|
Name |
Accession |
Description |
Interval |
E-value |
| Fdhalpha-like |
TIGR01701 |
oxidoreductase alpha (molybdopterin) subunit; This model represents a well-defined clade of ... |
17-753 |
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: 972.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 17 PAGGWGALKATAIAVRTQMDALEAPVTLLRTNQPDGFDCPGCAWPDK-EHKSTFQFCENGAKAVTWEATSKRVTPKFLAA 95
Cdd:TIGR01701 1 DAGGWGAVKSVALGKVKPMHIRQTLKLLLTLNKPEGYDCPGCAWGVSpQTLAGLEFCENGAKAIAWETTPRTIDPEFFAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 96 NTVTSLLAKSDFELEGYGRLTHPLVYDRASDTLRPTSWESAFARIGEVVSGMQPDEVEFYTSGRASNEAAWLFQLFAREL 175
Cdd:TIGR01701 81 HSVSELRTLDSHELEKLGRLTYPLSLRPGSDHYTPISWDDAYQEIAAKLNSLDPKQVAFYTSGRTSNEAAYLYQLFARSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 176 GTNNFPDCSNMCHESTSVGLPQSIGIGKGTVSLDDFDKTELVISIGHNPGTNHPRMMGTLHELARRGVPIIVFNPLKERA 255
Cdd:TIGR01701 161 GSNNLPDCSNMCHEPSSVALKRSIGIGKGSVNLEDFEHTDCLVFIGSNAGTNHPRMLKYLYAAKKRGAKIIAINPLRERG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 256 LERFADPQNVIEMATLRSTNIASTYFQVKAGGDAAALKGIAKALLQMEEEQ-GDVLDRPFITEHTQNFPAFADDLQKTSW 334
Cdd:TIGR01701 241 LERFWIPQIPESMLTGGGTQISSEYYQVRIGGDIALFNGVMKLLIEAEDAQpGSLIDHEFIANHTNGFDELRRHVLQLNW 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 335 QDIERESGLTRADLQRVAEAYAKSNATIVTYGMGITQHNKGTSNVRLIADLLLMRGNIGKPGAGICPLRGHSNVQGNRTV 414
Cdd:TIGR01701 321 NDIERSSGLSQEEILEFAKLLANSRRVVFCWAMGLTQHAHGVDNISQVANLALLRGNIGKPGAGVCPIRGHSNVQGDRTM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 415 GITEKPGAAFLAKLQEVFGFAPPQKHGHDAVKALQAMIEGKSKALLCLGGNFAVAMPDPERAFPAMRGLDLSVHVGTKLN 494
Cdd:TIGR01701 401 GITEKPEEEFLARLSQIYGFTPPDWPGDTTVAMIEAILTGKVRAFICLGGNFLEAMPDTAAIERALRQLDLRVHVATKLN 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 495 RSHLLVAKETFILPCLGRTELDLQESGRQSITVEDSMSMVHASSGKLKPASPLLRSEPAIVAGMAMATLANTKVDWLSLV 574
Cdd:TIGR01701 481 RSHVLAKEEALILPVLGRYEQDGQGTGKQAVSVESSMRMVHFSRGILKPRGAELRSEWAIIAEIAKALLPETPVAWEILV 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 575 ADYDRIRDLIERTVPGFDNYNARIRHPGGFRMPLPP-TERIWPTPTGKAMFSVFHGVHENVHVAGEEVLRLVTLRSHDQY 653
Cdd:TIGR01701 561 DTYDQIRDAIAATNPGYDDINHRKRRPDGFQLPGAAlCERKFPTPDGKANFIVIPLPEFRVPTGHEFELVLVTLRSHDQF 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 654 NTTIYAMDDRYRGIFGRRDVLFMNEQDMASQGFEHGDRVDITTALPDSNLR-LQDITLVAYNIAPGTVGAYYPEANVLVP 732
Cdd:TIGR01701 641 NTTIYGEDDRYRGVDGHRRVVFMNETDIKKLGLRNGERVDVYNQYGDGQKRkFDNLRIVFYDTPTGNAAAYYPEANPLLP 720
|
730 740
....*....|....*....|.
gi 695773365 733 LDYIDEESGTPSYKSVPIRLT 753
Cdd:TIGR01701 721 LDHHDPQSKTPEYKTIPVRLE 741
|
|
| PRK09939 |
PRK09939 |
acid resistance putative oxidoreductase YdeP; |
9-752 |
0e+00 |
|
acid resistance putative oxidoreductase YdeP;
Pssm-ID: 182156 [Multi-domain] Cd Length: 759 Bit Score: 933.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 9 PGVHPYDGPAGGWGALKATAIAVRTQMDALEAPVTLLRTNQPDGFDCPGCAWPDKEHKSTFQFCENGAKAVTWEATSKRV 88
Cdd:PRK09939 3 KKIESYQGAAGGWGAVKSVANAVRKQMDIRQDVIAMFDMNKPEGFDCPGCAWPDPKHSASFDICENGAKAIAWEVTDKQV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 89 TPKFLAANTVTSLLAKSDFELEGYGRLTHPLVYDRASDTLRPTSWESAFARIGEVVSGMQ-PDEVEFYTSGRASNEAAWL 167
Cdd:PRK09939 83 NASFFAENTVQSLLTWGDHELEAAGRLTQPLKYDAVSDCYKPLSWQQAFDEIGARLQSYSdPNQVEFYTSGRTSNEAAFL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 168 FQLFARELGTNNFPDCSNMCHESTSVGLPQSIGIGKGTVSLDDFDKTELVISIGHNPGTNHPRMMGTLHELARRGVPIIV 247
Cdd:PRK09939 163 YQLFAREYGSNNFPDCSNMCHEPTSVGLAASIGVGKGTVLLEDFEKCDLVICIGHNPGTNHPRMLTSLRALVKRGAKMIA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 248 FNPLKERALERFADPQNVIEMATLRSTNIASTYFQVKAGGDAAALKGIAKALLQMEEE-----QGDVLDRPFITEHTQNF 322
Cdd:PRK09939 243 INPLQERGLERFTAPQNPFEMLTNSETQLASAYYNVRIGGDMALLKGMMRLLIERDDAasaagRPSLLDDEFIQTHTVGF 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 323 PAFADDLQKTSWQDIERESGLTRADLQRVAEAYAKSNATIVTYGMGITQHNKGTSNVRLIADLLLMRGNIGKPGAGICPL 402
Cdd:PRK09939 323 DELRRDVLNSEWKDIERISGLSQTQIAELADAYAAAERTIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGICPL 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 403 RGHSNVQGNRTVGITEKPGAAFLAKLQEVFGFAPPQKHGHDAVKALQAMIEGKSKALLCLGGNFAVAMPDPERAFPAMRG 482
Cdd:PRK09939 403 RGHSNVQGDRTVGITEKPSAEFLARLGERYGFTPPHAPGHAAIASMQAICTGQARALICMGGNFALAMPDREASAVPLTQ 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 483 LDLSVHVGTKLNRSHLLVAKETFILPCLGRTELDLQESGRQSITVEDSMSMVHASSGKLKPASPLLRSEPAIVAGMAMAT 562
Cdd:PRK09939 483 LDLAVHVATKLNRSHLLTARHSYILPVLGRSEIDMQKSGAQAVTVEDSMSMIHASRGVLKPAGVMLKSECAVVAGIAQAA 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 563 LANTKVDWLSLVADYDRIRDLIERTVPGFDNYNARIRHPGGFRMPLPPTERIWPTPTGKAMFSVFHGVHENVHVAGEEVL 642
Cdd:PRK09939 563 LPQSVVAWEYLVEDYDRIRNDIEAVLPEFADYNQRIRHPGGFHLINAAAERRWMTPSGKANFITSKGLLEDPSSAFNSKL 642
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 643 RLVTLRSHDQYNTTIYAMDDRYRGIFGRRDVLFMNEQDMASQGFEHGDRVDITTALPD---SNLRLQDITLVAYNIAPGT 719
Cdd:PRK09939 643 VMATVRSHDQYNTTIYGMDDRYRGVFGQRDVVFMSAKQAKICRVKNGERVNLIALTPDgkrSSRRMDRLKVVIYPMADRS 722
|
730 740 750
....*....|....*....|....*....|...
