEAAFLYQLL---VRYYGTNNfpdcsnmcH 188
Cdd:cd02751 71 GEFVRISWDEALDLVASELKrireKYG--NEAIFGGSYgwasagrlhHAQSLLHRFLNLIggyLGSYGTYS--------T 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 189 EATSRGLPATVG---VGKGTVTLDD-FEQADTLLIFGQNPATN--------HPRMMGELRACAKRGATIVSINPLKERGL 256
Cdd:cd02751 141 GAAQVILPHVVGsdeVYEQGTSWDDiAEHSDLVVLFGANPLKTrqgggggpDHGSYYYLKQAKDAGVRFICIDPRYTDTA 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 257 ERFAspqhpAEMLTmsstpiastfvqPRVGGDLALIKGVAKRVLELDdaarerggarVLDVDFIAAHTAGFDTFAADLRA 336
Cdd:cd02751 221 AVLA-----AEWIP------------IRPGTDVALMLAMAHTLITED----------LHDQAFLARYTVGFDEFKDYLLG 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 337 QD--------WAAlvGESGVPREQIDALARIYVRGERVIATwGMGLTQHKHSVATVHMLSNLMLMRGNIGRPGAGLCPVR 408
Cdd:cd02751 274 ESdgvpktpeWAA--EITGVPAETIRALAREIASKRTMIAQ-GWGLQRAHHGEQPAWMLVTLAAMLGQIGLPGGGFGFGY 350
|
....*....
gi 490663230 409 GHSNVQGNR 417
Cdd:cd02751 351 GYSNGGGPP 359
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
113-404 |
4.47e-20 |
|
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: 94.29 E-value: 4.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 113 RLTDPM--VYDAATDRYVPIAWNAAFELIANHLRALGE---PNRAAFY-TSGRASNEAAFLYQL-LVRYYGTNNFPDCSN 185
Cdd:cd02759 54 RLLYPLkrVGERGENKWERISWDEALDEIAEKLAEIKAeygPESIATAvGTGRGTMWQDSLFWIrFVRLFGSPNLFLSGE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 186 MCHEATSRGLPATVGVGKGTVTLDdFEQADTLLIFGQNPATNHPRMMGE-LRACAKRGATIVSINPlkerglerfaspqh 264
Cdd:cd02759 134 SCYWPRDMAHALTTGFGLGYDEPD-WENPECIVLWGKNPLNSNLDLQGHwLVAAMKRGAKLIVVDP-------------- 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 265 paeMLTMSSTPiASTFVQPRVGGDLALIKGVAKRVLElddaarerggARVLDVDFIAAHTAGFDTFAAdlRAQ----DWA 340
Cdd:cd02759 199 ---RLTWLAAR-ADLWLPIRPGTDAALALGMLNVIIN----------EGLYDKDFVENWCYGFEELAE--RVQeytpEKV 262
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490663230 341 ALVgeSGVPREQIDALARIYVRGERVIATWGMGLTQHKHSVATVHMLSNLMLMRGNIGRPGAGL 404
Cdd:cd02759 263 AEI--TGVPAEKIRKAARLYATAKPACIQWGLAIDQQKNGTQTSRAIAILRAITGNLDVPGGNL 324
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
113-519 |
8.68e-16 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 79.75 E-value: 8.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 113 RLTDPMVYDAAtDRYVPIAWNAAFELIANHLRAL---GEPNRAAF--YTSGRASNEAAFLYQLLVRYYGTNNF---PDCS 184
Cdd:pfam00384 1 RLKYPMVRRGD-GKFVRVSWDEALDLIAKKLKRIikkYGPDAIAIngGSGGLTDVESLYALKKLLNRLGSKNGnteDHNG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 185 NMCHEATSRGLPATVGVGKGTVTLDDFEQADTLLIFGQNPATNHPRMMGELRACAKRGAT-IVSINPLKErglERFASpQ 263
Cdd:pfam00384 80 DLCTAAAAAFGSDLRSNYLFNSSIADIENADLILLIGTNPREEAPILNARIRKAALKGKAkVIVIGPRLD---LTYAD-E 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 264 HPAemltmsstpiastfvqPRVGGDLALikgvakrVLELddaarerggarvldvdfiaAHtagfdTFAADLraqdwaaLV 343
