|
Name |
Accession |
Description |
Interval |
E-value |
| MopB_ydeP |
cd02767 |
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
55-635 |
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: 995.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 55 GFDCPSCAWPDPKKP-HTFEYCENGAKALAWESTKKRVTPEFFAQHTVSELATWSDHDLEDQGRITEPMRYDAGSDKYLP 133
Cdd:cd02767 1 GFDCPGCAWGDPGQKlHGFEFCENGAKALAWETTPKRVTPEFFALHSVSELRTWSDYELEHLGRLTYPMRYDAGSDHYRP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 134 VSWDEAFAEIGQELRQLsDPWKLELYTSGRTSNEAAFLYQLFGRLYGMANFPDCSNMCHETTSVALPESIGVGKGTTTLE 213
Cdd:cd02767 81 ISWDEAFAEIAARLRAL-DPDRAAFYTSGRASNEAAYLYQLFARAYGTNNLPDCSNMCHEPSSVGLKKSIGVGKGTVSLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 214 DFENADAIFIFGQNPGTNSPRMMSELHAAARRGASIISFNPLREKALVRFASPQDPRDMLSrSGVKISSQYHQVRIGGDM 293
Cdd:cd02767 160 DFEHTDLIFFIGQNPGTNHPRMLHYLREAKKRGGKIIVINPLREPGLERFANPQNPESMLT-GGTKIADEYFQVRIGGDI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 294 IALQGICKVVIEADDAAqreglPRVLDVAFIEEHTHGLEQFADYCRQLPWEIIERHSGLTRQALEEVAAVYMRSERVICC 373
Cdd:cd02767 239 ALLNGMAKHLIERDDEP-----GNVLDHDFIAEHTSGFEEYVAALRALSWDEIERASGLSREEIEAFAAMYAKSERVVFV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 374 WGMGITQHKRGGDAMQQIINLLLLRGNIGKLGAGACPIRGHSNVQGDRTMGIYEKAGEPFLASMSKVFGFEASRKGGHDV 453
Cdd:cd02767 314 WGMGITQHAHGVDNVRAIVNLALLRGNIGRPGAGLMPIRGHSNVQGDRTMGITEKPFPEFLDALEEVFGFTPPRDPGLDT 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 454 AEACEALLRGEIEAFISMGGNFFRAIPDIDVVCPTVKRLKMTVLVNTKLNRSATVHGQKAFLLPCIARSELDMQNGVAQT 533
Cdd:cd02767 394 VEAIEAALEGKVKAFISLGGNFAEAMPDPAATEEALRRLDLTVHVATKLNRSHLVHGEEALILPCLGRTEIDMQAGGAQA 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 534 VTVEDSMSMVHGSTGMLEPASKHLISEVAIIAGIAKATLaPNPNVDWDSYVNDYARIRDKIEAVLPEQFYDFNQRIKEPG 613
Cdd:cd02767 474 VTVEDSMSMTHTSRGRLKPASRVLLSEEAIVAGIAGARL-GEAKPEWEILVEDYDRIRDEIAAVIYEGFADFNQRGDQPG 552
|
570 580
....*....|....*....|..
gi 1524502542 614 GFRLPNGASERKWNTESGKANF 635
Cdd:cd02767 553 GFHLPNGARERKFNTPSGKAQF 574
|
|
| Fdhalpha-like |
TIGR01701 |
oxidoreductase alpha (molybdopterin) subunit; This model represents a well-defined clade of ... |
20-767 |
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: 934.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 20 AAGGWPALNAVNKHLLHQHVLLKGNRTLLSMNKPDGFDCPSCAWPD-PKKPHTFEYCENGAKALAWESTKKRVTPEFFAQ 98
Cdd:TIGR01701 1 DAGGWGAVKSVALGKVKPMHIRQTLKLLLTLNKPEGYDCPGCAWGVsPQTLAGLEFCENGAKAIAWETTPRTIDPEFFAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 99 HTVSELATWSDHDLEDQGRITEPMRYDAGSDKYLPVSWDEAFAEIGQELRQLsDPWKLELYTSGRTSNEAAFLYQLFGRL 178
Cdd:TIGR01701 81 HSVSELRTLDSHELEKLGRLTYPLSLRPGSDHYTPISWDDAYQEIAAKLNSL-DPKQVAFYTSGRTSNEAAYLYQLFARS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 179 YGMANFPDCSNMCHETTSVALPESIGVGKGTTTLEDFENADAIFIFGQNPGTNSPRMMSELHAAARRGASIISFNPLREK 258
Cdd:TIGR01701 160 LGSNNLPDCSNMCHEPSSVALKRSIGIGKGSVNLEDFEHTDCLVFIGSNAGTNHPRMLKYLYAAKKRGAKIIAINPLRER 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 259 ALVRFASPQDPRDMLSRSGVKISSQYHQVRIGGDMIALQGICKVVIEADDAAQreglPRVLDVAFIEEHTHGLEQFADYC 338
Cdd:TIGR01701 240 GLERFWIPQIPESMLTGGGTQISSEYYQVRIGGDIALFNGVMKLLIEAEDAQP----GSLIDHEFIANHTNGFDELRRHV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 339 RQLPWEIIERHSGLTRQALEEVAAVYMRSERVICCWGMGITQHKRGGDAMQQIINLLLLRGNIGKLGAGACPIRGHSNVQ 418
Cdd:TIGR01701 316 LQLNWNDIERSSGLSQEEILEFAKLLANSRRVVFCWAMGLTQHAHGVDNISQVANLALLRGNIGKPGAGVCPIRGHSNVQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 419 GDRTMGIYEKAGEPFLASMSKVFGFEASRKGGHDVAEACEALLRGEIEAFISMGGNFFRAIPDIDVVCPTVKRLKMTVLV 498
Cdd:TIGR01701 396 GDRTMGITEKPEEEFLARLSQIYGFTPPDWPGDTTVAMIEAILTGKVRAFICLGGNFLEAMPDTAAIERALRQLDLRVHV 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 499 NTKLNRSATVHGQKAFLLPCIARSELDMQNGVAQTVTVEDSMSMVHGSTGMLEPASKHLISEVAIIAGIAKATLAPNPnV 578
Cdd:TIGR01701 476 ATKLNRSHVLAKEEALILPVLGRYEQDGQGTGKQAVSVESSMRMVHFSRGILKPRGAELRSEWAIIAEIAKALLPETP-V 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 579 DWDSYVNDYARIRDKIEAVLPEqFYDFNQRIKEPGGFRLPNGA-SERKWNTESGKANFLFPEGVFdEDDTPPGADHLQLM 657
Cdd:TIGR01701 555 AWEILVDTYDQIRDAIAATNPG-YDDINHRKRRPDGFQLPGAAlCERKFPTPDGKANFIVIPLPE-FRVPTGHEFELVLV 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 658 TIRSHDQFNTTVYSNDDRYRGIYGDRMVVMLNPQDIERLGLKAGDYVEFQTALDMTTPRRAPGFKVIPFDVPQGCCAAYY 737
Cdd:TIGR01701 633 TLRSHDQFNTTIYGEDDRYRGVDGHRRVVFMNETDIKKLGLRNGERVDVYNQYGDGQKRKFDNLRIVFYDTPTGNAAAYY 712
|
730 740 750
....*....|....*....|....*....|
gi 1524502542 738 PETNGLLPLANRDSRSNTPAAKSIPVNLVR 767
Cdd:TIGR01701 713 PEANPLLPLDHHDPQSKTPEYKTIPVRLEA 742
|
|
| PRK09939 |
PRK09939 |
acid resistance putative oxidoreductase YdeP; |
15-769 |
0e+00 |
|
acid resistance putative oxidoreductase YdeP;
