|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09939 |
PRK09939 |
acid resistance putative oxidoreductase YdeP; |
1-757 |
0e+00 |
|
acid resistance putative oxidoreductase YdeP;
Pssm-ID: 182156 [Multi-domain] Cd Length: 759 Bit Score: 1194.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 1 MKKKIEEYDGPAAGWGAVKAVAEALRGQMKVGHDIIAMFEMNKVDGFDCPGCAWPDPVHTASFDICENGAKAIAWEATSK 80
Cdd:PRK09939 1 MKKKIESYQGAAGGWGAVKSVANAVRKQMDIRQDVIAMFDMNKPEGFDCPGCAWPDPKHSASFDICENGAKAIAWEVTDK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 81 KTTPEFFSKYTVTELLEWDDFHLEDEGRLTHPMKYNSQTDKYEPIEWEEAFQQIGTRLQSYSDPNTVEFYTSGRTSNEAA 160
Cdd:PRK09939 81 QVNASFFAENTVQSLLTWGDHELEAAGRLTQPLKYDAVSDCYKPLSWQQAFDEIGARLQSYSDPNQVEFYTSGRTSNEAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 161 FLYQLLAREYGTNNFPDCSNMCHEPTSVGLADSIGVGKATVLLDDFDKADLVICIGHNPGTNHPRMLSSLREVSKRGAKI 240
Cdd:PRK09939 161 FLYQLFAREYGSNNFPDCSNMCHEPTSVGLAASIGVGKGTVLLEDFEKCDLVICIGHNPGTNHPRMLTSLRALVKRGAKM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 241 IAINPLRERGLERFAYPQDVVEMLTLESTPLAGHYYKVRIGGDTALLKGVMKLLIEKHQAAVDAGKEPILDTEFISTHTQ 320
Cdd:PRK09939 241 IAINPLQERGLERFTAPQNPFEMLTNSETQLASAYYNVRIGGDMALLKGMMRLLIERDDAASAAGRPSLLDDEFIQTHTV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 321 GYEALKNDLETTSWKDILRVSGLPRESIEEIADLYIEAKSTIICYGMGITQHEHGTQNVQQLVNLLLLKGNIGREGAGIC 400
Cdd:PRK09939 321 GFDELRRDVLNSEWKDIERISGLSQTQIAELADAYAAAERTIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGIC 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 401 PLRGHSNVQGDRTVGITEKPSKSFLDKIEQRFGFKPPSEFGHAAVASMQAISEGKANALICMGGNLAVAMPDRDACFSGM 480
Cdd:PRK09939 401 PLRGHSNVQGDRTVGITEKPSAEFLARLGERYGFTPPHAPGHAAIASMQAICTGQARALICMGGNFALAMPDREASAVPL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 481 KKLDLAVHTATKLNRSHLLTAKQTFILPVLGRSEIDRQSSGVQCVTVEDSMSMVHASKGLLKPCSPYLKSECAIVAGIAK 560
Cdd:PRK09939 481 TQLDLAVHVATKLNRSHLLTARHSYILPVLGRSEIDMQKSGAQAVTVEDSMSMIHASRGVLKPAGVMLKSECAVVAGIAQ 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 561 AAIPQSKVEWDDFIGNYDLIRDAMEAVLPGFDDYNARIKIPGGFHLTNAASERRWLTQSGKANFVPTEGVIEDPNSAVNS 640
Cdd:PRK09939 561 AALPQSVVAWEYLVEDYDRIRNDIEAVLPEFADYNQRIRHPGGFHLINAAAERRWMTPSGKANFITSKGLLEDPSSAFNS 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 641 ELILATLRSHDQYNTTIYGLNDRYRGVFGQRDVVFISGAEAQKQKLEAGDKVNLIALDREQKPTKRRLDNLTVVIYDMAD 720
Cdd:PRK09939 641 KLVMATVRSHDQYNTTIYGMDDRYRGVFGQRDVVFMSAKQAKICRVKNGERVNLIALTPDGKRSSRRMDRLKVVIYPMAD 720
|
730 740 750
....*....|....*....|....*....|....*..
gi 1327840248 721 RSVATYFPEANNLISLDNFDPQCGIPAYKNIPVKLER 757
Cdd:PRK09939 721 RSLVTYFPESNHMLTLDNHDPLSGIPGYKSIPVELEP 757
|
|
| Fdhalpha-like |
TIGR01701 |
oxidoreductase alpha (molybdopterin) subunit; This model represents a well-defined clade of ... |
11-757 |
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: 1007.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 11 PAAGWGAVKAVAEALRGQMKVGHDIIAMFEMNKVDGFDCPGCAWPD-PVHTASFDICENGAKAIAWEATSKKTTPEFFSK 89
Cdd:TIGR01701 1 DAGGWGAVKSVALGKVKPMHIRQTLKLLLTLNKPEGYDCPGCAWGVsPQTLAGLEFCENGAKAIAWETTPRTIDPEFFAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 90 YTVTELLEWDDFHLEDEGRLTHPMKYNSQTDKYEPIEWEEAFQQIGTRLQSYsDPNTVEFYTSGRTSNEAAFLYQLLARE 169
Cdd:TIGR01701 81 HSVSELRTLDSHELEKLGRLTYPLSLRPGSDHYTPISWDDAYQEIAAKLNSL-DPKQVAFYTSGRTSNEAAYLYQLFARS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 170 YGTNNFPDCSNMCHEPTSVGLADSIGVGKATVLLDDFDKADLVICIGHNPGTNHPRMLSSLREVSKRGAKIIAINPLRER 249
Cdd:TIGR01701 160 LGSNNLPDCSNMCHEPSSVALKRSIGIGKGSVNLEDFEHTDCLVFIGSNAGTNHPRMLKYLYAAKKRGAKIIAINPLRER 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 250 GLERFAYPQDVVEMLTLESTPLAGHYYKVRIGGDTALLKGVMKLLIEkhqaAVDAGKEPILDTEFISTHTQGYEALKNDL 329
Cdd:TIGR01701 240 GLERFWIPQIPESMLTGGGTQISSEYYQVRIGGDIALFNGVMKLLIE----AEDAQPGSLIDHEFIANHTNGFDELRRHV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 330 ETTSWKDILRVSGLPRESIEEIADLYIEAKSTIICYGMGITQHEHGTQNVQQLVNLLLLKGNIGREGAGICPLRGHSNVQ 409
Cdd:TIGR01701 316 LQLNWNDIERSSGLSQEEILEFAKLLANSRRVVFCWAMGLTQHAHGVDNISQVANLALLRGNIGKPGAGVCPIRGHSNVQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 410 GDRTVGITEKPSKSFLDKIEQRFGFKPPSEFGHAAVASMQAISEGKANALICMGGNLAVAMPDRDACFSGMKKLDLAVHT 489
Cdd:TIGR01701 396 GDRTMGITEKPEEEFLARLSQIYGFTPPDWPGDTTVAMIEAILTGKVRAFICLGGNFLEAMPDTAAIERALRQLDLRVHV 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 490 ATKLNRSHLLTAKQTFILPVLGRSEIDRQSSGVQCVTVEDSMSMVHASKGLLKPCSPYLKSECAIVAGIAKAAIPQSKVE 569
Cdd:TIGR01701 476 ATKLNRSHVLAKEEALILPVLGRYEQDGQGTGKQAVSVESSMRMVHFSRGILKPRGAELRSEWAIIAEIAKALLPETPVA 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 570 WDDFIGNYDLIRDAMEAVLPGFDDYNARIKIPGGFHLTNAA-SERRWLTQSGKANFVPTEGVIEDPNSAVNSELILATLR 648
Cdd:TIGR01701 556 WEILVDTYDQIRDAIAATNPGYDDINHRKRRPDGFQLPGAAlCERKFPTPDGKANFIVIPLPEFRVPTGHEFELVLVTLR 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 649 SHDQYNTTIYGLNDRYRGVFGQRDVVFISGAEAQKQKLEAGDKVNLIALDREQkpTKRRLDNLTVVIYDMADRSVATYFP 728
Cdd:TIGR01701 636 SHDQFNTTIYGEDDRYRGVDGHRRVVFMNETDIKKLGLRNGERVDVYNQYGDG--QKRKFDNLRIVFYDTPTGNAAAYYP 713
|
730 740
....*....|....*....|....*....
