|
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: 974.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 17 PAGGWGALKATAIAVRTQMDTLEAPVTLMRTNQPDGFDCPGCAWPDK-EHRSTFQFCENGAKAVTWEATSKRVTPEFLAQ 95
Cdd:TIGR01701 1 DAGGWGAVKSVALGKVKPMHIRQTLKLLLTLNKPEGYDCPGCAWGVSpQTLAGLEFCENGAKAIAWETTPRTIDPEFFAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 96 NTVTSLLQKTDYQLEDYGRLTTPLFYDAGTDTLRPLAWDEAFQRIAAVLQTLPPEQVEFYTSGRASNEAAYLFQLFAREF 175
Cdd:TIGR01701 81 HSVSELRTLDSHELEKLGRLTYPLSLRPGSDHYTPISWDDAYQEIAAKLNSLDPKQVAFYTSGRTSNEAAYLYQLFARSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 176 GSNNFPDCSNMCHEPTSVGLPQSIGIGKGTVSLDDFDSAELVISIGHNPGTNHPRMMGTLHELARKKVPIIVFNPLRERA 255
Cdd:TIGR01701 161 GSNNLPDCSNMCHEPSSVALKRSIGIGKGSVNLEDFEHTDCLVFIGSNAGTNHPRMLKYLYAAKKRGAKIIAINPLRERG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 256 LERFTDPQNVIEMATYSSTPIASTYYQVKAGGDAAALKGIAKALLQLDDEH-GNALDHAFIAEHTEGFTAFDADLRATHW 334
Cdd:TIGR01701 241 LERFWIPQIPESMLTGGGTQISSEYYQVRIGGDIALFNGVMKLLIEAEDAQpGSLIDHEFIANHTNGFDELRRHVLQLNW 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 335 EAIEAESGLTRQDLEQVAAAYAKSNATIVTYGMGITQHNKGTANVRLIADLLLLRGNIGKPGAGICPLRGHSNVQGNRTV 414
Cdd:TIGR01701 321 NDIERSSGLSQEEILEFAKLLANSRRVVFCWAMGLTQHAHGVDNISQVANLALLRGNIGKPGAGVCPIRGHSNVQGDRTM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 415 GITEKPSAEFLAKLETVFGFTPPKAHGHDAVKCMQAMIDGASKALICLGGNFAVALPDPEQSFPAMKALELSVHIGTKLN 494
Cdd:TIGR01701 401 GITEKPEEEFLARLSQIYGFTPPDWPGDTTVAMIEAILTGKVRAFICLGGNFLEAMPDTAAIERALRQLDLRVHVATKLN 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 495 RSHLLVAKETLILPCLGRTELDLQAGGRQSVTVEDSMSMVHASSGKLKPASELLRSEPAIVAGMAKAVMPASKVPWDELV 574
Cdd:TIGR01701 481 RSHVLAKEEALILPVLGRYEQDGQGTGKQAVSVESSMRMVHFSRGILKPRGAELRSEWAIIAEIAKALLPETPVAWEILV 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 575 EDYDVIRDLIEKTIPGFDDYNARIRQPGGFRMPLPP-TERQWPTATGKAMFSVFSGLHEDQIAAEQDTLRLITLRSHDQY 653
Cdd:TIGR01701 561 DTYDQIRDAIAATNPGYDDINHRKRRPDGFQLPGAAlCERKFPTPDGKANFIVIPLPEFRVPTGHEFELVLVTLRSHDQF 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 654 NTTIYALDDRYRGVFGRRDVLFMNDSDLQRLGLEHGDVVDLETALP-GSTQRLEGITVIAYNISAGSVGAYYPEANVLVP 732
Cdd:TIGR01701 641 NTTIYGEDDRYRGVDGHRRVVFMNETDIKKLGLRNGERVDVYNQYGdGQKRKFDNLRIVFYDTPTGNAAAYYPEANPLLP 720
|
730 740
....*....|....*....|.
gi 1778700535 733 LHYIDEESGTPSYKSVPIRVK 753
Cdd:TIGR01701 721 LDHHDPQSKTPEYKTIPVRLE 741
|
|
| PRK09939 |
PRK09939 |
acid resistance putative oxidoreductase YdeP; |
9-753 |
0e+00 |
|
acid resistance putative oxidoreductase YdeP;
Pssm-ID: 182156 [Multi-domain] Cd Length: 759 Bit Score: 944.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 9 PGVHPYDGPAGGWGALKATAIAVRTQMDTLEAPVTLMRTNQPDGFDCPGCAWPDKEHRSTFQFCENGAKAVTWEATSKRV 88
Cdd:PRK09939 3 KKIESYQGAAGGWGAVKSVANAVRKQMDIRQDVIAMFDMNKPEGFDCPGCAWPDPKHSASFDICENGAKAIAWEVTDKQV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 89 TPEFLAQNTVTSLLQKTDYQLEDYGRLTTPLFYDAGTDTLRPLAWDEAFQRIAAVLQTLP-PEQVEFYTSGRASNEAAYL 167
Cdd:PRK09939 83 NASFFAENTVQSLLTWGDHELEAAGRLTQPLKYDAVSDCYKPLSWQQAFDEIGARLQSYSdPNQVEFYTSGRTSNEAAFL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 168 FQLFAREFGSNNFPDCSNMCHEPTSVGLPQSIGIGKGTVSLDDFDSAELVISIGHNPGTNHPRMMGTLHELARKKVPIIV 247
Cdd:PRK09939 163 YQLFAREYGSNNFPDCSNMCHEPTSVGLAASIGVGKGTVLLEDFEKCDLVICIGHNPGTNHPRMLTSLRALVKRGAKMIA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 248 FNPLRERALERFTDPQNVIEMATYSSTPIASTYYQVKAGGDAAALKGIAKALLQLDDEHGNA-----LDHAFIAEHTEGF 322
Cdd:PRK09939 243 INPLQERGLERFTAPQNPFEMLTNSETQLASAYYNVRIGGDMALLKGMMRLLIERDDAASAAgrpslLDDEFIQTHTVGF 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 323 TAFDADLRATHWEAIEAESGLTRQDLEQVAAAYAKSNATIVTYGMGITQHNKGTANVRLIADLLLLRGNIGKPGAGICPL 402
Cdd:PRK09939 323 DELRRDVLNSEWKDIERISGLSQTQIAELADAYAAAERTIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGICPL 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 403 RGHSNVQGNRTVGITEKPSAEFLAKLETVFGFTPPKAHGHDAVKCMQAMIDGASKALICLGGNFAVALPDPEQSFPAMKA 482
Cdd:PRK09939 403 RGHSNVQGDRTVGITEKPSAEFLARLGERYGFTPPHAPGHAAIASMQAICTGQARALICMGGNFALAMPDREASAVPLTQ 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 483 LELSVHIGTKLNRSHLLVAKETLILPCLGRTELDLQAGGRQSVTVEDSMSMVHASSGKLKPASELLRSEPAIVAGMAKAV 562
Cdd:PRK09939 483 LDLAVHVATKLNRSHLLTARHSYILPVLGRSEIDMQKSGAQAVTVEDSMSMIHASRGVLKPAGVMLKSECAVVAGIAQAA 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 563 MPASKVPWDELVEDYDVIRDLIEKTIPGFDDYNARIRQPGGFRMPLPPTERQWPTATGKAMFSVFSGLHEDQIAAEQDTL 642
Cdd:PRK09939 563 LPQSVVAWEYLVEDYDRIRNDIEAVLPEFADYNQRIRHPGGFHLINAAAERRWMTPSGKANFITSKGLLEDPSSAFNSKL 642
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 643 RLITLRSHDQYNTTIYALDDRYRGVFGRRDVLFMNDSDLQRLGLEHGDVVDLETALPG---STQRLEGITVIAYNISAGS 719
Cdd:PRK09939 643 VMATVRSHDQYNTTIYGMDDRYRGVFGQRDVVFMSAKQAKICRVKNGERVNLIALTPDgkrSSRRMDRLKVVIYPMADRS 722
|
730 740 750
....*....|....*....|....*....|....
