|
Name |
Accession |
Description |
Interval |
E-value |
| Fdhalpha-like |
TIGR01701 |
oxidoreductase alpha (molybdopterin) subunit; This model represents a well-defined clade of ... |
38-764 |
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: 943.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 38 KNLRALLKTNQNGGFDCPGCAWGDSPEDGR-VKFCENGAKAVNWEATKRRVDAAFFARYSVSALREQSDYWLEYQGRLTG 116
Cdd:TIGR01701 23 QTLKLLLTLNKPEGYDCPGCAWGVSPQTLAgLEFCENGAKAIAWETTPRTIDPEFFAEHSVSELRTLDSHELEKLGRLTY 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 117 PMRYDPLSDHYQPITWDAAFALVAEHLRRLDsPDQAEFYTSGRASNEAAYLYQLFVRAFGTNNFPDCSNMCHEASGVALG 196
Cdd:TIGR01701 103 PLSLRPGSDHYTPISWDDAYQEIAAKLNSLD-PKQVAFYTSGRTSNEAAYLYQLFARSLGSNNLPDCSNMCHEPSSVALK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 197 RSVGVGKGSVTFDDFEHADAIFILGQNPGTNHPRMLEPLREAVKRGAQVVCFNPLKERGLERFQHPQNALEMLTNGSSPL 276
Cdd:TIGR01701 182 RSIGIGKGSVNLEDFEHTDCLVFIGSNAGTNHPRMLKYLYAAKKRGAKIIAINPLRERGLERFWIPQIPESMLTGGGTQI 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 277 NTAFFRPALGGDMAAIRGIAKFLLawEREAQAEGSepVFDHAFIAEHTDGLEAYLAELDATPWEHLERQSGLSLAEIEQA 356
Cdd:TIGR01701 262 SSEYYQVRIGGDIALFNGVMKLLI--EAEDAQPGS--LIDHEFIANHTNGFDELRRHVLQLNWNDIERSSGLSQEEILEF 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 357 ARMYRRANRVIVCWAMGITQHHHSVAIIQEIVNLQLLRGNLGRPGAGLCPVRGHSNVQGDRTMGINERPPAALLDALERR 436
Cdd:TIGR01701 338 AKLLANSRRVVFCWAMGLTQHAHGVDNISQVANLALLRGNIGKPGAGVCPIRGHSNVQGDRTMGITEKPEEEFLARLSQI 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 437 FGFEVPRHNGHNAVEAIAAMLAGKSKVFIGLGGNFAQATPDSPRTHAALASCDLTVHISTKLNRSHLTTGRDALILPCLG 516
Cdd:TIGR01701 418 YGFTPPDWPGDTTVAMIEAILTGKVRAFICLGGNFLEAMPDTAAIERALRQLDLRVHVATKLNRSHVLAKEEALILPVLG 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 517 RTDIDRQAEGPQAVTVEDSFSMIHASYGQLEPLSQQMRSEPAIIAGIAKATLGNHPVDWDALIANYERIRELIADTIPGF 596
Cdd:TIGR01701 498 RYEQDGQGTGKQAVSVESSMRMVHFSRGILKPRGAELRSEWAIIAEIAKALLPETPVAWEILVDTYDQIRDAIAATNPGY 577
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 597 ADFNRRVRHPGGFYLGNSA-GERRWNTASGKANFVANPLPrdLLPaqvRDSGLEPDLILQTLRSHDQYNTTIYGLDDRYR 675
Cdd:TIGR01701 578 DDINHRKRRPDGFQLPGAAlCERKFPTPDGKANFIVIPLP--EFR---VPTGHEFELVLVTLRSHDQFNTTIYGEDDRYR 652
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 676 GVKGQREVVFANEADIRRLGYQPGDKVDLVSLWSDGIERRVRRFTLLAFDIPAGQAAAYYPETNPLVPLESVGVGSHTPT 755
Cdd:TIGR01701 653 GVDGHRRVVFMNETDIKKLGLRNGERVDVYNQYGDGQKRKFDNLRIVFYDTPTGNAAAYYPEANPLLPLDHHDPQSKTPE 732
|
....*....
gi 15600374 756 SKFIAVRLE 764
Cdd:TIGR01701 733 YKTIPVRLE 741
|
|
| 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: 924.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 51 GFDCPGCAWGDSP-EDGRVKFCENGAKAVNWEATKRRVDAAFFARYSVSALREQSDYWLEYQGRLTGPMRYDPLSDHYQP 129
Cdd:cd02767 1 GFDCPGCAWGDPGqKLHGFEFCENGAKALAWETTPKRVTPEFFALHSVSELRTWSDYELEHLGRLTYPMRYDAGSDHYRP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 130 ITWDAAFALVAEHLRRLDsPDQAEFYTSGRASNEAAYLYQLFVRAFGTNNFPDCSNMCHEASGVALGRSVGVGKGSVTFD 209
Cdd:cd02767 81 ISWDEAFAEIAARLRALD-PDRAAFYTSGRASNEAAYLYQLFARAYGTNNLPDCSNMCHEPSSVGLKKSIGVGKGTVSLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 210 DFEHADAIFILGQNPGTNHPRMLEPLREAVKRGAQVVCFNPLKERGLERFQHPQNALEMLTnGSSPLNTAFFRPALGGDM 289
Cdd:cd02767 160 DFEHTDLIFFIGQNPGTNHPRMLHYLREAKKRGGKIIVINPLREPGLERFANPQNPESMLT-GGTKIADEYFQVRIGGDI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 290 AAIRGIAKFLLAWEREAQAegsepVFDHAFIAEHTDGLEAYLAELDATPWEHLERQSGLSLAEIEQAARMYRRANRVIVC 369
Cdd:cd02767 239 ALLNGMAKHLIERDDEPGN-----VLDHDFIAEHTSGFEEYVAALRALSWDEIERASGLSREEIEAFAAMYAKSERVVFV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 370 WAMGITQHHHSVAIIQEIVNLQLLRGNLGRPGAGLCPVRGHSNVQGDRTMGINERPPAALLDALERRFGFEVPRHNGHNA 449
Cdd:cd02767 314 WGMGITQHAHGVDNVRAIVNLALLRGNIGRPGAGLMPIRGHSNVQGDRTMGITEKPFPEFLDALEEVFGFTPPRDPGLDT 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 450 VEAIAAMLAGKSKVFIGLGGNFAQATPDSPRTHAALASCDLTVHISTKLNRSHLTTGRDALILPCLGRTDIDRQAEGPQA 529
Cdd:cd02767 394 VEAIEAALEGKVKAFISLGGNFAEAMPDPAATEEALRRLDLTVHVATKLNRSHLVHGEEALILPCLGRTEIDMQAGGAQA 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 530 VTVEDSFSMIHASYGQLEPLSQQMRSEPAIIAGIAKATLGNHPVDWDALIANYERIRELIADTIP-GFADFNRRVRHPGG 608
Cdd:cd02767 474 VTVEDSMSMTHTSRGRLKPASRVLLSEEAIVAGIAGARLGEAKPEWEILVEDYDRIRDEIAAVIYeGFADFNQRGDQPGG 553
|
570 580
....*....|....*....|.