gi 1327840248 729 EANNLISLDNFDPQCGIPAYKNIPVKLER 757
Cdd:TIGR01701 714 EANPLLPLDHHDPQSKTPEYKTIPVRLEA 742
|
|
| MopB_ydeP |
cd02767 |
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
46-624 |
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: 895.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 46 GFDCPGCAWPDPVHT-ASFDICENGAKAIAWEATSKKTTPEFFSKYTVTELLEWDDFHLEDEGRLTHPMKYNSQTDKYEP 124
Cdd:cd02767 1 GFDCPGCAWGDPGQKlHGFEFCENGAKALAWETTPKRVTPEFFALHSVSELRTWSDYELEHLGRLTYPMRYDAGSDHYRP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 125 IEWEEAFQQIGTRLQSYsDPNTVEFYTSGRTSNEAAFLYQLLAREYGTNNFPDCSNMCHEPTSVGLADSIGVGKATVLLD 204
Cdd:cd02767 81 ISWDEAFAEIAARLRAL-DPDRAAFYTSGRASNEAAYLYQLFARAYGTNNLPDCSNMCHEPSSVGLKKSIGVGKGTVSLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 205 DFDKADLVICIGHNPGTNHPRMLSSLREVSKRGAKIIAINPLRERGLERFAYPQDVVEMLTLeSTPLAGHYYKVRIGGDT 284
Cdd:cd02767 160 DFEHTDLIFFIGQNPGTNHPRMLHYLREAKKRGGKIIVINPLREPGLERFANPQNPESMLTG-GTKIADEYFQVRIGGDI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 285 ALLKGVMKLLIEKHQAAVDAgkepiLDTEFISTHTQGYEALKNDLETTSWKDILRVSGLPRESIEEIADLYIEAKSTIIC 364
Cdd:cd02767 239 ALLNGMAKHLIERDDEPGNV-----LDHDFIAEHTSGFEEYVAALRALSWDEIERASGLSREEIEAFAAMYAKSERVVFV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 365 YGMGITQHEHGTQNVQQLVNLLLLKGNIGREGAGICPLRGHSNVQGDRTVGITEKPSKSFLDKIEQRFGFKPPSEFGHAA 444
Cdd:cd02767 314 WGMGITQHAHGVDNVRAIVNLALLRGNIGRPGAGLMPIRGHSNVQGDRTMGITEKPFPEFLDALEEVFGFTPPRDPGLDT 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 445 VASMQAISEGKANALICMGGNLAVAMPDRDACFSGMKKLDLAVHTATKLNRSHLLTAKQTFILPVLGRSEIDRQSSGVQC 524
Cdd:cd02767 394 VEAIEAALEGKVKAFISLGGNFAEAMPDPAATEEALRRLDLTVHVATKLNRSHLVHGEEALILPCLGRTEIDMQAGGAQA 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 525 VTVEDSMSMVHASKGLLKPCSPYLKSECAIVAGIAKAAIPQSKVEWDDFIGNYDLIRDAMEAVLP-GFDDYNARIKIPGG 603
Cdd:cd02767 474 VTVEDSMSMTHTSRGRLKPASRVLLSEEAIVAGIAGARLGEAKPEWEILVEDYDRIRDEIAAVIYeGFADFNQRGDQPGG 553
|
570 580
....*....|....*....|.
gi 1327840248 604 FHLTNAASERRWLTQSGKANF 624
Cdd:cd02767 554 FHLPNGARERKFNTPSGKAQF 574
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
100-758 |
3.31e-143 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 435.81 E-value: 3.31e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 100 DFHLEDEGRLTHPMKYNSQ--TDKYEPIEWEEAFQQIGTRLQSYSD---PNTVEFYTSG----RTSNEAAFLYQLLAREY 170
Cdd:COG0243 70 DERLYSPDRLTYPMKRVGPrgSGKFERISWDEALDLIAEKLKAIIDeygPEAVAFYTSGgsagRLSNEAAYLAQRFARAL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 171 GTNNFPDCSNMCHEPTSVGLADSIGVGKATVLLDDFDKADLVICIGHNPGTNHPRMLSSLRE-VSKRGAKIIAINPLREr 249
Cdd:COG0243 150 GTNNLDDNSRLCHESAVAGLPRTFGSDKGTVSYEDLEHADLIVLWGSNPAENHPRLLRRLREaAKKRGAKIVVIDPRRT- 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 250 glerfaypqdvvemltlESTPLAGHYYKVRIGGDTALLKGVMKLLIEkhqaavdagkEPILDTEFISTHTQGYEALKNDL 329
Cdd:COG0243 229 -----------------ETAAIADEWLPIRPGTDAALLLALAHVLIE----------EGLYDRDFLARHTVGFDELAAYV 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 330 ETTSWKDILRVSGLPRESIEEIADLYIEAKSTIICYGMGITQHEHGTQNVQQLVNLLLLKGNIGREGAGICPLRGHsnvq 409
Cdd:COG0243 282 AAYTPEWAAEITGVPAEDIRELAREFATAKPAVILWGMGLQQHSNGTQTVRAIANLALLTGNIGKPGGGPFSLTGE---- 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 410 gdrtvgitekpsksfldkieqrfgfkppsefghaavasmqAISEGK---ANALICMGGNLAVAMPDRDACFSGMKKLDLA 486
Cdd:COG0243 358 ----------------------------------------AILDGKpypIKALWVYGGNPAVSAPDTNRVREALRKLDFV 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 487 VHTATKLNRSHLLTAkqtFILPVLGRSEIDrqssGVqCVTVEDsmSMVHASKGLLKPcsPY-LKSECAIVAGIAKA---- 561
Cdd:COG0243 398 VVIDTFLTETARYAD---IVLPATTWLERD----DI-VTNSED--RRVHLSRPAVEP--PGeARSDWEIFAELAKRlgfe 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 562 -AIPQSKVEWddfignyDLIRDAMEAVLPG---FDDYNARikipGGFHLTNAAS-----ERRWLTQSGKANFVPTEGVIE 632
Cdd:COG0243 466 eAFPWGRTEE-------DYLRELLEATRGRgitFEELREK----GPVQLPVPPEpafrnDGPFPTPSGKAEFYSETLALP 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 633 ------DPNSAVNSE-----LILATLRSHDQYNTTIYGlNDRYRGVFGqRDVVFISGAEAQKQKLEAGDKVNLIaldreq 701
Cdd:COG0243 535 plpryaPPYEGAEPLdaeypLRLITGRSRDQWHSTTYN-NPRLREIGP-RPVVEINPEDAAALGIKDGDLVRVE------ 606
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1327840248 702 kpTKR-RLDNLTVVIYDMADRSVATYF-----------PEANNLISlDNFDPQCGIPAYKNIPVKLERV 758
Cdd:COG0243 607 --SDRgEVLARAKVTEGIRPGVVFAPHgwwyepaddkgGNVNVLTP-DATDPLSGTPAFKSVPVRVEKA 672
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
102-758 |
2.27e-98 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 319.14 E-value: 2.27e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 102 HLEDEGRLTHPMKYnsQTDKYEPIEWEEAFQQIGTRLQSYSD---PNTVEFYTSGRTSNEAAFLYQLLAREY-GTNNFPD 177
Cdd:COG3383 55 FVNSPDRLTTPLIR--RGGEFREVSWDEALDLVAERLREIQAehgPDAVAFYGSGQLTNEENYLLQKLARGVlGTNNIDN 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 178 CSNMCHEPTSVGLADSIGVGKATVLLDDFDKADLVICIGHNPGTNHPRMLSSLREVSKRGAKIIAINPlRERGLERFAyp 257
Cdd:COG3383 133 NARLCMASAVAGLKQSFGSDAPPNSYDDIEEADVILVIGSNPAEAHPVLARRIKKAKKNGAKLIVVDP-RRTETARLA-- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 258 qdvvemltlestplaGHYYKVRIGGDTALLKGVMKLLIEkhqaavdagkEPILDTEFISTHTQGYEALKNDLETTSWKDI 337
Cdd:COG3383 210 ---------------DLHLQIKPGTDLALLNGLLHVIIE----------EGLVDEDFIAERTEGFEELKASVAKYTPERV 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 338 LRVSGLPRESIEEIADLYIEAKSTIICYGMGITQHEHGTQNVQQLVNLLLLKGNIGREGAGICPLRGHSNVQGDRTVGIt 417
Cdd:COG3383 265 AEITGVPAEDIREAARLIAEAKRAMILWGMGVNQHTQGTDNVNAIINLALATGNIGRPGTGPFPLTGQNNVQGGRDMGA- 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 418 eKPS-----KSFLD-----KIEQRFGFKP-PSEFGHAAVASMQAISEGKANALICMGGNLAVAMPDRDACFSGMKKLDLA 486