gi 1778700535 720 VGAYYPEANVLVPLHYIDEESGTPSYKSVPIRVK 753
Cdd:PRK09939 723 LVTYFPESNHMLTLDNHDPLSGIPGYKSIPVELE 756
|
|
| 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: 928.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 52 GFDCPGCAWPD-KEHRSTFQFCENGAKAVTWEATSKRVTPEFLAQNTVTSLLQKTDYQLEDYGRLTTPLFYDAGTDTLRP 130
Cdd:cd02767 1 GFDCPGCAWGDpGQKLHGFEFCENGAKALAWETTPKRVTPEFFALHSVSELRTWSDYELEHLGRLTYPMRYDAGSDHYRP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 131 LAWDEAFQRIAAVLQTLPPEQVEFYTSGRASNEAAYLFQLFAREFGSNNFPDCSNMCHEPTSVGLPQSIGIGKGTVSLDD 210
Cdd:cd02767 81 ISWDEAFAEIAARLRALDPDRAAFYTSGRASNEAAYLYQLFARAYGTNNLPDCSNMCHEPSSVGLKKSIGVGKGTVSLED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 211 FDSAELVISIGHNPGTNHPRMMGTLHELARKKVPIIVFNPLRERALERFTDPQNVIEMATySSTPIASTYYQVKAGGDAA 290
Cdd:cd02767 161 FEHTDLIFFIGQNPGTNHPRMLHYLREAKKRGGKIIVINPLREPGLERFANPQNPESMLT-GGTKIADEYFQVRIGGDIA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 291 ALKGIAKALLQLDDEHGNALDHAFIAEHTEGFTAFDADLRATHWEAIEAESGLTRQDLEQVAAAYAKSNATIVTYGMGIT 370
Cdd:cd02767 240 LLNGMAKHLIERDDEPGNVLDHDFIAEHTSGFEEYVAALRALSWDEIERASGLSREEIEAFAAMYAKSERVVFVWGMGIT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 371 QHNKGTANVRLIADLLLLRGNIGKPGAGICPLRGHSNVQGNRTVGITEKPSAEFLAKLETVFGFTPPKAHGHDAVKCMQA 450
Cdd:cd02767 320 QHAHGVDNVRAIVNLALLRGNIGRPGAGLMPIRGHSNVQGDRTMGITEKPFPEFLDALEEVFGFTPPRDPGLDTVEAIEA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 451 MIDGASKALICLGGNFAVALPDPEQSFPAMKALELSVHIGTKLNRSHLLVAKETLILPCLGRTELDLQAGGRQSVTVEDS 530
Cdd:cd02767 400 ALEGKVKAFISLGGNFAEAMPDPAATEEALRRLDLTVHVATKLNRSHLVHGEEALILPCLGRTEIDMQAGGAQAVTVEDS 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 531 MSMVHASSGKLKPASELLRSEPAIVAGMAKAVMPASKVPWDELVEDYDVIRDLIEKTIP-GFDDYNARIRQPGGFRMPLP 609
Cdd:cd02767 480 MSMTHTSRGRLKPASRVLLSEEAIVAGIAGARLGEAKPEWEILVEDYDRIRDEIAAVIYeGFADFNQRGDQPGGFHLPNG 559
|
570
....*....|....*
gi 1778700535 610 PTERQWPTATGKAMF 624
Cdd:cd02767 560 ARERKFNTPSGKAQF 574
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
55-753 |
1.22e-166 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 496.29 E-value: 1.22e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 55 CPGCAWpdkehrstfqFCENGAKAVTWEATskRVTPEflAQNTVTSLL-----QKTDYQLEDYGRLTTPLFYD--AGTDT 127
Cdd:COG0243 28 CPGCGV----------GCGLGVKVEDGRVV--RVRGD--PDHPVNRGRlcakgAALDERLYSPDRLTYPMKRVgpRGSGK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 128 LRPLAWDEAFQRIAAVLQTL----PPEQVEFYTSG----RASNEAAYLFQLFAREFGSNNFPDCSNMCHEPTSVGLPQSI 199
Cdd:COG0243 94 FERISWDEALDLIAEKLKAIideyGPEAVAFYTSGgsagRLSNEAAYLAQRFARALGTNNLDDNSRLCHESAVAGLPRTF 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 200 GIGKGTVSLDDFDSAELVISIGHNPGTNHPRMMGTLHELARKK-VPIIVFNPLRERalerftdpqnviematysSTPIAS 278
Cdd:COG0243 174 GSDKGTVSYEDLEHADLIVLWGSNPAENHPRLLRRLREAAKKRgAKIVVIDPRRTE------------------TAAIAD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 279 TYYQVKAGGDAAALKGIAKALLQLDdehgnALDHAFIAEHTEGFTAFDADLRATHWEAIEAESGLTRQDLEQVAAAYAKS 358
Cdd:COG0243 236 EWLPIRPGTDAALLLALAHVLIEEG-----LYDRDFLARHTVGFDELAAYVAAYTPEWAAEITGVPAEDIRELAREFATA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 359 NATIVTYGMGITQHNKGTANVRLIADLLLLRGNIGKPGAGICPLRGHsnvqgnrtvgitekpsaeflakletvfgftppk 438
Cdd:COG0243 311 KPAVILWGMGLQQHSNGTQTVRAIANLALLTGNIGKPGGGPFSLTGE--------------------------------- 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 439 ahghdavkcmqAMIDGAS---KALICLGGNFAVALPDPEQSFPAMKALELSVHIGTKLNRSHLLVAketLILPCLGRTEL 515
Cdd:COG0243 358 -----------AILDGKPypiKALWVYGGNPAVSAPDTNRVREALRKLDFVVVIDTFLTETARYAD---IVLPATTWLER 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 516 DLQAggrqsVTVEDsmSMVHASSGKLKPASElLRSEPAIVAGMAKAVMPASKVPWDELVEDYdvIRDLIEKTIPGFDDYn 595
Cdd:COG0243 424 DDIV-----TNSED--RRVHLSRPAVEPPGE-ARSDWEIFAELAKRLGFEEAFPWGRTEEDY--LRELLEATRGRGITF- 492
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 596 ARIRQPGGFRMPLPP-----TERQWPTATGKAMFSV----FSGL-------HEDQIAAEQDTLRLITLRSHDQYNTTIYA 659
Cdd:COG0243 493 EELREKGPVQLPVPPepafrNDGPFPTPSGKAEFYSetlaLPPLpryappyEGAEPLDAEYPLRLITGRSRDQWHSTTYN 572
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 660 LdDRYRGVFGRRdVLFMNDSDLQRLGLEHGDVVDLETAlpgsTQRLEGITVIAYNISAGSV----GAYYPEA-------N 728
Cdd:COG0243 573 N-PRLREIGPRP-VVEINPEDAAALGIKDGDLVRVESD----RGEVLARAKVTEGIRPGVVfaphGWWYEPAddkggnvN 646
|
730 740
....*....|....*....|....*
gi 1778700535 729 VLVPLHYiDEESGTPSYKSVPIRVK 753
Cdd:COG0243 647 VLTPDAT-DPLSGTPAFKSVPVRVE 670
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