gi 695773365 720 VGAYYPEANVLVPLDYIDEESGTPSYKSVPIRL 752
Cdd:PRK09939 723 LVTYFPESNHMLTLDNHDPLSGIPGYKSIPVEL 755
|
|
| MopB_ydeP |
cd02767 |
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
52-624 |
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: 920.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 52 GFDCPGCAWPD-KEHKSTFQFCENGAKAVTWEATSKRVTPKFLAANTVTSLLAKSDFELEGYGRLTHPLVYDRASDTLRP 130
Cdd:cd02767 1 GFDCPGCAWGDpGQKLHGFEFCENGAKALAWETTPKRVTPEFFALHSVSELRTWSDYELEHLGRLTYPMRYDAGSDHYRP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 131 TSWESAFARIGEVVSGMQPDEVEFYTSGRASNEAAWLFQLFARELGTNNFPDCSNMCHESTSVGLPQSIGIGKGTVSLDD 210
Cdd:cd02767 81 ISWDEAFAEIAARLRALDPDRAAFYTSGRASNEAAYLYQLFARAYGTNNLPDCSNMCHEPSSVGLKKSIGVGKGTVSLED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 211 FDKTELVISIGHNPGTNHPRMMGTLHELARRGVPIIVFNPLKERALERFADPQNVIEMATlRSTNIASTYFQVKAGGDAA 290
Cdd:cd02767 161 FEHTDLIFFIGQNPGTNHPRMLHYLREAKKRGGKIIVINPLREPGLERFANPQNPESMLT-GGTKIADEYFQVRIGGDIA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 291 ALKGIAKALLQMEEEQGDVLDRPFITEHTQNFPAFADDLQKTSWQDIERESGLTRADLQRVAEAYAKSNATIVTYGMGIT 370
Cdd:cd02767 240 LLNGMAKHLIERDDEPGNVLDHDFIAEHTSGFEEYVAALRALSWDEIERASGLSREEIEAFAAMYAKSERVVFVWGMGIT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 371 QHNKGTSNVRLIADLLLMRGNIGKPGAGICPLRGHSNVQGNRTVGITEKPGAAFLAKLQEVFGFAPPQKHGHDAVKALQA 450
Cdd:cd02767 320 QHAHGVDNVRAIVNLALLRGNIGRPGAGLMPIRGHSNVQGDRTMGITEKPFPEFLDALEEVFGFTPPRDPGLDTVEAIEA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 451 MIEGKSKALLCLGGNFAVAMPDPERAFPAMRGLDLSVHVGTKLNRSHLLVAKETFILPCLGRTELDLQESGRQSITVEDS 530
Cdd:cd02767 400 ALEGKVKAFISLGGNFAEAMPDPAATEEALRRLDLTVHVATKLNRSHLVHGEEALILPCLGRTEIDMQAGGAQAVTVEDS 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 531 MSMVHASSGKLKPASPLLRSEPAIVAGMAMATLANTKVDWLSLVADYDRIRDLIERTVP-GFDNYNARIRHPGGFRMPLP 609
Cdd:cd02767 480 MSMTHTSRGRLKPASRVLLSEEAIVAGIAGARLGEAKPEWEILVEDYDRIRDEIAAVIYeGFADFNQRGDQPGGFHLPNG 559
|
570
....*....|....*
gi 695773365 610 PTERIWPTPTGKAMF 624
Cdd:cd02767 560 ARERKFNTPSGKAQF 574
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
55-753 |
5.18e-158 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 474.33 E-value: 5.18e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 55 CPGCAWpdkehkstfqFCENGAKAVTWEATskRVTPKflAANTVTSLL-----AKSDFELEGYGRLTHPLVYD--RASDT 127
Cdd:COG0243 28 CPGCGV----------GCGLGVKVEDGRVV--RVRGD--PDHPVNRGRlcakgAALDERLYSPDRLTYPMKRVgpRGSGK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 128 LRPTSWESAFARIGEVVSGMQ----PDEVEFYTSG----RASNEAAWLFQLFARELGTNNFPDCSNMCHESTSVGLPQSI 199
Cdd:COG0243 94 FERISWDEALDLIAEKLKAIIdeygPEAVAFYTSGgsagRLSNEAAYLAQRFARALGTNNLDDNSRLCHESAVAGLPRTF 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 200 GIGKGTVSLDDFDKTELVISIGHNPGTNHPRMMGTLHELAR-RGVPIIVFNPLKERalerfadpqnviematlrSTNIAS 278
Cdd:COG0243 174 GSDKGTVSYEDLEHADLIVLWGSNPAENHPRLLRRLREAAKkRGAKIVVIDPRRTE------------------TAAIAD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 279 TYFQVKAGGDAAALKGIAKALLQMeeeqgDVLDRPFITEHTQNFPAFADDLQKTSWQDIERESGLTRADLQRVAEAYAKS 358
Cdd:COG0243 236 EWLPIRPGTDAALLLALAHVLIEE-----GLYDRDFLARHTVGFDELAAYVAAYTPEWAAEITGVPAEDIRELAREFATA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 359 NATIVTYGMGITQHNKGTSNVRLIADLLLMRGNIGKPGAGICPLRGHsnvqgnrtvgitekpgaaflaklqevfgfappq 438
Cdd:COG0243 311 KPAVILWGMGLQQHSNGTQTVRAIANLALLTGNIGKPGGGPFSLTGE--------------------------------- 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 439 khghdavkalqAMIEGKS---KALLCLGGNFAVAMPDPERAFPAMRGLDLSVHVGTKLNRSHLLVAketFILPCLGRTEl 515
Cdd:COG0243 358 -----------AILDGKPypiKALWVYGGNPAVSAPDTNRVREALRKLDFVVVIDTFLTETARYAD---IVLPATTWLE- 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 516 dlqesgRQSITVEDSMSMVHASSGKLKPASpLLRSEPAIVAGMAMATLANTKVDWLSLVADYdrIRDLIERT---VPGFD 592
Cdd:COG0243 423 ------RDDIVTNSEDRRVHLSRPAVEPPG-EARSDWEIFAELAKRLGFEEAFPWGRTEEDY--LRELLEATrgrGITFE 493
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 593 NYNARirhpGGFRMPLPP-----TERIWPTPTGKAMFSV----------FHGVHENVHVAGEE-VLRLVTLRSHDQYNTT 656
Cdd:COG0243 494 ELREK----GPVQLPVPPepafrNDGPFPTPSGKAEFYSetlalpplprYAPPYEGAEPLDAEyPLRLITGRSRDQWHST 569
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 657 IYAmDDRYRGIFGRRdVLFMNEQDMASQGFEHGDRVDITtalpdsNLR--LQDITLVAYNIAPGTV----GAYYPEA--- 727
Cdd:COG0243 570 TYN-NPRLREIGPRP-VVEINPEDAAALGIKDGDLVRVE------SDRgeVLARAKVTEGIRPGVVfaphGWWYEPAddk 641
|
730 740 750
....*....|....*....|....*....|
gi 695773365 728 ----NVLVPlDYIDEESGTPSYKSVPIRLT 753
Cdd:COG0243 642 ggnvNVLTP-DATDPLSGTPAFKSVPVRVE 670
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
113-753 |
