|
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: 974.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 17 PAGGWGALKATAIAVRTQMDAFEAPATLLRTNQPDGFDCPGCAWPDK-EHKSTFQFCENGAKAVTWEATTKRVTPAFLAA 95
Cdd:TIGR01701 1 DAGGWGAVKSVALGKVKPMHIRQTLKLLLTLNKPEGYDCPGCAWGVSpQTLAGLEFCENGAKAIAWETTPRTIDPEFFAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 96 NTVSSLLAKSDFELEGYGRLTHPLVYDRDSDTLRPVAWEQAFARIGKILRGLQPDEVEFYTSGRASNEAAWLFQLFAREY 175
Cdd:TIGR01701 81 HSVSELRTLDSHELEKLGRLTYPLSLRPGSDHYTPISWDDAYQEIAAKLNSLDPKQVAFYTSGRTSNEAAYLYQLFARSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 176 GTNNFPDCSNMCHESTSVGLPQSIGIGKGTVSLDDFDQTELVISIGHNPGTNHPRMMGTLHELSRRGVPIIVFNPLRERA 255
Cdd:TIGR01701 161 GSNNLPDCSNMCHEPSSVALKRSIGIGKGSVNLEDFEHTDCLVFIGSNAGTNHPRMLKYLYAAKKRGAKIIAINPLRERG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 256 LERFADPQNVMEMATRRSTPIASTYYQVRAGGDAAALKGIAKALLQLEEEQ-GNVLDHAFIAQHTQGFTAFADDLHATRW 334
Cdd:TIGR01701 241 LERFWIPQIPESMLTGGGTQISSEYYQVRIGGDIALFNGVMKLLIEAEDAQpGSLIDHEFIANHTNGFDELRRHVLQLNW 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 335 QDIEQESGLTRESLTQVAAAYAKSRATIVTYGMGITQHNKGTSNVRLIADLLLMRGNIGKPGAGICPLRGHSNVQGNRTV 414
Cdd:TIGR01701 321 NDIERSSGLSQEEILEFAKLLANSRRVVFCWAMGLTQHAHGVDNISQVANLALLRGNIGKPGAGVCPIRGHSNVQGDRTM 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 415 GISEKPSAAFLDSLQRVMGITPPRHHGHDAVKALEAMIAGEAKALICLGGNFAVAMPDHERAFPAMRGLELSVHVGTKLN 494
Cdd:TIGR01701 401 GITEKPEEEFLARLSQIYGFTPPDWPGDTTVAMIEAILTGKVRAFICLGGNFLEAMPDTAAIERALRQLDLRVHVATKLN 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 495 RSHLLTAKETFILPCLGRTELDLQASGRQSITVEDSMSMVHASSGKLKPASPMLRSEPAIVAGLAKATLPASKVDWQYLV 574
Cdd:TIGR01701 481 RSHVLAKEEALILPVLGRYEQDGQGTGKQAVSVESSMRMVHFSRGILKPRGAELRSEWAIIAEIAKALLPETPVAWEILV 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 575 EDYDRIRDLIEQTIPGFEDYNQRIRHPGGFRMPLPP-TERIWPTATGKAMFSVFKGVHENVVVEGEDVMRLVTLRSHDQY 653
Cdd:TIGR01701 561 DTYDQIRDAIAATNPGYDDINHRKRRPDGFQLPGAAlCERKFPTPDGKANFIVIPLPEFRVPTGHEFELVLVTLRSHDQF 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 654 NTTIYAMDDRYRGVFGRRDVLFMNEQDMAAQGLEHGDRVDIHTALP-GSALTLEDITVVAYGIAPGTVGAYYPEANVLVP 732
Cdd:TIGR01701 641 NTTIYGEDDRYRGVDGHRRVVFMNETDIKKLGLRNGERVDVYNQYGdGQKRKFDNLRIVFYDTPTGNAAAYYPEANPLLP 720
|
730 740
....*....|....*....|.