108-752 |
3.44e-104 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 334.54 E-value: 3.44e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 108 QLEDYGRLTTPLFYDAGTdtLRPLAWDEAFQRIAAVLQTL----PPEQVEFYTSGRASNEAAYLFQLFARE-FGSNNFPD 182
Cdd:COG3383 55 FVNSPDRLTTPLIRRGGE--FREVSWDEALDLVAERLREIqaehGPDAVAFYGSGQLTNEENYLLQKLARGvLGTNNIDN 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 183 CSNMCHEPTSVGLPQSIGIGKGTVSLDDFDSAELVISIGHNPGTNHPRMMGTLHELARKKVPIIVFNPlRERALERFtdp 262
Cdd:COG3383 133 NARLCMASAVAGLKQSFGSDAPPNSYDDIEEADVILVIGSNPAEAHPVLARRIKKAKKNGAKLIVVDP-RRTETARL--- 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 263 qnviematysstpiASTYYQVKAGGDAAALKGIAKALLqlddEHGnALDHAFIAEHTEGFTAFDADLRATHWEAIEAESG 342
Cdd:COG3383 209 --------------ADLHLQIKPGTDLALLNGLLHVII----EEG-LVDEDFIAERTEGFEELKASVAKYTPERVAEITG 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 343 LTRQDLEQVAAAYAKSNATIVTYGMGITQHNKGTANVRLIADLLLLRGNIGKPGAGICPLRGHSNVQGNRTVGI--TEKP 420
Cdd:COG3383 270 VPAEDIREAARLIAEAKRAMILWGMGVNQHTQGTDNVNAIINLALATGNIGRPGTGPFPLTGQNNVQGGRDMGAlpNVLP 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 421 ------SAEFLAKLETVFGFTP-PKAHGHDAVKCMQAMIDGASKALICLGGNFAVALPDPEQSFPAMKALELSVHIGTKL 493
Cdd:COG3383 350 gyrdvtDPEHRAKVADAWGVPPlPDKPGLTAVEMFDAIADGEIKALWIIGENPAVSDPDANHVREALEKLEFLVVQDIFL 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 494 NrshllvakET-----LILPCLGRTELDlqaGgrqsvTVEDSMSMVHASSGKLKPASElLRSEPAIVAGMAKAVmpASKV 568
Cdd:COG3383 430 T--------ETaeyadVVLPAASWAEKD---G-----TFTNTERRVQRVRKAVEPPGE-ARPDWEIIAELARRL--GYGF 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 569 PWDELVEdydvIRDLIEKTIPGFD--DYnARIRQPGGFRMPLPP-----TER----QWPTATGKAMFSVFSGLHEDQIAA 637
Cdd:COG3383 491 DYDSPEE----VFDEIARLTPDYSgiSY-ERLEALGGVQWPCPSedhpgTPRlftgRFPTPDGKARFVPVEYRPPAELPD 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 638 EQDTLRLITLRSHDQYNT-TIYALDDRYRGVFGrRDVLFMNDSDLQRLGLEHGDVVDLETALpGSTqrlEGITVIAYNIS 716
Cdd:COG3383 566 EEYPLVLTTGRLLDQWHTgTRTRRSPRLNKHAP-EPFVEIHPEDAARLGIKDGDLVRVSSRR-GEV---VLRARVTDRVR 640
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1778700535 717 AGSVGAY--YPE--ANVLVPlHYIDEESGTPSYKSVPIRV 752
Cdd:COG3383 641 PGTVFMPfhWGEgaANALTN-DALDPVSKQPEYKACAVRV 679
|
|
| Fdh-alpha |
TIGR01591 |
formate dehydrogenase, alpha subunit, archaeal-type; This model describes a subset of formate ... |
114-752 |
5.53e-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: 264.33 E-value: 5.53e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 114 RLTTPLFYDAgtDTLRPLAWDEAFQRIAAVLQTLP----PEQVEFYTSGRASNEAAYLFQLFARE-FGSNNFPDCSNMCH 188
Cdd:TIGR01591 53 RLTTPLIREG--DKFREVSWDEAISYIAEKLKEIKekygPDSIGFIGSSRGTNEENYLLQKLARAvIGTNNVDNCARVCH 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 189 EPTSVGLPQSIGIGKGTVSLDDFDSAELVISIGHNPGTNHPRMMGTLHELARKKVPIIVFNPLReralerftdpqnvIEM 268
Cdd:TIGR01591 131 GPSVAGLKQTVGIGAMSNTISEIENADLIVIIGYNPAESHPVVAQYLKNAKRNGAKIIVIDPRK-------------TET 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 269 ATysstpIASTYYQVKAGGDAAALKGIAKALLQlddehGNALDHAFIAEHTEGFTAFDADLRATHWEAIEAESGLTRQDL 348
Cdd:TIGR01591 198 AK-----IADLHIPLKPGTDIALLNAMANVIIE-----EGLYDKAFIEKRTEGFEEFREIVKGYTPEYVEDITGVPADLI 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 349 EQVAAAYAKSNATIVTYGMGITQHNKGTANVRLIADLLLLRGNIGKPGAGICPLRGHSNVQGNRTVGI--TEKP------ 420
Cdd:TIGR01591 268 REAARMYAKAGSAAILWGMGVTQHSQGVETVMALINLAMLTGNIGKPGGGVNPLRGQNNVQGACDMGAlpDFLPgyqpvs 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 421 SAEFLAKLETVFGFTPPKAH-GHDAVKCMQAMIDGASKALICLGGNFAVALPDPEQSFPAMKALELSVHIGTKLNRSHLL 499
Cdd:TIGR01591 348 DEEVREKFAKAWGVVKLPAEpGLRIPEMIDAAADGDVKALYIMGEDPLQSDPNTSKVRKALEKLELLVVQDIFMTETAKY 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 500 vAKETLILPCLGRTELDLQAGGRqsvTVEDSMSMVHAsSGKLKPASELLRsepaivagmakavMPASKVPWDELVEDYDV 579
Cdd:TIGR01591 428 -ADVVLPAAAWLEKEGTFTNAER---RIQRFFKAVEP-KGESKPDWEIIQ-------------ELANALGLDWNYNHPQE 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 580 IRDLIEKTIPGFDDYN-ARIRQPGGFRMPLPPTER---------QWPTATGKAMFSVFSGLHEDQIAAEQDTLRLITLRS 649
Cdd:TIGR01591 490 IMDEIRELTPLFAGLTyERLDELGSLQWPCNDSDAsptsylykdKFATPDGKAKFIPLEWVAPIEEPDDEYPLILTTGRV 569
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 650 HDQYNTTiyALDDRYRGVfgRRDV----LFMNDSDLQRLGLEHGDVVDLETALPGSTQRLE-------GITVIAYNisag 718
Cdd:TIGR01591 570 LTHYNVG--EMTRRVAGL--RRLSpepyVEINTEDAKKLGIKDGDLVKVKSRRGEITLRAKvsdrvnkGAIYITMH---- 641
|
650 660 670
....*....|....*....|....*....|....