Cdd:pfam00384 156 HLG----------------IKPGTDLAL-------ALAG-------------------AH-----VFIKEL-------KK 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 344 GESGVPREQIDalariyvrgerviatWGMGLTQHKHSVATVHMLSNLMLMRGNIGRPGAGLCPVRGHSNVqGNRTVGIEE 423
Cdd:pfam00384 182 DKDFAPKPIII---------------VGAGVLQRQDGEAIFRAIANLADLTGNIGRPGGGWNGLNILQGA-ASPVGALDL 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 424 KpsdaflerlgrvfdFAPprghGYDVVETIEAMLDGRIGVFIGLGGNFAMATPDTPRTWQGLRRCGLTV-----HITTKL 498
Cdd:pfam00384 246 G--------------LVP----GIKSVEMINAIKKGGIKVLYLLGNNPFVTHADENRVVKALQKLDLFVvydghHGDKTA 307
|
410 420
....*....|....*....|.
gi 490663230 499 NRSHlvhgreaLILPTLGRTE 519
Cdd:pfam00384 308 KYAD-------VILPAAAYTE 321
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
112-406 |
1.32e-15 |
|
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: 80.03 E-value: 1.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 112 GRLTDPM--VYDAATDRYVPIAWNAAFELIANHLRALGE--PNRAAFYTSGRASNEAAFlyQLLVRYYGTNNFPDCSNMC 187
Cdd:cd02755 54 DRLKKPLirVGERGEGKFREASWDEALQYIASKLKEIKEqhGPESVLFGGHGGCYSPFF--KHFAAAFGSPNIFSHESTC 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 188 HEATSRGLPATVGVGkGTVTLDDFEQADTLLIFGQN--PATNHPRMMGELRACAKrGATIVSINPlkergleRFAspqhp 265
Cdd:cd02755 132 LASKNLAWKLVIDSF-GGEVNPDFENARYIILFGRNlaEAIIVVDARRLMKALEN-GAKVVVVDP-------RFS----- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 266 aemlTMSStpIASTFVQPRVGGDLALIKGVAKRVL--ELDDAArerggarvldvdFIAAHTAGFDTFAADLRA--QDWAA 341
Cdd:cd02755 198 ----ELAS--KADEWIPIKPGTDLAFVLALIHVLIseNLYDAA------------FVEKYTNGFELLKAHVKPytPEWAA 259
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490663230 342 lvGESGVPREQIDALARIYVRGER--VIATWGMGLTQHkHSVATVHMLSNLMLMRGNIGRPGaGLCP 406
Cdd:cd02755 260 --QITDIPADTIRRIAREFAAAAPhaVVDPGWRGTFYS-NSFQTRRAIAIINALLGNIDKRG-GLYY 322
|
|
| 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 ... |
113-521 |
2.43e-15 |
|
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: 79.36 E-value: 2.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 113 RLTDPMVYDaaTDRYVPIAWNAAFELIANHLRALGEpnRAAFYTSGRASNEAAFLYQLLVR-YYGTNNFPDCSNMCHEAT 191
Cdd:cd02771 54 RLTQPLIRR--GGTLVPVSWNEALDVAAARLKEAKD--KVGGIGSPRASNESNYALQKLVGaVLGTNNVDHRARRLIAEI 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 192 SRGLPATVgvgkgtVTLDDFEQADTLLIFGQNPATNHPRMMGELRACAKRgativsinplkerglerfaspqHPAEMLTM 271
Cdd:cd02771 130 LRNGPIYI------PSLRDIESADAVLVLGEDLTQTAPRIALALRQAARR----------------------KAVELAAL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 272 SSTPIASTFVQPRVGGD----LALIKGVAKRvleLDDAARERGGArvlDVDFIAAHTAGFDTFAADlraqDWAALVGESg 347
Cdd:cd02771 182 SGIPKWQDAAVRNIAQGakspLFIVNALATR---LDDIAAESIRA---SPGGQARLGAALARAVDA----SAAGVSGLA- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 348 vPREQIDALARIYVRGERVIATWGMGLtqhkHSVATVHMLSNLMLMRGNIGRpGAGLCPVRGHSNVQGnrtvgieekpsd 427