gi 15600374 609 FYLGNSAGERRWNTASGKANF 629
Cdd:cd02767 554 FHLPNGARERKFNTPSGKAQF 574
|
|
| PRK09939 |
PRK09939 |
acid resistance putative oxidoreductase YdeP; |
6-766 |
0e+00 |
|
acid resistance putative oxidoreductase YdeP;
Pssm-ID: 182156 [Multi-domain] Cd Length: 759 Bit Score: 817.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 6 LQPRYKPYAGAAAGWGALRSVAHFWLDSKQPFKNLRALLKTNQNGGFDCPGCAWGDSPEDGRVKFCENGAKAVNWEATKR 85
Cdd:PRK09939 1 MKKKIESYQGAAGGWGAVKSVANAVRKQMDIRQDVIAMFDMNKPEGFDCPGCAWPDPKHSASFDICENGAKAIAWEVTDK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 86 RVDAAFFARYSVSALREQSDYWLEYQGRLTGPMRYDPLSDHYQPITWDAAFALVAEHLRRLDSPDQAEFYTSGRASNEAA 165
Cdd:PRK09939 81 QVNASFFAENTVQSLLTWGDHELEAAGRLTQPLKYDAVSDCYKPLSWQQAFDEIGARLQSYSDPNQVEFYTSGRTSNEAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 166 YLYQLFVRAFGTNNFPDCSNMCHEASGVALGRSVGVGKGSVTFDDFEHADAIFILGQNPGTNHPRMLEPLREAVKRGAQV 245
Cdd:PRK09939 161 FLYQLFAREYGSNNFPDCSNMCHEPTSVGLAASIGVGKGTVLLEDFEKCDLVICIGHNPGTNHPRMLTSLRALVKRGAKM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 246 VCFNPLKERGLERFQHPQNALEMLTNGSSPLNTAFFRPALGGDMAAIRGIAKFLLAWEREAQAEGSEPVFDHAFIAEHTD 325
Cdd:PRK09939 241 IAINPLQERGLERFTAPQNPFEMLTNSETQLASAYYNVRIGGDMALLKGMMRLLIERDDAASAAGRPSLLDDEFIQTHTV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 326 GLEAYLAELDATPWEHLERQSGLSLAEIEQAARMYRRANRVIVCWAMGITQHHHSVAIIQEIVNLQLLRGNLGRPGAGLC 405
Cdd:PRK09939 321 GFDELRRDVLNSEWKDIERISGLSQTQIAELADAYAAAERTIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGIC 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 406 PVRGHSNVQGDRTMGINERPPAALLDALERRFGFEVPRHNGHNAVEAIAAMLAGKSKVFIGLGGNFAQATPDSPRTHAAL 485
Cdd:PRK09939 401 PLRGHSNVQGDRTVGITEKPSAEFLARLGERYGFTPPHAPGHAAIASMQAICTGQARALICMGGNFALAMPDREASAVPL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 486 ASCDLTVHISTKLNRSHLTTGRDALILPCLGRTDIDRQAEGPQAVTVEDSFSMIHASYGQLEPLSQQMRSEPAIIAGIAK 565
Cdd:PRK09939 481 TQLDLAVHVATKLNRSHLLTARHSYILPVLGRSEIDMQKSGAQAVTVEDSMSMIHASRGVLKPAGVMLKSECAVVAGIAQ 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 566 ATLGNHPVDWDALIANYERIRELIADTIPGFADFNRRVRHPGGFYLGNSAGERRWNTASGKANFVANplpRDLLpaQVRD 645
Cdd:PRK09939 561 AALPQSVVAWEYLVEDYDRIRNDIEAVLPEFADYNQRIRHPGGFHLINAAAERRWMTPSGKANFITS---KGLL--EDPS 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 646 SGLEPDLILQTLRSHDQYNTTIYGLDDRYRGVKGQREVVFANEADIRRLGYQPGDKVDLVSLWSDGIE--RRVRRFTLLA 723
Cdd:PRK09939 636 SAFNSKLVMATVRSHDQYNTTIYGMDDRYRGVFGQRDVVFMSAKQAKICRVKNGERVNLIALTPDGKRssRRMDRLKVVI 715
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 15600374 724 FDIPAGQAAAYYPETNPLVPLESVGVGSHTPTSKFIAVRLEKA 766
Cdd:PRK09939 716 YPMADRSLVTYFPESNHMLTLDNHDPLSGIPGYKSIPVELEPS 758
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
54-768 |
2.15e-173 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 514.01 E-value: 2.15e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 54 CPGCAWGdspedgrvkfCENGAKAVNWEATKRRVDAAffarYSVSALR-----EQSDYWLEYQGRLTGPMRYDPL--SDH 126
Cdd:COG0243 28 CPGCGVG----------CGLGVKVEDGRVVRVRGDPD----HPVNRGRlcakgAALDERLYSPDRLTYPMKRVGPrgSGK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 127 YQPITWDAAFALVAEHLRRLDS---PDQAEFYTSG----RASNEAAYLYQLFVRAFGTNNFPDCSNMCHEASGVALGRSV 199
Cdd:COG0243 94 FERISWDEALDLIAEKLKAIIDeygPEAVAFYTSGgsagRLSNEAAYLAQRFARALGTNNLDDNSRLCHESAVAGLPRTF 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 200 GVGKGSVTFDDFEHADAIFILGQNPGTNHPRMLEPLREAVK-RGAQVVCFNPLKERglerfqhpqnalemltngssplnT 278
Cdd:COG0243 174 GSDKGTVSYEDLEHADLIVLWGSNPAENHPRLLRRLREAAKkRGAKIVVIDPRRTE-----------------------T 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 279 A-------FFRPalGGDMAAIRGIAKFLLAWEreaqaegsepVFDHAFIAEHTDGLEAYLAELDATPWEHLERQSGLSLA 351
Cdd:COG0243 231 AaiadewlPIRP--GTDAALLLALAHVLIEEG----------LYDRDFLARHTVGFDELAAYVAAYTPEWAAEITGVPAE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 352 EIEQAARMYRRANRVIVCWAMGITQHHHSVAIIQEIVNLQLLRGNLGRPGAGLCPVRGHsnvqgdrtmginerppaalld 431
Cdd:COG0243 299 DIRELAREFATAKPAVILWGMGLQQHSNGTQTVRAIANLALLTGNIGKPGGGPFSLTGE--------------------- 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 432 alerrfgfevprhnghnaveaiaAMLAGKS---KVFIGLGGNFAQATPDSPRTHAALASCDLTVHISTKLNRSHLttgRD 508
Cdd:COG0243 358 -----------------------AILDGKPypiKALWVYGGNPAVSAPDTNRVREALRKLDFVVVIDTFLTETAR---YA 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 509 ALILPCLG---RTDIdrqaegpqAVTVEDsfSMIHASYGQLEPLSqQMRSEPAIIAGIAKAtLG-NHPVDWDALIANYer 584
Cdd:COG0243 412 DIVLPATTwleRDDI--------VTNSED--RRVHLSRPAVEPPG-EARSDWEIFAELAKR-LGfEEAFPWGRTEEDY-- 477
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 585 IRELIADTIPGFADFnRRVRHPGGFYLGNSAG-----ERRWNTASGKANFVANPLPRDLLPAQVR--DSGLEPD----LI 653
Cdd:COG0243 478 LRELLEATRGRGITF-EELREKGPVQLPVPPEpafrnDGPFPTPSGKAEFYSETLALPPLPRYAPpyEGAEPLDaeypLR 556
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 654 LQTLRSHDQYNTTIYGLdDRYRGVKGqREVVFANEADIRRLGYQPGDKVDLVSLWSdgierRVRRFTLLAFDIPAGQAAA 733