2.08e-110 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 351.11 E-value: 2.08e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 113 GRLTHPLVydRASDTLRPTSWESAFARIGEVVSGMQ----PDEVEFYTSGRASNEAAWLFQLFARE-LGTNNFPDCSNMC 187
Cdd:COG3383 60 DRLTTPLI--RRGGEFREVSWDEALDLVAERLREIQaehgPDAVAFYGSGQLTNEENYLLQKLARGvLGTNNIDNNARLC 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 188 HESTSVGLPQSIGIGKGTVSLDDFDKTELVISIGHNPGTNHPRMMGTLHELARRGVPIIVFNPlKERALERFADpqnvie 267
Cdd:COG3383 138 MASAVAGLKQSFGSDAPPNSYDDIEEADVILVIGSNPAEAHPVLARRIKKAKKNGAKLIVVDP-RRTETARLAD------ 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 268 matlrstniasTYFQVKAGGDAAALKGIAKALLqmeeEQGDVlDRPFITEHTQNFPAFADDLQKTSWQDIERESGLTRAD 347
Cdd:COG3383 211 -----------LHLQIKPGTDLALLNGLLHVII----EEGLV-DEDFIAERTEGFEELKASVAKYTPERVAEITGVPAED 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 348 LQRVAEAYAKSNATIVTYGMGITQHNKGTSNVRLIADLLLMRGNIGKPGAGICPLRGHSNVQGNRTVGI--TEKPG---- 421
Cdd:COG3383 275 IREAARLIAEAKRAMILWGMGVNQHTQGTDNVNAIINLALATGNIGRPGTGPFPLTGQNNVQGGRDMGAlpNVLPGyrdv 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 422 --AAFLAKLQEVFGFAP-PQKHGHDAVKALQAMIEGKSKALLCLGGNFAVAMPDPERAFPAMRGLDlsvhvgtklnrshL 498
Cdd:COG3383 355 tdPEHRAKVADAWGVPPlPDKPGLTAVEMFDAIADGEIKALWIIGENPAVSDPDANHVREALEKLE-------------F 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 499 LVAKETF----------ILPCLGRTEldlqESGrqsiTVEDSMSMVHassgklkpaspllRSEPaivagmAMATLANTKV 568
Cdd:COG3383 422 LVVQDIFltetaeyadvVLPAASWAE----KDG----TFTNTERRVQ-------------RVRK------AVEPPGEARP 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 569 DW--LSLVA-------DYDR---IRDLIERTVPGFDNYN-ARIRHPGGFRMPLPP-----TERIW----PTPTGKAMFSV 626
Cdd:COG3383 475 DWeiIAELArrlgygfDYDSpeeVFDEIARLTPDYSGISyERLEALGGVQWPCPSedhpgTPRLFtgrfPTPDGKARFVP 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 627 --FHGVHENvhVAGEEVLRLVTLRSHDQYNTTiyAMDDRYRGIFGR--RDVLFMNEQDMASQGFEHGDRVDITTALPDSN 702
Cdd:COG3383 555 veYRPPAEL--PDEEYPLVLTTGRLLDQWHTG--TRTRRSPRLNKHapEPFVEIHPEDAARLGIKDGDLVRVSSRRGEVV 630
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 695773365 703 LRLQditlVAYNIAPGTVGAY--YPE--ANVLVPlDYIDEESGTPSYKSVPIRLT 753
Cdd:COG3383 631 LRAR----VTDRVRPGTVFMPfhWGEgaANALTN-DALDPVSKQPEYKACAVRVE 680
|
|
| Fdh-alpha |
TIGR01591 |
formate dehydrogenase, alpha subunit, archaeal-type; This model describes a subset of formate ... |
114-752 |
1.54e-83 |
|
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: 279.35 E-value: 1.54e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 114 RLTHPLVydRASDTLRPTSWESAFA----RIGEVVSGMQPDEVEFYTSGRASNEAAWLFQLFARE-LGTNNFPDCSNMCH 188
Cdd:TIGR01591 53 RLTTPLI--REGDKFREVSWDEAISyiaeKLKEIKEKYGPDSIGFIGSSRGTNEENYLLQKLARAvIGTNNVDNCARVCH 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 189 ESTSVGLPQSIGIGKGTVSLDDFDKTELVISIGHNPGTNHPRMMGTLHELARRGVPIIVFNPLKeralerfadpqnvIEM 268
Cdd:TIGR01591 131 GPSVAGLKQTVGIGAMSNTISEIENADLIVIIGYNPAESHPVVAQYLKNAKRNGAKIIVIDPRK-------------TET 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 269 AtlrstNIASTYFQVKAGGDAAALKGIAKALLqmeeEQGdVLDRPFITEHTQNFPAFADDLQKTSWQDIERESGLTRADL 348
Cdd:TIGR01591 198 A-----KIADLHIPLKPGTDIALLNAMANVII----EEG-LYDKAFIEKRTEGFEEFREIVKGYTPEYVEDITGVPADLI 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 349 QRVAEAYAKSNATIVTYGMGITQHNKGTSNVRLIADLLLMRGNIGKPGAGICPLRGHSNVQGNRTVGI--TEKPG----- 421
Cdd:TIGR01591 268 REAARMYAKAGSAAILWGMGVTQHSQGVETVMALINLAMLTGNIGKPGGGVNPLRGQNNVQGACDMGAlpDFLPGyqpvs 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 422 -AAFLAKLQEVFGFAP-PQKHGHDAVKALQAMIEGKSKALLCLGGNfaVAMPDPERAfpamrgldlsvHVGTKLNRSHLL 499
Cdd:TIGR01591 348 dEEVREKFAKAWGVVKlPAEPGLRIPEMIDAAADGDVKALYIMGED--PLQSDPNTS-----------KVRKALEKLELL 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 500 VAKETFIlpclgrteldlqesgrqsitvEDSMSMVHAssgkLKPASPLLRSEPAIVAG--------MAMATLANTKVDW- 570
Cdd:TIGR01591 415 VVQDIFM---------------------TETAKYADV----VLPAAAWLEKEGTFTNAerriqrffKAVEPKGESKPDWe 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 571 -LSLVA----------DYDRIRDLIERTVPGFDNYNAR-----------IRHPGGFRMPLPPTERiWPTPTGKAMFSVFH 628
Cdd:TIGR01591 470 iIQELAnalgldwnynHPQEIMDEIRELTPLFAGLTYErldelgslqwpCNDSDASPTSYLYKDK-FATPDGKAKFIPLE 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 629 GVHENVHVAGEEVLRLVTLRSHDQYNTTiyAMDDRYRGIfgRRDV----LFMNEQDMASQGFEHGDRVDITTALPDSNLR 704
Cdd:TIGR01591 549 WVAPIEEPDDEYPLILTTGRVLTHYNVG--EMTRRVAGL--RRLSpepyVEINTEDAKKLGIKDGDLVKVKSRRGEITLR 624
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 695773365 705 LQDITLVAYNIAPGTVGAYYPEANVLVPLDyIDEESGTPSYKSVPIRL 752
Cdd:TIGR01591 625 AKVSDRVNKGAIYITMHFWDGAVNNLTTDD-LDPISGTPEYKYTAVRI 671
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
114-487 |
1.89e-73 |
|