Cdd:cd02771 251 -PKEKAARIAARLTGAKKPLIVSGTLS----GSLELIKAAANLAKALKRRGE-NAGLTLAVEEGNSPG------------ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 428 afLERLGRvfdfaPPRGHGYDVVETIEAMLDGRIGVFIGLGGNFAMATPDTpRTWQGLRRCGLTVHITTKLNRshlVHGR 507
Cdd:cd02771 313 --LLLLGG-----HVTEPGLDLDGALAALEDGSADALIVLGNDLYRSAPER-RVEAALDAAEFVVVLDHFLTE---TAER 381
|
410
....*....|....
gi 490663230 508 EALILPTLGRTEID 521
Cdd:cd02771 382 ADVVLPAASFAEKS 395
|
|
| MopB_DMSOR-BSOR-TMAOR |
cd02769 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
125-403 |
1.18e-13 |
|
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: 74.61 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 125 DRYVPIAWNAAFELIANHLR----ALGepNRAAFYTS------GRASNEAAflyqLLVRYYG-----TNNFPDCSnmcHE 189
Cdd:cd02769 71 EEFVRVSWDEALDLVAAELKrvrkTYG--NEAIFGGSygwssaGRFHHAQS----LLHRFLNlaggyVGSVGDYS---TG 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 190 ATSRGLPATVG----VGKGTVTLDDF-EQADTLLIFGQNPATN---------HPRMMGELRACAKRGATIVSINPLKERG 255
Cdd:cd02769 142 AAQVILPHVVGsmevYTEQQTSWPVIaEHTELVVAFGADPLKNaqiawggipDHQAYSYLKALKDRGIRFISISPLRDDT 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 256 LERFAspqhpAEMLTmsstpiastfvqPRVGGDLALIKGVAkRVLELDDAArerggarvlDVDFIAAHTAGFDTFAADLR 335
Cdd:cd02769 222 AAELG-----AEWIA------------IRPGTDVALMLALA-HTLVTEGLH---------DKAFLARYTVGFDKFLPYLL 274
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490663230 336 AQD--------WAALVgeSGVPREQIDALARIYVRGeRVIATWGMGLTQHKHSVATVHMLSNLMLMRGNIGRPGAG 403
Cdd:cd02769 275 GESdgvpktpeWAAAI--CGIPAETIRELARRFASK-RTMIMAGWSLQRAHHGEQPHWMAVTLAAMLGQIGLPGGG 347
|
|
| MopB_DmsA-EC |
cd02770 |
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
113-422 |
1.24e-13 |
|
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: 74.28 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 113 RLTDPM--VYDAATDRYVPIAWNAAFELIANHLRALGEP--NRAAFYTSGRASNEAAFLYQLLVR-----------YYGT 177
Cdd:cd02770 59 RLKYPMkrVGKRGEGKFVRISWDEALDTIASELKRIIEKygNEAIYVNYGTGTYGGVPAGRGAIArllnltggylnYYGT 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 178 nnfpdCSNMCheaTSRGLPATVGVGKGTVTLDDFEQADTLLIFGQNPATNhpRMMG-----ELRACAKRGATIVSINPlk 252
Cdd:cd02770 139 -----YSWAQ---ITTATPYTYGAAASGSSLDDLKDSKLVVLFGHNPAET--RMGGggstyYYLQAKKAGAKFIVIDP-- 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 253 ergleRFaspqhpaemlTMSSTPIASTFVQPRVGGDLALIKGVAKRVLELDdaarerggarVLDVDFIAAHTAGFDtfAA 332
Cdd:cd02770 207 -----RY----------TDTAVTLADEWIPIRPGTDAALVAAMAYVMITEN----------LHDQAFLDRYCVGFD--AE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 333 DL-----------------------RAQDWAALVgeSGVPREQIDALARIYVRGERVIATWGMGLTQHKHSVATVHMLSN 389
Cdd:cd02770 260 HLpegappnesykdyvlgtgydgtpKTPEWASEI--TGVPAETIRRLAREIATTKPAAILQGWGPQRHANGEQAARAIMM 337
|
330 340 350
....*....|....*....|....*....|...