Cdd:COG3383 344 -LPNvlpgyRDVTDpehraKVADAWGVPPlPDKPGLTAVEMFDAIADGEIKALWIIGENPAVSDPDANHVREALEKLEFL 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 487 VHTATKLNRshllTAKQ-TFILPVLGRSEIDrqssGvqcvTVEDSMSMVHASKGLLKPcSPYLKSECAIVAGIAKAAipq 565
Cdd:COG3383 423 VVQDIFLTE----TAEYaDVVLPAASWAEKD----G----TFTNTERRVQRVRKAVEP-PGEARPDWEIIAELARRL--- 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 566 sKVEWDdfignYD---LIRDAMEAVLPGFD--DYnARIKIPGGFHLTNAASER---------RWLTQSGKANFVPTEGVi 631
Cdd:COG3383 487 -GYGFD-----YDspeEVFDEIARLTPDYSgiSY-ERLEALGGVQWPCPSEDHpgtprlftgRFPTPDGKARFVPVEYR- 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 632 eDPNSAVNSE--LILATLRSHDQYNTT-----IYGLNDRYrgvfgQRDVVFISGAEAQKQKLEAGDKVnLIALDREQKPT 704
Cdd:COG3383 559 -PPAELPDEEypLVLTTGRLLDQWHTGtrtrrSPRLNKHA-----PEPFVEIHPEDAARLGIKDGDLV-RVSSRRGEVVL 631
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 1327840248 705 KRRLDNltvviyDMADRSVATYF--PEAN-NLISLDNFDPQCGIPAYKNIPVKLERV 758
Cdd:COG3383 632 RARVTD------RVRPGTVFMPFhwGEGAaNALTNDALDPVSKQPEYKACAVRVEKV 682
|
|
| Fdh-alpha |
TIGR01591 |
formate dehydrogenase, alpha subunit, archaeal-type; This model describes a subset of formate ... |
98-755 |
2.47e-78 |
|
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: 265.10 E-value: 2.47e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 98 WDdfHLEDEGRLTHPMKynSQTDKYEPIEWEEAFQQIGTRL---QSYSDPNTVEFYTSGRTSNEAAFLYQLLARE-YGTN 173
Cdd:TIGR01591 45 WE--FINSKDRLTTPLI--REGDKFREVSWDEAISYIAEKLkeiKEKYGPDSIGFIGSSRGTNEENYLLQKLARAvIGTN 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 174 NFPDCSNMCHEPTSVGLADSIGVGKATVLLDDFDKADLVICIGHNPGTNHPRMLSSLREVSKRGAKIIAINPlRERGLER 253
Cdd:TIGR01591 121 NVDNCARVCHGPSVAGLKQTVGIGAMSNTISEIENADLIVIIGYNPAESHPVVAQYLKNAKRNGAKIIVIDP-RKTETAK 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 254 FAypqdvvemltlestplaGHYYKVRIGGDTALLKGVMKLLIEkhqaavdagkEPILDTEFISTHTQGYEALKNDLETTS 333
Cdd:TIGR01591 200 IA-----------------DLHIPLKPGTDIALLNAMANVIIE----------EGLYDKAFIEKRTEGFEEFREIVKGYT 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 334 WKDILRVSGLPRESIEEIADLYIEAKSTIICYGMGITQHEHGTQNVQQLVNLLLLKGNIGREGAGICPLRGHSNVQGDRT 413
Cdd:TIGR01591 253 PEYVEDITGVPADLIREAARMYAKAGSAAILWGMGVTQHSQGVETVMALINLAMLTGNIGKPGGGVNPLRGQNNVQGACD 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 414 VGI--TEKP------SKSFLDKIEQRFGFKP-PSEFGHAAVASMQAISEGKANALICMGGNLAVAMPDRDACFSGMKKLD 484
Cdd:TIGR01591 333 MGAlpDFLPgyqpvsDEEVREKFAKAWGVVKlPAEPGLRIPEMIDAAADGDVKALYIMGEDPLQSDPNTSKVRKALEKLE 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 485 LAVHTATKLNRshllTAKQT-FILPVLGRSEIDrqssGVqCVTVEDSMSMVHaskgllKPCSPY--LKSECAIVAGIAKA 561
Cdd:TIGR01591 413 LLVVQDIFMTE----TAKYAdVVLPAAAWLEKE----GT-FTNAERRIQRFF------KAVEPKgeSKPDWEIIQELANA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 562 aipqskVEWDDFIGNYDLIRDAMEAVLPGF--------DDYNA--RIKIPGGFHLTNAASERRWLTQSGKANFVPTEGVI 631
Cdd:TIGR01591 478 ------LGLDWNYNHPQEIMDEIRELTPLFagltyerlDELGSlqWPCNDSDASPTSYLYKDKFATPDGKAKFIPLEWVA 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 632 EDPNSAVNSELILATLRSHDQYNTTiyGLNDRYRGV--FGQRDVVFISGAEAQKQKLEAGDKVNLIALDREQKPTKRRLD 709
Cdd:TIGR01591 552 PIEEPDDEYPLILTTGRVLTHYNVG--EMTRRVAGLrrLSPEPYVEINTEDAKKLGIKDGDLVKVKSRRGEITLRAKVSD 629
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1327840248 710 NLTVVIYDMAdrsVATYFPEANNLISlDNFDPQCGIPAYKNIPVKL 755
Cdd:TIGR01591 630 RVNKGAIYIT---MHFWDGAVNNLTT-DDLDPISGTPEYKYTAVRI 671
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
98-487 |
1.88e-70 |
|
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: 239.81 E-value: 1.88e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 98 WDDFHLEDegRLTHPMKynSQTDKYEPIEWEEAFQQIGTRLQSYSD---PNTVEFYTSGRTSNEAAFLYQLLARE-YGTN 173
Cdd:cd02753 46 FDFVNSKD--RLTKPLI--RKNGKFVEASWDEALSLVASRLKEIKDkygPDAIAFFGSAKCTNEENYLFQKLARAvGGTN 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 174 NFPDCSNMCHEPTSVGLADSIGVGKATVLLDDFDKADLVICIGHNPGTNHPRMLSSLREVSKRGAKIIAINPlRERGLER 253
Cdd:cd02753 122 NVDHCARLCHSPTVAGLAETLGSGAMTNSIADIEEADVILVIGSNTTEAHPVIARRIKRAKRNGAKLIVADP-RRTELAR 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 254 FAYpqdvvemltlestplagHYYKVRIGGDTALLKGVMKLLIEkhqaavdagkEPILDTEFISTHTQGYEALKNDLETTS 333
Cdd:cd02753 201 FAD-----------------LHLQLRPGTDVALLNAMAHVIIE----------EGLYDEEFIEERTEGFEELKEIVEKYT 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 334 WKDILRVSGLPRESIEEIADLYIEAKSTIICYGMGITQHEHGTQNVQQLVNLLLLKGNIGREGAGICPLRGHSNVQGDRT 413
Cdd:cd02753 254 PEYAERITGVPAEDIREAARMYATAKSAAILWGMGVTQHSHGTDNVMALSNLALLTGNIGRPGTGVNPLRGQNNVQGACD 333
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1327840248 414 VGitekpsksfldkieqrfgfKPPSEFghaavasmqaisEGKANALICMGGNLAVAMPDRDACFSGMKKLDLAV 487
Cdd:cd02753 334 MG-------------------ALPNVL------------PGYVKALYIMGENPALSDPNTNHVRKALESLEFLV 376
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
102-561 |
1.49e-62 |
|
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: 214.11 E-value: 1.49e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 102 HLEDEGRLTHPMKYNSQTDKYEPIEWEEAFQQIGTRLQSYSD---PNTVEFYTSGRTSNEAAFLYQLLAREYGTNNFPDC 178
Cdd:cd00368 48 GLYSPDRLKYPLIRVGGRGKFVPISWDEALDEIAEKLKEIREkygPDAIAFYGGGGASNEEAYLLQKLLRALGSNNVDSH 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 179 SNMCHEPTSVGLADsIGVGKATVLLDDFDKADLVICIGHNPGTNHPRMLSSLREVSKRGAKIIAINPLRERglerfaypq 258
Cdd:cd00368 128 ARLCHASAVAALKA-FGGGAPTNTLADIENADLILLWGSNPAETHPVLAARLRRAKKRGAKLIVIDPRRTE--------- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 259 dvvemltleSTPLAGHYYKVRIGGDTALLKGvmklliekhqaavdagkepildtefisthtqgyealkndlettswKDIL 338