gi 1778700535 719 svgAYYPEANVLVPLhYIDEESGTPSYKSVPIRV 752
Cdd:TIGR01591 642 ---FWDGAVNNLTTD-DLDPISGTPEYKYTAVRI 671
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
114-487 |
1.74e-72 |
|
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: 245.20 E-value: 1.74e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 114 RLTTPLFYDagTDTLRPLAWDEAFQRIAAVLQTL----PPEQVEFYTSGRASNEAAYLFQLFARE-FGSNNFPDCSNMCH 188
Cdd:cd02753 54 RLTKPLIRK--NGKFVEASWDEALSLVASRLKEIkdkyGPDAIAFFGSAKCTNEENYLFQKLARAvGGTNNVDHCARLCH 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 189 EPTSVGLPQSIGIGKGTVSLDDFDSAELVISIGHNPGTNHPRMMGTLHELARKKVPIIVFNPLReralerftdpqnvIEM 268
Cdd:cd02753 132 SPTVAGLAETLGSGAMTNSIADIEEADVILVIGSNTTEAHPVIARRIKRAKRNGAKLIVADPRR-------------TEL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 269 ATysstpIASTYYQVKAGGDAAALKGIAKALLqlddEHGNAlDHAFIAEHTEGFTAFDADLRATHWEAIEAESGLTRQDL 348
Cdd:cd02753 199 AR-----FADLHLQLRPGTDVALLNAMAHVII----EEGLY-DEEFIEERTEGFEELKEIVEKYTPEYAERITGVPAEDI 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 349 EQVAAAYAKSNATIVTYGMGITQHNKGTANVRLIADLLLLRGNIGKPGAGICPLRGHSNVQGNRTVGitekpsaeflakl 428
Cdd:cd02753 269 REAARMYATAKSAAILWGMGVTQHSHGTDNVMALSNLALLTGNIGRPGTGVNPLRGQNNVQGACDMG------------- 335
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1778700535 429 etvfgftppkahghdavkCMQAMIDGASKALICLGGNFAVALPDPEQSFPAMKALELSV 487
Cdd:cd02753 336 ------------------ALPNVLPGYVKALYIMGENPALSDPNTNHVRKALESLEFLV 376
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
108-562 |
1.22e-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: 214.50 E-value: 1.22e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 108 QLEDYGRLTTPLFYDAGTDTLRPLAWDEAFQRIAAVLQTLP----PEQVEFYTSGRASNEAAYLFQLFAREFGSNNFPDC 183
Cdd:cd00368 48 GLYSPDRLKYPLIRVGGRGKFVPISWDEALDEIAEKLKEIRekygPDAIAFYGGGGASNEEAYLLQKLLRALGSNNVDSH 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 184 SNMCHEPTSVGLPQsIGIGKGTVSLDDFDSAELVISIGHNPGTNHPRMMGTLHELARKKVPIIVFNPLRERalerftdpq 263
Cdd:cd00368 128 ARLCHASAVAALKA-FGGGAPTNTLADIENADLILLWGSNPAETHPVLAARLRRAKKRGAKLIVIDPRRTE--------- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 264 nviematysSTPIASTYYQVKAGGDAAALKGiakallqlddehgnaldhafiaehtegftafdadlrathwEAIEAESGL 343
Cdd:cd00368 198 ---------TAAKADEWLPIRPGTDAALALA----------------------------------------EWAAEITGV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 344 TRQDLEQVAAAYAKSNATIVTYGMGITQHNKGTANVRLIADLLLLRGNIGKPGAGICPlrghsnvqgnrtvgitekpsae 423
Cdd:cd00368 229 PAETIRALAREFAAAKRAVILWGMGLTQHTNGTQNVRAIANLAALTGNIGRPGGGLGP---------------------- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 424 flakletvfgftppkahghdavkcmqamidgaskaliclGGNFAVALPDPEQSFPAMKALELSVHIGTKLNRSHLLvakE 503
Cdd:cd00368 287 ---------------------------------------GGNPLVSAPDANRVRAALKKLDFVVVIDIFMTETAAY---A 324
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1778700535 504 TLILPCLGRTEldlqaggrQSVTVEDSMSMVHASSGKLKPASElLRSEPAIVAGMAKAV 562
Cdd:cd00368 325 DVVLPAATYLE--------KEGTYTNTEGRVQLFRQAVEPPGE-ARSDWEILRELAKRL 374
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
113-487 |
6.80e-57 |
|
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to nitrite. Monomeric Nas is located in the cytoplasm and participates in nitrogen assimilation. Dimeric Nap is located in the periplasm and is coupled to quinol oxidation via a membrane-anchored tetraheme cytochrome. Members of the MopB_Nitrate-R-NapA CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239155 [Multi-domain] Cd Length: 565 Bit Score: 204.00 E-value: 6.80e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 113 GRLTTPLFYDAGTDtLRPLAWDEAFQRIAAVLQTL----PPEQVEFYTSGRASNEAAYLFQLFAREF-GSNNFPDCSNMC 187
Cdd:cd02754 53 ERLTRPLLRRNGGE-LVPVSWDEALDLIAERFKAIqaeyGPDSVAFYGSGQLLTEEYYAANKLAKGGlGTNNIDTNSRLC 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 188 HEPTSVGLPQSIGIGKGTVSLDDFDSAELVISIGHNPGTNHPRMMGTLHE--LARKKVPIIVFNPLRERalerftdpqnv 265
Cdd:cd02754 132 MASAVAGYKRSFGADGPPGSYDDIEHADCFFLIGSNMAECHPILFRRLLDrkKANPGAKIIVVDPRRTR----------- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 266 iematysSTPIASTYYQVKAGGDAAALKGIAKALLqlddEHGnALDHAFIAEHTEGFTAFDADLRATHWEAIEAESGLTR 345
Cdd:cd02754 201 -------TADIADLHLPIRPGTDLALLNGLLHVLI----EEG-LIDRDFIDAHTEGFEELKAFVADYTPEKVAEITGVPE 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 346 QDLEQVAAAYAKSNATIVTYGMGITQHNKGTANVRLIADLLLLRGNIGKPGAGICPLRGHSNVQGNRTVG---------- 415
Cdd:cd02754 269 ADIREAARLFGEARKVMSLWTMGVNQSTQGTAANNAIINLHLATGKIGRPGSGPFSLTGQPNAMGGREVGglanllpghr 348
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1778700535 416 -ITEKPSAEFLAKLETVFGFTPPKAHGHDAVKCMQAMIDGASKALICLGGNFAVALPDPEQSFPAMKALELSV 487
Cdd:cd02754 349 sVNNPEHRAEVAKFWGVPEGTIPPKPGLHAVEMFEAIEDGEIKALWVMCTNPAVSLPNANRVREALERLEFVV 421
|
|
| MopB_CT_ydeP |
cd02787 |
The MopB_CT_ydeP CD includes a group of related uncharacterized bacterial ... |
642-752 |
3.20e-52 |
|
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: 176.70 E-value: 3.20e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 642 LRLITLRSHDQYNTTIYALDDRYRGVFGRRDVLFMNDSDLQRLGLEHGDVVDLETALP-GSTQRLEGITVIAYNISAGSV 720
Cdd:cd02787 1 LFLVTTRSHDQFNTTIYGLDDRYRGVFGRRDVVFMNPDDIARLGLKAGDRVDLESAFGdGQGRIVRGFRVVEYDIPRGCL 80
|
90 100 110
....*....|....*....|....*....|..
gi 1778700535 721 GAYYPEANVLVPLHYIDEESGTPSYKSVPIRV 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 |
3.07e-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: 3.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 114 RLTTPLFYDAGTDTLRPLAWDEAFQRIAA-VLQT---------------LPPEQVEFYTSGRASNEAAYLFQLFAREFGS 177
Cdd:cd02752 54 RLKYPMYRAPGSGKWEEISWDEALDEIARkMKDIrdasfveknaagvvvNRPDSIAFLGSAKLSNEECYLIRKFARALGT 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 178 NNFPDCSNMCHEPTSVGLPQSIGIGKGTVSLDDFDSAELVISIGHNPGTNHPRMMGTLHElARKKV--PIIVFNPlrera 255
Cdd:cd02752 134 NNLDHQARIUHSPTVAGLANTFGRGAMTNSWNDIKNADVILVMGGNPAEAHPVSFKWILE-AKEKNgaKLIVVDP----- 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 256 leRFTDPQNViematysstpiASTYYQVKAGGDAAALKGIAKALLQlddehgnaldhafiaehtegFTAfdadlrathwE 335
Cdd:cd02752 208 --RFTRTAAK-----------ADLYVPIRSGTDIAFLGGMINYIIR--------------------YTP----------E 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1778700535 336 AIEAESGLTRQDLEQVAAAYAKSN----ATIVTYGMGITQHNKGTANVRLIADLLLLRGNIGKPGAGICPLRGHSNVQG 410
Cdd:cd02752 245 EVEDICGVPKEDFLKVAEMFAATGrpdkPGTILYAMGWTQHTVGSQNIRAMCILQLLLGNIGVAGGGVNALRGHSNVQG 323
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
114-508 |
4.83e-24 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 104.40 E-value: 4.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 114 RLTTPLfYDAGTDTLRPLAWDEAFQRIAAVLQTLPPE------QVEFYTSGRASNEAAYLFQLFAREFGSNNF---PDCS 184
Cdd:pfam00384 1 RLKYPM-VRRGDGKFVRVSWDEALDLIAKKLKRIIKKygpdaiAINGGSGGLTDVESLYALKKLLNRLGSKNGnteDHNG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 185 NMCHEPTSVGLPQSIGIGKGTVSLDDFDSAELVISIGHNPGTNHPRMMGTLH-ELARKKVPIIVFNPlreralerftdpq 263
Cdd:pfam00384 80 DLCTAAAAAFGSDLRSNYLFNSSIADIENADLILLIGTNPREEAPILNARIRkAALKGKAKVIVIGP------------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 264 nviemaTYSSTpIASTYYQVKAGGDAAALkgiakallqlddehgNALDHAFIAEhtegftafdadlrathweaieaesgl 343
Cdd:pfam00384 147 ------RLDLT-YADEHLGIKPGTDLALA---------------LAGAHVFIKE-------------------------- 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 344 trqdleqvaAAYAKSNAT--IVTYGMGITQHNKGTANVRLIADLLLLRGNIGKPGAGICPLRGHSNVqgnrtvgitekps 421
Cdd:pfam00384 179 ---------LKKDKDFAPkpIIIVGAGVLQRQDGEAIFRAIANLADLTGNIGRPGGGWNGLNILQGA------------- 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 422 AEFLAKLEtvFGFTPPKahghDAVKCMQAMIDGASKALICLGGNFAVALPDPEQSFPAMKALELSV----HIGTKL-NRS 496
Cdd:pfam00384 237 ASPVGALD--LGLVPGI----KSVEMINAIKKGGIKVLYLLGNNPFVTHADENRVVKALQKLDLFVvydgHHGDKTaKYA 310
|
410
....*....|..