gi 490663230 390 LMLMRGNIGRPGAGLCPVRGHSNVQGNRTVGIE 422
Cdd:cd02770 338 LAAMTGNVGIPGGNTGARPGGSAYNGAGLPAGK 370
|
|
| MopB_Arsenite-Ox |
cd02756 |
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the ... |
110-410 |
3.75e-10 |
|
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the electrons obtained from the oxidation of arsenite towards the soluble periplasmic electron carriers cytochrome c and/or amicyanin. Arsenite oxidase is a heterodimeric enzyme containing a large and a small subunit. The large catalytic subunit harbors the molybdopterin cofactor and the [3Fe-4S] cluster; and the small subunit belongs to the structural class of the Rieske proteins. The small subunit is not included in this alignment. Members of MopB_Arsenite-Ox CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239157 [Multi-domain] Cd Length: 676 Bit Score: 63.27 E-value: 3.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 110 QHGRLTDPMVYdaATDRYVPIAWNAAFELIANHLRAL----GEPNRAAFYTS-------GRASNEAA---FLYQLLVRYY 175
Cdd:cd02756 114 GETRLTTPLVR--RGGQLQPTTWDDAIDLVARVIKGIldkdGNDDAVFASRFdhgggggGFENNWGVgkfFFMALQTPFV 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 176 GTNNFPDCSNMCHEATSRGlpatvgVGKGTVTLDDFEQADTLLIFGQNP---ATNH--PRMMGELRacakrGATivsinp 250
Cdd:cd02756 192 RIHNRPAYNSEVHATREMG------VGELNNSYEDARLADTIVLWGNNPyetQTVYflNHWLPNLR-----GAT------ 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 251 lKERGLERF-ASPQHPAEML-------TMSSTPIASTFVQPRV-------GGDLALIKGVAKRVLE-----LDDAARERG 310
Cdd:cd02756 255 -VSEKQQWFpPGEPVPPGRIivvdprrTETVHAAEAAAGKDRVlhlqvnpGTDTALANAIARYIYEsldevLAEAEQITG 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 311 garvLDVDFIAahtagfdtfaadlRAQDWAALVGESGVPREQIdalaRIYVRGerVIatWGMGltqhkhSVATVHMLSNL 390
Cdd:cd02756 334 ----VPRAQIE-------------KAADWIAKPKEGGYRKRVM----FEYEKG--II--WGND------NYRPIYSLVNL 382
|
330 340
....*....|....*....|
gi 490663230 391 MLMRGNIGRPGAGLCPVRGH 410
Cdd:cd02756 383 AIITGNIGRPGTGCVRQGGH 402
|
|
| FwdB |
COG1029 |
Formylmethanofuran dehydrogenase subunit B [Energy production and conversion]; |
111-415 |
3.81e-09 |
|
Formylmethanofuran dehydrogenase subunit B [Energy production and conversion];