Cdd:cd00368 198 ---------TAAKADEWLPIRPGTDAALALA---------------------------------------------EWAA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 339 RVSGLPRESIEEIADLYIEAKSTIICYGMGITQHEHGTQNVQQLVNLLLLKGNIGREGAGICPlrghsnvqgdrtvgite 418
Cdd:cd00368 224 EITGVPAETIRALAREFAAAKRAVILWGMGLTQHTNGTQNVRAIANLAALTGNIGRPGGGLGP----------------- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 419 kpsksfldkieqrfgfkppsefghaavasmqaisegkanalicmGGNLAVAMPDRDACFSGMKKLDLAVHTATKLNRSHL 498
Cdd:cd00368 287 --------------------------------------------GGNPLVSAPDANRVRAALKKLDFVVVIDIFMTETAA 322
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1327840248 499 LTakqTFILPVLGRSEidrqSSGvqcvTVEDSMSMVHASKGLLKPcsPY-LKSECAIVAGIAKA 561
Cdd:cd00368 323 YA---DVVLPAATYLE----KEG----TYTNTEGRVQLFRQAVEP--PGeARSDWEILRELAKR 373
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
102-487 |
6.21e-53 |
|
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: 192.83 E-value: 6.21e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 102 HLEDEGRLTHPMkYNSQTDKYEPIEWEEAFQQIGTRLQSYSD---PNTVEFYTSGRTSNEAAFLYQLLAREY-GTNNFPD 177
Cdd:cd02754 48 TLNGPERLTRPL-LRRNGGELVPVSWDEALDLIAERFKAIQAeygPDSVAFYGSGQLLTEEYYAANKLAKGGlGTNNIDT 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 178 CSNMCHEPTSVGLADSIGVGKATVLLDDFDKADLVICIGHNPGTNHPRMLSSLREVSK--RGAKIIAINPLRERglerfa 255
Cdd:cd02754 127 NSRLCMASAVAGYKRSFGADGPPGSYDDIEHADCFFLIGSNMAECHPILFRRLLDRKKanPGAKIIVVDPRRTR------ 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 256 ypqdvvemltleSTPLAGHYYKVRIGGDTALLKGVMKLLIEKHQAavdagkepilDTEFISTHTQGYEALKNDLETTSWK 335
Cdd:cd02754 201 ------------TADIADLHLPIRPGTDLALLNGLLHVLIEEGLI----------DRDFIDAHTEGFEELKAFVADYTPE 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 336 DILRVSGLPRESIEEIADLYIEAKSTIICYGMGITQHEHGTQNVQQLVNLLLLKGNIGREGAGICPLRGHSNVQGDRTVG 415
Cdd:cd02754 259 KVAEITGVPEADIREAARLFGEARKVMSLWTMGVNQSTQGTAANNAIINLHLATGKIGRPGSGPFSLTGQPNAMGGREVG 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 416 -----------ITEKPSKSFLDKI----EQRFGFKPpsefGHAAVASMQAISEGKANALICMGGNLAVAMPDRDACFSGM 480
Cdd:cd02754 339 glanllpghrsVNNPEHRAEVAKFwgvpEGTIPPKP----GLHAVEMFEAIEDGEIKALWVMCTNPAVSLPNANRVREAL 414
|
....*..
gi 1327840248 481 KKLDLAV 487
Cdd:cd02754 415 ERLEFVV 421
|
|
| MopB_CT_ydeP |
cd02787 |
The MopB_CT_ydeP CD includes a group of related uncharacterized bacterial ... |
642-755 |
8.51e-47 |
|
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: 161.67 E-value: 8.51e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 642 LILATLRSHDQYNTTIYGLNDRYRGVFGQRDVVFISGAEAQKQKLEAGDKVNLIALDREQKPtkRRLDNLTVVIYDMADR 721
Cdd:cd02787 1 LFLVTTRSHDQFNTTIYGLDDRYRGVFGRRDVVFMNPDDIARLGLKAGDRVDLESAFGDGQG--RIVRGFRVVEYDIPRG 78
|
90 100 110
....*....|....*....|....*....|....
gi 1327840248 722 SVATYFPEANNLISLDNFDPQCGIPAYKNIPVKL 755
Cdd:cd02787 79 CLAAYYPEGNVLVPLDHRDPQSKTPAYKSVPVRL 112
|
|
| MopB_Formate-Dh-Na-like |
cd02752 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
102-410 |
2.87e-38 |
|
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: 151.78 E-value: 2.87e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 102 HLEDEGRLTHPMKYNSQTDKYEPIEWEEAFQQIGTRLQSYSD---------------PNTVEFYTSGRTSNEAAFLYQLL 166
Cdd:cd02752 48 FVHSPKRLKYPMYRAPGSGKWEEISWDEALDEIARKMKDIRDasfveknaagvvvnrPDSIAFLGSAKLSNEECYLIRKF 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 167 AREYGTNNFPDCSNMCHEPTSVGLADSIGVGKATVLLDDFDKADLVICIGHNPGTNHP-RMLSSLREVSKRGAKIIAINP 245
Cdd:cd02752 128 ARALGTNNLDHQARIUHSPTVAGLANTFGRGAMTNSWNDIKNADVILVMGGNPAEAHPvSFKWILEAKEKNGAKLIVVDP 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 246 LRERglerfaypqdvvemltleSTPLAGHYYKVRIGGDTALLKGVMKLLIekhqaavdagkepildtefisthtqgyeal 325
Cdd:cd02752 208 RFTR------------------TAAKADLYVPIRSGTDIAFLGGMINYII------------------------------ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 326 KNDLETTSwkdilRVSGLPRESIEEIADLYIE----AKSTIICYGMGITQHEHGTQNVQQLVNLLLLKGNIGREGAGICP 401
Cdd:cd02752 240 RYTPEEVE-----DICGVPKEDFLKVAEMFAAtgrpDKPGTILYAMGWTQHTVGSQNIRAMCILQLLLGNIGVAGGGVNA 314
|
....*....
gi 1327840248 402 LRGHSNVQG 410
Cdd:cd02752 315 LRGHSNVQG 323
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
87-487 |
3.01e-27 |
|
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: 116.73 E-value: 3.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 87 FSK-YTVTELLEWDDFHlEDEGRLTHPMKynSQTDKYEPIEWEEAFQQIGTRL---QSYSDPNTVEFYTSGRTSNEAA-- 160
Cdd:cd02762 33 LSKgYICPKAAALGDYQ-NDPDRLRTPMR--RRGGSFEEIDWDEAFDEIAERLraiRARHGGDAVGVYGGNPQAHTHAgg 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 161 -----FLYQLLAREYGTNNFPDcsNMCHEPTSVGLADSIGvgkaTVLLDDFDKADLVICIGHNPGTNH------PRMLSS 229
Cdd:cd02762 110 ayspaLLKALGTSNYFSAATAD--QKPGHFWSGLMFGHPG----LHPVPDIDRTDYLLILGANPLQSNgslrtaPDRVLR 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 230 LREVSKRGAKIIAINPLRErglerfaypqdvvemltlESTPLAGHYYKVRIGGDTALLKGVMKLLIEkhqaavdagkEPI 309
Cdd:cd02762 184 LKAAKDRGGSLVVIDPRRT------------------ETAKLADEHLFVRPGTDAWLLAAMLAVLLA----------EGL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 310 LDTEFISTHTQGYEALKNDLETTSWKDILRVSGLPRESIEEIADlYIEAKSTIICYG-MGITQHEHGTQNVQQLVNLLLL 388
Cdd:cd02762 236 TDRRFLAEHCDGLDEVRAALAEFTPEAYAPRCGVPAETIRRLAR-EFAAAPSAAVYGrLGVQTQLFGTLCSWLVKLLNLL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 389 KGNIGREGAGICPLrghSNVQGdrtVGITEKPSKSFLDKIEQRFGFKP-PSEFGHAAVA-SMQAISEGKANALICMGGNL 466
Cdd:cd02762 315 TGNLDRPGGAMFTT---PALDL---VGQTSGRTIGRGEWRSRVSGLPEiAGELPVNVLAeEILTDGPGRIRAMIVVAGNP 388
|
410 420
....*....|....*....|.