gi 523681045 733 LNYLDEESGTPSYKSVPVRLT 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: 937.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 9 PGVHPYDGPAGGWGALKATAIAVRTQMDAFEAPATLLRTNQPDGFDCPGCAWPDKEHKSTFQFCENGAKAVTWEATTKRV 88
Cdd:PRK09939 3 KKIESYQGAAGGWGAVKSVANAVRKQMDIRQDVIAMFDMNKPEGFDCPGCAWPDPKHSASFDICENGAKAIAWEVTDKQV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 89 TPAFLAANTVSSLLAKSDFELEGYGRLTHPLVYDRDSDTLRPVAWEQAFARIGKILRGLQ-PDEVEFYTSGRASNEAAWL 167
Cdd:PRK09939 83 NASFFAENTVQSLLTWGDHELEAAGRLTQPLKYDAVSDCYKPLSWQQAFDEIGARLQSYSdPNQVEFYTSGRTSNEAAFL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 168 FQLFAREYGTNNFPDCSNMCHESTSVGLPQSIGIGKGTVSLDDFDQTELVISIGHNPGTNHPRMMGTLHELSRRGVPIIV 247
Cdd:PRK09939 163 YQLFAREYGSNNFPDCSNMCHEPTSVGLAASIGVGKGTVLLEDFEKCDLVICIGHNPGTNHPRMLTSLRALVKRGAKMIA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 248 FNPLRERALERFADPQNVMEMATRRSTPIASTYYQVRAGGDAAALKGIAKALLQLEEE-----QGNVLDHAFIAQHTQGF 322
Cdd:PRK09939 243 INPLQERGLERFTAPQNPFEMLTNSETQLASAYYNVRIGGDMALLKGMMRLLIERDDAasaagRPSLLDDEFIQTHTVGF 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 323 TAFADDLHATRWQDIEQESGLTRESLTQVAAAYAKSRATIVTYGMGITQHNKGTSNVRLIADLLLMRGNIGKPGAGICPL 402
Cdd:PRK09939 323 DELRRDVLNSEWKDIERISGLSQTQIAELADAYAAAERTIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGICPL 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 403 RGHSNVQGNRTVGISEKPSAAFLDSLQRVMGITPPRHHGHDAVKALEAMIAGEAKALICLGGNFAVAMPDHERAFPAMRG 482
Cdd:PRK09939 403 RGHSNVQGDRTVGITEKPSAEFLARLGERYGFTPPHAPGHAAIASMQAICTGQARALICMGGNFALAMPDREASAVPLTQ 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 483 LELSVHVGTKLNRSHLLTAKETFILPCLGRTELDLQASGRQSITVEDSMSMVHASSGKLKPASPMLRSEPAIVAGLAKAT 562
Cdd:PRK09939 483 LDLAVHVATKLNRSHLLTARHSYILPVLGRSEIDMQKSGAQAVTVEDSMSMIHASRGVLKPAGVMLKSECAVVAGIAQAA 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 563 LPASKVDWQYLVEDYDRIRDLIEQTIPGFEDYNQRIRHPGGFRMPLPPTERIWPTATGKAMFSVFKGVHENVVVEGEDVM 642
Cdd:PRK09939 563 LPQSVVAWEYLVEDYDRIRNDIEAVLPEFADYNQRIRHPGGFHLINAAAERRWMTPSGKANFITSKGLLEDPSSAFNSKL 642
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 643 RLVTLRSHDQYNTTIYAMDDRYRGVFGRRDVLFMNEQDMAAQGLEHGDRVDIHTALPG---SALTLEDITVVAYGIAPGT 719
Cdd:PRK09939 643 VMATVRSHDQYNTTIYGMDDRYRGVFGQRDVVFMSAKQAKICRVKNGERVNLIALTPDgkrSSRRMDRLKVVIYPMADRS 722
|
730 740 750
....*....|....*....|....*....|...