Pssm-ID: 440652 [Multi-domain] Cd Length: 428 Bit Score: 59.48 E-value: 3.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 111 HGRLTDPMVydaatdRYVPIAWNAAFELIANHLRalgEPNRAAFYTSGRASNEAAFLYQLLVRYYGTNnFPDCSNMCHEA 190
Cdd:COG1029 49 DHRITSPRI------RGKEVSLEEAIDKAAEILA---NAKRPLIYGLSSTDCEAMRAGLALAERVGAV-VDNTASVCHGP 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 191 TSRGLPAtvgVGKGTVTLDDFEQ-ADTLLIFGQNPATNHPRMM--------GELRACAKRGATIVSINPLKerglerfaS 261
Cdd:COG1029 119 SLLALQD---VGWPTCTLGEVKNrADVIIYWGCNPVHAHPRHMsrysvfprGFFTPKGRKDRTVIVVDPRP--------T 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 262 PqhpaemltmsSTPIASTFVQPRVGGDLALIkgvakrvleldDAARerggarvldvdfiaAHTAGFDTFAADLraqdwaa 341
Cdd:COG1029 188 D----------TAKVADLHLQVKPGRDYEVL-----------SALR--------------ALVRGKELSPEEV------- 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490663230 342 lvgeSGVPREQIDALARIYVRGERVIATWGMGLTQHKHSVATVHMLSNLMLMRGNIGRpgAGLCPVRGHSNVQG 415
Cdd:COG1029 226 ----AGIPVEDLEELAERLKNAKYGVIFWGMGLTQSPGKHLNVDAAIELVRDLNRYTK--FSILPLRGHYNVAG 293
|
|
| MopB_2 |
cd02763 |
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
113-401 |
5.23e-09 |
|
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: 59.85 E-value: 5.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 113 RLTDPM--VYDAATDRYVPIAWNAAFELIANHLRALG--EPNRAAFYTsGRASNEAafLYQLLVRYYGTNNFPDCSNMCH 188
Cdd:cd02763 54 RLTKPLlrKGPRGSGQFEEIEWEEAFSIATKRLKAARatDPKKFAFFT-GRDQMQA--LTGWFAGQFGTPNYAAHGGFCS 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 189 EATSRGLPATVGVGKGTVTLDDFEQADTLLIFGQnpATNH---PRMMGeLRACAKRGATIVSINPLKerglerfaspqhp 265
Cdd:cd02763 131 VNMAAGGLYSIGGSFWEFGGPDLEHTKYFMMIGV--AEDHhsnPFKIG-IQKLKRRGGKFVAVNPVR------------- 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 266 aemltMSSTPIASTFVQPRVGGDLALIKGVAKRVLELDdaarerggarVLDVDFIAAHTAgfdtfAADL--RAQDWAAlv 343
Cdd:cd02763 195 -----TGYAAIADEWVPIKPGTDGAFILALAHELLKAG----------LIDWEFLKRYTN-----AAELvdYTPEWVE-- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 344 GESGVPREQIDALAR------IYVRGERVIA---TWGM----------------GLTQHKHSVATVHMLSNLMLMRGNIG 398
Cdd:cd02763 253 KITGIPADTIRRIAKelgvtaRDQPIELPIAwtdVWGRkhekitgrpvsfhamrGIAAHSNGFQTIRALFVLMMLLGTID 332
|
...