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: 247.90 E-value: 1.89e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 114 RLTHPLVydRASDTLRPTSWESAFARIGEVVSGMQ----PDEVEFYTSGRASNEAAWLFQLFARE-LGTNNFPDCSNMCH 188
Cdd:cd02753 54 RLTKPLI--RKNGKFVEASWDEALSLVASRLKEIKdkygPDAIAFFGSAKCTNEENYLFQKLARAvGGTNNVDHCARLCH 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 189 ESTSVGLPQSIGIGKGTVSLDDFDKTELVISIGHNPGTNHPRMMGTLHELARRGVPIIVFNPLKeralerfadpqnvIEM 268
Cdd:cd02753 132 SPTVAGLAETLGSGAMTNSIADIEEADVILVIGSNTTEAHPVIARRIKRAKRNGAKLIVADPRR-------------TEL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 269 AtlrstNIASTYFQVKAGGDAAALKGIAKALLqmeeEQGdVLDRPFITEHTQNFPAFADDLQKTSWQDIERESGLTRADL 348
Cdd:cd02753 199 A-----RFADLHLQLRPGTDVALLNAMAHVII----EEG-LYDEEFIEERTEGFEELKEIVEKYTPEYAERITGVPAEDI 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 349 QRVAEAYAKSNATIVTYGMGITQHNKGTSNVRLIADLLLMRGNIGKPGAGICPLRGHSNVQGNRTVGitekpgaaflakl 428
Cdd:cd02753 269 REAARMYATAKSAAILWGMGVTQHSHGTDNVMALSNLALLTGNIGRPGTGVNPLRGQNNVQGACDMG------------- 335
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 695773365 429 qevfgfappqkhghdavkALQAMIEGKSKALLCLGGNFAVAMPDPERAFPAMRGLDLSV 487
Cdd:cd02753 336 ------------------ALPNVLPGYVKALYIMGENPALSDPNTNHVRKALESLEFLV 376
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
66-514 |
3.50e-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: 210.65 E-value: 3.50e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 66 KSTFQFCENGA--KAVTWEATSKRVTPKFLAANTVTSLLAKSDFELEG---YGRLTHPLVYDRASDTLRPTSWESAFARI 140
Cdd:cd00368 1 PSVCPFCGVGCgiLVYVKDGKVVRIEGDPNHPVNEGRLCDKGRAGLDGlysPDRLKYPLIRVGGRGKFVPISWDEALDEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 141 GE----VVSGMQPDEVEFYTSGRASNEAAWLFQLFARELGTNNFPDCSNMCHESTSVGLPQsIGIGKGTVSLDDFDKTEL 216
Cdd:cd00368 81 AEklkeIREKYGPDAIAFYGGGGASNEEAYLLQKLLRALGSNNVDSHARLCHASAVAALKA-FGGGAPTNTLADIENADL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 217 VISIGHNPGTNHPRMMGTLHELARRGVPIIVFNPLKEralerfadpqnviematlRSTNIASTYFQVKAGGDAAALKGia 296
Cdd:cd00368 160 ILLWGSNPAETHPVLAARLRRAKKRGAKLIVIDPRRT------------------ETAAKADEWLPIRPGTDAALALA-- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 297 kallqmeeeqgdvldrpfitehtqnfpafaddlqktswQDIERESGLTRADLQRVAEAYAKSNATIVTYGMGITQHNKGT 376
Cdd:cd00368 220 --------------------------------------EWAAEITGVPAETIRALAREFAAAKRAVILWGMGLTQHTNGT 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 377 SNVRLIADLLLMRGNIGKPGAGICPlrghsnvqgnrtvgitekpgaaflaklqevfgfappqkhghdavkalqamiegks 456
Cdd:cd00368 262 QNVRAIANLAALTGNIGRPGGGLGP------------------------------------------------------- 286
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 695773365 457 kallclGGNFAVAMPDPERAFPAMRGLDLSVHVGTKLNRSHLLvakETFILPCLGRTE 514
Cdd:cd00368 287 ------GGNPLVSAPDANRVRAALKKLDFVVVIDIFMTETAAY---ADVVLPAATYLE 335
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
113-487 |
3.53e-59 |
|
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: 210.55 E-value: 3.53e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 113 GRLTHPLVyDRASDTLRPTSWESAFARIGEVVSGMQ----PDEVEFYTSGRASNEAAWLFQLFARE-LGTNNFPDCSNMC 187
Cdd:cd02754 53 ERLTRPLL-RRNGGELVPVSWDEALDLIAERFKAIQaeygPDSVAFYGSGQLLTEEYYAANKLAKGgLGTNNIDTNSRLC 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 188 HESTSVGLPQSIGIGKGTVSLDDFDKTELVISIGHNPGTNHPRMMGTLHE--LARRGVPIIVfnplkeralerfADPQnv 265
Cdd:cd02754 132 MASAVAGYKRSFGADGPPGSYDDIEHADCFFLIGSNMAECHPILFRRLLDrkKANPGAKIIV------------VDPR-- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 266 iemaTLRSTNIASTYFQVKAGGDAAALKGIAKALLQMeeeqgDVLDRPFITEHTQNFPAFADDLQKTSWQDIERESGLTR 345
Cdd:cd02754 198 ----RTRTADIADLHLPIRPGTDLALLNGLLHVLIEE-----GLIDRDFIDAHTEGFEELKAFVADYTPEKVAEITGVPE 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 346 ADLQRVAEAYAKSNATIVTYGMGITQHNKGTSNVRLIADLLLMRGNIGKPGAGICPLRGHSNVQGNRTVG-ITEKPGA-- 422
Cdd:cd02754 269 ADIREAARLFGEARKVMSLWTMGVNQSTQGTAANNAIINLHLATGKIGRPGSGPFSLTGQPNAMGGREVGgLANLLPGhr 348
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695773365 423 --------AFLAKLQEVFGFAPPQKHGHDAVKALQAMIEGKSKALLCLGGNFAVAMPDPERAFPAMRGLDLSV 487
Cdd:cd02754 349 svnnpehrAEVAKFWGVPEGTIPPKPGLHAVEMFEAIEDGEIKALWVMCTNPAVSLPNANRVREALERLEFVV 421
|
|
| MopB_CT_ydeP |
cd02787 |
The MopB_CT_ydeP CD includes a group of related uncharacterized bacterial ... |
642-752 |
4.76e-55 |
|
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: 184.40 E-value: 4.76e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 642 LRLVTLRSHDQYNTTIYAMDDRYRGIFGRRDVLFMNEQDMASQGFEHGDRVDITTALPDSNLRLQD-ITLVAYNIAPGTV 720
Cdd:cd02787 1 LFLVTTRSHDQFNTTIYGLDDRYRGVFGRRDVVFMNPDDIARLGLKAGDRVDLESAFGDGQGRIVRgFRVVEYDIPRGCL 80
|
90 100 110
....*....|....*....|....*....|..