Pssm-ID: 182156 [Multi-domain] Cd Length: 759 Bit Score: 843.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 15 QSNGSAAGGWPALNAVNKHLLHQHVLLKGNRTLLSMNKPDGFDCPSCAWPDPKKPHTFEYCENGAKALAWESTKKRVTPE 94
Cdd:PRK09939 6 ESYQGAAGGWGAVKSVANAVRKQMDIRQDVIAMFDMNKPEGFDCPGCAWPDPKHSASFDICENGAKAIAWEVTDKQVNAS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 95 FFAQHTVSELATWSDHDLEDQGRITEPMRYDAGSDKYLPVSWDEAFAEIGQELRQLSDPWKLELYTSGRTSNEAAFLYQL 174
Cdd:PRK09939 86 FFAENTVQSLLTWGDHELEAAGRLTQPLKYDAVSDCYKPLSWQQAFDEIGARLQSYSDPNQVEFYTSGRTSNEAAFLYQL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 175 FGRLYGMANFPDCSNMCHETTSVALPESIGVGKGTTTLEDFENADAIFIFGQNPGTNSPRMMSELHAAARRGASIISFNP 254
Cdd:PRK09939 166 FAREYGSNNFPDCSNMCHEPTSVGLAASIGVGKGTVLLEDFEKCDLVICIGHNPGTNHPRMLTSLRALVKRGAKMIAINP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 255 LREKALVRFASPQDPRDMLSRSGVKISSQYHQVRIGGDMIALQGICKVVIEADDAAQREGLPRVLDVAFIEEHTHGLEQF 334
Cdd:PRK09939 246 LQERGLERFTAPQNPFEMLTNSETQLASAYYNVRIGGDMALLKGMMRLLIERDDAASAAGRPSLLDDEFIQTHTVGFDEL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 335 ADYCRQLPWEIIERHSGLTRQALEEVAAVYMRSERVICCWGMGITQHKRGGDAMQQIINLLLLRGNIGKLGAGACPIRGH 414
Cdd:PRK09939 326 RRDVLNSEWKDIERISGLSQTQIAELADAYAAAERTIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGICPLRGH 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 415 SNVQGDRTMGIYEKAGEPFLASMSKVFGFEASRKGGHDVAEACEALLRGEIEAFISMGGNFFRAIPDIDVVCPTVKRLKM 494
Cdd:PRK09939 406 SNVQGDRTVGITEKPSAEFLARLGERYGFTPPHAPGHAAIASMQAICTGQARALICMGGNFALAMPDREASAVPLTQLDL 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 495 TVLVNTKLNRSATVHGQKAFLLPCIARSELDMQNGVAQTVTVEDSMSMVHGSTGMLEPASKHLISEVAIIAGIAKATLaP 574
Cdd:PRK09939 486 AVHVATKLNRSHLLTARHSYILPVLGRSEIDMQKSGAQAVTVEDSMSMIHASRGVLKPAGVMLKSECAVVAGIAQAAL-P 564
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 575 NPNVDWDSYVNDYARIRDKIEAVLPEqFYDFNQRIKEPGGFRLPNGASERKWNTESGKANFLFPEGVFdEDDTPPGADHL 654
Cdd:PRK09939 565 QSVVAWEYLVEDYDRIRNDIEAVLPE-FADYNQRIRHPGGFHLINAAAERRWMTPSGKANFITSKGLL-EDPSSAFNSKL 642
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 655 QLMTIRSHDQFNTTVYSNDDRYRGIYGDRMVVMLNPQDIERLGLKAGDYVEF--QTALDMTTPRRAPGFKVIPFDVPQGC 732
Cdd:PRK09939 643 VMATVRSHDQYNTTIYGMDDRYRGVFGQRDVVFMSAKQAKICRVKNGERVNLiaLTPDGKRSSRRMDRLKVVIYPMADRS 722
|
730 740 750
....*....|....*....|....*....|....*..
gi 1524502542 733 CAAYYPETNGLLPLANRDSRSNTPAAKSIPVNLVRMN 769
Cdd:PRK09939 723 LVTYFPESNHMLTLDNHDPLSGIPGYKSIPVELEPSN 759
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
58-770 |
4.99e-161 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 482.81 E-value: 4.99e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 58 CPSCAwpdpkkphtfEYCENGAKalawesTK----KRVTPEffAQHTVSELATW-----SDHDLEDQGRITEPMRYD--A 126
Cdd:COG0243 28 CPGCG----------VGCGLGVK------VEdgrvVRVRGD--PDHPVNRGRLCakgaaLDERLYSPDRLTYPMKRVgpR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 127 GSDKYLPVSWDEAFAEIGQELRQLSD---PWKLELYTSG----RTSNEAAFLYQLFGRLYGMANFPDCSNMCHETTSVAL 199
Cdd:COG0243 90 GSGKFERISWDEALDLIAEKLKAIIDeygPEAVAFYTSGgsagRLSNEAAYLAQRFARALGTNNLDDNSRLCHESAVAGL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 200 PESIGVGKGTTTLEDFENADAIFIFGQNPGTNSPRMMSELHAAAR-RGASIISFNPLREKalvrfaspqdprdmlsrsGV 278
Cdd:COG0243 170 PRTFGSDKGTVSYEDLEHADLIVLWGSNPAENHPRLLRRLREAAKkRGAKIVVIDPRRTE------------------TA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 279 KISSQYHQVRIGGDMIALQGICKVVIEADdaaqreglprVLDVAFIEEHTHGLEQFADYCRQLPWEIIERHSGLTRQALE 358
Cdd:COG0243 232 AIADEWLPIRPGTDAALLLALAHVLIEEG----------LYDRDFLARHTVGFDELAAYVAAYTPEWAAEITGVPAEDIR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 359 EVAAVYMRSERVICCWGMGITQHKRGGDAMQQIINLLLLRGNIGKLGAGACPIRGhsnvqgdrtmgiyekagepflasms 438
Cdd:COG0243 302 ELAREFATAKPAVILWGMGLQQHSNGTQTVRAIANLALLTGNIGKPGGGPFSLTG------------------------- 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 439 kvfgfeasrkgghdvaeacEALLRGE---IEAFISMGGNFFRAIPDIDVVCPTVKRLKMTVLVNTKLNRSATVHgqkAFL 515
Cdd:COG0243 357 -------------------EAILDGKpypIKALWVYGGNPAVSAPDTNRVREALRKLDFVVVIDTFLTETARYA---DIV 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 516 LPCIARSEldmQNGVAqtVTVEDsmSMVHGSTGMLEPASkHLISEVAIIAGIAKAtLAPNPNVDWDSYVNDYarIRDKIE 595
Cdd:COG0243 415 LPATTWLE---RDDIV--TNSED--RRVHLSRPAVEPPG-EARSDWEIFAELAKR-LGFEEAFPWGRTEEDY--LRELLE 483
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 596 AVLPEQFyDFnQRIKEPGGFRLPNGAS-----ERKWNTESGKANFLFPEGVFD---------EDDTPPGADH-LQLMTIR 660
Cdd:COG0243 484 ATRGRGI-TF-EELREKGPVQLPVPPEpafrnDGPFPTPSGKAEFYSETLALPplpryappyEGAEPLDAEYpLRLITGR 561
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 661 SHDQFNTTVYsNDDRYRGIYGdRMVVMLNPQDIERLGLKAGDYVEfqtaldMTTPR-RAPGFKVIPFDVPQGCCAAYY-- 737
Cdd:COG0243 562 SRDQWHSTTY-NNPRLREIGP-RPVVEINPEDAAALGIKDGDLVR------VESDRgEVLARAKVTEGIRPGVVFAPHgw 633