gi 1327840248 467 AVAMPDRDACFSGMKKLDLAV 487
Cdd:cd02762 389 VLSAPDGARLEAALGGLEFMV 409
|
|
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
108-399 |
3.82e-26 |
|
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: 113.11 E-value: 3.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 108 RLTHPMKY-NSQTDKYEPIEWEEAFQQIGTRLQSYSD---PNTVEFY----TSGRTSNEA-AFLYQLLareyGTNNF--P 176
Cdd:cd02766 55 RLLTPLKRvGRKGGQWERISWDEALDTIAAKLKEIKAeygPESILPYsyagTMGLLQRAArGRFFHAL----GASELrgT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 177 DCSNMCHEPTSVGLADSIGVgkatvLLDDFDKADLVICIGHNPGTNHPRMLSSLREVSKRGAKIIAINPLRerglerfay 256
Cdd:cd02766 131 ICSGAGIEAQKYDFGASLGN-----DPEDMVNADLIVIWGINPAATNIHLMRIIQEARKRGAKVVVIDPYR--------- 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 257 pqdvvemltlesTPLAGH---YYKVRIGGDTALLKGVMKLLIEkhqaavdagkEPILDTEFISTHTQGYEALKNDLETTS 333
Cdd:cd02766 197 ------------TATAARadlHIQIRPGTDGALALGVAKVLFR----------EGLYDRDFLARHTEGFEELKAHLETYT 254
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1327840248 334 WKDILRVSGLPRESIEEIADLYIEAKSTIICYGMGITQHEHGTQNVQQLVNLLLLKGNIGREGAGI 399
Cdd:cd02766 255 PEWAAEITGVSAEEIEELARLYGEAKPPSIRLGYGMQRYRNGGQNVRAIDALPALTGNIGVPGGGA 320
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
102-399 |
9.81e-22 |
|
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: 99.30 E-value: 9.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 102 HLEDEGRLTHPMKYNSQ--TDKYEPIEWEEAFQQIGTRLQSYSD---PNTVEFY-TSGRTSNEAAFLYQL-LAREYGTNN 174
Cdd:cd02759 48 IVYHPDRLLYPLKRVGErgENKWERISWDEALDEIAEKLAEIKAeygPESIATAvGTGRGTMWQDSLFWIrFVRLFGSPN 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 175 FPDCSNMCHEPTSVGLADSIGVGkATVLLDDFDKADLVICIGHNP-GTNHPRMLSSLREVSKRGAKIIAINPLRERGLER 253
Cdd:cd02759 128 LFLSGESCYWPRDMAHALTTGFG-LGYDEPDWENPECIVLWGKNPlNSNLDLQGHWLVAAMKRGAKLIVVDPRLTWLAAR 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 254 faypqdvvemltlestplAGHYYKVRIGGDTALLKGVMKLLIEkhqaavdagkEPILDTEFISTHTQGYEALKNDLETTS 333
Cdd:cd02759 207 ------------------ADLWLPIRPGTDAALALGMLNVIIN----------EGLYDKDFVENWCYGFEELAERVQEYT 258
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1327840248 334 WKDILRVSGLPRESIEEIADLYIEAKSTIICYGMGITQHEHGTQNVQQLVNLLLLKGNIGREGAGI 399
Cdd:cd02759 259 PEKVAEITGVPAEKIRKAARLYATAKPACIQWGLAIDQQKNGTQTSRAIAILRAITGNLDVPGGNL 324
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
105-487 |
9.75e-20 |
|
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: 92.75 E-value: 9.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 105 DEGRLTHPMKYNSQ--TDKYEPIEWEEAFQQIGTRLQSYSDPNTVEFYTSGRTSNEAAFLYQLLAREYGTNNFPDCSNMC 182
Cdd:cd02755 52 DPDRLKKPLIRVGErgEGKFREASWDEALQYIASKLKEIKEQHGPESVLFGGHGGCYSPFFKHFAAAFGSPNIFSHESTC 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 183 HEPTSVGLADSIGVGkATVLLDDFDKADLVICIGHN--PGTNHPRMlSSLREVSKRGAKIIAINPlrergleRFAypqdv 260
Cdd:cd02755 132 LASKNLAWKLVIDSF-GGEVNPDFENARYIILFGRNlaEAIIVVDA-RRLMKALENGAKVVVVDP-------RFS----- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 261 vemltlESTPLAGHYYKVRIGGDTALLKGVMKLLIEkhqaavdagkEPILDTEFISTHTQGYEALKNDLE--TTSWKDil 338
Cdd:cd02755 198 ------ELASKADEWIPIKPGTDLAFVLALIHVLIS----------ENLYDAAFVEKYTNGFELLKAHVKpyTPEWAA-- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 339 RVSGLPRESIEEIADLYIEAKSTIICYgmgitqhehgtqnvqqlvnllllkgnIGREGAgicplRGHSNVQGDRTVGITe 418
Cdd:cd02755 260 QITDIPADTIRRIAREFAAAAPHAVVD--------------------------PGWRGT-----FYSNSFQTRRAIAII- 307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1327840248 419 kpsKSFLDKIEQRFGFKPPsefghaavasmQAISEGKANALICMGGNLAVAMPDRDACFSGMKKLDLAV 487
Cdd:cd02755 308 ---NALLGNIDKRGGLYYA-----------GSAKPYPIKALFIYRTNPFHSMPDRARLIKALKNLDLVV 362
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
108-487 |
4.99e-19 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 89.38 E-value: 4.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 108 RLTHPMKYNSQtDKYEPIEWEEAFQQIGTRLQSY-----SDPNTVEFYTSGRTSNEAAFLYQLLAREYGTNNF---PDCS 179
Cdd:pfam00384 1 RLKYPMVRRGD-GKFVRVSWDEALDLIAKKLKRIikkygPDAIAINGGSGGLTDVESLYALKKLLNRLGSKNGnteDHNG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 180 NMCHEPTSVGLADSIGVGKATVLLDDFDKADLVICIGHNPGTNHPRMLSSLR-EVSKRGAKIIAINPLRErglerfaypq 258
Cdd:pfam00384 80 DLCTAAAAAFGSDLRSNYLFNSSIADIENADLILLIGTNPREEAPILNARIRkAALKGKAKVIVIGPRLD---------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 259 dvvemLTLESTPLAghyykVRIGGDTALLKGVMKLLIEKhqaavdagkepildtefisthtqgyeaLKNDlettswKDIl 338
Cdd:pfam00384 150 -----LTYADEHLG-----IKPGTDLALALAGAHVFIKE---------------------------LKKD------KDF- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 339 rvsglpresieeiadlyieAKSTIICYGMGITQHEHGTQNVQQLVNLLLLKGNIGREGAGICPLRGHSNVQGDrtVGITE 418
Cdd:pfam00384 186 -------------------APKPIIIVGAGVLQRQDGEAIFRAIANLADLTGNIGRPGGGWNGLNILQGAASP--VGALD 244
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1327840248 419 kpsksfldkieqrFGFKPPSEFghaaVASMQAISEGKANALICMGGNLAVAMPDRDACFSGMKKLDLAV 487
Cdd:pfam00384 245 -------------LGLVPGIKS----VEMINAIKKGGIKVLYLLGNNPFVTHADENRVVKALQKLDLFV 296
|
|
| MopB_NADH-Q-OR-NuoG2 |
cd02768 |
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone ... |
102-257 |
5.00e-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: 83.87 E-value: 5.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 102 HLEDEGRLTHPMKynSQTDKYEPIEWEEAFQQIGTRLQSySDPNTVEFYTSGRTSNEAAFLYQLLAREYGTNNFpDCSNM 181
Cdd:cd02768 48 GLNSRQRLTQPLI--KKGGKLVPVSWEEALKTVAEGLKA-VKGDKIGGIAGPRADLESLFLLKKLLNKLGSNNI-DHRLR 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1327840248 182 CHEPTSVGLADSIGVgkATVLLDDFDKADLVICIGHNPGTNHPRMLSSLRE-VSKRGAKIIAINPLRERGLERFAYP 257
Cdd:cd02768 124 QSDLPADNRLRGNYL--FNTSIAEIEEADAVLLIGSNLRKEAPLLNARLRKaVKKKGAKIAVIGPKDTDLIADLTYP 198
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
108-412 |
2.69e-15 |
|
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: 79.58 E-value: 2.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 108 RLTHPMK--------YNSQT----DKYEPIEWEEAFQQIGTRLQSYSDpntvefyTSGrtsNEAAFLYQllareYG---T 172
Cdd:cd02751 47 RIKYPMKrvgwlgngPGSRElrgeGEFVRISWDEALDLVASELKRIRE-------KYG---NEAIFGGS-----YGwasA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 173 NNFPDCSNMCHE-------------PTSVG---------LADSIGVGKATVLLDDFDKADLVICIGHNPGTN-------- 222
Cdd:cd02751 112 GRLHHAQSLLHRflnliggylgsygTYSTGaaqvilphvVGSDEVYEQGTSWDDIAEHSDLVVLFGANPLKTrqgggggp 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 223 HPRMLSSLREVSKRGAKIIAINPLRErglerfaypqDVVEMLTLESTPlaghyykVRIGGDTALLKGVMKLLIekhqaav 302
Cdd:cd02751 192 DHGSYYYLKQAKDAGVRFICIDPRYT----------DTAAVLAAEWIP-------IRPGTDVALMLAMAHTLI------- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 303 dagKEPILDTEFISTHTQGYEALKNDLE--------TTSWKDilRVSGLPRESIEEIADLyIEAKSTIICYGMGITQHEH 374
Cdd:cd02751 248 ---TEDLHDQAFLARYTVGFDEFKDYLLgesdgvpkTPEWAA--EITGVPAETIRALARE-IASKRTMIAQGWGLQRAHH 321
|
330 340 350
....*....|....*....|....*....|....*...