Cdd:COG0243 557 LITGRSRDQWHSTTYNN-PRLREIGP-RPVVEINPEDAAALGIKDGDLVRVESDRG-----EVLARAKVTEGIRPGVVFA 629
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 15600374 734 YY-----------PETNPLVPlESVGVGSHTPTSKFIAVRLEKATG 768
Cdd:COG0243 630 PHgwwyepaddkgGNVNVLTP-DATDPLSGTPAFKSVPVRVEKAAA 674
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
112-768 |
1.18e-101 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 328.00 E-value: 1.18e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 112 GRLTGPMRYDPlsDHYQPITWDAAFALVAEHLRRL---DSPDQAEFYTSGRASNEAAYLYQLFVRA-FGTNNFPDCSNMC 187
Cdd:COG3383 60 DRLTTPLIRRG--GEFREVSWDEALDLVAERLREIqaeHGPDAVAFYGSGQLTNEENYLLQKLARGvLGTNNIDNNARLC 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 188 HEASGVALGRSVGVGKGSVTFDDFEHADAIFILGQNPGTNHPRMLEPLREAVKRGAQVVCFNPlKERGLERFQHpqnale 267
Cdd:COG3383 138 MASAVAGLKQSFGSDAPPNSYDDIEEADVILVIGSNPAEAHPVLARRIKKAKKNGAKLIVVDP-RRTETARLAD------ 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 268 mltngssplntAFFRPALGGDMAAIRGIAKFLLAwereaqaegsEPVFDHAFIAEHTDGLEAYLAELDATPWEHLERQSG 347
Cdd:COG3383 211 -----------LHLQIKPGTDLALLNGLLHVIIE----------EGLVDEDFIAERTEGFEELKASVAKYTPERVAEITG 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 348 LSLAEIEQAARMYRRANRVIVCWAMGITQHHHSVAIIQEIVNLQLLRGNLGRPGAGLCPVRGHSNVQGDRTMGI--NERP 425
Cdd:COG3383 270 VPAEDIREAARLIAEAKRAMILWGMGVNQHTQGTDNVNAIINLALATGNIGRPGTGPFPLTGQNNVQGGRDMGAlpNVLP 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 426 -------PAAlLDALERRFGFE-VPRHNGHNAVEAIAAMLAGKSKVFIGLGGNFAQATPDSPRTHAALASCDLTVHISTK 497
Cdd:COG3383 350 gyrdvtdPEH-RAKVADAWGVPpLPDKPGLTAVEMFDAIADGEIKALWIIGENPAVSDPDANHVREALEKLEFLVVQDIF 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 498 LNRshltTGRDA-LILPCLGR-------TDIDRQaegpqavtvedsfsmIHASYGQLEPLSqQMRSEPAIIAGIAKAtLG 569
Cdd:COG3383 429 LTE----TAEYAdVVLPAASWaekdgtfTNTERR---------------VQRVRKAVEPPG-EARPDWEIIAELARR-LG 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 570 nHPVDWDaliaNYERIRELIADTIPGFA--DFNRRVRHPGGFYLGNSAGER--------RWNTASGKANFVANPLprdLL 639
Cdd:COG3383 488 -YGFDYD----SPEEVFDEIARLTPDYSgiSYERLEALGGVQWPCPSEDHPgtprlftgRFPTPDGKARFVPVEY---RP 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 640 PAQVRDSglEPDLILQTLRSHDQYNT-TIYGLDDRYRGVKGqREVVFANEADIRRLGYQPGDKVDLVSLWSDgIERRVRr 718
Cdd:COG3383 560 PAELPDE--EYPLVLTTGRLLDQWHTgTRTRRSPRLNKHAP-EPFVEIHPEDAARLGIKDGDLVRVSSRRGE-VVLRAR- 634
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 15600374 719 ftlLAFDIPAGQAAAY--YPET--NPLVPlESVGVGSHTPTSKFIAVRLEKATG 768
Cdd:COG3383 635 ---VTDRVRPGTVFMPfhWGEGaaNALTN-DALDPVSKQPEYKACAVRVEKVAE 684
|
|
| Fdh-alpha |
TIGR01591 |
formate dehydrogenase, alpha subunit, archaeal-type; This model describes a subset of formate ... |
113-763 |
1.48e-76 |
|
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: 260.86 E-value: 1.48e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 113 RLTGPMRYDplSDHYQPITWDAAFALVAEHLRRLDS---PDQAEFYTSGRASNEAAYLYQLFVRA-FGTNNFPDCSNMCH 188
Cdd:TIGR01591 53 RLTTPLIRE--GDKFREVSWDEAISYIAEKLKEIKEkygPDSIGFIGSSRGTNEENYLLQKLARAvIGTNNVDNCARVCH 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 189 EASGVALGRSVGVGKGSVTFDDFEHADAIFILGQNPGTNHPRMLEPLREAVKRGAQVVCFNPlKERGLERF--QHPQnal 266
Cdd:TIGR01591 131 GPSVAGLKQTVGIGAMSNTISEIENADLIVIIGYNPAESHPVVAQYLKNAKRNGAKIIVIDP-RKTETAKIadLHIP--- 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 267 emltngssplntafFRPalGGDMAAIRGIAKFLLawereaqaegSEPVFDHAFIAEHTDGLEAYLAELDATPWEHLERQS 346
Cdd:TIGR01591 207 --------------LKP--GTDIALLNAMANVII----------EEGLYDKAFIEKRTEGFEEFREIVKGYTPEYVEDIT 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 347 GLSLAEIEQAARMYRRANRVIVCWAMGITQHHHSVAIIQEIVNLQLLRGNLGRPGAGLCPVRGHSNVQGDRTMG-INERP 425
Cdd:TIGR01591 261 GVPADLIREAARMYAKAGSAAILWGMGVTQHSQGVETVMALINLAMLTGNIGKPGGGVNPLRGQNNVQGACDMGaLPDFL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 426 PA-------ALLDALERRFGFE-VPRHNGHNAVEAIAAMLAGKSKVFIGLGGNFAQATPDSPRTHAALASCDLTVHISTK 497
Cdd:TIGR01591 341 PGyqpvsdeEVREKFAKAWGVVkLPAEPGLRIPEMIDAAADGDVKALYIMGEDPLQSDPNTSKVRKALEKLELLVVQDIF 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 498 LNRshltTGRDA-LILPClgrtdidrQAEGPQAVTVEDSFSMIHASYGQLEPLSqQMRSEPAIIAGIAKAtLGnhpVDWD 576
Cdd:TIGR01591 421 MTE----TAKYAdVVLPA--------AAWLEKEGTFTNAERRIQRFFKAVEPKG-ESKPDWEIIQELANA-LG---LDWN 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 577 AliANYERIRELIADTIPGFADFN-RRVRHPGG--FYLGNSAGER-------RWNTASGKANFVAnplprdlLPAQVRDS 646
Cdd:TIGR01591 484 Y--NHPQEIMDEIRELTPLFAGLTyERLDELGSlqWPCNDSDASPtsylykdKFATPDGKAKFIP-------LEWVAPIE 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 647 GLEPD--LILQTLRSHDQYNTTiyGLDDRYRGVKGQREVVFA--NEADIRRLGYQPGDKVDLVSlwsdgierRVRRFTLL 722
Cdd:TIGR01591 555 EPDDEypLILTTGRVLTHYNVG--EMTRRVAGLRRLSPEPYVeiNTEDAKKLGIKDGDLVKVKS--------RRGEITLR 624
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 15600374 723 AF--DIPAGQAA-----AYYPETNPLVPLESVGVgSHTPTSKFIAVRL 763