gi 1778700535 497 HllvaketLILP 508
Cdd:pfam00384 311 D-------VILP 315
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
105-508 |
5.53e-24 |
|
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: 106.71 E-value: 5.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 105 TDYQlEDYGRLTTPLFYDAGTdtLRPLAWDEAF----QRIAAVLQTLPPEQVEFYTSGRASNE---AAYLFQLFAREFGS 177
Cdd:cd02762 46 GDYQ-NDPDRLRTPMRRRGGS--FEEIDWDEAFdeiaERLRAIRARHGGDAVGVYGGNPQAHThagGAYSPALLKALGTS 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 178 NNFPDCS--NMCHEPTSVGLPQSigigKGTVSLDDFDSAELVISIGHNPGTNHPRMM-----GTLHELARKKV-PIIVFN 249
Cdd:cd02762 123 NYFSAATadQKPGHFWSGLMFGH----PGLHPVPDIDRTDYLLILGANPLQSNGSLRtapdrVLRLKAAKDRGgSLVVID 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 250 PLRERALERftdpqnviematysstpiASTYYQVKAGGDAAALKGIAKALLQlddehGNALDHAFIAEHTEGFTAFDADL 329
Cdd:cd02762 199 PRRTETAKL------------------ADEHLFVRPGTDAWLLAAMLAVLLA-----EGLTDRRFLAEHCDGLDEVRAAL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 330 RATHWEAIEAESGLTRQDLEQVAAAYAkSNATIVTYG-MGITQHNKGTANVRLIADLLLLRGNIGKPGAGIC-----PLR 403
Cdd:cd02762 256 AEFTPEAYAPRCGVPAETIRRLAREFA-AAPSAAVYGrLGVQTQLFGTLCSWLVKLLNLLTGNLDRPGGAMFttpalDLV 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 404 GHSnvqGNRTVGITEKPSAefLAKLETVFGFTPPKAHGHDavkcMQAMIDGASKALICLGGNFAVALPDPEQSFPAMKAL 483
Cdd:cd02762 335 GQT---SGRTIGRGEWRSR--VSGLPEIAGELPVNVLAEE----ILTDGPGRIRAMIVVAGNPVLSAPDGARLEAALGGL 405
|
410 420 430
....*....|....*....|....*....|
gi 1778700535 484 ELSVHIGTKLNrshllvakET-----LILP 508
Cdd:cd02762 406 EFMVSVDVYMT--------ETtrhadYILP 427
|
|
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
114-399 |
1.07e-23 |
|
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins
Pssm-ID: 239167 [Multi-domain] Cd Length: 501 Bit Score: 105.41 E-value: 1.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 114 RLTTPLFYD-AGTDTLRPLAWDEAFQRIAAVLQ----TLPPEQVEFY----TSGRASNEA-AYLFQL--FAREFGSnnfp 181
Cdd:cd02766 55 RLLTPLKRVgRKGGQWERISWDEALDTIAAKLKeikaEYGPESILPYsyagTMGLLQRAArGRFFHAlgASELRGT---- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 182 dcsnMCHEPTSVGLPQSIGIGKGtVSLDDFDSAELVISIGHNPGTNHPRMMGTLHElARKK-VPIIVFNPLRERALERft 260
Cdd:cd02766 131 ----ICSGAGIEAQKYDFGASLG-NDPEDMVNADLIVIWGINPAATNIHLMRIIQE-ARKRgAKVVVIDPYRTATAAR-- 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 261 dpqnviematysstpiASTYYQVKAGGDAA-ALkGIAKALLqlddEHGnALDHAFIAEHTEGFTAFDADLRATHWEAIEA 339
Cdd:cd02766 203 ----------------ADLHIQIRPGTDGAlAL-GVAKVLF----REG-LYDRDFLARHTEGFEELKAHLETYTPEWAAE 260
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 340 ESGLTRQDLEQVAAAYAKSNATIVTYGMGITQHNKGTANVRLIADLLLLRGNIGKPGAGI 399
Cdd:cd02766 261 ITGVSAEEIEELARLYGEAKPPSIRLGYGMQRYRNGGQNVRAIDALPALTGNIGVPGGGA 320
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
108-401 |
2.79e-23 |
|
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: 103.53 E-value: 2.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 108 QLEDYGRLTTPLFYDA--GTDTLRPLAWDEAFQRIAAVLQTL----PPEQVEFytsGRASNEAAYLFQLFAREFGSNNFP 181
Cdd:cd02755 49 LLYDPDRLKKPLIRVGerGEGKFREASWDEALQYIASKLKEIkeqhGPESVLF---GGHGGCYSPFFKHFAAAFGSPNIF 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 182 DCSNMCHEPTSVGLPQSIGIGKGTVsLDDFDSAELVISIGHN--PGTNHPRMMGTLHELArKKVPIIVFNPlreraleRF 259
Cdd:cd02755 126 SHESTCLASKNLAWKLVIDSFGGEV-NPDFENARYIILFGRNlaEAIIVVDARRLMKALE-NGAKVVVVDP-------RF 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 260 TdpqnviEMATysstpIASTYYQVKAGGDAAALKGIAKALLqldDEhgNALDHAFIAEHTEGFTAFDADLRATHWEAIEA 339
Cdd:cd02755 197 S------ELAS-----KADEWIPIKPGTDLAFVLALIHVLI---SE--NLYDAAFVEKYTNGFELLKAHVKPYTPEWAAQ 260
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1778700535 340 ESGLTRQDLEQVAA--AYAKSNATIVTYGMGITQHNKgTANVRLIADLLLLRGNIGKPGaGICP 401
Cdd:cd02755 261 ITDIPADTIRRIARefAAAAPHAVVDPGWRGTFYSNS-FQTRRAIAIINALLGNIDKRG-GLYY 322
|
|
| MopB_NADH-Q-OR-NuoG2 |
cd02768 |
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone ... |
109-301 |
4.06e-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: 4.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 109 LEDYGRLTTPLFydAGTDTLRPLAWDEAFQRIAAVLQTLPPEQVEFYTSGRASNEAAYLFQLFAREFGSNNFpDCSNMCH 188
Cdd:cd02768 49 LNSRQRLTQPLI--KKGGKLVPVSWEEALKTVAEGLKAVKGDKIGGIAGPRADLESLFLLKKLLNKLGSNNI-DHRLRQS 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 189 EPTSVGLPQSIGIgkGTVSLDDFDSAELVISIGHNPGTNHPRMMGTLHELARK-KVPIIVFNPLreralerftdPQNVIE 267
Cdd:cd02768 126 DLPADNRLRGNYL--FNTSIAEIEEADAVLLIGSNLRKEAPLLNARLRKAVKKkGAKIAVIGPK----------DTDLIA 193
|
170 180 190
....*....|....*....|....*....|....