gi 490663230 399 RPG 401
Cdd:cd02763 333 RPG 335
|
|
| MopB_FmdB-FwdB |
cd02761 |
The MopB_FmdB-FwdB CD contains the molybdenum/tungsten formylmethanofuran dehydrogenases, ... |
54-415 |
2.07e-08 |
|
The MopB_FmdB-FwdB CD contains the molybdenum/tungsten formylmethanofuran dehydrogenases, subunit B (FmdB/FwdB), and other related proteins. Formylmethanofuran dehydrogenase catalyzes the first step in methane formation from CO2 in methanogenic archaea and some eubacteria. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239162 [Multi-domain] Cd Length: 415 Bit Score: 57.34 E-value: 2.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 54 CPGCAW--PDREhastFEFCENGVKAVAaeaTAKRVTPAFFAEHTVsalfdqsdyaleqhgRLTDPMVydaatdRYVPIA 131
Cdd:cd02761 4 CPFCGLlcDDIE----VEVEDNKITKVR---NACRIGAAKFARYER---------------RITTPRI------DGKPVS 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 132 WNAAFELIANHLRalgEPNRAAFYTSGRASNEAAFLYQLLVRYYGTNnFPDCSNMCHEATSRGLpatVGVGKGTVTLDDF 211
Cdd:cd02761 56 LEEAIEKAAEILK---EAKRPLFYGLGTTVCEAQRAGIELAEKLGAI-IDHAASVCHGPNLLAL---QDSGWPTTTLGEV 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 212 E-QADTLLIFGQNPATNHPRMMGElracakrgatiVSINPlkeRGLERFASPQhpaemltmSSTPIastFVQPRVGGDLA 290
Cdd:cd02761 129 KnRADVIVYWGTNPMHAHPRHMSR-----------YSVFP---RGFFREGGRE--------DRTLI---VVDPRKSDTAK 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 291 LikgvAKRVLELDDAArerggarvlDVDFIAAHTAGfdTFAADLRAQDWAalvgesGVPREQIDALARIYVRGERVIATW 370
Cdd:cd02761 184 L----ADIHLQIDPGS---------DYELLAALRAL--LRGAGLVPDEVA------GIPAETILELAERLKNAKFGVIFW 242
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 490663230 371 GMGLTQHKHSVATVHMLSNLMLMRGNIGRpgAGLCPVRGHSNVQG 415
Cdd:cd02761 243 GLGLLPSRGAHRNIEAAIRLVKALNEYTK--FALLPLRGHYNVRG 285
|
|
| PRK13532 |
PRK13532 |
nitrate reductase catalytic subunit NapA; |
113-403 |
6.28e-08 |
|
nitrate reductase catalytic subunit NapA;
Pssm-ID: 237416 [Multi-domain] Cd Length: 830 Bit Score: 56.45 E-value: 6.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 113 RLTDPM------VYDAATDrYVPIAWNAAFELIANH----LRALGePNRAAFYTSGRAS----NEAAFLYQLLVRyygTN 178
Cdd:PRK13532 97 RLTQPLlrmkdgKYDKEGE-FTPVSWDQAFDVMAEKfkkaLKEKG-PTAVGMFGSGQWTiwegYAASKLMKAGFR---SN 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 179 NFPDCSNMCHEATSRGLPATVGVGKGTVTLDDFEQADTLLIFGQNPATNHPRMMGEL--RACAKRGATIVSINPLKERGL 256
Cdd:PRK13532 172 NIDPNARHCMASAVVGFMRTFGIDEPMGCYDDIEAADAFVLWGSNMAEMHPILWSRVtdRRLSNPDVKVAVLSTFEHRSF 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 257 ErfaspqhpaemltMSSTPIasTFvqpRVGGDLALIKGVAKRVLELDdaarerggaRVlDVDFIAAHTAgFDTFAAD--- 333
Cdd:PRK13532 252 E-------------LADNGI--IF---TPQTDLAILNYIANYIIQNN---------AV-NWDFVNKHTN-FRKGATDigy 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 334 -LRA----------------------QDWAALVGE---------SGVPREQIDALARIYVRGER-VIATWGMGLTQHKHS 380
Cdd:PRK13532 303 gLRPthplekaaknpgtagksepisfEEFKKFVAPytlektakmSGVPKEQLEQLAKLYADPNRkVVSFWTMGFNQHTRG 382
|
330 340
....*....|....*....|...