Cdd:TIGR01591 625 AKvsDRVNKGAIyitmhFWDGAVNNLTTDDLDPI-SGTPEYKYTAVRI 671
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
113-492 |
1.05e-71 |
|
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: 243.27 E-value: 1.05e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 113 RLTGPMRYDPlsDHYQPITWDAAFALVAEHLRRLDS---PDQAEFYTSGRASNEAAYLYQLFVRA-FGTNNFPDCSNMCH 188
Cdd:cd02753 54 RLTKPLIRKN--GKFVEASWDEALSLVASRLKEIKDkygPDAIAFFGSAKCTNEENYLFQKLARAvGGTNNVDHCARLCH 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 189 EASGVALGRSVGVGKGSVTFDDFEHADAIFILGQNPGTNHPRMLEPLREAVKRGAQVVCFNPlKERGLERF--QHPQnal 266
Cdd:cd02753 132 SPTVAGLAETLGSGAMTNSIADIEEADVILVIGSNTTEAHPVIARRIKRAKRNGAKLIVADP-RRTELARFadLHLQ--- 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 267 emltngssplntafFRPalGGDMAAIRGIAKFLLawereaqaegSEPVFDHAFIAEHTDGLEAYLAELDATPWEHLERQS 346
Cdd:cd02753 208 --------------LRP--GTDVALLNAMAHVII----------EEGLYDEEFIEERTEGFEELKEIVEKYTPEYAERIT 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 347 GLSLAEIEQAARMYRRANRVIVCWAMGITQHHHSVAIIQEIVNLQLLRGNLGRPGAGLCPVRGHSNVQGDRTMGinerpp 426
Cdd:cd02753 262 GVPAEDIREAARMYATAKSAAILWGMGVTQHSHGTDNVMALSNLALLTGNIGRPGTGVNPLRGQNNVQGACDMG------ 335
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600374 427 aalldalerrfgfevprhnghnaveAIAAMLAGKSKVFIGLGGNFAQATPDSPRTHAALASCDLTV 492
Cdd:cd02753 336 -------------------------ALPNVLPGYVKALYIMGENPALSDPNTNHVRKALESLEFLV 376
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
112-566 |
1.02e-61 |
|
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: 212.19 E-value: 1.02e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 112 GRLTGPMRYDPLSDHYQPITWDAAFALVAEHLRRL---DSPDQAEFYTSGRASNEAAYLYQLFVRAFGTNNFPDCSNMCH 188
Cdd:cd00368 53 DRLKYPLIRVGGRGKFVPISWDEALDEIAEKLKEIrekYGPDAIAFYGGGGASNEEAYLLQKLLRALGSNNVDSHARLCH 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 189 EASGVALGRsVGVGKGSVTFDDFEHADAIFILGQNPGTNHPRMLEPLREAVKRGAQVVCFNPLKERglerfqhpqnalem 268
Cdd:cd00368 133 ASAVAALKA-FGGGAPTNTLADIENADLILLWGSNPAETHPVLAARLRRAKKRGAKLIVIDPRRTE-------------- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 269 ltngSSPLNTAFFRPALGGDMAairgiakFLLAwereaqaegsepvfdhafiaehtdgleaylaeldatpwEHLERQSGL 348
Cdd:cd00368 198 ----TAAKADEWLPIRPGTDAA-------LALA--------------------------------------EWAAEITGV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 349 SLAEIEQAARMYRRANRVIVCWAMGITQHHHSVAIIQEIVNLQLLRGNLGRPGAGLCPvrghsnvqgdrtmginerppaa 428
Cdd:cd00368 229 PAETIRALAREFAAAKRAVILWGMGLTQHTNGTQNVRAIANLAALTGNIGRPGGGLGP---------------------- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 429 lldalerrfgfevprhnghnaveaiaamlagkskvfiglGGNFAQATPDSPRTHAALASCDLTVHISTKLNrshlTTGRD 508
Cdd:cd00368 287 ---------------------------------------GGNPLVSAPDANRVRAALKKLDFVVVIDIFMT----ETAAY 323
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 15600374 509 A-LILPCLGRTDidrqAEGpqavTVEDSFSMIHASYGQLEPLSqQMRSEPAIIAGIAKA 566
Cdd:cd00368 324 AdVVLPAATYLE----KEG----TYTNTEGRVQLFRQAVEPPG-EARSDWEILRELAKR 373
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
111-492 |
7.73e-56 |
|
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: 201.30 E-value: 7.73e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 111 QGRLTGPMRYDPLSDhYQPITWDAAFALVAEHLRRL---DSPDQAEFYTSGRASNEAAYLYQLFVRAF-GTNNFPDCSNM 186
Cdd:cd02754 52 PERLTRPLLRRNGGE-LVPVSWDEALDLIAERFKAIqaeYGPDSVAFYGSGQLLTEEYYAANKLAKGGlGTNNIDTNSRL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 187 CHEASGVALGRSVGVGKGSVTFDDFEHADAIFILGQNPGTNHPRMLEPLREAVK--RGAQVVCFNPLKERglerfqhpqn 264
Cdd:cd02754 131 CMASAVAGYKRSFGADGPPGSYDDIEHADCFFLIGSNMAECHPILFRRLLDRKKanPGAKIIVVDPRRTR---------- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 265 alemltngSSPLNTAFFRPALGGDMAAIRGIAKFLLAWEReaqaegsepvFDHAFIAEHTDGLEAYLAELDATPWEHLER 344
Cdd:cd02754 201 --------TADIADLHLPIRPGTDLALLNGLLHVLIEEGL----------IDRDFIDAHTEGFEELKAFVADYTPEKVAE 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 345 QSGLSLAEIEQAARMYRRANRVIVCWAMGITQHHHSVAIIQEIVNLQLLRGNLGRPGAGLCPVRGHSNVQGDRTMG-INE 423
Cdd:cd02754 263 ITGVPEADIREAARLFGEARKVMSLWTMGVNQSTQGTAANNAIINLHLATGKIGRPGSGPFSLTGQPNAMGGREVGgLAN 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 424 RPP--------------AALLDALERRFGFEVPRHnghnAVEAIAAMLAGKSKVFIGLGGNFAQATPDSPRTHAALASCD 489
Cdd:cd02754 343 LLPghrsvnnpehraevAKFWGVPEGTIPPKPGLH----AVEMFEAIEDGEIKALWVMCTNPAVSLPNANRVREALERLE 418
|
...
gi 15600374 490 LTV 492
Cdd:cd02754 419 FVV 421
|
|
| MopB_CT_ydeP |
cd02787 |
The MopB_CT_ydeP CD includes a group of related uncharacterized bacterial ... |
652-763 |
1.23e-54 |
|
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: 183.25 E-value: 1.23e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 652 LILQTLRSHDQYNTTIYGLDDRYRGVKGQREVVFANEADIRRLGYQPGDKVDLVSLWSDGIERRVRRFTLLAFDIPAGQA 731
Cdd:cd02787 1 LFLVTTRSHDQFNTTIYGLDDRYRGVFGRRDVVFMNPDDIARLGLKAGDRVDLESAFGDGQGRIVRGFRVVEYDIPRGCL 80
|
90 100 110
....*....|....*....|....*....|..