gi 523681045 720 VGAYYPEANVLVPLNYLDEESGTPSYKSVPVRL 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: 922.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 52 GFDCPGCAWPD-KEHKSTFQFCENGAKAVTWEATTKRVTPAFLAANTVSSLLAKSDFELEGYGRLTHPLVYDRDSDTLRP 130
Cdd:cd02767 1 GFDCPGCAWGDpGQKLHGFEFCENGAKALAWETTPKRVTPEFFALHSVSELRTWSDYELEHLGRLTYPMRYDAGSDHYRP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 131 VAWEQAFARIGKILRGLQPDEVEFYTSGRASNEAAWLFQLFAREYGTNNFPDCSNMCHESTSVGLPQSIGIGKGTVSLDD 210
Cdd:cd02767 81 ISWDEAFAEIAARLRALDPDRAAFYTSGRASNEAAYLYQLFARAYGTNNLPDCSNMCHEPSSVGLKKSIGVGKGTVSLED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 211 FDQTELVISIGHNPGTNHPRMMGTLHELSRRGVPIIVFNPLRERALERFADPQNVMEMATRrSTPIASTYYQVRAGGDAA 290
Cdd:cd02767 161 FEHTDLIFFIGQNPGTNHPRMLHYLREAKKRGGKIIVINPLREPGLERFANPQNPESMLTG-GTKIADEYFQVRIGGDIA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 291 ALKGIAKALLQLEEEQGNVLDHAFIAQHTQGFTAFADDLHATRWQDIEQESGLTRESLTQVAAAYAKSRATIVTYGMGIT 370
Cdd:cd02767 240 LLNGMAKHLIERDDEPGNVLDHDFIAEHTSGFEEYVAALRALSWDEIERASGLSREEIEAFAAMYAKSERVVFVWGMGIT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 371 QHNKGTSNVRLIADLLLMRGNIGKPGAGICPLRGHSNVQGNRTVGISEKPSAAFLDSLQRVMGITPPRHHGHDAVKALEA 450
Cdd:cd02767 320 QHAHGVDNVRAIVNLALLRGNIGRPGAGLMPIRGHSNVQGDRTMGITEKPFPEFLDALEEVFGFTPPRDPGLDTVEAIEA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 451 MIAGEAKALICLGGNFAVAMPDHERAFPAMRGLELSVHVGTKLNRSHLLTAKETFILPCLGRTELDLQASGRQSITVEDS 530
Cdd:cd02767 400 ALEGKVKAFISLGGNFAEAMPDPAATEEALRRLDLTVHVATKLNRSHLVHGEEALILPCLGRTEIDMQAGGAQAVTVEDS 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 531 MSMVHASSGKLKPASPMLRSEPAIVAGLAKATLPASKVDWQYLVEDYDRIRDLIEQTIP-GFEDYNQRIRHPGGFRMPLP 609
Cdd:cd02767 480 MSMTHTSRGRLKPASRVLLSEEAIVAGIAGARLGEAKPEWEILVEDYDRIRDEIAAVIYeGFADFNQRGDQPGGFHLPNG 559
|
570
....*....|....*
gi 523681045 610 PTERIWPTATGKAMF 624
Cdd:cd02767 560 ARERKFNTPSGKAQF 574
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
55-753 |
3.04e-166 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 495.52 E-value: 3.04e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 55 CPGCAWpdkehkstfqFCENGAKAVtwEATTKRVTPAflAANTVSSLL-----AKSDFELEGYGRLTHPLVYD--RDSDT 127