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 1524502542 738 -----PETNGL---LPLANRDSRSNTPAAKSIPVNLVRMNP 770
Cdd:COG0243 634 wyepaDDKGGNvnvLTPDATDPLSGTPAFKSVPVRVEKAAA 674
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
112-770 |
9.95e-89 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 294.10 E-value: 9.95e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 112 LEDQGRITEPMRYDAGsdKYLPVSWDEAFAEIGQELRQLSD---PWKLELYTSGRTSNEAAFLYQLFGRLY-GMANFPDC 187
Cdd:COG3383 56 VNSPDRLTTPLIRRGG--EFREVSWDEALDLVAERLREIQAehgPDAVAFYGSGQLTNEENYLLQKLARGVlGTNNIDNN 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 188 SNMCHETTSVALPESIGVGKGTTTLEDFENADAIFIFGQNPGTNSPRMMSELHAAARRGASIISFNPlREKALVRFASpq 267
Cdd:COG3383 134 ARLCMASAVAGLKQSFGSDAPPNSYDDIEEADVILVIGSNPAEAHPVLARRIKKAKKNGAKLIVVDP-RRTETARLAD-- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 268 dprdmlsrsgvkissqYH-QVRIGGDMIALQGICKVVIEaddaaqrEGLprvLDVAFIEEHTHGLEQFADYCRQLPWEII 346
Cdd:COG3383 211 ----------------LHlQIKPGTDLALLNGLLHVIIE-------EGL---VDEDFIAERTEGFEELKASVAKYTPERV 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 347 ERHSGLTRQALEEVAAVYMRSERVICCWGMGITQHKRGGDAMQQIINLLLLRGNIGKLGAGACPIRGHSNVQGDRTMGI- 425
Cdd:COG3383 265 AEITGVPAEDIREAARLIAEAKRAMILWGMGVNQHTQGTDNVNAIINLALATGNIGRPGTGPFPLTGQNNVQGGRDMGAl 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 426 ------YEKAGEP-FLASMSKVFGFEA-SRKGGHDVAEACEALLRGEIEAFISMGGNFFRAIPDIDVVCPTVKRLKMTV- 496
Cdd:COG3383 345 pnvlpgYRDVTDPeHRAKVADAWGVPPlPDKPGLTAVEMFDAIADGEIKALWIIGENPAVSDPDANHVREALEKLEFLVv 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 497 --LVNTKLNRSATVhgqkafLLPCIARSEldmQNGvaqTVTveDSMSMVHGSTGMLEPA--SKhliSEVAIIAGIAKATl 572
Cdd:COG3383 425 qdIFLTETAEYADV------VLPAASWAE---KDG---TFT--NTERRVQRVRKAVEPPgeAR---PDWEIIAELARRL- 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 573 apnpNVDWDSyvNDYARIRDKIEAVLPEqFYDFN-QRIKEPGGFRLPNGASER---------KWNTESGKANFLFPEgvF 642
Cdd:COG3383 487 ----GYGFDY--DSPEEVFDEIARLTPD-YSGISyERLEALGGVQWPCPSEDHpgtprlftgRFPTPDGKARFVPVE--Y 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 643 DEDDTPPGADH-LQLMTIRSHDQFNTTVYSNDDRYRGIYGDRMVVMLNPQDIERLGLKAGDYVEfqtaldMTTPRRAPGF 721
Cdd:COG3383 558 RPPAELPDEEYpLVLTTGRLLDQWHTGTRTRRSPRLNKHAPEPFVEIHPEDAARLGIKDGDLVR------VSSRRGEVVL 631
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 1524502542 722 KV-IPFDVPQGCCAAY--YPETN-GLLPLANRDSRSNTPAAKSIPVNLVRMNP 770
Cdd:COG3383 632 RArVTDRVRPGTVFMPfhWGEGAaNALTNDALDPVSKQPEYKACAVRVEKVAE 684
|
|
| Fdh-alpha |
TIGR01591 |
formate dehydrogenase, alpha subunit, archaeal-type; This model describes a subset of formate ... |
117-763 |
2.00e-74 |
|
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: 255.08 E-value: 2.00e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 117 RITEPMRYDagSDKYLPVSWDEAFAEIGQELRQLS---DPWKLELYTSGRTSNEAAFLYQLFGR-LYGMANFPDCSNMCH 192
Cdd:TIGR01591 53 RLTTPLIRE--GDKFREVSWDEAISYIAEKLKEIKekyGPDSIGFIGSSRGTNEENYLLQKLARaVIGTNNVDNCARVCH 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 193 ETTSVALPESIGVGKGTTTLEDFENADAIFIFGQNPGTNSPRMMSELHAAARRGASIISFNPlREKALVRFASpqdprdm 272
Cdd:TIGR01591 131 GPSVAGLKQTVGIGAMSNTISEIENADLIVIIGYNPAESHPVVAQYLKNAKRNGAKIIVIDP-RKTETAKIAD------- 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 273 lsrsgvkissQYHQVRIGGDMIALQGICKVVIEaddaaqrEGLprvLDVAFIEEHTHGLEQFADYCRQLPWEIIERHSGL 352
Cdd:TIGR01591 203 ----------LHIPLKPGTDIALLNAMANVIIE-------EGL---YDKAFIEKRTEGFEEFREIVKGYTPEYVEDITGV 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 353 TRQALEEVAAVYMRSERVICCWGMGITQHKRGGDAMQQIINLLLLRGNIGKLGAGACPIRGHSNVQGDRTMGI------- 425
Cdd:TIGR01591 263 PADLIREAARMYAKAGSAAILWGMGVTQHSQGVETVMALINLAMLTGNIGKPGGGVNPLRGQNNVQGACDMGAlpdflpg 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 426 YEK-AGEPFLASMSKVFGFEA-SRKGGHDVAEACEALLRGEIEAFISMGGNFFRAIPDIDVVCPTVKRLKMTVLVNTKLN 503
Cdd:TIGR01591 343 YQPvSDEEVREKFAKAWGVVKlPAEPGLRIPEMIDAAADGDVKALYIMGEDPLQSDPNTSKVRKALEKLELLVVQDIFMT 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 504 RSAT-VHgqkaFLLPCIARSEldmQNGVaqTVTVEDSMSMVHGStgmLEPASKhLISEVAIIAGIAKATlapnpNVDWdS 582
Cdd:TIGR01591 423 ETAKyAD----VVLPAAAWLE---KEGT--FTNAERRIQRFFKA---VEPKGE-SKPDWEIIQELANAL-----GLDW-N 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 583 YvNDYARIRDKIEAVLPeQFYDFN-QRIKEPGGFRLPNGASER---------KWNTESGKANFLFPEGVFdEDDTPPGAD 652
Cdd:TIGR01591 484 Y-NHPQEIMDEIRELTP-LFAGLTyERLDELGSLQWPCNDSDAsptsylykdKFATPDGKAKFIPLEWVA-PIEEPDDEY 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 653 HLQLMTIRSHDQFNT-TVYSNDDRYRGIYGDRMvVMLNPQDIERLGLKAGDYVEFQTALDMT------TPRRAPGFKVIP 725
Cdd:TIGR01591 561 PLILTTGRVLTHYNVgEMTRRVAGLRRLSPEPY-VEINTEDAKKLGIKDGDLVKVKSRRGEItlrakvSDRVNKGAIYIT 639
|
650 660 670
....*....|....*....|....*....|....*...