gi 15600374 732 AAYYPETNPLVPLESVGVGSHTPTSKFIAVRL 763
Cdd:cd02787 81 AAYYPEGNVLVPLDHRDPQSKTPAYKSVPVRL 112
|
|
| MopB_Formate-Dh-Na-like |
cd02752 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
113-422 |
2.74e-33 |
|
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: 136.38 E-value: 2.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 113 RLTGPMRYDPLSDHYQPITWDAAFALVAEHL---------------RRLDSPDQAEFYTSGRASNEAAYLYQLFVRAFGT 177
Cdd:cd02752 54 RLKYPMYRAPGSGKWEEISWDEALDEIARKMkdirdasfveknaagVVVNRPDSIAFLGSAKLSNEECYLIRKFARALGT 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 178 NNFPDCSNMCHEASGVALGRSVGVGKGSVTFDDFEHADAIFILGQNPGTNHP-RMLEPLREAVKRGAQVVCFNPlkergl 256
Cdd:cd02752 134 NNLDHQARIUHSPTVAGLANTFGRGAMTNSWNDIKNADVILVMGGNPAEAHPvSFKWILEAKEKNGAKLIVVDP------ 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 257 eRFqhpqnalemlTNGSSPLNT-AFFRPalGGDMAAIRGIAKFLLAWereaqaegsepvfdhafiaehtdgleaylaeld 335
Cdd:cd02752 208 -RF----------TRTAAKADLyVPIRS--GTDIAFLGGMINYIIRY--------------------------------- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 336 aTPwEHLERQSGLSLAEIEQAARMY---RRANR--VIVcWAMGITQHHHSVAIIQEIVNLQLLRGNLGRPGAGLCPVRGH 410
Cdd:cd02752 242 -TP-EEVEDICGVPKEDFLKVAEMFaatGRPDKpgTIL-YAMGWTQHTVGSQNIRAMCILQLLLGNIGVAGGGVNALRGH 318
|
330
....*....|..
gi 15600374 411 SNVQGDRTMGIN 422
Cdd:cd02752 319 SNVQGATDLGLL 330
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
113-566 |
2.10e-28 |
|
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: 120.58 E-value: 2.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 113 RLTGPMRYDPlsDHYQPITWDAAFALVAEHLRRL---DSPDQAEFYTSGRASNE---AAYLYQLfVRAFGTNNFPDCS-- 184
Cdd:cd02762 54 RLRTPMRRRG--GSFEEIDWDEAFDEIAERLRAIrarHGGDAVGVYGGNPQAHThagGAYSPAL-LKALGTSNYFSAAta 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 185 -NMCHE-ASGVALGRSVGVgkgsvTFDDFEHADAIFILGQNPGTNH------PRMLEPLREAVKRGAQVVCFNPLKERGL 256
Cdd:cd02762 131 dQKPGHfWSGLMFGHPGLH-----PVPDIDRTDYLLILGANPLQSNgslrtaPDRVLRLKAAKDRGGSLVVIDPRRTETA 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 257 ERfqhpqnALEMLtngssplntaFFRPalGGDMAAIRGIAKFLLAwereaqaegsEPVFDHAFIAEHTDGLEAYLAELDA 336
Cdd:cd02762 206 KL------ADEHL----------FVRP--GTDAWLLAAMLAVLLA----------EGLTDRRFLAEHCDGLDEVRAALAE 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 337 TPWEHLERQSGLSLAEIEQAARMYRRANRVIVCWAMGITQHHHSvAIIQEIVN-LQLLRGNLGRPGAGLCP---VRGHSN 412
Cdd:cd02762 258 FTPEAYAPRCGVPAETIRRLAREFAAAPSAAVYGRLGVQTQLFG-TLCSWLVKlLNLLTGNLDRPGGAMFTtpaLDLVGQ 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 413 VQGDRTMGINERPPAALLdalerrfgfevPRHNGHNAVEAIAAML--AGKSKV--FIGLGGNFAQATPDSPRTHAALASC 488
Cdd:cd02762 337 TSGRTIGRGEWRSRVSGL-----------PEIAGELPVNVLAEEIltDGPGRIraMIVVAGNPVLSAPDGARLEAALGGL 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 489 DLTVHISTKLNRshltTGRDA-LILPCLGrtdidrQAEGPQAVTVEDSFSMIHASYGQ-LEPLSQQMRSEPAIIAGIAKA 566
Cdd:cd02762 406 EFMVSVDVYMTE----TTRHAdYILPPAS------QLEKPHATFFNLEFPRNAFRYRRpLFPPPPGTLPEWEILARLVEA 475
|
|
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
113-403 |
9.31e-24 |
|
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: 105.79 E-value: 9.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 113 RLTGPMRYD-PLSDHYQPITWDAAFALVAEHLRRLDSPDQAE-----FYTSGRASNEAAYLYQLFvRAFGTNNF--PDCS 184
Cdd:cd02766 55 RLLTPLKRVgRKGGQWERISWDEALDTIAAKLKEIKAEYGPEsilpySYAGTMGLLQRAARGRFF-HALGASELrgTICS 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 185 NMCHEASGVALGRSVGVGKgsvtfDDFEHADAIFILGQNPGTNHPRMLEPLREAVKRGAQVVCFNPLKerglerfqhpqn 264
Cdd:cd02766 134 GAGIEAQKYDFGASLGNDP-----EDMVNADLIVIWGINPAATNIHLMRIIQEARKRGAKVVVIDPYR------------ 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 265 alemltNGSSPLNTAFFRPALGGDMAAIRGIAKFLLAwereaqaEGSEpvfDHAFIAEHTDGLEAYLAELDATPWEHLER 344
Cdd:cd02766 197 ------TATAARADLHIQIRPGTDGALALGVAKVLFR-------EGLY---DRDFLARHTEGFEELKAHLETYTPEWAAE 260
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 15600374 345 QSGLSLAEIEQAARMYRRANRVIVCWAMGITQHHHSVAIIQEIVNLQLLRGNLGRPGAG 403
Cdd:cd02766 261 ITGVSAEEIEELARLYGEAKPPSIRLGYGMQRYRNGGQNVRAIDALPALTGNIGVPGGG 319
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
112-406 |
8.55e-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: 86.97 E-value: 8.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 112 GRLTGPM-RYDPLSD-HYQPITWDAAFALVAEHLRRLDSPDQAEFYTSGRASNEAAYLYQLFVRAFGTNNFPDCSNMCHE 189
Cdd:cd02755 54 DRLKKPLiRVGERGEgKFREASWDEALQYIASKLKEIKEQHGPESVLFGGHGGCYSPFFKHFAAAFGSPNIFSHESTCLA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 190 ASGVAlGRSVGVGKGSVTFDDFEHADAIFILGQN--PGTNHPRMLEpLREAVKRGAQVVCFNPlkergleRFQH-PQNAL 266
Cdd:cd02755 134 SKNLA-WKLVIDSFGGEVNPDFENARYIILFGRNlaEAIIVVDARR-LMKALENGAKVVVVDP-------RFSElASKAD 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 267 EMLtngssPLntaffRPalGGDMAAIRGIAKFLLawereaqaegSEPVFDHAFIAEHTDGLEAYLAEL-DATPwEHLERQ 345
Cdd:cd02755 205 EWI-----PI-----KP--GTDLAFVLALIHVLI----------SENLYDAAFVEKYTNGFELLKAHVkPYTP-EWAAQI 261
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600374 346 SGLSLAEIEQAARMYRRANRVIVcWAMG--ITQHHHSVAIIQEIVNLQLLRGNLGRPGaGLCP 406
Cdd:cd02755 262 TDIPADTIRRIAREFAAAAPHAV-VDPGwrGTFYSNSFQTRRAIAIINALLGNIDKRG-GLYY 322
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
113-404 |
1.15e-17 |
|
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: 86.59 E-value: 1.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 113 RLTGPMRY--DPLSDHYQPITWDAAFALVAEHLRRLDSPDQAE---FY-TSGRASNEAAYLYQL-FVRAFGTNNFPDCSN 185
Cdd:cd02759 54 RLLYPLKRvgERGENKWERISWDEALDEIAEKLAEIKAEYGPEsiaTAvGTGRGTMWQDSLFWIrFVRLFGSPNLFLSGE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 186 MCHEASGVALGRSVGVGkGSVTFDDFEHADAIFILGQNPG-TNHPRMLEPLREAVKRGAQVVCFNPlkeRGLERFQHPQN 264