Cdd:COG0243 28 CPGCGV----------GCGLGVKVE--DGRVVRVRGD--PDHPVNRGRlcakgAALDERLYSPDRLTYPMKRVgpRGSGK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 128 LRPVAWEQAFARIGKILRGLQ----PDEVEFYTSG----RASNEAAWLFQLFAREYGTNNFPDCSNMCHESTSVGLPQSI 199
Cdd:COG0243 94 FERISWDEALDLIAEKLKAIIdeygPEAVAFYTSGgsagRLSNEAAYLAQRFARALGTNNLDDNSRLCHESAVAGLPRTF 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 200 GIGKGTVSLDDFDQTELVISIGHNPGTNHPRMMGTLHE-LSRRGVPIIVFNPLRERalerfadpqnvmematrrSTPIAS 278
Cdd:COG0243 174 GSDKGTVSYEDLEHADLIVLWGSNPAENHPRLLRRLREaAKKRGAKIVVIDPRRTE------------------TAAIAD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 279 TYYQVRAGGDAAALKGIAKALLQLeeeqgNVLDHAFIAQHTQGFTAFADDLHATRWQDIEQESGLTRESLTQVAAAYAKS 358
Cdd:COG0243 236 EWLPIRPGTDAALLLALAHVLIEE-----GLYDRDFLARHTVGFDELAAYVAAYTPEWAAEITGVPAEDIRELAREFATA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 359 RATIVTYGMGITQHNKGTSNVRLIADLLLMRGNIGKPGAGICPLRGhsnvqgnrtvgisekpsaafldslqrvmgitppr 438
Cdd:COG0243 311 KPAVILWGMGLQQHSNGTQTVRAIANLALLTGNIGKPGGGPFSLTG---------------------------------- 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 439 hhghdavkalEAMIAGE---AKALICLGGNFAVAMPDHERAFPAMRGLELSVHVGTKLNRSHLLTAketFILPCLGRTEl 515
Cdd:COG0243 357 ----------EAILDGKpypIKALWVYGGNPAVSAPDTNRVREALRKLDFVVVIDTFLTETARYAD---IVLPATTWLE- 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 516 dlqasgRQSITVEDSMSMVHASSGKLKPASpMLRSEPAIVAGLAKATLPASKVDWQYLVEDYdrIRDLIEQTIPG---FE 592
Cdd:COG0243 423 ------RDDIVTNSEDRRVHLSRPAVEPPG-EARSDWEIFAELAKRLGFEEAFPWGRTEEDY--LRELLEATRGRgitFE 493
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 593 DYNQRirhpGGFRMPLPP-----TERIWPTATGKAMFSVFKGVHENV-----------VVEGEDVMRLVTLRSHDQYNTT 656
Cdd:COG0243 494 ELREK----GPVQLPVPPepafrNDGPFPTPSGKAEFYSETLALPPLpryappyegaePLDAEYPLRLITGRSRDQWHST 569
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 657 IYAmDDRYRGVFGRRdVLFMNEQDMAAQGLEHGDRVDIHTALpGSALTledITVVAYGIAPGTV----GAYYPEA----- 727
Cdd:COG0243 570 TYN-NPRLREIGPRP-VVEINPEDAAALGIKDGDLVRVESDR-GEVLA---RAKVTEGIRPGVVfaphGWWYEPAddkgg 643
|
730 740
....*....|....*....|....*...