gi 490663230 381 VATVHMLSNLMLMRGNIGRPGAG 403
Cdd:PRK13532 383 VWANNLVYNIHLLTGKISTPGNG 405
|
|
| PRK07860 |
PRK07860 |
NADH dehydrogenase subunit G; Validated |
110-350 |
1.38e-07 |
|
NADH dehydrogenase subunit G; Validated
Pssm-ID: 236118 [Multi-domain] Cd Length: 797 Bit Score: 55.34 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 110 QHGRLTDPMVYDAaTDRYVPIAWNAAFELIANHLRALGEpnRAAFYTSGRASNEAAFLYQLLVRY-YGTNNFpDCSNMCH 188
Cdd:PRK07860 275 QPDRITTPLVRDE-DGELEPASWSEALAVAARGLAAARG--RVGVLVGGRLTVEDAYAYAKFARVaLGTNDI-DFRARPH 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 189 EAT-SRGLPATV-GVGKGtVTLDDFEQADTLLIFGQNPATNHPRMMGELR-ACAKRGATIVSINPLKERGLERfaspqhp 265
Cdd:PRK07860 351 SAEeADFLAARVaGRGLG-VTYADLEKAPAVLLVGFEPEEESPIVFLRLRkAARKHGLKVYSIAPFATRGLEK------- 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 266 aemltMSSTPIASTfvqPrvGGDLALIKGVAKRVLELDDAARERGGarVLDVDFIAAHTAGFDTFAADLRAQDWAALVge 345
Cdd:PRK07860 423 -----MGGTLLRTA---P--GGEAAALDALATGAPDVAELLRTPGA--VILVGERLATVPGALSAAARLADATGARLA-- 488
|
....*
gi 490663230 346 sGVPR 350
Cdd:PRK07860 489 -WVPR 492
|
|
| MopB_NDH-1_NuoG2 |
cd02772 |
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase ... |
113-325 |
4.94e-07 |
|
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase/NADH dehydrogenase-1 (NDH-1), found in beta- and gammaproteobacteria. 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. 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: 239173 [Multi-domain] Cd Length: 414 Bit Score: 52.74 E-value: 4.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 113 RLTDPMVydAATDRYVPIAWNAAFELIANHLRALGE---PNRAAFYTSGRASNEAAFLYQLLVRYYGTNNF---PDCSNM 186
Cdd:cd02772 54 RLTKPMI--KKDGQWQEVDWETALEYVAEGLSAIIKkhgADQIGALASPHSTLEELYLLQKLARGLGSDNIdhrLRQSDF 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 187 CHEATSRGLPatvGVGkgtVTLDDFEQADTLLIFGQNPATNHPRMMGELRACAKRGATIVSINPLKERGLERFASPQ--H 264
Cdd:cd02772 132 RDDAKASGAP---WLG---MPIAEISELDRVLVIGSNLRKEHPLLAQRLRQAVKKGAKLSAINPADDDFLFPLSGKAivA 205
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490663230 265 PAEMLTMSStpiastfvqpRVGGDLALIKGVAkrVLELDDAARERGGARVLDVDFIAAHTA 325
Cdd:cd02772 206 PSALANALA----------QVAKALAEEKGLA--VPDEDAKVEASEEARKIAASLVSAERA 254
|
|
| MopB_Nitrate-R-NarG-like |
cd02750 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
194-404 |
1.28e-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. 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: 51.55 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 194 GLPATVGVGKGTVTLDDFEQADTLLIFGQN-PATNHP--RMMGELRacaKRGATIVSINPlkergleRFASpqhpaemlt 270