Cdd:cd02759 134 SCYWPRDMAHALTTGFG-LGYDEPDWENPECIVLWGKNPLnSNLDLQGHWLVAAMKRGAKLIVVDP---RLTWLAARADL 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 265 ALemltngssPLntaffRPalGGDMAAIRGIAKFLLawereaqaegSEPVFDHAFIAEHTDGLEAYLAELDATPWEHLER 344
Cdd:cd02759 210 WL--------PI-----RP--GTDAALALGMLNVII----------NEGLYDKDFVENWCYGFEELAERVQEYTPEKVAE 264
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 345 QSGLSLAEIEQAARMYRRANRVIVCWAMGITQHHHSVAIIQEIVNLQLLRGNLGRPGAGL 404
Cdd:cd02759 265 ITGVPAEKIRKAARLYATAKPACIQWGLAIDQQKNGTQTSRAIAILRAITGNLDVPGGNL 324
|
|
| MopB_NADH-Q-OR-NuoG2 |
cd02768 |
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone ... |
106-380 |
7.78e-17 |
|
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: 83.10 E-value: 7.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 106 YWL------EYQG-----RLTGPM-RydpLSDHYQPITWDAAFALVAEHLRRLdSPDQAEFYTSGRASNEAAYLYQLFVR 173
Cdd:cd02768 36 EWIsdkgrfGYDGlnsrqRLTQPLiK---KGGKLVPVSWEEALKTVAEGLKAV-KGDKIGGIAGPRADLESLFLLKKLLN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 174 AFGTNNFpDCSNMCHEASGVALGRSVGVGkgSVTFDDFEHADAIFILGQNPGTNHPRMLEPLREAVKR-GAQVVCFNPLK 252
Cdd:cd02768 112 KLGSNNI-DHRLRQSDLPADNRLRGNYLF--NTSIAEIEEADAVLLIGSNLRKEAPLLNARLRKAVKKkGAKIAVIGPKD 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 253 ERGLERF----QHPQNALEMLTNGSSPLNTAFF--------RPA-LGGDMAAIRGIAKFLLAWEREAQAEGSEPVFDHAF 319
Cdd:cd02768 189 TDLIADLtypvSPLGASLATLLDIAEGKHLKPFakslkkakKPLiILGSSALRKDGAAILKALANLAAKLGTGAGLWNGL 268
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600374 320 IAEHTDGLEAYLAELDATPWEHLERQSG-LSLAEIE------QAARMYRRANRVIVcwamgiTQHHHS 380
Cdd:cd02768 269 NVLNSVGARLGGAGLDAGLALLEPGKAKlLLLGEDEldrsnpPAAVALAAADAFVV------YQGHHG 330
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
113-513 |
1.45e-16 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 82.06 E-value: 1.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 113 RLTGPMrYDPLSDHYQPITWDAAFALVAEHLRRL-----DSPDQAEFYTSGRASNEAAYLYQLFVRAFGTNNF---PDCS 184
Cdd:pfam00384 1 RLKYPM-VRRGDGKFVRVSWDEALDLIAKKLKRIikkygPDAIAINGGSGGLTDVESLYALKKLLNRLGSKNGnteDHNG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 185 NMCHEASGVALGRSVGVGKGSVTFDDFEHADAIFILGQNPGTNHPRMLEPLREAVKRG-AQVVCFNPLKERGLErFQHpq 263
Cdd:pfam00384 80 DLCTAAAAAFGSDLRSNYLFNSSIADIENADLILLIGTNPREEAPILNARIRKAALKGkAKVIVIGPRLDLTYA-DEH-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 264 nalemltngssplntaffrpaLGGDMAAIRGIAkfllawereaqAEGSepvfdHAFIAEhtdgleaylaeldatpwehle 343
Cdd:pfam00384 157 ---------------------LGIKPGTDLALA-----------LAGA-----HVFIKE--------------------- 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 344 rqsgLSLAEieqaarmyRRANRVIVCWAMGITQHHHSVAIIQEIVNLQLLRGNLGRPGAGlcpVRGHSNVQGDRtmgine 423
Cdd:pfam00384 179 ----LKKDK--------DFAPKPIIIVGAGVLQRQDGEAIFRAIANLADLTGNIGRPGGG---WNGLNILQGAA------ 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 424 RPPAALldalerrfgfEVPRHNGHNAVEAIAAMLAGKSKVFIGLGGNFAQATPDSPRTHAALASCDLTV----HISTKln 499
Cdd:pfam00384 238 SPVGAL----------DLGLVPGIKSVEMINAIKKGGIKVLYLLGNNPFVTHADENRVVKALQKLDLFVvydgHHGDK-- 305
|
410
....*....|....*
gi 15600374 500 rshltTGRDA-LILP 513
Cdd:pfam00384 306 -----TAKYAdVILP 315
|
|
| 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 ... |
113-513 |
1.98e-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: 79.74 E-value: 1.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 113 RLTGPMRYDplSDHYQPITWDAAFALVAEHLRRldSPDQAEFYTSGRASNEAAYLYQLFVRAF-GTNNFpDCSNMCHEAS 191
Cdd:cd02771 54 RLTQPLIRR--GGTLVPVSWNEALDVAAARLKE--AKDKVGGIGSPRASNESNYALQKLVGAVlGTNNV-DHRARRLIAE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 192 GVALGRSVgvgkgSVTFDDFEHADAIFILGQNPGTNHPRMLEPLREAVKRGAQVVcfnpLKERGLERFQHPQNALEMLTN 271
Cdd:cd02771 129 ILRNGPIY-----IPSLRDIESADAVLVLGEDLTQTAPRIALALRQAARRKAVEL----AALSGIPKWQDAAVRNIAQGA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 272 GSSPLNTAFFRPALgGDMAAirgiakfllaweREAQAegsepvfDHAFIAEHTDGLEAYLAelDATPwehlerqSGLSLA 351
Cdd:cd02771 200 KSPLFIVNALATRL-DDIAA------------ESIRA-------SPGGQARLGAALARAVD--ASAA-------GVSGLA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 352 EIEQAARMYRR---ANRVIVCWAmgitQHHHSVAIIQEIVNLQLLRGNLGRpGAGLCPVRGHSNVQGDRTMGineRPPAA 428
Cdd:cd02771 251 PKEKAARIAARltgAKKPLIVSG----TLSGSLELIKAAANLAKALKRRGE-NAGLTLAVEEGNSPGLLLLG---GHVTE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 429 lldalerrfgfevprhNGHNAVEAIAAMLAGKSKVFIGLGGNFAQATPDSpRTHAALASCDLTVHISTKLNRshlTTGRD 508
Cdd:cd02771 323 ----------------PGLDLDGALAALEDGSADALIVLGNDLYRSAPER-RVEAALDAAEFVVVLDHFLTE---TAERA 382
|
....*
gi 15600374 509 ALILP 513
Cdd:cd02771 383 DVVLP 387
|
|
| PRK13532 |
PRK13532 |
nitrate reductase catalytic subunit NapA; |
113-403 |
1.23e-10 |
|
nitrate reductase catalytic subunit NapA;
Pssm-ID: 237416 [Multi-domain] Cd Length: 830 Bit Score: 64.92 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 113 RLTGPM------RYDPLSDhYQPITWDAAFALVAEHLRRL---DSPDQAEFYTSGRASNEAAYLYQLFVRA-FGTNNFPD 182
Cdd:PRK13532 97 RLTQPLlrmkdgKYDKEGE-FTPVSWDQAFDVMAEKFKKAlkeKGPTAVGMFGSGQWTIWEGYAASKLMKAgFRSNNIDP 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 183 CSNMCHEASGVALGRSVGVGKGSVTFDDFEHADAIFILGQNPGTNHP----RMLEplREAVKRGAQVVCfnplkergLER 258
Cdd:PRK13532 176 NARHCMASAVVGFMRTFGIDEPMGCYDDIEAADAFVLWGSNMAEMHPilwsRVTD--RRLSNPDVKVAV--------LST 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 259 FQH-------------PQNALEML--------TNGssPLNTAFF-----------------RPALGGDMAAirgiakfll 300
Cdd:PRK13532 246 FEHrsfeladngiiftPQTDLAILnyianyiiQNN--AVNWDFVnkhtnfrkgatdigyglRPTHPLEKAA--------- 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 301 awEREAQAEGSEPV-FDH--AFIAEHTdgLEaYLAELdatpwehlerqSGLSLAEIEQAARMYRRANRVIVC-WAMGITQ 376
Cdd:PRK13532 315 --KNPGTAGKSEPIsFEEfkKFVAPYT--LE-KTAKM-----------SGVPKEQLEQLAKLYADPNRKVVSfWTMGFNQ 378
|
330 340
....*....|....*....|....*..