gi 1524502542 726 FDvpqgccaAYYPETNgLLPLANRDSRSNTPAAKSIPV 763
Cdd:TIGR01591 640 MH-------FWDGAVN-NLTTDDLDPISGTPEYKYTAV 669
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
117-424 |
6.24e-59 |
|
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: 208.61 E-value: 6.24e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 117 RITEPMRYDagSDKYLPVSWDEAFAEIGQELRQLSD---PWKLELYTSGRTSNEAAFLYQLFGRLYGMANFPD-CSNMCH 192
Cdd:cd02753 54 RLTKPLIRK--NGKFVEASWDEALSLVASRLKEIKDkygPDAIAFFGSAKCTNEENYLFQKLARAVGGTNNVDhCARLCH 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 193 ETTSVALPESIGVGKGTTTLEDFENADAIFIFGQNPGTNSPRMMSELHAAARRGASIISFNPlREKALVRFASpqdprdm 272
Cdd:cd02753 132 SPTVAGLAETLGSGAMTNSIADIEEADVILVIGSNTTEAHPVIARRIKRAKRNGAKLIVADP-RRTELARFAD------- 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 273 lsrsgvkissQYHQVRIGGDMIALQGICKVVIEaddaaqrEGLprvLDVAFIEEHTHGLEQFADYCRQLPWEIIERHSGL 352
Cdd:cd02753 204 ----------LHLQLRPGTDVALLNAMAHVIIE-------EGL---YDEEFIEERTEGFEELKEIVEKYTPEYAERITGV 263
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1524502542 353 TRQALEEVAAVYMRSERVICCWGMGITQHKRGGDAMQQIINLLLLRGNIGKLGAGACPIRGHSNVQGDRTMG 424
Cdd:cd02753 264 PAEDIREAARMYATAKSAAILWGMGVTQHSHGTDNVMALSNLALLTGNIGRPGTGVNPLRGQNNVQGACDMG 335
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
91-410 |
2.23e-58 |
|
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: 203.33 E-value: 2.23e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 91 VTPEFFAQHTVSELATWSDHDledqgRITEPMRYDAGSDKYLPVSWDEAFAEIGQELRQLSD---PWKLELYTSGRTSNE 167
Cdd:cd00368 33 VNEGRLCDKGRAGLDGLYSPD-----RLKYPLIRVGGRGKFVPISWDEALDEIAEKLKEIREkygPDAIAFYGGGGASNE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 168 AAFLYQLFGRLYGMANFPDCSNMCHETTSVALPEsIGVGKGTTTLEDFENADAIFIFGQNPGTNSPRMMSELHAAARRGA 247
Cdd:cd00368 108 EAYLLQKLLRALGSNNVDSHARLCHASAVAALKA-FGGGAPTNTLADIENADLILLWGSNPAETHPVLAARLRRAKKRGA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 248 SIISFNPLREKalvrfaspqdprdmlsrsGVKISSQYHQVRIGGDMIALQGickvvieaddaaqreglprvldvafieeh 327
Cdd:cd00368 187 KLIVIDPRRTE------------------TAAKADEWLPIRPGTDAALALA----------------------------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 328 thgleqfadycrqlpwEIIERHSGLTRQALEEVAAVYMRSERVICCWGMGITQHKRGGDAMQQIINLLLLRGNIGKLGAG 407
Cdd:cd00368 220 ----------------EWAAEITGVPAETIRALAREFAAAKRAVILWGMGLTQHTNGTQNVRAIANLAALTGNIGRPGGG 283
|
...
gi 1524502542 408 ACP 410
Cdd:cd00368 284 LGP 286
|
|
| MopB_CT_ydeP |
cd02787 |
The MopB_CT_ydeP CD includes a group of related uncharacterized bacterial ... |
654-765 |
2.11e-57 |
|
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: 190.95 E-value: 2.11e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 654 LQLMTIRSHDQFNTTVYSNDDRYRGIYGDRMVVMLNPQDIERLGLKAGDYVEFQTALDMTTPRRAPGFKVIPFDVPQGCC 733
Cdd:cd02787 1 LFLVTTRSHDQFNTTIYGLDDRYRGVFGRRDVVFMNPDDIARLGLKAGDRVDLESAFGDGQGRIVRGFRVVEYDIPRGCL 80
|
90 100 110
....*....|....*....|....*....|..
gi 1524502542 734 AAYYPETNGLLPLANRDSRSNTPAAKSIPVNL 765
Cdd:cd02787 81 AAYYPEGNVLVPLDHRDPQSKTPAYKSVPVRL 112
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
115-497 |
6.51e-42 |
|
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: 161.62 E-value: 6.51e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 115 QGRITEPMrYDAGSDKYLPVSWDEAFAEIGQELRQLSD---PWKLELYTSGRTSNEAAFLYQLFGRLY-GMANFPDCSNM 190
Cdd:cd02754 52 PERLTRPL-LRRNGGELVPVSWDEALDLIAERFKAIQAeygPDSVAFYGSGQLLTEEYYAANKLAKGGlGTNNIDTNSRL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 191 CHETTSVALPESIGVGKGTTTLEDFENADAIFIFGQNPGTNSPRMMSEL--HAAARRGASIISFnplrekalvrfaspqD 268
Cdd:cd02754 131 CMASAVAGYKRSFGADGPPGSYDDIEHADCFFLIGSNMAECHPILFRRLldRKKANPGAKIIVV---------------D 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 269 PRdmlsRSGV-KISSQYHQVRIGGDMIALQGICKVVIEaddaaqrEGLprvLDVAFIEEHTHGLEQFADYCRQLPWEIIE 347
Cdd:cd02754 196 PR----RTRTaDIADLHLPIRPGTDLALLNGLLHVLIE-------EGL---IDRDFIDAHTEGFEELKAFVADYTPEKVA 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 348 RHSGLTRQALEEVAAVYMRSERVICCWGMGITQHKRGGDAMQQIINLLLLRGNIGKLGAGACPIRGHSNVQGDRTMGIY- 426
Cdd:cd02754 262 EITGVPEADIREAARLFGEARKVMSLWTMGVNQSTQGTAANNAIINLHLATGKIGRPGSGPFSLTGQPNAMGGREVGGLa 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 427 -------EKAGEPFLASMSKVFGFEASR---KGGHDVAEACEALLRGEIEAFISMGGNFFRAIPDIDVVCPTVKRLKMTV 496
Cdd:cd02754 342 nllpghrSVNNPEHRAEVAKFWGVPEGTippKPGLHAVEMFEAIEDGEIKALWVMCTNPAVSLPNANRVREALERLEFVV 421
|
.
gi 1524502542 497 L 497
Cdd:cd02754 422 V 422
|
|
| MopB_Formate-Dh-Na-like |
cd02752 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
117-425 |
5.91e-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: 129.44 E-value: 5.91e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 117 RITEPMRYDAGSDKYLPVSWDEAFAEIGQELRQLSDPWKLELYTSGRT---------------SNEAAFLYQLFGRLYGM 181
Cdd:cd02752 54 RLKYPMYRAPGSGKWEEISWDEALDEIARKMKDIRDASFVEKNAAGVVvnrpdsiaflgsaklSNEECYLIRKFARALGT 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 182 ANFPDCSNMCHETTSVALPESIGVGKGTTTLEDFENADAIFIFGQNPGTNSPRMMSE-LHAAARRGASIISFnplrekal 260
Cdd:cd02752 134 NNLDHQARIUHSPTVAGLANTFGRGAMTNSWNDIKNADVILVMGGNPAEAHPVSFKWiLEAKEKNGAKLIVV-------- 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 261 vrfaspqDPRdmLSRSGVKiSSQYHQVRIGGDMIALQGICKVVIE--ADDAAQREGLPRvldvafieehthglEQFADYC 338
Cdd:cd02752 206 -------DPR--FTRTAAK-ADLYVPIRSGTDIAFLGGMINYIIRytPEEVEDICGVPK--------------EDFLKVA 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 339 rqlpweiierhsgltrqalEEVAAVYMRSERVICCWGMGITQHKRGgdamQQIIN----LLLLRGNIGKLGAGACPIRGH 414
Cdd:cd02752 262 -------------------EMFAATGRPDKPGTILYAMGWTQHTVG----SQNIRamciLQLLLGNIGVAGGGVNALRGH 318
|
330
....*....|.