gi 1778700535 268 MATYSSTPIASTYYQVKAGGDAAALKGIAKALLQ 301
Cdd:cd02768 194 DLTYPVSPLGASLATLLDIAEGKHLKPFAKSLKK 227
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
114-489 |
7.18e-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: 84.28 E-value: 7.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 114 RLTTPL--FYDAGTDTLRPLAWDEAFQRIAAVLQTLP----PEQVEFY-TSGRASNEAAYLFQL-FAREFGSNNFPDCSN 185
Cdd:cd02759 54 RLLYPLkrVGERGENKWERISWDEALDEIAEKLAEIKaeygPESIATAvGTGRGTMWQDSLFWIrFVRLFGSPNLFLSGE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 186 MCHEPTSVGLPQSIGIGkGTVSLDDFDSAELVISIGHNPG-TNHPRMMGTLHELARKKVPIIVFNPLRERALERftdpqn 264
Cdd:cd02759 134 SCYWPRDMAHALTTGFG-LGYDEPDWENPECIVLWGKNPLnSNLDLQGHWLVAAMKRGAKLIVVDPRLTWLAAR------ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 265 viematysstpiASTYYQVKAGGDAAALKGIAKALLQLDdehgnALDHAFIAEHTEGFTAFDADLRATHWEAIEAESGLT 344
Cdd:cd02759 207 ------------ADLWLPIRPGTDAALALGMLNVIINEG-----LYDKDFVENWCYGFEELAERVQEYTPEKVAEITGVP 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 345 RQDLEQVAAAYAKSNATIVTYGMGITQHNKGTANVRLIADLLLLRGNIGKPGAGIcplrghsnvqgnrtvgitekpsaef 424
Cdd:cd02759 270 AEKIRKAARLYATAKPACIQWGLAIDQQKNGTQTSRAIAILRAITGNLDVPGGNL------------------------- 324
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1778700535 425 lakletvfgFTPPKAhghdavkcmqamidgasKALICLGGNFAVALPDPEQSFPAMKALELSVHI 489
Cdd:cd02759 325 ---------LIPYPV-----------------KMLIVFGTNPLASYADTAPVLEALKALDFIVVV 363
|
|
| PRK13532 |
PRK13532 |
nitrate reductase catalytic subunit NapA; |
112-459 |
4.61e-14 |
|
nitrate reductase catalytic subunit NapA;
Pssm-ID: 237416 [Multi-domain] Cd Length: 830 Bit Score: 76.09 E-value: 4.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 112 YG--RLTTPLF------YDAGTDtLRPLAWDEAF----QRIAAVLQTLPPEQVEFYTSGRASNEAAYLFQ-LFAREFGSN 178
Cdd:PRK13532 93 YGkdRLTQPLLrmkdgkYDKEGE-FTPVSWDQAFdvmaEKFKKALKEKGPTAVGMFGSGQWTIWEGYAASkLMKAGFRSN 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 179 NFPDCSNMCHEPTSVGLPQSIGIGKGTVSLDDFDSAELVISIGHNPGTNHPrmmgtlhelarkkvpiIVFNPLRERaleR 258
Cdd:PRK13532 172 NIDPNARHCMASAVVGFMRTFGIDEPMGCYDDIEAADAFVLWGSNMAEMHP----------------ILWSRVTDR---R 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 259 FTDPQ-NVIEMATYS--STPIASTYYQVKAGGDAAALKGIAKALLQlddehGNALDHAFIAEHTEgFTAFDAD----LRA 331
Cdd:PRK13532 233 LSNPDvKVAVLSTFEhrSFELADNGIIFTPQTDLAILNYIANYIIQ-----NNAVNWDFVNKHTN-FRKGATDigygLRP 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 332 TH--------------WEAIEAE-----------------SGLTRQDLEQVAAAYAKSNATIVTY-GMGITQHNKGT-AN 378
Cdd:PRK13532 307 THplekaaknpgtagkSEPISFEefkkfvapytlektakmSGVPKEQLEQLAKLYADPNRKVVSFwTMGFNQHTRGVwAN 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 379 vRLIADLLLLRGNIGKPGAGICPLRGHSNVQGN-RTVG-------------------ITEKpsaefLAKLETvfGFTPPK 438
Cdd:PRK13532 387 -NLVYNIHLLTGKISTPGNGPFSLTGQPSACGTaREVGtfshrlpadmvvtnpkhreIAEK-----IWKLPE--GTIPPK 458
|
410 420
....*....|....*....|.
gi 1778700535 439 AHGHdAVKCMQAMIDGASKAL 459
Cdd:PRK13532 459 PGYH-AVAQDRMLKDGKLNAY 478
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
108-487 |
2.04e-13 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 73.93 E-value: 2.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 108 QLEDYGRLTTPLFY--DAGTDTLRPLAWDEAFQRIAAVL----QTLPPEQVEFytSGRASNEAAYLFQlFAREFGSnnfP 181
Cdd:PRK15488 92 LLYDPQRIVKPLKRvgERGEGKWQEISWDEAYQEIAAKLnaikQQHGPESVAF--SSKSGSLSSHLFH-LATAFGS---P 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 182 DCsnMCHEPTSvglPQSIGI-GKGTVSLD---DFDSAELVISIGHN--PGTNHPRMMGTLHELARKKVPIIVFNPlrera 255
Cdd:PRK15488 166 NT--FTHASTC---PAGYAIaAKVMFGGKlkrDLANSKYIINFGHNlyEGINMSDTRGLMTAQMEKGAKLVVFEP----- 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 256 leRFTdpqnviemaTYSSTpiASTYYQVKAGGDAAALKGIAKALLqlddeHGNALDHAFIAEHTEGFTAFDADLRATHWE 335
Cdd:PRK15488 236 --RFS---------VVASK--ADEWHAIRPGTDLAVVLALCHVLI-----EENLYDKAFVERYTSGFEELAASVKEYTPE 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 336 AIEAESGLTRQDLEQVAAAYAK-SNATIVTYGMGITQHNKGTANVRLIADLLLLRGNIGKPGaGIcpLRGHSNVQGNRTV 414
Cdd:PRK15488 298 WAEAISDVPADDIRRIARELAAaAPHAIVDFGHRATFTPEEFDMRRAIFAANVLLGNIERKG-GL--YFGKNASVYNKLA 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 415 GITEKPSaefLAKLeTVFGFTPPKAHGHDAVK-----------CMQAMIDGASKALIC-LGG------NFAVALPDPEQS 476
Cdd:PRK15488 375 GEKVAPT---LAKP-GVKGMPKPTAKRIDLVGeqfkyiaagggVVQSIIDATLTQKPYqIKGwvmsrhNPMQTVTDRADV 450
|
410
....*....|.
gi 1778700535 477 FPAMKALELSV 487
Cdd:PRK15488 451 VKALKKLDLVV 461
|
|
| Molydop_binding |
pfam01568 |
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
642-749 |
3.51e-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: 66.53 E-value: 3.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 642 LRLITLRSHDQYNTTIYALDDRYRGVFgRRDVLFMNDSDLQRLGLEHGDVVDLETAlpgsTQRLEGITVIAYNISAGSVG 721
Cdd:pfam01568 1 LYLITGRVLGQYHSQTRTRRVLRLAKP-EPEVVEIHPEDAAALGIKDGDLVEVTSR----RGSVVVRAKVTDRVRPGVVF 75
|
90 100 110
....*....|....*....|....*....|....*.