gi 15600374 377 HHHSVAIIQEIVNLQLLRGNLGRPGAG 403
Cdd:PRK13532 379 HTRGVWANNLVYNIHLLTGKISTPGNG 405
|
|
| MopB_NDH-1_NuoG2 |
cd02772 |
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase ... |
107-357 |
1.12e-09 |
|
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: 61.22 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 107 WL------EYQG-----RLTGPM-RYDplsDHYQPITWDAAFALVAEHL---RRLDSPDQAEFYTSGRASNEAAYLYQLF 171
Cdd:cd02772 37 WLsdrdrfSYEGlnsedRLTKPMiKKD---GQWQEVDWETALEYVAEGLsaiIKKHGADQIGALASPHSTLEELYLLQKL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 172 VRAFGTNNFP------DCSNMCHEASGVALGRSVgvgkgsvtfDDFEHADAIFILGQNPGTNHPRMLEPLREAVKRGAQV 245
Cdd:cd02772 114 ARGLGSDNIDhrlrqsDFRDDAKASGAPWLGMPI---------AEISELDRVLVIGSNLRKEHPLLAQRLRQAVKKGAKL 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 246 VCFNPLKERGL-----ERFQHPQNALEMLTNGSSPLNTAFFRPALGGDMAAI-----RGIAKFLLAWEREAQAEGSepvf 315
Cdd:cd02772 185 SAINPADDDFLfplsgKAIVAPSALANALAQVAKALAEEKGLAVPDEDAKVEaseeaRKIAASLVSAERAAVFLGN---- 260
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 15600374 316 dhafIAEHTDGLEAYLAELDAtpwehLERQSGLSLAEIEQAA 357
Cdd:cd02772 261 ----LAQNHPQAATLRALAQE-----IAKLTGATLGVLGEGA 293
|
|
| MopB_Arsenate-R |
cd02757 |
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ... |
113-409 |
1.27e-09 |
|
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: 61.30 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 113 RLTGPM-RYDP-----LSDHYQPITWDAAFALVAEHLRRLDSPDQA-EF-YTSGRASNEAAYLYQLFVRAFGTNNFPDCS 184
Cdd:cd02757 56 RILYPMkRTNPrkgrdVDPKFVPISWDEALDTIADKIRALRKENEPhKImLHRGRYGHNNSILYGRFTKMIGSPNNISHS 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 185 NMCHEASGValGRS-VGVGKGsvtFDDFEHADAIFIL--GQNP-GTNHPrmlEPLR----EAVKRGAQVVCFNPlkergl 256
Cdd:cd02757 136 SVCAESEKF--GRYyTEGGWD---YNSYDYANAKYILffGADPlESNRQ---NPHAqriwGGKMDQAKVVVVDP------ 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 257 eRFQhpqnalemltngssplNTAFF-----RPALGGDMAAIRGIAKFLLA---WERE---------AQAEGSEPVFDHAF 319
Cdd:cd02757 202 -RLS----------------NTAAKadewlPIKPGEDGALALAIAHVILTeglWDKDfvgdfvdgkNYFKAGETVDEESF 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 320 IAEHTDGLEAYL-AEL-DATPwEHLERQSGLSLAEIEQAARMYRRANRVIVCWAM-GITQHHHSVAIIQEIVNLQLLRGN 396
Cdd:cd02757 265 KEKSTEGLVKWWnLELkDYTP-EWAAKISGIPAETIERVAREFATAAPAAAAFTWrGATMQNRGSYNSMACHALNGLVGS 343
|
330
....*....|...
gi 15600374 397 LGRPGaGLCPVRG 409
Cdd:cd02757 344 IDSKG-GLCPNMG 355
|
|
| MopB_Arsenite-Ox |
cd02756 |
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the ... |
95-410 |
1.32e-09 |
|
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: 61.73 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 95 YSVSALREQSDYWLE----YQGRLTGPMRYdpLSDHYQPITWDAAFALVAEHLRRL---DSPDQAEFYT--------SGR 159
Cdd:cd02756 95 YSTRGGTNAERIWSPdnrvGETRLTTPLVR--RGGQLQPTTWDDAIDLVARVIKGIldkDGNDDAVFASrfdhggggGGF 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 160 ASNEAA---YLYQLFVRAFGTNNFPDCSNMCHEAsgvalgRSVGVGKGSVTFDDFEHADAIFILGQNP---GTNH--PRM 231
Cdd:cd02756 173 ENNWGVgkfFFMALQTPFVRIHNRPAYNSEVHAT------REMGVGELNNSYEDARLADTIVLWGNNPyetQTVYflNHW 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 232 LEPLREAVKRGAQVVcFNPLKERGLERF----QHPQNALEMLTNGSSPLNTAFFRPALGGDMAAIRGIAkfllawereaq 307
Cdd:cd02756 247 LPNLRGATVSEKQQW-FPPGEPVPPGRIivvdPRRTETVHAAEAAAGKDRVLHLQVNPGTDTALANAIA----------- 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 308 aegsepvfdhAFIAEhtdGLEAYLAELdatpwehlERQSGLSLAEIEQAARM--------YRRanRVIVCWAMGITQHHH 379
Cdd:cd02756 315 ----------RYIYE---SLDEVLAEA--------EQITGVPRAQIEKAADWiakpkeggYRK--RVMFEYEKGIIWGND 371
|
330 340 350
....*....|....*....|....*....|.