gi 695773365 721 GAYYPEANVLVPLDYIDEESGTPSYKSVPIRL 752
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 ... |
114-410 |
2.72e-39 |
|
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: 154.86 E-value: 2.72e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 114 RLTHPLVYDRASDTLRPTSWESAFARI------------------GEVVSGmqPDEVEFYTSGRASNEAAWLFQLFAREL 175
Cdd:cd02752 54 RLKYPMYRAPGSGKWEEISWDEALDEIarkmkdirdasfveknaaGVVVNR--PDSIAFLGSAKLSNEECYLIRKFARAL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 176 GTNNFPDCSNMCHESTSVGLPQSIGIGKGTVSLDDFDKTELVISIGHNPGTNHP-RMMGTLHELARRGVPIIVFNPlker 254
Cdd:cd02752 132 GTNNLDHQARIUHSPTVAGLANTFGRGAMTNSWNDIKNADVILVMGGNPAEAHPvSFKWILEAKEKNGAKLIVVDP---- 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 255 aleRFAdpqnviematlRSTNIASTYFQVKAGGDAAALKGIAKALLQMEEEQgdvldrpfitehtqnfpafaddlqktsw 334
Cdd:cd02752 208 ---RFT-----------RTAAKADLYVPIRSGTDIAFLGGMINYIIRYTPEE---------------------------- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 335 qdIERESGLTRADLQRVAEAYAKSN----ATIVTYGMGITQHNKGTSNVRLIADLLLMRGNIGKPGAGICPLRGHSNVQG 410
Cdd:cd02752 246 --VEDICGVPKEDFLKVAEMFAATGrpdkPGTILYAMGWTQHTVGSQNIRAMCILQLLLGNIGVAGGGVNALRGHSNVQG 323
|
|
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
114-399 |
6.68e-22 |
|
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: 100.02 E-value: 6.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 114 RLTHPLVYD-RASDTLRPTSWESAF----ARIGEVVSGMQPDEVEFYtsgRASNEAAWLFQL----FARELGTNNF--PD 182
Cdd:cd02766 55 RLLTPLKRVgRKGGQWERISWDEALdtiaAKLKEIKAEYGPESILPY---SYAGTMGLLQRAargrFFHALGASELrgTI 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 183 CSNMCHEStsvglpQSIGIGkGTVSLD--DFDKTELVISIGHNPGTNHPRMMGTLHELARRGVPIIVFNPLKERALERfa 260
Cdd:cd02766 132 CSGAGIEA------QKYDFG-ASLGNDpeDMVNADLIVIWGINPAATNIHLMRIIQEARKRGAKVVVIDPYRTATAAR-- 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 261 dpqnviematlrstniASTYFQVKAGGDAA-ALkGIAKALLQMeeeqgDVLDRPFITEHTQNFPAFADDLQKTSWQDIER 339
Cdd:cd02766 203 ----------------ADLHIQIRPGTDGAlAL-GVAKVLFRE-----GLYDRDFLARHTEGFEELKAHLETYTPEWAAE 260
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 340 ESGLTRADLQRVAEAYAKSNATIVTYGMGITQHNKGTSNVRLIADLLLMRGNIGKPGAGI 399
Cdd:cd02766 261 ITGVSAEEIEELARLYGEAKPPSIRLGYGMQRYRNGGQNVRAIDALPALTGNIGVPGGGA 320
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
114-494 |
3.30e-21 |
|
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: 98.24 E-value: 3.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 114 RLTHPLVydRASDTLRPTSWESAFARIGEVVSGMQ----PDEVEFYTSGRASNEAAWLFQL--FARELGTNNFPDCS--- 184
Cdd:cd02762 54 RLRTPMR--RRGGSFEEIDWDEAFDEIAERLRAIRarhgGDAVGVYGGNPQAHTHAGGAYSpaLLKALGTSNYFSAAtad 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 185 NMCHESTSVGLPQSigigKGTVSLDDFDKTELVISIGHNPGTNHPRMM------GTLHELARRGVPIIVFNPLKERALER 258
Cdd:cd02762 132 QKPGHFWSGLMFGH----PGLHPVPDIDRTDYLLILGANPLQSNGSLRtapdrvLRLKAAKDRGGSLVVIDPRRTETAKL 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 259 fadpqnviematlrstniASTYFQVKAGGDAAALKGIAKALLQmeeeQGDVlDRPFITEHTQNFPAFADDLQKTSWQDIE 338
Cdd:cd02762 208 ------------------ADEHLFVRPGTDAWLLAAMLAVLLA----EGLT-DRRFLAEHCDGLDEVRAALAEFTPEAYA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 339 RESGLTRADLQRVAEAYAkSNATIVTYG-MGITQHNKGTSNVRLIADLLLMRGNIGKPGAGICPLrghSNVQGnrtVGIT 417
Cdd:cd02762 265 PRCGVPAETIRRLAREFA-AAPSAAVYGrLGVQTQLFGTLCSWLVKLLNLLTGNLDRPGGAMFTT---PALDL---VGQT 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 418 EKPGAAFLAKLQEVFGFapPQKHGHDAVKALQAMI----EGKSKALLCLGGNFAVAMPDPERAFPAMRGLDLSVHVGTKL 493
Cdd:cd02762 338 SGRTIGRGEWRSRVSGL--PEIAGELPVNVLAEEIltdgPGRIRAMIVVAGNPVLSAPDGARLEAALGGLEFMVSVDVYM 415
|
.
gi 695773365 494 N 494
Cdd:cd02762 416 T 416
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
114-508 |
3.06e-18 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 87.07 E-value: 3.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 114 RLTHPLVyDRASDTLRPTSWESAFARIGEVVSGMQPD------EVEFYTSGRASNEAAWLFQLFARELGTNNF---PDCS 184
Cdd:pfam00384 1 RLKYPMV-RRGDGKFVRVSWDEALDLIAKKLKRIIKKygpdaiAINGGSGGLTDVESLYALKKLLNRLGSKNGnteDHNG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 185 NMCHESTSVGLPQSIGIGKGTVSLDDFDKTELVISIGHNPGTNHPRMMGTLHELARRG-VPIIVFnplkeralerfaDPQ 263
Cdd:pfam00384 80 DLCTAAAAAFGSDLRSNYLFNSSIADIENADLILLIGTNPREEAPILNARIRKAALKGkAKVIVI------------GPR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 264 nviematlRSTNIASTYFQVKAGGDAAALKGIAKallqmeeeqgdvldrPFITEhtqnfpafaddlqktswqdieresgl 343
Cdd:pfam00384 148 --------LDLTYADEHLGIKPGTDLALALAGAH---------------VFIKE-------------------------- 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 344 tradlQRVAEAYAKSNATIVtyGMGITQHNKGTSNVRLIADLLLMRGNIGKPGAGICPLRGHSNvqgnrtvgitekpGAA 423
Cdd:pfam00384 179 -----LKKDKDFAPKPIIIV--GAGVLQRQDGEAIFRAIANLADLTGNIGRPGGGWNGLNILQG-------------AAS 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 424 FLAKLqeVFGFAPPQKhghdAVKALQAMIEGKSKALLCLGGNFAVAMPDPERAFPAMRGLDLSV----HVGTKL-NRSHL 498
Cdd:pfam00384 239 PVGAL--DLGLVPGIK----SVEMINAIKKGGIKVLYLLGNNPFVTHADENRVVKALQKLDLFVvydgHHGDKTaKYADV 312
|
410
....*....|
gi 695773365 499 lvaketfILP 508
Cdd:pfam00384 313 -------ILP 315
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
113-401 |
9.81e-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: 86.58 E-value: 9.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 113 GRLTHPL--VYDRASDTLRPTSWESAF----ARIGEVVSGMQPDEVEFytsGRASNEAAWLFQLFARELGTNNFPDCSNM 186