gi 1778700535 722 AYYPE--------ANVLVPLHyIDEESGTPSYKSVP 749
Cdd:pfam01568 76 MPFGWwyeprggnANALTDDA-TDPLSGGPEFKTCA 110
|
|
| MopB_2 |
cd02763 |
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
114-396 |
9.00e-13 |
|
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: 71.79 E-value: 9.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 114 RLTTPLFY--DAGTDTLRPLAWDEAF----QRIAAVLQTlPPEQVEFYTsGRASNEAayLFQLFAREFGSNNFPDCSNMC 187
Cdd:cd02763 54 RLTKPLLRkgPRGSGQFEEIEWEEAFsiatKRLKAARAT-DPKKFAFFT-GRDQMQA--LTGWFAGQFGTPNYAAHGGFC 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 188 HEPTSVGLPQSIGIGKGTVSLDDFDSAELVISIGHNPGTNHPRMMGTLHELARKKVPIIVFNPLReralerftdpqnvie 267
Cdd:cd02763 130 SVNMAAGGLYSIGGSFWEFGGPDLEHTKYFMMIGVAEDHHSNPFKIGIQKLKRRGGKFVAVNPVR--------------- 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 268 matYSSTPIASTYYQVKAGGDAAALKGIAKALLQlddehGNALDHAFIAEHTEGftafdADLRATHWEAIEAESGLTRQD 347
Cdd:cd02763 195 ---TGYAAIADEWVPIKPGTDGAFILALAHELLK-----AGLIDWEFLKRYTNA-----AELVDYTPEWVEKITGIPADT 261
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1778700535 348 LEQVAA-------------------AYAKSNATIVT-----YGM-GITQHNKGTANVRLIADLLLLRGNIGKPG 396
Cdd:cd02763 262 IRRIAKelgvtardqpielpiawtdVWGRKHEKITGrpvsfHAMrGIAAHSNGFQTIRALFVLMMLLGTIDRPG 335
|
|
| 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 |
2.14e-12 |
|
MopB_NDH-1_NuoG2-N7: The second domain of the NuoG subunit (with a [4Fe-4S] cluster, N7) of the NADH-quinone oxidoreductase/NADH dehydrogenase-1 (NDH-1) found in various bacteria. The NDH-1 is the first energy-transducting complex in the respiratory chain and functions as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. In Escherichia coli NDH-1, the largest subunit is encoded by the nuoG gene, and is part of the 14 distinct subunits constituting the functional enzyme. The NuoG subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Unique to this group, compared to the other prokaryotic and eukaryotic groups in this domain protein family (NADH-Q-OR-NuoG2), is an N-terminal [4Fe-4S] cluster (N7/N1c) present in the second domain. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain belongs to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239172 [Multi-domain] Cd Length: 472 Bit Score: 70.11 E-value: 2.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 114 RLTTPLFydAGTDTLRPLAWDEAFQRIAAVLQTLPpEQVEFYTSGRASNEAAYLFQLFAREF-GSNNFpDCSNMCHepts 192
Cdd:cd02771 54 RLTQPLI--RRGGTLVPVSWNEALDVAAARLKEAK-DKVGGIGSPRASNESNYALQKLVGAVlGTNNV-DHRARRL---- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 193 vgLPQSIGIGKG-TVSLDDFDSAELVISIGHNPGTNHPRMMGTLHELARKKVPII-----VFNPLRERALERFTDPQN-- 264
Cdd:cd02771 126 --IAEILRNGPIyIPSLRDIESADAVLVLGEDLTQTAPRIALALRQAARRKAVELaalsgIPKWQDAAVRNIAQGAKSpl 203
|
170 180 190
....*....|....*....|....*....|....*.
gi 1778700535 265 -VIEMATYSSTPIASTYYQVKAGGDAAALKGIAKAL 299
Cdd:cd02771 204 fIVNALATRLDDIAAESIRASPGGQARLGAALARAV 239
|
|
| MopB_CT |
cd02775 |
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a ... |
649-746 |
4.93e-11 |
|
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: 60.03 E-value: 4.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 649 SHDQYNTTIYALDDRYRGVFgRRDVLFMNDSDLQRLGLEHGDVVDLETAlpgsTQRLEGITVIAYNISAGSVGAYYP--- 725
Cdd:cd02775 1 LRDHFHSGTRTRNPWLRELA-PEPVVEINPEDAAALGIKDGDLVRVESR----RGSVVLRAKVTDGVPPGVVFLPHGwgh 75
|
90 100
....*....|....*....|....*..
gi 1778700535 726 ------EANVLVPLHYiDEESGTPSYK 746
Cdd:cd02775 76 rggrggNANVLTPDAL-DPPSGGPAYK 101
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
193-412 |
1.35e-10 |
|
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: 64.56 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 193 VGLPQSIG---IGKGTVSLDD-FDSAELVISIGHNPGTNhpRM---MGTLH-------ELARKKVPIIVFNPLRERALER 258
Cdd:cd02751 145 VILPHVVGsdeVYEQGTSWDDiAEHSDLVVLFGANPLKT--RQgggGGPDHgsyyylkQAKDAGVRFICIDPRYTDTAAV 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 259 FTDPQNVIEMATysstpiastyyqvkaggDAAALKGIAKALLqldDEhgNALDHAFIAEHTEGFTAFDADLRAT------ 332
Cdd:cd02751 223 LAAEWIPIRPGT-----------------DVALMLAMAHTLI---TE--DLHDQAFLARYTVGFDEFKDYLLGEsdgvpk 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 333 --HWEaiEAESGLTRQDLEQVAAAYAKSNATIVTyGMGITQHNKGTANVRLIADLLLLRGNIGKPGAGICPLRGHSNVQG 410
Cdd:cd02751 281 tpEWA--AEITGVPAETIRALAREIASKRTMIAQ-GWGLQRAHHGEQPAWMLVTLAAMLGQIGLPGGGFGFGYGYSNGGG 357
|
..
gi 1778700535 411 NR 412
Cdd:cd02751 358 PP 359
|
|
| MopB_Nitrate-R-NarG-like |
cd02750 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
271-399 |
2.10e-07 |
|
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: 54.25 E-value: 2.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 271 YS-STPIASTYYQVKAGGDAAALKGIAKALLQlddehGNALDHAFIAEHTE-GFTAFDAdlrathwEAIEAESGLTRQDL 348
Cdd:cd02750 209 YSpSAKHADLWVPIKPGTDAALALAMAHVIIK-----EKLYDEDYLKEYTDlPFLVYTP-------AWQEAITGVPRETV 276
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1778700535 349 EQVAAAYAKSNATIVTYGMGITQHNKGTANVRLIADLLLLRGNIGKPGAGI 399
Cdd:cd02750 277 IRLAREFATNGRSMIIVGAGINHWYHGDLCYRALILLLALTGNEGKNGGGW 327
|
|
| MopB_Arsenite-Ox |
cd02756 |
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the ... |
114-405 |
1.79e-06 |
|
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: 51.33 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 114 RLTTPLFYDAGTdtLRPLAWDEAFQRIAAVLQTL-----PPEQVEFYTS-------GRASNEAA--YLFQLFAREFGS-N 178
Cdd:cd02756 117 RLTTPLVRRGGQ--LQPTTWDDAIDLVARVIKGIldkdgNDDAVFASRFdhgggggGFENNWGVgkFFFMALQTPFVRiH 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 179 NFPDCSNMCHEPtsvglpQSIGIGKGTVSLDDFDSAELVISIGHNP---GTNH------PRMMGTlhELARKK------- 242
Cdd:cd02756 195 NRPAYNSEVHAT------REMGVGELNNSYEDARLADTIVLWGNNPyetQTVYflnhwlPNLRGA--TVSEKQqwfppge 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 243 -VP---IIVFNPLRE---RALERFTDPQNVIEMatysstpiastyyQVKAGGDAAALKGIAKALLQLDDEhgnaldhaFI 315
Cdd:cd02756 267 pVPpgrIIVVDPRRTetvHAAEAAAGKDRVLHL-------------QVNPGTDTALANAIARYIYESLDE--------VL 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 316 AEhTEGFTAFDADL--RATHWEAIEAESGLTRQdleqvaaayaksnaTIVTYGMGITQHNKGTANVRLIADLLLLRGNIG 393
Cdd:cd02756 326 AE-AEQITGVPRAQieKAADWIAKPKEGGYRKR--------------VMFEYEKGIIWGNDNYRPIYSLVNLAIITGNIG 390
|
330
....*....|..