gi 1524502542 415 SNVQGDRTMGI 425
Cdd:cd02752 319 SNVQGATDLGL 329
|
|
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
117-408 |
2.59e-25 |
|
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: 110.42 E-value: 2.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 117 RITEPMRYD-AGSDKYLPVSWDEAFAEIGQELRQLSDPWKLE--LYTSGrtSNEAAFLYQLF-GRLYGMANfpdcsnmch 192
Cdd:cd02766 55 RLLTPLKRVgRKGGQWERISWDEALDTIAAKLKEIKAEYGPEsiLPYSY--AGTMGLLQRAArGRFFHALG--------- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 193 ettSVALPESIGVGKGTTTL------------EDFENADAIFIFGQNPGTNSPRMMSELHAAARRGASIISFNPLREKAl 260
Cdd:cd02766 124 ---ASELRGTICSGAGIEAQkydfgaslgndpEDMVNADLIVIWGINPAATNIHLMRIIQEARKRGAKVVVIDPYRTAT- 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 261 vrfaspqdprdmlsrsgVKISSQYHQVRIGGD-MIALqGICKVVIeaddaaqREGLprvLDVAFIEEHTHGLEQFADYCR 339
Cdd:cd02766 200 -----------------AARADLHIQIRPGTDgALAL-GVAKVLF-------REGL---YDRDFLARHTEGFEELKAHLE 251
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1524502542 340 QLPWEIIERHSGLTRQALEEVAAVYMRSERVICCWGMGITQHKRGGDAMQQIINLLLLRGNIGKLGAGA 408
Cdd:cd02766 252 TYTPEWAAEITGVSAEEIEELARLYGEAKPPSIRLGYGMQRYRNGGQNVRAIDALPALTGNIGVPGGGA 320
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
117-407 |
4.72e-21 |
|
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: 97.38 E-value: 4.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 117 RITEPMRY--DAGSDKYLPVSWDEAFAEIGQELRQLSDPWKLE----LYTSGRTSNEAAFLYQLFG-RLYGMANFPDCSN 189
Cdd:cd02759 54 RLLYPLKRvgERGENKWERISWDEALDEIAEKLAEIKAEYGPEsiatAVGTGRGTMWQDSLFWIRFvRLFGSPNLFLSGE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 190 MCHETTSVALPESIGVGKGTTTLeDFENADAIFIFGQNPG-TNSPRMMSELHAAARRGASIISFnplrekalvrfaspqD 268
Cdd:cd02759 134 SCYWPRDMAHALTTGFGLGYDEP-DWENPECIVLWGKNPLnSNLDLQGHWLVAAMKRGAKLIVV---------------D 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 269 PRdmlsRSGVKISSQYH-QVRIGGD-MIALqGICKVVIEaddaaqrEGLprvLDVAFIEEHTHGLEQFADYCRQLPWEII 346
Cdd:cd02759 198 PR----LTWLAARADLWlPIRPGTDaALAL-GMLNVIIN-------EGL---YDKDFVENWCYGFEELAERVQEYTPEKV 262
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1524502542 347 ERHSGLTRQALEEVAAVYMRSERVICCWGMGITQHKRGGDAMQQIINLLLLRGNIGKLGAG 407
Cdd:cd02759 263 AEITGVPAEKIRKAARLYATAKPACIQWGLAIDQQKNGTQTSRAIAILRAITGNLDVPGGN 323
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
113-410 |
1.18e-18 |
|
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: 90.15 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 113 EDQGRITEPMRYDAGSdkYLPVSWDEAFAEIGQELRQLSD---PWKLELYTSGRTSNEAA-------FLYQLFGRLYGMA 182
Cdd:cd02762 50 NDPDRLRTPMRRRGGS--FEEIDWDEAFDEIAERLRAIRArhgGDAVGVYGGNPQAHTHAggayspaLLKALGTSNYFSA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 183 NFPDcsNMCHETTSVALPESigvgKGTTTLEDFENADAIFIFGQNP--GTNSPRMMSE----LHAAARRGASIISFNPLR 256
Cdd:cd02762 128 ATAD--QKPGHFWSGLMFGH----PGLHPVPDIDRTDYLLILGANPlqSNGSLRTAPDrvlrLKAAKDRGGSLVVIDPRR 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 257 -EKAlvrfaspqdprdmlsrsgvKISSQYHQVRIGGDMIALQGICKVVIEaddaaqrEGLprvLDVAFIEEHTHGLEQFA 335
Cdd:cd02762 202 tETA-------------------KLADEHLFVRPGTDAWLLAAMLAVLLA-------EGL---TDRRFLAEHCDGLDEVR 252
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1524502542 336 DYCRQLPWEIIERHSGLTRQALEEVAAVYMRSERVICCWGMGItQHKRGGDAMQQIINLL-LLRGNIGKLGAGACP 410
Cdd:cd02762 253 AALAEFTPEAYAPRCGVPAETIRRLAREFAAAPSAAVYGRLGV-QTQLFGTLCSWLVKLLnLLTGNLDRPGGAMFT 327
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
114-413 |
4.16e-18 |
|
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: 87.74 E-value: 4.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 114 DQGRITEPM-RYDA-GSDKYLPVSWDEAFAEIGQELRQLSD--PWKLELYTSGRTSNEAAFlyQLFGRLYGMANFpdCSN 189
Cdd:cd02755 52 DPDRLKKPLiRVGErGEGKFREASWDEALQYIASKLKEIKEqhGPESVLFGGHGGCYSPFF--KHFAAAFGSPNI--FSH 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 190 MCHETTSVALP-ESIGVGKGTTTLEDFENADAIFIFGQN--PGTNSPRMMsELHAAARRGASIISFnplrekalvrfasp 266
Cdd:cd02755 128 ESTCLASKNLAwKLVIDSFGGEVNPDFENARYIILFGRNlaEAIIVVDAR-RLMKALENGAKVVVV-------------- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 267 qDPRdmLSRSGVKiSSQYHQVRIGGDMIALQGICKVVIeaddaaqREGLprvLDVAFIEEHTHGLEQFADYCRQLPWEII 346
Cdd:cd02755 193 -DPR--FSELASK-ADEWIPIKPGTDLAFVLALIHVLI-------SENL---YDAAFVEKYTNGFELLKAHVKPYTPEWA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 347 ERHSGLTRQALEEVAAVYMRSERViccwGMGITQHK--RGGDAMQQ-----IINLLLlrGNIGKLG-------AGACPIR 412
Cdd:cd02755 259 AQITDIPADTIRRIAREFAAAAPH----AVVDPGWRgtFYSNSFQTrraiaIINALL--GNIDKRGglyyagsAKPYPIK 332
|
.
gi 1524502542 413 G 413
Cdd:cd02755 333 A 333
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
117-496 |
1.33e-16 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 82.06 E-value: 1.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 117 RITEPMrYDAGSDKYLPVSWDEAFAEIGQELRQL-----SDPWKLELYTSGRTSNEAAFLYQLFGRLYGMANF---PDCS 188
Cdd:pfam00384 1 RLKYPM-VRRGDGKFVRVSWDEALDLIAKKLKRIikkygPDAIAINGGSGGLTDVESLYALKKLLNRLGSKNGnteDHNG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 189 NMCHETTSVALPESIGVGKGTTTLEDFENADAIFIFGQNPGTNSPRMMSELHAAARRG-ASIISFNPlrekalvRFASpq 267
Cdd:pfam00384 80 DLCTAAAAAFGSDLRSNYLFNSSIADIENADLILLIGTNPREEAPILNARIRKAALKGkAKVIVIGP-------RLDL-- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 268 dprdmlsrsgvKISSQYHQVRIGGDMIALQGICKVVIEADDAAQreglprvldvafiEEHTHGLeqfadycrqlpweIIe 347
Cdd:pfam00384 151 -----------TYADEHLGIKPGTDLALALAGAHVFIKELKKDK-------------DFAPKPI-------------II- 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 348 rhsgltrqaleevaavymrserviccWGMGITQHKRGGDAMQQIINLLLLRGNIGKLGAGACPIRghsNVQGDRtmgiye 427
Cdd:pfam00384 193 --------------------------VGAGVLQRQDGEAIFRAIANLADLTGNIGRPGGGWNGLN---ILQGAA------ 237
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1524502542 428 kagepflasmSKVFGFEASRKGGHDVAEACEALLRGEIEAFISMGGNFFRAIPDIDVVCPTVKRLKMTV 496
Cdd:pfam00384 238 ----------SPVGALDLGLVPGIKSVEMINAIKKGGIKVLYLLGNNPFVTHADENRVVKALQKLDLFV 296
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
127-476 |
2.24e-14 |
|
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: 76.88 E-value: 2.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 127 GSDKYLPVSWDEAFAEIGQELRQLSDpwklelyTSGrtsNEAAFLYQLFGRLYGmaNFPDCSNMCHE------------- 193
Cdd:cd02751 69 GEGEFVRISWDEALDLVASELKRIRE-------KYG---NEAIFGGSYGWASAG--RLHHAQSLLHRflnliggylgsyg 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 194 TTS-----VALPESIG---VGKGTTTLED-FENADAIFIFGQNPGTNSP--------RMMSELHAAARRGASIISFNPLR 256
Cdd:cd02751 137 TYStgaaqVILPHVVGsdeVYEQGTSWDDiAEHSDLVVLFGANPLKTRQgggggpdhGSYYYLKQAKDAGVRFICIDPRY 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 257 EKALVRFASPQDPrdmlsrsgvkissqyhqVRIGGDmIALQ-GICKVVIEaddaaqrEGLprvLDVAFIEEHTHGLEQFA 335
Cdd:cd02751 217 TDTAAVLAAEWIP-----------------IRPGTD-VALMlAMAHTLIT-------EDL---HDQAFLARYTVGFDEFK 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 336 DYCRQLP--------W--EIierhSGLTRQALEEVAAVYMRSERVICCwGMGITQHKRGGDAMQQIINLLLLRGNIGKLG 405
Cdd:cd02751 269 DYLLGESdgvpktpeWaaEI----TGVPAETIRALAREIASKRTMIAQ-GWGLQRAHHGEQPAWMLVTLAAMLGQIGLPG 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 406 AGACPIRGHSNVQGDRTMGIyekagepflasmsKVFGFEASRKGGHD---VAEACEALLRG--------------EIEAF 468
Cdd:cd02751 344 GGFGFGYGYSNGGGPPRGGA-------------GGPGLPQGKNPVKDsipVARIADALLNPgkeftangklktypDIKMI 410
|
....*...