Cdd:cd02755 54 DRLKKPLirVGERGEGKFREASWDEALqyiaSKLKEIKEQHGPESVLF---GGHGGCYSPFFKHFAAAFGSPNIFSHEST 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 187 CHESTSVGLPQSIGIGKGTVsLDDFDKTELVISIGHN--PGTNHPRMMGTLHELARrGVPIIVFNPlkeraleRFAdpqn 264
Cdd:cd02755 131 CLASKNLAWKLVIDSFGGEV-NPDFENARYIILFGRNlaEAIIVVDARRLMKALEN-GAKVVVVDP-------RFS---- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 265 viEMATlrstnIASTYFQVKAGGDAAALKGIAKALLQmeeeqGDVLDRPFITEHTQNFPAFADDLQKTSWQDIERESGLT 344
Cdd:cd02755 198 --ELAS-----KADEWIPIKPGTDLAFVLALIHVLIS-----ENLYDAAFVEKYTNGFELLKAHVKPYTPEWAAQITDIP 265
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 695773365 345 RADLQRVAE--AYAKSNATIVTYGMGITQHNKgTSNVRLIADLLLMRGNIGKPGaGICP 401
Cdd:cd02755 266 ADTIRRIARefAAAAPHAVVDPGWRGTFYSNS-FQTRRAIAIINALLGNIDKRG-GLYY 322
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
114-489 |
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 695773365 114 RLTHPL--VYDRASDTLRPTSWESAFARIGEVVSGMQ----PDEVEFY-TSGRASNEAAWLFQL-FARELGTNNFPDCSN 185
Cdd:cd02759 54 RLLYPLkrVGERGENKWERISWDEALDEIAEKLAEIKaeygPESIATAvGTGRGTMWQDSLFWIrFVRLFGSPNLFLSGE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 186 MCHESTSVGLPQSIGIGkGTVSLDDFDKTELVISIGHNPG-TNHPRMMGTLHELARRGVPIIVFNPlkeRALErfadpqn 264
Cdd:cd02759 134 SCYWPRDMAHALTTGFG-LGYDEPDWENPECIVLWGKNPLnSNLDLQGHWLVAAMKRGAKLIVVDP---RLTW------- 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 265 VIEMATLrstniastYFQVKAGGDAAALKGIAKALLQMEeeqgdVLDRPFITEHTQNFPAFADDLQKTSWQDIERESGLT 344
Cdd:cd02759 203 LAARADL--------WLPIRPGTDAALALGMLNVIINEG-----LYDKDFVENWCYGFEELAERVQEYTPEKVAEITGVP 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 345 RADLQRVAEAYAKSNATIVTYGMGITQHNKGTSNVRLIADLLLMRGNIGKPGAGIcplrghsnvqgnrtvgitekpgaaf 424
Cdd:cd02759 270 AEKIRKAARLYATAKPACIQWGLAIDQQKNGTQTSRAIAILRAITGNLDVPGGNL------------------------- 324
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695773365 425 laklqevfgfappqkhghdavkalqaMIEGKSKALLCLGGNFAVAMPDPERAFPAMRGLDLSVHV 489
Cdd:cd02759 325 --------------------------LIPYPVKMLIVFGTNPLASYADTAPVLEALKALDFIVVV 363
|
|
| Molydop_binding |
pfam01568 |
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
642-749 |
1.21e-13 |
|
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: 67.68 E-value: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 642 LRLVTLRSHDQYNTTIYAMDDRYRGIFgRRDVLFMNEQDMASQGFEHGDRVDITTAlpdsNLRLQDITLVAYNIAPGTVG 721
Cdd:pfam01568 1 LYLITGRVLGQYHSQTRTRRVLRLAKP-EPEVVEIHPEDAAALGIKDGDLVEVTSR----RGSVVVRAKVTDRVRPGVVF 75
|
90 100 110
....*....|....*....|....*....|....*.
gi 695773365 722 AYYPE--------ANVLVPlDYIDEESGTPSYKSVP 749
Cdd:pfam01568 76 MPFGWwyeprggnANALTD-DATDPLSGGPEFKTCA 110
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
189-412 |
5.86e-13 |
|
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: 72.26 E-value: 5.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 189 ESTSVGLPQSIG---IGKGTVSLDD-FDKTELVISIGHNPGTNhpRM---MGTLH-------ELARRGVPIIVFNPLKER 254
Cdd:cd02751 141 GAAQVILPHVVGsdeVYEQGTSWDDiAEHSDLVVLFGANPLKT--RQgggGGPDHgsyyylkQAKDAGVRFICIDPRYTD 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 255 ALERFADpqnviematlrstniasTYFQVKAGGDAAALKGIAKALlqMEEeqgDVLDRPFITEHTQNFPAFADDL----- 329
Cdd:cd02751 219 TAAVLAA-----------------EWIPIRPGTDVALMLAMAHTL--ITE---DLHDQAFLARYTVGFDEFKDYLlgesd 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 330 --QKT-SWQdiERESGLTRADLQRVAEAYAKSNATIVTyGMGITQHNKGTSNVRLIADLLLMRGNIGKPGAGICPLRGHS 406
Cdd:cd02751 277 gvPKTpEWA--AEITGVPAETIRALAREIASKRTMIAQ-GWGLQRAHHGEQPAWMLVTLAAMLGQIGLPGGGFGFGYGYS 353
|
....*.
gi 695773365 407 NVQGNR 412
Cdd:cd02751 354 NGGGPP 359
|
|
| MopB_CT |
cd02775 |
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a ... |
649-746 |
2.54e-12 |
|
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a large, diverse, heterogeneous superfamily of enzymes that, in general, bind molybdopterin as a cofactor. The MopB domain is found in a wide variety of molybdenum- and tungsten-containing enzymes, including formate dehydrogenase-H (Fdh-H) and -N (Fdh-N), several forms of nitrate reductase (Nap, Nas, NarG), dimethylsulfoxide reductase (DMSOR), thiosulfate reductase, formylmethanofuran dehydrogenase, and arsenite oxidase. Molybdenum is present in most of these enzymes in the form of molybdopterin, a modified pterin ring with a dithiolene side chain, which is responsible for ligating the Mo. In many bacterial and archaeal species, molybdopterin is in the form of a dinucleotide, with two molybdopterin dinucleotide units per molybdenum. These proteins can function as monomers, heterodimers, or heterotrimers, depending on the protein and organism. Also included in the MopB superfamily is the eukaryotic/eubacterial protein domain family of the 75-kDa subunit/Nad11/NuoG (second domain) of respiratory complex 1/NADH-quinone oxidoreductase which is postulated to have lost an ancestral formate dehydrogenase activity and only vestigial sequence evidence remains of a molybdopterin binding site. This hierarchy is of the conserved MopB_CT domain present in many, but not all, MopB homologs.
Pssm-ID: 239176 [Multi-domain] Cd Length: 101 Bit Score: 63.49 E-value: 2.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 649 SHDQYNTTIYAMDDRYRGIFgRRDVLFMNEQDMASQGFEHGDRVDITTALPDSNLRLQditlVAYNIAPGTVGAYYP--- 725
Cdd:cd02775 1 LRDHFHSGTRTRNPWLRELA-PEPVVEINPEDAAALGIKDGDLVRVESRRGSVVLRAK----VTDGVPPGVVFLPHGwgh 75
|
90 100
....*....|....*....|....*..