Cdd:cd02750 151 GSPQTWGEQTDVPESADWYNADYIIMWGSNvPVTRTPdaHFLTEAR---YNGAKVVVVSP-------DYSP--------- 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 271 msSTPIASTFVQPRVGGDLALIKGVAKRVLElddaarerggARVLDVDFIAAHTagfdtfaaDL----RAQDWAAlvGES 346
Cdd:cd02750 212 --SAKHADLWVPIKPGTDAALALAMAHVIIK----------EKLYDEDYLKEYT--------DLpflvYTPAWQE--AIT 269
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490663230 347 GVPREQIDALARIYVRGERVIATWGMGLTQHKHSVATVHMLSNLMLMRGNIGRPGAGL 404
Cdd:cd02750 270 GVPRETVIRLAREFATNGRSMIIVGAGINHWYHGDLCYRALILLLALTGNEGKNGGGW 327
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
130-401 |
2.47e-06 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 51.21 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 130 IAWNAAFELIANHLRALGE---PNRAAFytSGRASNEAAFLYQLLVRYYGTNNFpdcsnmCHEATSrglPATVGVGK--- 203
Cdd:PRK15488 117 ISWDEAYQEIAAKLNAIKQqhgPESVAF--SSKSGSLSSHLFHLATAFGSPNTF------THASTC---PAGYAIAAkvm 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 204 -GTVTLDDFEQADTLLIFGQN--PATNHPRMMGELRACAKRGATIVSINPlkergleRFAspqhpaemlTMSSTpiASTF 280
Cdd:PRK15488 186 fGGKLKRDLANSKYIINFGHNlyEGINMSDTRGLMTAQMEKGAKLVVFEP-------RFS---------VVASK--ADEW 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 281 VQPRVGGDLALIKGVAKRVLElddaarerggARVLDVDFIAAHTAGFDTFAADLRAQ--DWAAlvGESGVPREQIDALAR 358
Cdd:PRK15488 248 HAIRPGTDLAVVLALCHVLIE----------ENLYDKAFVERYTSGFEELAASVKEYtpEWAE--AISDVPADDIRRIAR 315
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 490663230 359 -IYVRGERVIATWGMGLTQHKHSVATVHMLSNLMLMRGNIGRPG 401
Cdd:PRK15488 316 eLAAAAPHAIVDFGHRATFTPEEFDMRRAIFAANVLLGNIERKG 359
|
|
| Molydop_binding |
pfam01568 |
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
652-760 |
3.94e-06 |
|
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: 46.11 E-value: 3.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 652 MTLMTTRSHDQYNTTIYALDDRYRGVFgERRVVFAHPDDLAMLGFEAGERVDLETvwddgiER-RVAGFLLVAYDIPRGC 730
Cdd:pfam01568 1 LYLITGRVLGQYHSQTRTRRVLRLAKP-EPEVVEIHPEDAAALGIKDGDLVEVTS------RRgSVVVRAKVTDRVRPGV 73
|
90 100 110
....*....|....*....|....*....|....*...
gi 490663230 731 LGAYYPE--------TNPLVPlDSVGDVCNTPTSKSIP 760
Cdd:pfam01568 74 VFMPFGWwyeprggnANALTD-DATDPLSGGPEFKTCA 110
|
|
| PRK15102 |
PRK15102 |
trimethylamine-N-oxide reductase TorA; |
316-404 |
5.12e-04 |
|
trimethylamine-N-oxide reductase TorA;
Pssm-ID: 237909 [Multi-domain] Cd Length: 825 Bit Score: 43.51 E-value: 5.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490663230 316 DVDFIAAHTAGFDTFAADLRAQ--------DWAALVgeSGVPREQIDALARIYVRGE-RVIATWGMGLTQHKHSVAtvHM 386
Cdd:PRK15102 301 DKKFIDNYCLGFEQFLPYLLGEkdgvpktpEWAEKI--CGIDAETIRELARQMAKGRtQIIAGWCIQRQQHGEQPY--WM 376
|
90
....*....|....*...
gi 490663230 387 LSNLMLMRGNIGRPGAGL 404
Cdd:PRK15102 377 GAVLAAMLGQIGLPGGGI 394
|
|
| |