gi 1524502542 469 ISMGGNFF 476
Cdd:cd02751 411 YWAGGNPL 418
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
112-405 |
3.86e-14 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 76.24 E-value: 3.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 112 LEDQGRITEPMRY--DAGSDKYLPVSWDEAFAEIGQELRQLSDPWKLELYT----SGRTSNEAAFLYQLFGRlygmanfP 185
Cdd:PRK15488 93 LYDPQRIVKPLKRvgERGEGKWQEISWDEAYQEIAAKLNAIKQQHGPESVAfsskSGSLSSHLFHLATAFGS-------P 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 186 DCsnMCHETTSvalPESIGVGK----GTTTLEDFENADAIFIFGQN--PGTNsprmMSELH----AAARRGASIISFNPl 255
Cdd:PRK15488 166 NT--FTHASTC---PAGYAIAAkvmfGGKLKRDLANSKYIINFGHNlyEGIN----MSDTRglmtAQMEKGAKLVVFEP- 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 256 rekalvRFASPQDPRDmlsrsgvkissQYHQVRIGGDMIALQGICKVVIEaddaaqrEGLprvLDVAFIEEHTHGLEQFA 335
Cdd:PRK15488 236 ------RFSVVASKAD-----------EWHAIRPGTDLAVVLALCHVLIE-------ENL---YDKAFVERYTSGFEELA 288
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1524502542 336 DYCRQLPWEIIERHSGLTRQALEEVAA-VYMRSERVICCWGMGITQHKRGGDAMQQIINLLLLRGNIGKLG 405
Cdd:PRK15488 289 ASVKEYTPEWAEAISDVPADDIRRIAReLAAAAPHAIVDFGHRATFTPEEFDMRRAIFAANVLLGNIERKG 359
|
|
| MopB_CT |
cd02775 |
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a ... |
661-759 |
3.67e-12 |
|
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: 63.11 E-value: 3.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 661 SHDQFNTTVYSNDDRYRGIYGdRMVVMLNPQDIERLGLKAGDYVEFqtaldmTTPRRAPGFKVIPFD-VPQGCCAAYYP- 738
Cdd:cd02775 1 LRDHFHSGTRTRNPWLRELAP-EPVVEINPEDAAALGIKDGDLVRV------ESRRGSVVLRAKVTDgVPPGVVFLPHGw 73
|
90 100
....*....|....*....|....*....
gi 1524502542 739 --------ETNGLLPLAnRDSRSNTPAAK 759
Cdd:cd02775 74 ghrggrggNANVLTPDA-LDPPSGGPAYK 101
|
|
| 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 ... |
117-484 |
4.34e-12 |
|
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: 68.95 E-value: 4.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 117 RITEPMRydAGSDKYLPVSWDEAFAEIGQELRQLSDpwKLELYTSGRTSNEAAFLYQLFGRLY-GMANFpDCSNMCHett 195
Cdd:cd02771 54 RLTQPLI--RRGGTLVPVSWNEALDVAAARLKEAKD--KVGGIGSPRASNESNYALQKLVGAVlGTNNV-DHRARRL--- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 196 svaLPESIGVGKG-TTTLEDFENADAIFIFGQNPGTNSPRMMSELHAAARRgasiisfNPLREKALVRFASPQDPrdmls 274
Cdd:cd02771 126 ---IAEILRNGPIyIPSLRDIESADAVLVLGEDLTQTAPRIALALRQAARR-------KAVELAALSGIPKWQDA----- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 275 rsGVKISSQYHQVRIggdmialqgickVVIEADDAAQREGLPR--VLDVAFIEEHTHGLeqfaDYCrqLPWEIIERHSGL 352
Cdd:cd02771 191 --AVRNIAQGAKSPL------------FIVNALATRLDDIAAEsiRASPGGQARLGAAL----ARA--VDASAAGVSGLA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 353 TRQALEEVAAVYMRSERVICCWGmgitQHKRGGDAMQQIINLLLLRGNIGKLGAgacpirghsnvqgdrTMGIYEKAGEP 432
Cdd:cd02771 251 PKEKAARIAARLTGAKKPLIVSG----TLSGSLELIKAAANLAKALKRRGENAG---------------LTLAVEEGNSP 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1524502542 433 FLASMskvfgFEASRKGGHDVAEACEALLRGEIEAFISMGGNFFRAIPDIDV 484
Cdd:cd02771 312 GLLLL-----GGHVTEPGLDLDGALAALEDGSADALIVLGNDLYRSAPERRV 358
|
|
| MopB_NADH-Q-OR-NuoG2 |
cd02768 |
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone ... |
117-255 |
4.11e-11 |
|
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone oxidoreductase (NADH-Q-OR)/respiratory complex I/NADH dehydrogenase-1 (NDH-1). The NADH-Q-OR is the first energy-transducting complex in the respiratory chains of many prokaryotes and eukaryotes. Mitochondrial complex I and its bacterial counterpart, NDH-1, function as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. The atomic structure of complex I is not known and the mechanisms of electron transfer and proton pumping are not established. The nad11 gene codes for the largest (75-kDa) subunit of the mitochondrial NADH:ubiquinone oxidoreductase, it constitutes the electron input part of the enzyme, or the so-called NADH dehydrogenase fragment. In Escherichia coli, this subunit is encoded by the nuoG gene, and is part of the 14 distinct subunits constituting the 'minimal' functional enzyme. The nad11 gene is nuclear-encoded in animals, plants, and fungi, but is still encoded in the mitochondrial genome of some protists. The Nad11/NuoG subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain family belongs to the molybdopterin_binding (MopB) superfamily of proteins. Bacterial type II NADH-quinone oxidoreductases and NQR-type sodium-motive NADH-quinone oxidoreductases are not homologs of this domain family.
Pssm-ID: 239169 [Multi-domain] Cd Length: 386 Bit Score: 65.77 E-value: 4.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 117 RITEPM-RydaGSDKYLPVSWDEAFAEIGQELrQLSDPWKLELYTSGRTSNEAAFLYQ-LFGRLygmanfpDCSNMCHET 194
Cdd:cd02768 54 RLTQPLiK---KGGKLVPVSWEEALKTVAEGL-KAVKGDKIGGIAGPRADLESLFLLKkLLNKL-------GSNNIDHRL 122
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1524502542 195 TSVALPESIGVGKG---TTTLEDFENADAIFIFGQNPGTNSPRMMSELHAAARR-GASIISFNPL 255
Cdd:cd02768 123 RQSDLPADNRLRGNylfNTSIAEIEEADAVLLIGSNLRKEAPLLNARLRKAVKKkGAKIAVIGPK 187
|
|
| Molydop_binding |
pfam01568 |
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
654-762 |
7.45e-11 |
|
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: 59.59 E-value: 7.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 654 LQLMTIRSHDQFNTTVYSNDDRYRGIyGDRMVVMLNPQDIERLGLKAGDYVEfqtaldMTTPRRAPGFKVIPFD-VPQGC 732
Cdd:pfam01568 1 LYLITGRVLGQYHSQTRTRRVLRLAK-PEPEVVEIHPEDAAALGIKDGDLVE------VTSRRGSVVVRAKVTDrVRPGV 73
|
90 100 110
....*....|....*....|....*....|....*...