gi 1327840248 375 GTQNVQQLVNLLLLKGNIGREGAGICPLRGHSNVQGDR 412
Cdd:cd02751 322 GEQPAWMLVTLAAMLGQIGLPGGGFGFGYGYSNGGGPP 359
|
|
| MopB_FmdB-FwdB |
cd02761 |
The MopB_FmdB-FwdB CD contains the molybdenum/tungsten formylmethanofuran dehydrogenases, ... |
123-410 |
1.87e-14 |
|
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: 76.22 E-value: 1.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 123 EPIEWEEAFQQIGTRLQSYSDPntvEFYTSGRTSNEAAFLYQLLAREYGTNnFPDCSNMCHEPTSVGLADSigvGKATVL 202
Cdd:cd02761 52 KPVSLEEAIEKAAEILKEAKRP---LFYGLGTTVCEAQRAGIELAEKLGAI-IDHAASVCHGPNLLALQDS---GWPTTT 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 203 LDDF-DKADLVICIGHNPGTNHPRMLSSlrevskrgakiIAINPlreRGLERFAYPQD----VVEMLTLESTPLAGHYYK 277
Cdd:cd02761 125 LGEVkNRADVIVYWGTNPMHAHPRHMSR-----------YSVFP---RGFFREGGREDrtliVVDPRKSDTAKLADIHLQ 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 278 VRIGGDTALLKGVMklliekhqaAVDAGKEPILDTefisthtqgyealkndlettswkdilrVSGLPRESIEEIADLYIE 357
Cdd:cd02761 191 IDPGSDYELLAALR---------ALLRGAGLVPDE---------------------------VAGIPAETILELAERLKN 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1327840248 358 AKSTIICYGMGITQHEHGTQNVQQLVNLLLLKGNIGRegAGICPLRGHSNVQG 410
Cdd:cd02761 235 AKFGVIFWGLGLLPSRGAHRNIEAAIRLVKALNEYTK--FALLPLRGHYNVRG 285
|
|
| 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 ... |
102-243 |
4.11e-13 |
|
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: 72.42 E-value: 4.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 102 HLEDEGRLTHPMKynSQTDKYEPIEWEEAFQQIGTRLQSYSDpnTVEFYTSGRTSNEAAFLYQLLAREY-GTNNFpDCSN 180
Cdd:cd02771 48 YVNSRDRLTQPLI--RRGGTLVPVSWNEALDVAAARLKEAKD--KVGGIGSPRASNESNYALQKLVGAVlGTNNV-DHRA 122
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1327840248 181 MCHeptsvgLADSIGVGKA-TVLLDDFDKADLVICIGHNPGTNHPRMLSSLREVSKRGAKIIAI 243
Cdd:cd02771 123 RRL------IAEILRNGPIyIPSLRDIESADAVLVLGEDLTQTAPRIALALRQAARRKAVELAA 180
|
|
| MopB_2 |
cd02763 |
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
108-352 |
5.48e-12 |
|
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: 69.09 E-value: 5.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 108 RLTHPMKYNSQ--TDKYEPIEWEEAFQQIGTRLQSY--SDPNTVEFYTsGRTSNEAafLYQLLAREYGTNNFPDCSNMCH 183
Cdd:cd02763 54 RLTKPLLRKGPrgSGQFEEIEWEEAFSIATKRLKAAraTDPKKFAFFT-GRDQMQA--LTGWFAGQFGTPNYAAHGGFCS 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 184 EPTSVGLADSIGVGKATVLLDDFDKADLVICIGHNPGTNHPRMLSSLREVSKRGAKIIAINPLrergleRFAYpqdvvem 263
Cdd:cd02763 131 VNMAAGGLYSIGGSFWEFGGPDLEHTKYFMMIGVAEDHHSNPFKIGIQKLKRRGGKFVAVNPV------RTGY------- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 264 ltlesTPLAGHYYKVRIGGDTALLKGVMKLLIekhqaavdagKEPILDTEFISTHTQGYEALKNdleTTSWkdILRVSGL 343
Cdd:cd02763 198 -----AAIADEWVPIKPGTDGAFILALAHELL----------KAGLIDWEFLKRYTNAAELVDY---TPEW--VEKITGI 257
|
....*....
gi 1327840248 344 PRESIEEIA 352
Cdd:cd02763 258 PADTIRRIA 266
|
|
| MopB_DmsA-EC |
cd02770 |
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
108-429 |
7.85e-12 |
|
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: 68.50 E-value: 7.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 108 RLTHPMKYNSQT--DKYEPIEWEEAFQQIGTRLQS----------YSDPNTVEFYTSGRTSNEAAFLYQLLAREYGTNNF 175
Cdd:cd02770 59 RLKYPMKRVGKRgeGKFVRISWDEALDTIASELKRiiekygneaiYVNYGTGTYGGVPAGRGAIARLLNLTGGYLNYYGT 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 176 PDCSNMCHEPTSVGLADSIGVgkatvLLDDFDKADLVICIGHNP--------GTNHprmlsSLREVSKRGAKIIAINPlr 247
Cdd:cd02770 139 YSWAQITTATPYTYGAAASGS-----SLDDLKDSKLVVLFGHNPaetrmgggGSTY-----YYLQAKKAGAKFIVIDP-- 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 248 ergleRFAypqDVVEMLTLESTPLaghyykvRIGGDTALLKGVMKLLIekhqaavdagKEPILDTEFISTHTQGYEA--- 324
Cdd:cd02770 207 -----RYT---DTAVTLADEWIPI-------RPGTDAALVAAMAYVMI----------TENLHDQAFLDRYCVGFDAehl 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 325 ---------LKNDLE---------TTSWKDilRVSGLPRESIEEIADLYIEAKSTIICYGMGITQHEHGTQNVQQLVNLL 386
Cdd:cd02770 262 pegappnesYKDYVLgtgydgtpkTPEWAS--EITGVPAETIRRLAREIATTKPAAILQGWGPQRHANGEQAARAIMMLA 339
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1327840248 387 LLKGNIGREGAGICPLRGHSNVQGDRTVGITEK-----PSKSFLDKIE 429
Cdd:cd02770 340 AMTGNVGIPGGNTGARPGGSAYNGAGLPAGKNPvktsiPCFMWTDAIE 387
|
|
| FwdB |
COG1029 |
Formylmethanofuran dehydrogenase subunit B [Energy production and conversion]; |
102-410 |
4.62e-11 |
|
Formylmethanofuran dehydrogenase subunit B [Energy production and conversion];
Pssm-ID: 440652 [Multi-domain] Cd Length: 428 Bit Score: 65.64 E-value: 4.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 102 HLEDEGRLTHPMKynsqtdKYEPIEWEEAFQQIGTRLQSYSDPntvEFYTSGRTSNEAAFLYQLLAREYGTNnFPDCSNM 181
Cdd:COG1029 45 RAVSDHRITSPRI------RGKEVSLEEAIDKAAEILANAKRP---LIYGLSSTDCEAMRAGLALAERVGAV-VDNTASV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 182 CHEPTSVGLADsigVGKATVLLDDF-DKADLVICIGHNPGTNHPRMLSS--------LREVSKRGAKIIAINPLRErgle 252
Cdd:COG1029 115 CHGPSLLALQD---VGWPTCTLGEVkNRADVIIYWGCNPVHAHPRHMSRysvfprgfFTPKGRKDRTVIVVDPRPT---- 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 253 rfaypqdvvemltlESTPLAGHYYKVRIGGDTALLkGVMKLLIekhqaavdAGKEPILDTefisthtqgyealkndlett 332
Cdd:COG1029 188 --------------DTAKVADLHLQVKPGRDYEVL-SALRALV--------RGKELSPEE-------------------- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 333 swkdilrVSGLPRESIEEIADLYIEAKSTIICYGMGITQHEHGTQnvqqlvnllllkgNIG------RE-----GAGICP 401
Cdd:COG1029 225 -------VAGIPVEDLEELAERLKNAKYGVIFWGMGLTQSPGKHL-------------NVDaaielvRDlnrytKFSILP 284
|
....*....