gi 1778700535 394 KPGAGICPLRGH 405
Cdd:cd02756 391 RPGTGCVRQGGH 402
|
|
| MopB_Res-Cmplx1_Nad11 |
cd02773 |
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone ... |
112-224 |
9.66e-05 |
|
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone oxidoreductase/respiratory complex I/NADH dehydrogenase-1(NDH-1) of eukaryotes and the Nqo3/G subunit of alphaproteobacteria NDH-1. The NADH-quinone oxidoreductase is the first energy-transducting complex in the respiratory chains of many prokaryotes and eukaryotes. Mitochondrial complex I and its bacterial counterpart, NDH-1, function as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. The nad11 gene codes for the largest (75 kDa) subunit of the mitochondrial NADH:ubiquinone oxidoreductase, it constitutes the electron input part of the enzyme, or the so-called NADH dehydrogenase fragment. In Paracoccus denitrificans, this subunit is encoded by the nqo3 gene, and is part of the 14 distinct subunits constituting the 'minimal' functional enzyme. The Nad11/Nqo3 subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain belongs to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239174 [Multi-domain] Cd Length: 375 Bit Score: 45.33 E-value: 9.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 112 YGRLTTPlfYDAGTDTLRPLAWDEAFQRIAAVLQTLPPEQVEFYTSGRASNEAAYLFQLFAREFGSNnfpdcsNMCHEPT 191
Cdd:cd02773 51 RQRLDKP--YIRKNGKLKPATWEEALAAIAKALKGVKPDEIAAIAGDLADVESMVALKDLLNKLGSE------NLACEQD 122
|
90 100 110
....*....|....*....|....*....|....
gi 1778700535 192 SVGLPQSIGIGK-GTVSLDDFDSAELVISIGHNP 224
Cdd:cd02773 123 GPDLPADLRSNYlFNTTIAGIEEADAVLLVGTNP 156
|
|
| PRK07860 |
PRK07860 |
NADH dehydrogenase subunit G; Validated |
114-304 |
2.66e-04 |
|
NADH dehydrogenase subunit G; Validated
Pssm-ID: 236118 [Multi-domain] Cd Length: 797 Bit Score: 44.55 E-value: 2.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 114 RLTTPLFYDAgTDTLRPLAWDEAFQRIAAVLQTlPPEQVEFYTSGRASNEAAYLFQLFAR-EFGSNNFpDCSNMCHEPTS 192
Cdd:PRK07860 278 RITTPLVRDE-DGELEPASWSEALAVAARGLAA-ARGRVGVLVGGRLTVEDAYAYAKFARvALGTNDI-DFRARPHSAEE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 193 VGLPQSIGIGKG-TVSLDDFDSAELVISIGHNPGTNHPrmmgtlhelarkkvpiIVFNPLRERALERFTDPQNVIEMATY 271
Cdd:PRK07860 355 ADFLAARVAGRGlGVTYADLEKAPAVLLVGFEPEEESP----------------IVFLRLRKAARKHGLKVYSIAPFATR 418
|
170 180 190
....*....|....*....|....*....|...
gi 1778700535 272 SSTPIASTYYQVKAGGDAAALKGIAKALLQLDD 304
Cdd:PRK07860 419 GLEKMGGTLLRTAPGGEAAALDALATGAPDVAE 451
|
|
| MopB_CT_Fdh-Nap-like |
cd00508 |
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and ... |
642-752 |
9.16e-04 |
|
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: 39.80 E-value: 9.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 642 LRLITLRSHDQYNT-----TIYALDDRYRGVFgrrdvLFMNDSDLQRLGLEHGDVVDLETAlPGS-------TQRLEGIT 709
Cdd:cd00508 5 LVLTTGRLLEHWHTgtmtrRSPRLAALAPEPF-----VEIHPEDAARLGIKDGDLVRVSSR-RGSvvvrarvTDRVRPGT 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1778700535 710 V-IAYNISAGSVGAyypEANVLVPLHYiDEESGTPSYKSVPIRV 752
Cdd:cd00508 79 VfMPFHWGGEVSGG---AANALTNDAL-DPVSGQPEFKACAVRI 118
|
|
| MopB_DMSOR-BSOR-TMAOR |
cd02769 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
215-399 |
1.11e-03 |
|
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide reductase (BSOR), trimethylamine N-oxide reductase (TMAOR) and other related proteins. DMSOR always catalyzes the reduction of DMSO to dimethylsulfide, but its cellular location and oligomerization state are organism-dependent. For example, in Rhodobacter sphaeriodes and Rhodobacter capsulatus, it is an 82-kDa monomeric soluble protein found in the periplasmic space; in E. coli, it is membrane-bound and exists as a heterotrimer. BSOR catalyzes the reduction of biotin sulfixode to biotin, and is unique among Mo enzymes because no additional auxiliary proteins or cofactors are required. TMAOR is similar to DMSOR, but its only natural substrate is TMAO. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239170 [Multi-domain] Cd Length: 609 Bit Score: 42.25 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 215 ELVISIGHNP---------GTNHPRMMGTLHELARKKVPIIVFNPLRERALERFtdpqnviematysstpiASTYYQVKA 285
Cdd:cd02769 172 ELVVAFGADPlknaqiawgGIPDHQAYSYLKALKDRGIRFISISPLRDDTAAEL-----------------GAEWIAIRP 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 286 GGDAAALKGIAKALLqLDDEHgnalDHAFIAEHTEGFTAFDADLRAT--------HW-EAIeaeSGLTRQDLEQVAAAYA 356
Cdd:cd02769 235 GTDVALMLALAHTLV-TEGLH----DKAFLARYTVGFDKFLPYLLGEsdgvpktpEWaAAI---CGIPAETIRELARRFA 306
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1778700535 357 kSNATIVTYGMGITQHNKGTANVRLIADLLLLRGNIGKPGAGI 399
Cdd:cd02769 307 -SKRTMIMAGWSLQRAHHGEQPHWMAVTLAAMLGQIGLPGGGF 348
|
|
| MopB_CT_1 |
cd02782 |
The MopB_CT_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
642-752 |
6.88e-03 |
|
The MopB_CT_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239183 [Multi-domain] Cd Length: 129 Bit Score: 37.37 E-value: 6.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 642 LRLITLRSHDQYNTTIYAlDDRYRGVfGRRDVLFMNDSDLQRLGLEHGDVVDLETA--------------------LP-G 700
Cdd:cd02782 5 LLLIGRRHLRSNNSWLHN-DPRLVKG-RNRCTLRIHPDDAAALGLADGDKVRVTSAagsveaevevtddmmpgvvsLPhG 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1778700535 701 STQRLEGITViaynisAGSVgaYYPEANVLVPLHYIDEESGTPSYKSVPIRV 752
Cdd:cd02782 83 WGHDYPGVSG------AGSR--PGVNVNDLTDDTQRDPLSGNAAHNGVPVRL 126
|
|
| MopB_CT_Acetylene-hydratase |
cd02781 |
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related ... |
673-752 |
8.65e-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: 37.29 E-value: 8.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778700535 673 VLFMNDSDLQRLGLEHGDVVDLETALPGSTQRLEGITVIAYNISAGSVGAYYPE---------------ANVLVPLHYID 737
Cdd:cd02781 34 VAEINPETAAKLGIADGDWVWVETPRGRARQKARLTPGIRPGVVRAEHGWWYPEreagepalggvwesnANALTSDDWND 113
|
90
....*....|....*
gi 1778700535 738 EESGTPSYKSVPIRV 752
Cdd:cd02781 114 PVSGSSPLRSMLCKI 128
|
|
| |