gi 1524502542 733 CAAYYPE--------TNgLLPLANRDSRSNTPAAKSIP 762
Cdd:pfam01568 74 VFMPFGWwyeprggnAN-ALTDDATDPLSGGPEFKTCA 110
|
|
| MopB_DmsA-EC |
cd02770 |
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
117-419 |
1.58e-10 |
|
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: 64.65 E-value: 1.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 117 RITEPMRY--DAGSDKYLPVSWDEAFAEIGQELRQLSDPWKLEL----YTSGRT------SNEAAFLYQLFG---RLYG- 180
Cdd:cd02770 59 RLKYPMKRvgKRGEGKFVRISWDEALDTIASELKRIIEKYGNEAiyvnYGTGTYggvpagRGAIARLLNLTGgylNYYGt 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 181 --MANFPDcsnmchettsvALPESIGVGKGTTTLEDFENADAIFIFGQNPGTNSprmMS------ELHAAARRGASIISF 252
Cdd:cd02770 139 ysWAQITT-----------ATPYTYGAAASGSSLDDLKDSKLVVLFGHNPAETR---MGgggstyYYLQAKKAGAKFIVI 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 253 nplrekalvrfaspqDPRdmLSRSGVKISSQYHQVRIGGDMIALQGICKVVIEaddaaqrEGLprvLDVAFIEEHTHGL- 331
Cdd:cd02770 205 ---------------DPR--YTDTAVTLADEWIPIRPGTDAALVAAMAYVMIT-------ENL---HDQAFLDRYCVGFd 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 332 -----------EQFADYCRQLPW-------EIIERHSGLTRQALEEVAAVYMRSERVICCWGMGITQHKRGGDAMQQIIN 393
Cdd:cd02770 258 aehlpegappnESYKDYVLGTGYdgtpktpEWASEITGVPAETIRRLAREIATTKPAAILQGWGPQRHANGEQAARAIMM 337
|
330 340
....*....|....*....|....*.
gi 1524502542 394 LLLLRGNIGKLGAGACPIRGHSNVQG 419
Cdd:cd02770 338 LAAMTGNVGIPGGNTGARPGGSAYNG 363
|
|
| MopB_Arsenate-R |
cd02757 |
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ... |
114-413 |
9.04e-10 |
|
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: 62.07 E-value: 9.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 114 DQGRITEPMR------YDAGSDKYLPVSWDEAFAEIGQELRQL---SDPWKLeLYTSGRTSNEAAFLYQLFGRLYGMANF 184
Cdd:cd02757 53 DPDRILYPMKrtnprkGRDVDPKFVPISWDEALDTIADKIRALrkeNEPHKI-MLHRGRYGHNNSILYGRFTKMIGSPNN 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 185 PDCSNMCHETTSVAlPESIGVGKGTTTLeDFENADAIFIFGQNP------GTNSPRMMSELhaaaRRGASIISFnplrek 258
Cdd:cd02757 132 ISHSSVCAESEKFG-RYYTEGGWDYNSY-DYANAKYILFFGADPlesnrqNPHAQRIWGGK----MDQAKVVVV------ 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 259 alvrfaspqDPRdmLSRSGVKiSSQYHQVRIGGDMIALQGICKVVIEAD-----------DAAQ--REGLPrVLDVAFIE 325
Cdd:cd02757 200 ---------DPR--LSNTAAK-ADEWLPIKPGEDGALALAIAHVILTEGlwdkdfvgdfvDGKNyfKAGET-VDEESFKE 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 326 EHTHGLEQF--ADYCRQLPwEIIERHSGLTRQALEEVAAVYMRSE-RVICCWGMGITQHKRGGDAMQQIINLLLLRGNIG 402
Cdd:cd02757 267 KSTEGLVKWwnLELKDYTP-EWAAKISGIPAETIERVAREFATAApAAAAFTWRGATMQNRGSYNSMACHALNGLVGSID 345
|
330
....*....|.
gi 1524502542 403 KLGaGACPIRG 413
Cdd:cd02757 346 SKG-GLCPNMG 355
|
|
| MopB_2 |
cd02763 |
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
117-405 |
9.27e-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: 59.07 E-value: 9.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 117 RITEPMRY--DAGSDKYLPVSWDEAFAEIGQELRQL--SDPWKLELYTsGRTSNEAafLYQLFGRLYGMANFPDCSNMCH 192
Cdd:cd02763 54 RLTKPLLRkgPRGSGQFEEIEWEEAFSIATKRLKAAraTDPKKFAFFT-GRDQMQA--LTGWFAGQFGTPNYAAHGGFCS 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 193 ETTSVALPESIGVGKGTTTLEDFENADAIFIFGQNPGTNSPRMMSELHAAARRGASIISFNPLREkalvrfaspqdprdm 272
Cdd:cd02763 131 VNMAAGGLYSIGGSFWEFGGPDLEHTKYFMMIGVAEDHHSNPFKIGIQKLKRRGGKFVAVNPVRT--------------- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 273 lsrSGVKISSQYHQVRIGGDMIALQGICKVVIEADdaaqreglprVLDVAFIEEHTHGLEqFADYCrqlPwEIIERHSGL 352
Cdd:cd02763 196 ---GYAAIADEWVPIKPGTDGAFILALAHELLKAG----------LIDWEFLKRYTNAAE-LVDYT---P-EWVEKITGI 257
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1524502542 353 TRQALEEVA------AVYMRSERVIC---CWGM----------------GITQHKRGGDAMQQIINLLLLRGNIGKLG 405
Cdd:cd02763 258 PADTIRRIAkelgvtARDQPIELPIAwtdVWGRkhekitgrpvsfhamrGIAAHSNGFQTIRALFVLMMLLGTIDRPG 335
|
|
| MopB_Res-Cmplx1_Nad11 |
cd02773 |
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone ... |
117-233 |
1.09e-06 |
|
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone oxidoreductase/respiratory complex I/NADH dehydrogenase-1(NDH-1) of eukaryotes and the Nqo3/G subunit of alphaproteobacteria NDH-1. The NADH-quinone oxidoreductase is the first energy-transducting complex in the respiratory chains of many prokaryotes and eukaryotes. Mitochondrial complex I and its bacterial counterpart, NDH-1, function as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. The nad11 gene codes for the largest (75 kDa) subunit of the mitochondrial NADH:ubiquinone oxidoreductase, it constitutes the electron input part of the enzyme, or the so-called NADH dehydrogenase fragment. In Paracoccus denitrificans, this subunit is encoded by the nqo3 gene, and is part of the 14 distinct subunits constituting the 'minimal' functional enzyme. The Nad11/Nqo3 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: 239174 [Multi-domain] Cd Length: 375 Bit Score: 51.50 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 117 RITEPM-RydaGSDKYLPVSWDEAFAEIGQELRQlSDPWKLELYTSGRTSNEAAF-LYQLFGRLygmanfpDCSNMCHET 194
Cdd:cd02773 53 RLDKPYiR---KNGKLKPATWEEALAAIAKALKG-VKPDEIAAIAGDLADVESMVaLKDLLNKL-------GSENLACEQ 121
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1524502542 195 TSVALPESIGVGK-GTTTLEDFENADAIFIFGQNPGTNSP 233
Cdd:cd02773 122 DGPDLPADLRSNYlFNTTIAGIEEADAVLLVGTNPRFEAP 161
|
|
| MopB_FmdB-FwdB |
cd02761 |
The MopB_FmdB-FwdB CD contains the molybdenum/tungsten formylmethanofuran dehydrogenases, ... |
117-419 |
3.62e-05 |
|
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: 46.94 E-value: 3.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 117 RITEPMRydAGSdkylPVSWDEAF---AEIGQELRQlsdPWkleLYTSGRTSNEA-AFLYQLFGRLYGManFPDCSNMCH 192