gi 1327840248 402 LRGHSNVQG 410
Cdd:COG1029 285 LRGHYNVAG 293
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
103-358 |
5.13e-11 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 66.23 E-value: 5.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 103 LEDEGRLTHPMKYNSQ--TDKYEPIEWEEAFQQIGTRL----QSYSdPNTVEFytSGRTSNEAAFLYQlLAREYGT-NNF 175
Cdd:PRK15488 93 LYDPQRIVKPLKRVGErgEGKWQEISWDEAYQEIAAKLnaikQQHG-PESVAF--SSKSGSLSSHLFH-LATAFGSpNTF 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 176 PDCSNmChePTSVGLADSIGVGkaTVLLDDFDKADLVICIGHN--PGTNHPRMLSSLREVSKRGAKIIAINPlrergleR 253
Cdd:PRK15488 169 THAST-C--PAGYAIAAKVMFG--GKLKRDLANSKYIINFGHNlyEGINMSDTRGLMTAQMEKGAKLVVFEP-------R 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 254 FAYPQDVvemltlestplAGHYYKVRIGGDTALLKGVMKLLIEkhqaavdagkEPILDTEFISTHTQGYEALKNDLE--T 331
Cdd:PRK15488 237 FSVVASK-----------ADEWHAIRPGTDLAVVLALCHVLIE----------ENLYDKAFVERYTSGFEELAASVKeyT 295
|
250 260
....*....|....*....|....*..
gi 1327840248 332 TSWKDIlrVSGLPRESIEEIADLYIEA 358
Cdd:PRK15488 296 PEWAEA--ISDVPADDIRRIARELAAA 320
|
|
| MopB_4 |
cd02765 |
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
108-410 |
3.32e-10 |
|
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: 63.27 E-value: 3.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 108 RLTHPMKYNSQ--TDKYEPIEWEEAFQQIGTRLQSYSD---PNTVEFYTSgrtSNEAAFLYQLLAREYGTNNFPDCSNMC 182
Cdd:cd02765 55 RLKYPMKRVGErgEGKFERITWDEALDTIADKLTEAKReygGKSILWMSS---SGDGAILSYLRLALLGGGLQDALTYGI 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 183 HEPTSVG--LADSIGVGKATVLLDDFDKADLVICIGHNPGTNHPRMLSSLREVSKRGAKIIAINPLRERGLERfaypqdv 260
Cdd:cd02765 132 DTGVGQGfnRVTGGGFMPPTNEITDWVNAKTIIIWGSNILETQFQDAEFFLDARENGAKIVVIDPVYSTTAAK------- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 261 vemltlestplAGHYYKVRIGGDTALLKGVMKLLIE-------------------------------------KHQAAV- 302
Cdd:cd02765 205 -----------ADQWVPIRPGTDPALALGMINYILEhnwydeaflksntsapflvredngtllrqadvtatpaEDGYVVw 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 303 -----------DAGKEPILDTEF----ISTHTqGYEALKNDLETTSWKDILRVSGLPRESIEEIADLYIEAKSTIICYGM 367
Cdd:cd02765 274 dtnsdspepvaATNINPALEGEYtingVKVHT-VLTALREQAASYPPKAAAEICGLEEAIIETLAEWYATGKPSGIWGFG 352
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1327840248 368 GITQHEHGTQNVQQLVNLLLLKGNIGREGAGICPLRG----HSNVQG 410
Cdd:cd02765 353 GVDRYYHSHVFGRTAAILAALTGNIGRVGGGVGQIKFmyfmGSNFLG 399
|
|
| MopB_Arsenate-R |
cd02757 |
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ... |
105-404 |
2.77e-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: 60.15 E-value: 2.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 105 DEGRLTHPMK------YNSQTDKYEPIEWEEAFQQIGTRLQSYSDPN-TVEF-YTSGRTSNEAAFLYQLLAREYGTNNFP 176
Cdd:cd02757 53 DPDRILYPMKrtnprkGRDVDPKFVPISWDEALDTIADKIRALRKENePHKImLHRGRYGHNNSILYGRFTKMIGSPNNI 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 177 DCSNMCHEPTSVG-LADSIGVGKATVlldDFDKADLVICIGHNP-GTNH--PRMLSSLREVSKRgAKIIAINPlrergle 252
Cdd:cd02757 133 SHSSVCAESEKFGrYYTEGGWDYNSY---DYANAKYILFFGADPlESNRqnPHAQRIWGGKMDQ-AKVVVVDP------- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 253 RFAypqdvvemltlESTPLAGHYYKVRIGGDTALLKGVMKLLIEKHQAAVD-------------AGKePILDTEFISTHT 319
Cdd:cd02757 202 RLS-----------NTAAKADEWLPIKPGEDGALALAIAHVILTEGLWDKDfvgdfvdgknyfkAGE-TVDEESFKEKST 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 320 QGY-EALKNDLE--TTSWKDilRVSGLPRESIEEIADLYIEAKSTIICY-GMGITQHEHGTQNVQQLVNLLLLKGNIGRE 395
Cdd:cd02757 270 EGLvKWWNLELKdyTPEWAA--KISGIPAETIERVAREFATAAPAAAAFtWRGATMQNRGSYNSMACHALNGLVGSIDSK 347
|
....*....
gi 1327840248 396 GaGICPLRG 404
Cdd:cd02757 348 G-GLCPNMG 355
|
|
| MopB_NDH-1_NuoG2 |
cd02772 |
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase ... |
103-246 |
6.09e-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: 58.90 E-value: 6.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 103 LEDEGRLTHPMKynSQTDKYEPIEWEEAFQQIGTRLQSYSD---PNTVEFYTSGRTSNEAAFLYQLLAREYGTNNFPdcs 179
Cdd:cd02772 49 LNSEDRLTKPMI--KKDGQWQEVDWETALEYVAEGLSAIIKkhgADQIGALASPHSTLEELYLLQKLARGLGSDNID--- 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 180 nmcHEPTSVGLADSIGVGKATVL---LDDFDKADLVICIGHNPGTNHPRMLSSLREVSKRGAKIIAINPL 246
Cdd:cd02772 124 ---HRLRQSDFRDDAKASGAPWLgmpIAEISELDRVLVIGSNLRKEHPLLAQRLRQAVKKGAKLSAINPA 190
|
|
| MopB_DMSOR-BSOR-TMAOR |
cd02769 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
210-375 |
1.91e-08 |
|
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: 57.66 E-value: 1.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 210 DLVICIGHNP---------GTNHPRMLSSLREVSKRGAKIIAINPLRErglerfaypqDVVEMLTLEstplaghYYKVRI 280
Cdd:cd02769 172 ELVVAFGADPlknaqiawgGIPDHQAYSYLKALKDRGIRFISISPLRD----------DTAAELGAE-------WIAIRP 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 281 GGDTALLKGVMKLLIEKHQAavdagkepilDTEFISTHTQGYEALKNDLE--------TTSWKDilRVSGLPRESIEEIA 352
Cdd:cd02769 235 GTDVALMLALAHTLVTEGLH----------DKAFLARYTVGFDKFLPYLLgesdgvpkTPEWAA--AICGIPAETIRELA 302
|
170 180
....*....|....*....|...