gi 695773365 726 ------EANVLVPlDYIDEESGTPSYK 746
Cdd:cd02775 76 rggrggNANVLTP-DALDPPSGGPAYK 101
|
|
| MopB_2 |
cd02763 |
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
114-396 |
5.86e-11 |
|
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins
Pssm-ID: 239164 [Multi-domain] Cd Length: 679 Bit Score: 66.01 E-value: 5.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 114 RLTHPL--VYDRASDTLRPTSWESAFA----RIGEVvSGMQPDEVEFYTsGRASNEAawLFQLFARELGTNNFPDCSNMC 187
Cdd:cd02763 54 RLTKPLlrKGPRGSGQFEEIEWEEAFSiatkRLKAA-RATDPKKFAFFT-GRDQMQA--LTGWFAGQFGTPNYAAHGGFC 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 188 HESTSVGLPQSIGIGKGTVSLDDFDKTELVISIGHNPGTNHPRMMGTLHELARRGVPIIVFNPLKEralerfadpqnvie 267
Cdd:cd02763 130 SVNMAAGGLYSIGGSFWEFGGPDLEHTKYFMMIGVAEDHHSNPFKIGIQKLKRRGGKFVAVNPVRT-------------- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 268 matlRSTNIASTYFQVKAGGDAAALKGIAKALLqmeeeQGDVLDRPFITEHTQN------FPAFADDLQKTSWQDIER-- 339
Cdd:cd02763 196 ----GYAAIADEWVPIKPGTDGAFILALAHELL-----KAGLIDWEFLKRYTNAaelvdyTPEWVEKITGIPADTIRRia 266
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 340 -ESGLTRADlQRV------AEAYAKSNATIVT-----YGM-GITQHNKGTSNVRLIADLLLMRGNIGKPG 396
Cdd:cd02763 267 kELGVTARD-QPIelpiawTDVWGRKHEKITGrpvsfHAMrGIAAHSNGFQTIRALFVLMMLLGTIDRPG 335
|
|
| PRK13532 |
PRK13532 |
nitrate reductase catalytic subunit NapA; |
112-459 |
1.20e-09 |
|
nitrate reductase catalytic subunit NapA;
Pssm-ID: 237416 [Multi-domain] Cd Length: 830 Bit Score: 61.84 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 112 YG--RLTHPL------VYDRASDtLRPTSWESAF----ARIGEVVSGMQPDEVEFYTSGRasneaaWLFQ-------LFA 172
Cdd:PRK13532 93 YGkdRLTQPLlrmkdgKYDKEGE-FTPVSWDQAFdvmaEKFKKALKEKGPTAVGMFGSGQ------WTIWegyaaskLMK 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 173 RELGTNNFPDCSNMCHESTSVGLPQSIGIGKGTVSLDDFDKTELVISIGHNPGTNHPrmmgtlhelarrgvpiIVFNPLK 252
Cdd:PRK13532 166 AGFRSNNIDPNARHCMASAVVGFMRTFGIDEPMGCYDDIEAADAFVLWGSNMAEMHP----------------ILWSRVT 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 253 ERaleRFADPQ-NVIEMATL--RSTNIASTYFQVKAGGDAAALKGIAKALLQmeeeqGDVLDRPFITEHTqNFPAFADD- 328
Cdd:PRK13532 230 DR---RLSNPDvKVAVLSTFehRSFELADNGIIFTPQTDLAILNYIANYIIQ-----NNAVNWDFVNKHT-NFRKGATDi 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 329 ---------LQKTS--------WQDIERE-----------------SGLTRADLQRVAEAYAKSNATIVTY-GMGITQHN 373
Cdd:PRK13532 301 gyglrpthpLEKAAknpgtagkSEPISFEefkkfvapytlektakmSGVPKEQLEQLAKLYADPNRKVVSFwTMGFNQHT 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 374 KGTSNVRLIADLLLMRGNIGKPGAGICPLRGHSNVQGN-RTVG-------------------ITEKpgaafLAKLQEvfG 433
Cdd:PRK13532 381 RGVWANNLVYNIHLLTGKISTPGNGPFSLTGQPSACGTaREVGtfshrlpadmvvtnpkhreIAEK-----IWKLPE--G 453
|
410 420
....*....|....*....|....*.
gi 695773365 434 FAPPqKHGHDAVKALQAMIEGKSKAL 459
Cdd:PRK13532 454 TIPP-KPGYHAVAQDRMLKDGKLNAY 478
|
|
| MopB_DmsA-EC |
cd02770 |
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
207-417 |
1.46e-09 |
|
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: 61.18 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 207 SLDDFDKTELVISIGHNPGTNHPRMMGTLHELA---RRGVPIIVFNPlkeraleRFADpqnviEMATLrstniASTYFQV 283
Cdd:cd02770 160 SLDDLKDSKLVVLFGHNPAETRMGGGGSTYYYLqakKAGAKFIVIDP-------RYTD-----TAVTL-----ADEWIPI 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 284 KAGGDAAALKGIAKALlqMEEeqgDVLDRPFITEHTQNFPA--------------------FADDLQKT-SWQdiERESG 342
Cdd:cd02770 223 RPGTDAALVAAMAYVM--ITE---NLHDQAFLDRYCVGFDAehlpegappnesykdyvlgtGYDGTPKTpEWA--SEITG 295
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695773365 343 LTRADLQRVAEAYAKSNATIVTYGMGITQHNKGTSNVRLIADLLLMRGNIGKPGAGICPLRGHSNVQGNRTVGIT 417
Cdd:cd02770 296 VPAETIRRLAREIATTKPAAILQGWGPQRHANGEQAARAIMMLAAMTGNVGIPGGNTGARPGGSAYNGAGLPAGK 370
|
|
| MopB_Arsenite-Ox |
cd02756 |
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the ... |
105-405 |
1.58e-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: 61.34 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 105 SDFELEGYGRLTHPLVydRASDTLRPTSWESAFARIGEVVSGM-----QPDEVEFYTS-------GRASNEAAWLFQLFA 172
Cdd:cd02756 108 SPDNRVGETRLTTPLV--RRGGQLQPTTWDDAIDLVARVIKGIldkdgNDDAVFASRFdhgggggGFENNWGVGKFFFMA 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 173 reLGT-----NNFPDCSNMCHEStsvglpQSIGIGKGTVSLDDFDKTELVISIGHNP---GTNH------PRMMG-TLHE 237
Cdd:cd02756 186 --LQTpfvriHNRPAYNSEVHAT------REMGVGELNNSYEDARLADTIVLWGNNPyetQTVYflnhwlPNLRGaTVSE 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 238 LARRGVP--------IIVFNPLKE---RALERFADPQNVIematlrstniastYFQVKAGGDAAALKGIAKALLqmeEEQ 306
Cdd:cd02756 258 KQQWFPPgepvppgrIIVVDPRRTetvHAAEAAAGKDRVL-------------HLQVNPGTDTALANAIARYIY---ESL 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 307 GDVLDrpfitehtqnfpafaddlqktswqDIERESGLTRADLQRVAEAYAKSNA------TIVTYGMGITQHNKGTSNVR 380
Cdd:cd02756 322 DEVLA------------------------EAEQITGVPRAQIEKAADWIAKPKEggyrkrVMFEYEKGIIWGNDNYRPIY 377
|
330 340
....*....|....*....|....*
gi 695773365 381 LIADLLLMRGNIGKPGAGICPLRGH 405
Cdd:cd02756 378 SLVNLAIITGNIGRPGTGCVRQGGH 402
|
|
| 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 ... |
114-299 |
1.63e-08 |
|
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: 57.78 E-value: 1.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 114 RLTHPLVydRASDTLRPTSWESAF----ARIGEVVsgmqpDEVEFYTSGRASNEAAWLFQLFARE-LGTNNFpDCSNMCH 188
Cdd:cd02771 54 RLTQPLI--RRGGTLVPVSWNEALdvaaARLKEAK-----DKVGGIGSPRASNESNYALQKLVGAvLGTNNV-DHRARRL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 189 estsvgLPQSIGIGKG-TVSLDDFDKTELVISIGHNPGTNHPRMMGTLHELARR---------GVPIIVFNPLKERAlER 258
Cdd:cd02771 126 ------IAEILRNGPIyIPSLRDIESADAVLVLGEDLTQTAPRIALALRQAARRkavelaalsGIPKWQDAAVRNIA-QG 198
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 695773365 259 FADPQNVIEMATLRSTNIASTYFQVKAGGDAAALKGIAKAL 299
Cdd:cd02771 199 AKSPLFIVNALATRLDDIAAESIRASPGGQARLGAALARAV 239
|
|
| MopB_Nitrate-R-NarG-like |
cd02750 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
273-399 |
6.97e-08 |
|
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under anaerobic conditions in the presence of nitrate, E. coli synthesizes the cytoplasmic membrane-bound quinol-nitrate oxidoreductase (NarGHI), which reduces nitrate to nitrite and forms part of a redox loop generating a proton-motive force. Found in prokaryotes and some archaea, NarGHI usually functions as a heterotrimer. The alpha chain contains the molybdenum cofactor-containing Mo-bisMGD catalytic subunit. Members of the MopB_Nitrate-R-NarG-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239151 [Multi-domain] Cd Length: 461 Bit Score: 55.79 E-value: 6.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 273 STNIASTYFQVKAGGDAAALKGIAKALLQmeeeqGDVLDRPFITEHTQ-----NFPAfaddlqktsWQdiERESGLTRAD 347