Cdd:cd02761 43 RITTPRI--DGK----PVSLEEAIekaAEILKEAKR---PL---FYGLGTTVCEAqRAGIELAEKLGAI--IDHAASVCH 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 193 ETTSVALPESigvGKGTTTLEDFEN-ADAIFIFGQNPGTNSPRMMSelhaaaRRgasiiSFNPlreKALVRFASPQDpRD 271
Cdd:cd02761 109 GPNLLALQDS---GWPTTTLGEVKNrADVIVYWGTNPMHAHPRHMS------RY-----SVFP---RGFFREGGRED-RT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 272 MlsrsgvkissqyhqVRIGGDMIALQGICKVVIEADDAAQREGLPRVLDVAfieeHTHGLEqfadycrqlpweiIERHSG 351
Cdd:cd02761 171 L--------------IVVDPRKSDTAKLADIHLQIDPGSDYELLAALRALL----RGAGLV-------------PDEVAG 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1524502542 352 LTRQALEEVAAVYMRSERVICCWGMGITQhkrGGDAMQQIINLLLLrgnIGKLG----AGACPIRGHSNVQG 419
Cdd:cd02761 220 IPAETILELAERLKNAKFGVIFWGLGLLP---SRGAHRNIEAAIRL---VKALNeytkFALLPLRGHYNVRG 285
|
|
| FwdB |
COG1029 |
Formylmethanofuran dehydrogenase subunit B [Energy production and conversion]; |
116-472 |
4.22e-05 |
|
Formylmethanofuran dehydrogenase subunit B [Energy production and conversion];
Pssm-ID: 440652 [Multi-domain] Cd Length: 428 Bit Score: 46.76 E-value: 4.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 116 GRITEPMRydagsdKYLPVSWDEAFAEIGQELRQLSDPWkleLYTSGRTSNEAA-FLYQLfGRLYGmANFPDCSNMCHET 194
Cdd:COG1029 50 HRITSPRI------RGKEVSLEEAIDKAAEILANAKRPL---IYGLSSTDCEAMrAGLAL-AERVG-AVVDNTASVCHGP 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 195 TSVALPEsigVGKGTTTLEDFEN-ADAIFIFGQNPGTNSPRMMSelhaaaRRGASIISF---NPLREKALVRFaspqDPR 270
Cdd:COG1029 119 SLLALQD---VGWPTCTLGEVKNrADVIIYWGCNPVHAHPRHMS------RYSVFPRGFftpKGRKDRTVIVV----DPR 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 271 dmlsRSG-VKISSQYHQVRIGGDmialqgickvvieaddaaqreglPRVLDV--AFIEEHThgleqfadycrqlpwEIIE 347
Cdd:COG1029 186 ----PTDtAKVADLHLQVKPGRD-----------------------YEVLSAlrALVRGKE---------------LSPE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 348 RHSGLTRQALEEVAAVyMRSER-VICCWGMGITqHKRGGDA-MQQIINLLLLRGNIGKLGAGacPIRGHSNVQG-DRTMG 424
Cdd:COG1029 224 EVAGIPVEDLEELAER-LKNAKyGVIFWGMGLT-QSPGKHLnVDAAIELVRDLNRYTKFSIL--PLRGHYNVAGaNQVAS 299
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1524502542 425 -IYekaGEPFLASMSKVFGFeasrkggHDVAE--ACEALLRGEIEAFISMG 472
Cdd:COG1029 300 wQT---GYPFRVDFSRGYPR-------YNPGEtsAVDLLARGEVDALLWVA 340
|
|
| PRK13532 |
PRK13532 |
nitrate reductase catalytic subunit NapA; |
117-408 |
1.78e-04 |
|
nitrate reductase catalytic subunit NapA;
Pssm-ID: 237416 [Multi-domain] Cd Length: 830 Bit Score: 45.27 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 117 RITEPM-RYDAGS-DK---YLPVSWDEAFAEIGQELRQL---SDPWKLELYTSGR-TSNE---AAFLYQlfgrlygmANF 184
Cdd:PRK13532 97 RLTQPLlRMKDGKyDKegeFTPVSWDQAFDVMAEKFKKAlkeKGPTAVGMFGSGQwTIWEgyaASKLMK--------AGF 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 185 PdcSN-------MCHETTSVALPESIGVGKGTTTLEDFENADAIFIFGQNpgtnsprmMSELHaaarrgasiisfnPlre 257
Cdd:PRK13532 169 R--SNnidpnarHCMASAVVGFMRTFGIDEPMGCYDDIEAADAFVLWGSN--------MAEMH-------------P--- 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 258 kalVRFASPQDPRdmLSRSGVKI---SSQYHQ----------VRIGGDMIALQGICKVVIEADdaaqreglpRVlDVAFI 324
Cdd:PRK13532 223 ---ILWSRVTDRR--LSNPDVKVavlSTFEHRsfeladngiiFTPQTDLAILNYIANYIIQNN---------AV-NWDFV 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 325 EEHT----------------HGLEQ---------------FADYCRQL-PW--EIIERHSGLTRQALEEVAAVYMRSER- 369
Cdd:PRK13532 288 NKHTnfrkgatdigyglrptHPLEKaaknpgtagksepisFEEFKKFVaPYtlEKTAKMSGVPKEQLEQLAKLYADPNRk 367
|
330 340 350
....*....|....*....|....*....|....*....
gi 1524502542 370 VICCWGMGITQHKRGGDAMQQIINLLLLRGNIGKLGAGA 408
Cdd:PRK13532 368 VVSFWTMGFNQHTRGVWANNLVYNIHLLTGKISTPGNGP 406
|
|
| PRK14991 |
PRK14991 |
tetrathionate reductase subunit TtrA; |
641-708 |
4.91e-04 |
|
tetrathionate reductase subunit TtrA;
Pssm-ID: 237883 [Multi-domain] Cd Length: 1031 Bit Score: 43.83 E-value: 4.91e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1524502542 641 VFDEDDTPpgadhLQLMTIRSHDQFNTTVYSndDRYRGIYGDRMVVMlNPQDIERLGLKAGDYVEFQT 708
Cdd:PRK14991 881 QFPESQWP-----LLLISFKSNLMSSMSIAS--PRLRQVKPANPVAL-NPQDAARLGIQHGDRVRIST 940
|
|
| MopB_CT_1 |
cd02782 |
The MopB_CT_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
660-767 |
1.67e-03 |
|
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: 39.30 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 660 RSHDQFNTTVYSNDDRYRGIyGDRMVVMLNPQDIERLGLKAGDYVEFQTALDMT------TPRRAPGFKVIP----FDVP 729
Cdd:cd02782 10 RRHLRSNNSWLHNDPRLVKG-RNRCTLRIHPDDAAALGLADGDKVRVTSAAGSVeaevevTDDMMPGVVSLPhgwgHDYP 88
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1524502542 730 QGCCAA--YYPETNGLLPLANRDSRSNTPAAKSIPVNLVR 767
Cdd:cd02782 89 GVSGAGsrPGVNVNDLTDDTQRDPLSGNAAHNGVPVRLAR 128
|
|
| MopB_4 |
cd02765 |
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
89-254 |
3.05e-03 |
|
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: 40.93 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 89 KRVTPEFFAQHTVSELATWSDHDLE---DQGRITEPMRY--DAGSDKYLPVSWDEAFAEIGQELRQLSDPW--KLELYTS 161
Cdd:cd02765 24 VKVEPNEWPDKTYKRGCTRGLSHLQrvySPDRLKYPMKRvgERGEGKFERITWDEALDTIADKLTEAKREYggKSILWMS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524502542 162 GrtSNEAAFLYQLFGRLYGmANFPDcsnmcHETTSVALPESIGV--------GKGTTTLEDFENADAIFIFGQNPGTNSp 233
Cdd:cd02765 104 S--SGDGAILSYLRLALLG-GGLQD-----ALTYGIDTGVGQGFnrvtgggfMPPTNEITDWVNAKTIIIWGSNILETQ- 174
|
170 180
....*....|....*....|....
gi 1524502542 234 rmMSELH---AAARRGASIISFNP 254
Cdd:cd02765 175 --FQDAEfflDARENGAKIVVIDP 196
|
|
| |