gi 1327840248 353 DLYIeAKSTIICYGMGITQHEHG 375
Cdd:cd02769 303 RRFA-SKRTMIMAGWSLQRAHHG 324
|
|
| PRK14990 |
PRK14990 |
anaerobic dimethyl sulfoxide reductase subunit A; Provisional |
108-397 |
5.81e-07 |
|
anaerobic dimethyl sulfoxide reductase subunit A; Provisional
Pssm-ID: 184952 [Multi-domain] Cd Length: 814 Bit Score: 53.11 E-value: 5.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 108 RLTHPMKYNSQ--TDKYEPIEWEEAFQQIGTRLQ----SYSDPNTVEFYTSGRTSNEAAFLY----QLLAREYGT----- 172
Cdd:PRK14990 119 RLKYPMKRVGArgEGKFERISWEEAYDIIATNMQrlikEYGNESIYLNYGTGTLGGTMTRSWppgnTLVARLMNCcggyl 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 173 NNFPDCSNmchEPTSVGLADSIGVGKATVLLDDFDKADLVICIGHNPGTNhpRM--------LSSLREvsKRGAKIIAIN 244
Cdd:PRK14990 199 NHYGDYSS---AQIAEGLNYTYGGWADGNSPSDIENSKLVVLFGNNPGET--RMsgggvtyyLEQARQ--KSNARMIIID 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 245 PlreRGLERFAYPQDvvemltlestplagHYYKVRIGGDTALLKGVMKLLIekhqaavdagKEPILDTEFISTHTQGYE- 323
Cdd:PRK14990 272 P---RYTDTGAGRED--------------EWIPIRPGTDAALVNGLAYVMI----------TENLVDQPFLDKYCVGYDe 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 324 ------ALKND--------------LETTSWKDilRVSGLPRESIEEIADLYIEAKSTIICYGMGITQHEHGTQNVQQLV 383
Cdd:PRK14990 325 ktlpasAPKNGhykayilgegpdgvAKTPEWAS--QITGVPADKIIKLAREIGSTKPAFISQGWGPQRHANGEIATRAIS 402
|
330
....*....|....
gi 1327840248 384 NLLLLKGNIGREGA 397
Cdd:PRK14990 403 MLAILTGNVGINGG 416
|
|
| MopB_Tetrathionate-Ra |
cd02758 |
The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other ... |
108-375 |
1.27e-06 |
|
The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other related proteins. The Salmonella enterica tetrathionate reductase catalyses the reduction of trithionate but not sulfur or thiosulfate. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239159 [Multi-domain] Cd Length: 735 Bit Score: 51.96 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 108 RLTHPMKYNSQ--TDKYEPIEWEEAFQQI-------------GTR----LQSYSDPNTVEF--------YTSGRTSNEAA 160
Cdd:cd02758 83 RVLQPLKRVGPrgSGKWKPISWEQLIEEVveggdlfgeghveGLKairdLDTPIDPDHPDLgpkanqllYTFGRDEGRTP 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 161 FLYQLLAREYGTNNFPDCSNMCHEPTSVG-LADSIGVGKATVLLDDFDKADLVICIGHNPGTNHPRMlsslrevsKRGAK 239
Cdd:cd02758 163 FIKRFANQAFGTVNFGGHGSYCGLSYRAGnGALMNDLDGYPHVKPDFDNAEFALFIGTSPAQAGNPF--------KRQAR 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 240 IIAiNPLRERGLErfAYPQDVVEMLTLESTPLAGHYYKVRIGGDTALLKGVMKLLIEKH-----------QAAVDAGKEP 308
Cdd:cd02758 235 RLA-EARTEGNFK--YVVVDPVLPNTTSAAGENIRWVPIKPGGDGALAMAMIRWIIENErynaeylsipsKEAAKAAGEP 311
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1327840248 309 ILDTefiSTH-------TQGYEALKNDLETTSWKDILRVSGLPRESIEEIADLYIEA--KSTIICYgmGITQHEHG 375
Cdd:cd02758 312 SWTN---ATHlvitvrvKSALQLLKEEAFSYSLEEYAEICGVPEAKIIELAKEFTSHgrAAAVVHH--GGTMHSNG 382
|
|
| PRK13532 |
PRK13532 |
nitrate reductase catalytic subunit NapA; |
108-376 |
2.65e-06 |
|
nitrate reductase catalytic subunit NapA;
Pssm-ID: 237416 [Multi-domain] Cd Length: 830 Bit Score: 51.05 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 108 RLTHPM--KYNSQTDK---YEPIEWEEAF----QQIGTRLQSySDPNTVEFYTSGR-TSNEAAFLYQLLAREYGTNNFPD 177
Cdd:PRK13532 97 RLTQPLlrMKDGKYDKegeFTPVSWDQAFdvmaEKFKKALKE-KGPTAVGMFGSGQwTIWEGYAASKLMKAGFRSNNIDP 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 178 CSNMCHEPTSVGLADSIGVGKATVLLDDFDKADLVICIGHNPGTNHPRMLSSL--REVSKRGAKIIAINPLRERglerfa 255
Cdd:PRK13532 176 NARHCMASAVVGFMRTFGIDEPMGCYDDIEAADAFVLWGSNMAEMHPILWSRVtdRRLSNPDVKVAVLSTFEHR------ 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 256 ypqdvvemltleSTPLAGHYYKVRIGGDTALLKGVMKLLIEKHqaAVDagkepildTEFISTHTQ--------GY----- 322
Cdd:PRK13532 250 ------------SFELADNGIIFTPQTDLAILNYIANYIIQNN--AVN--------WDFVNKHTNfrkgatdiGYglrpt 307
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1327840248 323 ----EALKNDLETTSWKDI-----------------LRVSGLPRESIEEIADLYIEAKSTIICY-GMGITQHEHGT 376
Cdd:PRK13532 308 hpleKAAKNPGTAGKSEPIsfeefkkfvapytlektAKMSGVPKEQLEQLAKLYADPNRKVVSFwTMGFNQHTRGV 383
|
|
| Molydop_binding |
pfam01568 |
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
642-752 |
8.24e-06 |
|
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - containing oxidoreductases and tungsten formylmethanofuran dehydrogenase subunit d (FwdD) and molybdenum formylmethanofuran dehydrogenase subunit (FmdD); where the domain constitutes almost the entire subunit. The formylmethanofuran dehydrogenase catalyzes the first step in methane formation from CO2 in methanogenic archaea and has a molybdopterin dinucleotide cofactor. This domain corresponds to the C-terminal domain IV in dimethyl sulfoxide (DMSO)reductase which interacts with the 2-amino pyrimidone ring of both molybdopterin guanine dinucleotide molecules.
Pssm-ID: 426328 [Multi-domain] Cd Length: 110 Bit Score: 45.34 E-value: 8.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 642 LILATLRSHDQYNTTIYGLNDRYRGVFgQRDVVFISGAEAQKQKLEAGDKVnLIALDREQKPTKRRLDnltvviYDMADR 721
Cdd:pfam01568 1 LYLITGRVLGQYHSQTRTRRVLRLAKP-EPEVVEIHPEDAAALGIKDGDLV-EVTSRRGSVVVRAKVT------DRVRPG 72
|
90 100 110
....*....|....*....|....*....|....*....
gi 1327840248 722 SVATYFPE--------ANNLISlDNFDPQCGIPAYKNIP 752
Cdd:pfam01568 73 VVFMPFGWwyeprggnANALTD-DATDPLSGGPEFKTCA 110
|
|
| MopB_Res-Cmplx1_Nad11 |
cd02773 |
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone ... |
108-245 |
1.30e-04 |
|
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: 44.95 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 108 RLTHPMKYNSqtDKYEPIEWEEAFQQIGTRLQSySDPNTVEFYTSGRTSNEAAF-LYQLLAREygtnnfpDCSNMCHEPT 186
Cdd:cd02773 53 RLDKPYIRKN--GKLKPATWEEALAAIAKALKG-VKPDEIAAIAGDLADVESMVaLKDLLNKL-------GSENLACEQD 122
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1327840248 187 SVGLADSIgvgKATVLL----DDFDKADLVICIGHNPGTNHPRMLSSLRE-VSKRGAKIIAINP 245
Cdd:cd02773 123 GPDLPADL---RSNYLFnttiAGIEEADAVLLVGTNPRFEAPVLNARIRKaWLHGGLKVGVIGP 183
|
|
| PRK07860 |
PRK07860 |
NADH dehydrogenase subunit G; Validated |
108-255 |
3.21e-04 |
|
NADH dehydrogenase subunit G; Validated
Pssm-ID: 236118 [Multi-domain] Cd Length: 797 Bit Score: 44.17 E-value: 3.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327840248 108 RLTHPMKYNSqTDKYEPIEWEEAFQQIGTRLQSYSDPntVEFYTSGRTSNEAAFLYQLLAR-EYGTNNFpDCSNMCHEPT 186
Cdd:PRK07860 278 RITTPLVRDE-DGELEPASWSEALAVAARGLAAARGR--VGVLVGGRLTVEDAYAYAKFARvALGTNDI-DFRARPHSAE 353
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1327840248 187 SVG-LADSI-GVGKAtVLLDDFDKADLVICIGHNPGTNHPRMLSSLRE-VSKRGAKIIAINPLRERGLERFA 255
Cdd:PRK07860 354 EADfLAARVaGRGLG-VTYADLEKAPAVLLVGFEPEEESPIVFLRLRKaARKHGLKVYSIAPFATRGLEKMG 424
|
|
| |