Cdd:cd02750 212 SAKHADLWVPIKPGTDAALALAMAHVIIK-----EKLYDEDYLKEYTDlpflvYTPA---------WQ--EAITGVPRET 275
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 695773365 348 LQRVAEAYAKSNATIVTYGMGITQHNKGTSNVRLIADLLLMRGNIGKPGAGI 399
Cdd:cd02750 276 VIRLAREFATNGRSMIIVGAGINHWYHGDLCYRALILLLALTGNEGKNGGGW 327
|
|
| MopB_Res-Cmplx1_Nad11 |
cd02773 |
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone ... |
104-224 |
3.09e-06 |
|
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone oxidoreductase/respiratory complex I/NADH dehydrogenase-1(NDH-1) of eukaryotes and the Nqo3/G subunit of alphaproteobacteria NDH-1. The NADH-quinone oxidoreductase is the first energy-transducting complex in the respiratory chains of many prokaryotes and eukaryotes. Mitochondrial complex I and its bacterial counterpart, NDH-1, function as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. The nad11 gene codes for the largest (75 kDa) subunit of the mitochondrial NADH:ubiquinone oxidoreductase, it constitutes the electron input part of the enzyme, or the so-called NADH dehydrogenase fragment. In Paracoccus denitrificans, this subunit is encoded by the nqo3 gene, and is part of the 14 distinct subunits constituting the 'minimal' functional enzyme. The Nad11/Nqo3 subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain belongs to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239174 [Multi-domain] Cd Length: 375 Bit Score: 49.96 E-value: 3.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 104 KSDFELEG--YGRLTHPLVydRASDTLRPTSWESAFARIGEVVSGMQPDEVEFYTSGRASNEAAWLFQLFARELGtnnfp 181
Cdd:cd02773 41 KTRFAYDGlkRQRLDKPYI--RKNGKLKPATWEEALAAIAKALKGVKPDEIAAIAGDLADVESMVALKDLLNKLG----- 113
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 695773365 182 dCSNMCHESTSVGLPQSIGIGK-GTVSLDDFDKTELVISIGHNP 224
Cdd:cd02773 114 -SENLACEQDGPDLPADLRSNYlFNTTIAGIEEADAVLLVGTNP 156
|
|
| MopB_DMSOR-BSOR-TMAOR |
cd02769 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
214-399 |
2.17e-04 |
|
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: 44.56 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 214 TELVISIGHNP---------GTNHPRMMGTLHELARRGVPIIVFNPLKERALERFadpqnviematlrstniASTYFQVK 284
Cdd:cd02769 171 TELVVAFGADPlknaqiawgGIPDHQAYSYLKALKDRGIRFISISPLRDDTAAEL-----------------GAEWIAIR 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 285 AGGDAAALKGIAKALLqmEEeqgDVLDRPFITEHTQNFPAFADDL-------QKTS-WQdiERESGLTRADLQRVAEAYA 356
Cdd:cd02769 234 PGTDVALMLALAHTLV--TE---GLHDKAFLARYTVGFDKFLPYLlgesdgvPKTPeWA--AAICGIPAETIRELARRFA 306
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 695773365 357 kSNATIVTYGMGITQHNKGTSNVRLIADLLLMRGNIGKPGAGI 399
Cdd:cd02769 307 -SKRTMIMAGWSLQRAHHGEQPHWMAVTLAAMLGQIGLPGGGF 348
|
|
| FwdD |
COG1153 |
Formylmethanofuran dehydrogenase subunit D [Energy production and conversion]; |
673-765 |
4.30e-04 |
|
Formylmethanofuran dehydrogenase subunit D [Energy production and conversion];
Pssm-ID: 440767 [Multi-domain] Cd Length: 127 Bit Score: 40.99 E-value: 4.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 673 VLFMNEQDMASQGFEHGDRVDITTALPDSNLRlqdiTLVAYNIAPGTV----GayyPEANVLVPLDyiDEESGTPSYKSV 748
Cdd:COG1153 32 VCELNPEDMKKLGIKEGDKVKVTSEYGEVVVK----AKESEDLHPGLVfipmG---PWANAVVPPE--THSTGMPDFKGV 102
|
90
....*....|....*..
gi 695773365 749 PIRLTLRSKEILPVSGL 765
Cdd:COG1153 103 PVEVEPTDEEVLSAEEL 119
|
|
| MopB_CT_Fdh-Nap-like |
cd00508 |
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and ... |
642-753 |
1.34e-03 |
|
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and other related proteins. Formate dehydrogenase H is a component of the anaerobic formate hydrogen lyase complex and catalyzes the reversible oxidation of formate to CO2 with the release of a proton and two electrons. Formate dehydrogenase N (alpha subunit) is the major electron donor to the bacterial nitrate respiratory chain and nitrate reductases, Nap and Nas, catalyze the reduction of nitrate to nitrite. This CD (MopB_CT_Fdh-Nap-like) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 238282 [Multi-domain] Cd Length: 120 Bit Score: 39.41 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 642 LRLVTLRSHDQYNTTiyAMDDRYRGIFGRRD--VLFMNEQDMASQGFEHGDRVDITTalPDSNLRLQdiTLVAYNIAPGT 719
Cdd:cd00508 5 LVLTTGRLLEHWHTG--TMTRRSPRLAALAPepFVEIHPEDAARLGIKDGDLVRVSS--RRGSVVVR--ARVTDRVRPGT 78
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 695773365 720 VGAYY--------PEANVLVPLDYiDEESGTPSYKSVPIRLT 753
Cdd:cd00508 79 VFMPFhwggevsgGAANALTNDAL-DPVSGQPEFKACAVRIE 119
|
|
| MopB_CT_Acetylene-hydratase |
cd02781 |
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related ... |
673-751 |
2.14e-03 |
|
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. The acetylene hydratase of Pelobacter acetylenicus is a tungsten iron-sulfur protein involved in the fermentation of acetylene to ethanol and acetate. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239182 [Multi-domain] Cd Length: 130 Bit Score: 38.83 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 673 VLFMNEQDMASQGFEHGDRVDITTalPDSNLRLQdiTLVAYNIAPGTV----GAYYPE---------------ANVLVPL 733
Cdd:cd02781 34 VAEINPETAAKLGIADGDWVWVET--PRGRARQK--ARLTPGIRPGVVraehGWWYPEreagepalggvwesnANALTSD 109
|
90
....*....|....*...
gi 695773365 734 DYIDEESGTPSYKSVPIR 751
Cdd:cd02781 110 DWNDPVSGSSPLRSMLCK 127
|
|
| PRK07860 |
PRK07860 |
NADH dehydrogenase subunit G; Validated |
114-179 |
2.83e-03 |
|
NADH dehydrogenase subunit G; Validated
Pssm-ID: 236118 [Multi-domain] Cd Length: 797 Bit Score: 41.08 E-value: 2.83e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695773365 114 RLTHPLVYDrASDTLRPTSWESAFARIGEVVSGMQpDEVEFYTSGRASNEAAWLFQLFAR-ELGTNN 179
Cdd:PRK07860 278 RITTPLVRD-EDGELEPASWSEALAVAARGLAAAR-GRVGVLVGGRLTVEDAYAYAKFARvALGTND 342
|
|
| PRK14991 |
PRK14991 |
tetrathionate reductase subunit TtrA; |
642-721 |
4.40e-03 |
|
tetrathionate reductase subunit TtrA;
Pssm-ID: 237883 [Multi-domain] Cd Length: 1031 Bit Score: 40.75 E-value: 4.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695773365 642 LRLVTLRSHDQYNTTIyaMDDRYRGIFGRRDVLfMNEQDMASQGFEHGDRVDITTalPDSNLRLQdiTLVAYNIAPGTVG 721
Cdd:PRK14991 889 LLLISFKSNLMSSMSI--ASPRLRQVKPANPVA-LNPQDAARLGIQHGDRVRIST--PGGSVVAQ--ASVLNGVMPGVIA 961
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| |