gi 15600374 380 SVAIIQEIVNLQLLRGNLGRPGAGLCPVRGH 410
Cdd:cd02756 372 NYRPIYSLVNLAIITGNIGRPGTGCVRQGGH 402
|
|
| PRK07860 |
PRK07860 |
NADH dehydrogenase subunit G; Validated |
113-258 |
4.03e-08 |
|
NADH dehydrogenase subunit G; Validated
Pssm-ID: 236118 [Multi-domain] Cd Length: 797 Bit Score: 56.88 E-value: 4.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 113 RLTGPMRYDPlSDHYQPITWDAAFALVAEHLRRldSPDQAEFYTSGRASNEAAYLYQLFVR-AFGTNNFpDCSNMCHEAS 191
Cdd:PRK07860 278 RITTPLVRDE-DGELEPASWSEALAVAARGLAA--ARGRVGVLVGGRLTVEDAYAYAKFARvALGTNDI-DFRARPHSAE 353
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 192 GVA-LGRSVgVGKG-SVTFDDFEHADAIFILGQNPGTNHPRMLEPLREAV-KRGAQVVCFNPLKERGLER 258
Cdd:PRK07860 354 EADfLAARV-AGRGlGVTYADLEKAPAVLLVGFEPEEESPIVFLRLRKAArKHGLKVYSIAPFATRGLEK 422
|
|
| MopB_CT |
cd02775 |
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a ... |
659-757 |
1.02e-06 |
|
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: 47.70 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 659 SHDQYNTTIYGLDDRYRGVKGqREVVFANEADIRRLGYQPGDKVDLVSLWSDgIERRVRrftlLAFDIPAGQAAAYYP-- 736
Cdd:cd02775 1 LRDHFHSGTRTRNPWLRELAP-EPVVEINPEDAAALGIKDGDLVRVESRRGS-VVLRAK----VTDGVPPGVVFLPHGwg 74
|
90 100
....*....|....*....|....*...
gi 15600374 737 -------ETNPLVPLESVGVgSHTPTSK 757
Cdd:cd02775 75 hrggrggNANVLTPDALDPP-SGGPAYK 101
|
|
| MopB_FmdB-FwdB |
cd02761 |
The MopB_FmdB-FwdB CD contains the molybdenum/tungsten formylmethanofuran dehydrogenases, ... |
54-415 |
3.12e-06 |
|
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: 50.41 E-value: 3.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 54 CPGCawGDSPEDGRVKFCENGAKAVNweaTKRRVDAAFFARYSVsalreqsdywleyqgRLTGPMRydplsdHYQPITWD 133
Cdd:cd02761 4 CPFC--GLLCDDIEVEVEDNKITKVR---NACRIGAAKFARYER---------------RITTPRI------DGKPVSLE 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 134 AAFALVAEHLRRLDSPdqaEFYTSGRASNEA-AYLYQLfvrAFGTNN-FPDCSNMCHEASGVALGRSvgvGKGSVTFDDF 211
Cdd:cd02761 58 EAIEKAAEILKEAKRP---LFYGLGTTVCEAqRAGIEL---AEKLGAiIDHAASVCHGPNLLALQDS---GWPTTTLGEV 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 212 EH-ADAIFILGQNPGTNHPRMLEplREAVkrgaqvvcFNplkeRGLERfQHPQNALEMLTNGSSPLNTAffrpalggdma 290
Cdd:cd02761 129 KNrADVIVYWGTNPMHAHPRHMS--RYSV--------FP----RGFFR-EGGREDRTLIVVDPRKSDTA----------- 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 291 airGIAKFLLawereaQAegsEPVFDHAFIAEhtdgLEAYLAELDATPwehlERQSGLSLAEIEQAARMYRRANRVIVCW 370
Cdd:cd02761 183 ---KLADIHL------QI---DPGSDYELLAA----LRALLRGAGLVP----DEVAGIPAETILELAERLKNAKFGVIFW 242
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 15600374 371 AMGITQHHHSVAIIQEIVNLQLLRGNLGRpgAGLCPVRGHSNVQG 415
Cdd:cd02761 243 GLGLLPSRGAHRNIEAAIRLVKALNEYTK--FALLPLRGHYNVRG 285
|
|
| MopB_Res-Cmplx1_Nad11 |
cd02773 |
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone ... |
108-245 |
7.67e-05 |
|
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: 45.72 E-value: 7.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 108 LEYQgRLTGPMRYDPlsDHYQPITWDAAFALVAEHLRRLdSPDQAEFYTSGRASNEAAYLYQLFVRAFGtnnfpdCSNMC 187
Cdd:cd02773 49 LKRQ-RLDKPYIRKN--GKLKPATWEEALAAIAKALKGV-KPDEIAAIAGDLADVESMVALKDLLNKLG------SENLA 118
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600374 188 HEASGVALGRSVgvgKGSVTF----DDFEHADAIFILGQNPGTNHPRMLEPLREAV-KRGAQV 245
Cdd:cd02773 119 CEQDGPDLPADL---RSNYLFnttiAGIEEADAVLLVGTNPRFEAPVLNARIRKAWlHGGLKV 178
|
|
| Molydop_binding |
pfam01568 |
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
652-736 |
1.01e-04 |
|
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: 42.26 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 652 LILQTLRSHDQYNTTIYGLDDRYRGvKGQREVVFANEADIRRLGYQPGDKVDLVSLWSDgIERRVRRFTllafDIPAGQA 731
Cdd:pfam01568 1 LYLITGRVLGQYHSQTRTRRVLRLA-KPEPEVVEIHPEDAAALGIKDGDLVEVTSRRGS-VVVRAKVTD----RVRPGVV 74
|
....*
gi 15600374 732 AAYYP 736
Cdd:pfam01568 75 FMPFG 79
|
|
| MopB_DMSOR-BSOR-TMAOR |
cd02769 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
107-403 |
1.63e-03 |
|
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: 41.86 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 107 WLEYQGRLTGPMRYDplsDHYQPITWDAAFALVAEHLRRldspdqaefyTSGRASNEAaylyqLFVRAFG---TNNFPDC 183
Cdd:cd02769 56 WLEKGPGSDRSLRGK---EEFVRVSWDEALDLVAAELKR----------VRKTYGNEA-----IFGGSYGwssAGRFHHA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 184 SNMCHEASGVALG--RSVG---VGKGSV-------TFDDF-----------EHADAIFILGQNP---------GTNHPRM 231
Cdd:cd02769 118 QSLLHRFLNLAGGyvGSVGdysTGAAQVilphvvgSMEVYteqqtswpviaEHTELVVAFGADPlknaqiawgGIPDHQA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 232 LEPLREAVKRGAQVVCFNPLKerglerfqhpqnalemlTNGSSPLNTAFFRPALGGDMAAIRGIAKFLLawereaqaegS 311
Cdd:cd02769 198 YSYLKALKDRGIRFISISPLR-----------------DDTAAELGAEWIAIRPGTDVALMLALAHTLV----------T 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600374 312 EPVFDHAFIAEHTDGLEAYLAEL----DATP----WEhlERQSGLSLAEIEQ-AARMYRRANRVIVCWAMgiTQHHHSVA 382
Cdd:cd02769 251 EGLHDKAFLARYTVGFDKFLPYLlgesDGVPktpeWA--AAICGIPAETIRElARRFASKRTMIMAGWSL--QRAHHGEQ 326
|
330 340
....*....|....*....|.
gi 15600374 383 IIQEIVNLQLLRGNLGRPGAG 403
Cdd:cd02769 327 PHWMAVTLAAMLGQIGLPGGG 347
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