gi 523681045 728 --NVLVPlNYLDEESGTPSYKSVPVRLT 753
Cdd:COG0243 644 nvNVLTP-DATDPLSGTPAFKSVPVRVE 670
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
113-753 |
1.01e-104 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 336.09 E-value: 1.01e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 113 GRLTHPLVydRDSDTLRPVAWEQAFARIGKILRGLQ----PDEVEFYTSGRASNEAAWLFQLFAREY-GTNNFPDCSNMC 187
Cdd:COG3383 60 DRLTTPLI--RRGGEFREVSWDEALDLVAERLREIQaehgPDAVAFYGSGQLTNEENYLLQKLARGVlGTNNIDNNARLC 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 188 HESTSVGLPQSIGIGKGTVSLDDFDQTELVISIGHNPGTNHPRMMGTLHELSRRGVPIIVFNPlRERALERFADpqnvme 267
Cdd:COG3383 138 MASAVAGLKQSFGSDAPPNSYDDIEEADVILVIGSNPAEAHPVLARRIKKAKKNGAKLIVVDP-RRTETARLAD------ 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 268 matrrstpiasTYYQVRAGGDAAALKGIAKALLqleeEQGNVlDHAFIAQHTQGFTAFADDLHATRWQDIEQESGLTRES 347
Cdd:COG3383 211 -----------LHLQIKPGTDLALLNGLLHVII----EEGLV-DEDFIAERTEGFEELKASVAKYTPERVAEITGVPAED 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 348 LTQVAAAYAKSRATIVTYGMGITQHNKGTSNVRLIADLLLMRGNIGKPGAGICPLRGHSNVQGNRTVGIseKP------- 420
Cdd:COG3383 275 IREAARLIAEAKRAMILWGMGVNQHTQGTDNVNAIINLALATGNIGRPGTGPFPLTGQNNVQGGRDMGA--LPnvlpgyr 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 421 ---SAAFLDSLQRVMGITP-PRHHGHDAVKALEAMIAGEAKALICLGGNFAVAMPDHERAFPAMRGLELSVHVGTKLNRs 496
Cdd:COG3383 353 dvtDPEHRAKVADAWGVPPlPDKPGLTAVEMFDAIADGEIKALWIIGENPAVSDPDANHVREALEKLEFLVVQDIFLTE- 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 497 hllTAKE-TFILPCLGRTELDlqasGrqsiTVEDSMSMVHASSgKLKPASPMLRSEPAIVAGLAKATlpasKVDWQYlvE 575
Cdd:COG3383 432 ---TAEYaDVVLPAASWAEKD----G----TFTNTERRVQRVR-KAVEPPGEARPDWEIIAELARRL----GYGFDY--D 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 576 DYDRIRDLIEQTIPGFE--DYnQRIRHPGGFRMPLPP-----TERIW----PTATGKAMFSVFKGVHENVVVEGEDVMRL 644
Cdd:COG3383 494 SPEEVFDEIARLTPDYSgiSY-ERLEALGGVQWPCPSedhpgTPRLFtgrfPTPDGKARFVPVEYRPPAELPDEEYPLVL 572
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 645 VTLRSHDQYNTTiyAMDDRYRGVFGR--RDVLFMNEQDMAAQGLEHGDRVDIHTALpGSaltledITVVAY---GIAPGT 719
Cdd:COG3383 573 TTGRLLDQWHTG--TRTRRSPRLNKHapEPFVEIHPEDAARLGIKDGDLVRVSSRR-GE------VVLRARvtdRVRPGT 643
|
650 660 670
....*....|....*....|....*....|....*...
gi 523681045 720 VGAY--YPE--ANVLVPlNYLDEESGTPSYKSVPVRLT 753
Cdd:COG3383 644 VFMPfhWGEgaANALTN-DALDPVSKQPEYKACAVRVE 680
|
|
| Fdh-alpha |
TIGR01591 |
formate dehydrogenase, alpha subunit, archaeal-type; This model describes a subset of formate ... |
114-752 |
1.52e-80 |
|
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: 271.26 E-value: 1.52e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 114 RLTHPLVydRDSDTLRPVAWEQAFARIGKILRGLQ----PDEVEFYTSGRASNEAAWLFQLFARE-YGTNNFPDCSNMCH 188
Cdd:TIGR01591 53 RLTTPLI--REGDKFREVSWDEAISYIAEKLKEIKekygPDSIGFIGSSRGTNEENYLLQKLARAvIGTNNVDNCARVCH 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 189 ESTSVGLPQSIGIGKGTVSLDDFDQTELVISIGHNPGTNHPRMMGTLHELSRRGVPIIVFNPlRERALERFADpqnvmem 268
Cdd:TIGR01591 131 GPSVAGLKQTVGIGAMSNTISEIENADLIVIIGYNPAESHPVVAQYLKNAKRNGAKIIVIDP-RKTETAKIAD------- 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 269 atrrstpiasTYYQVRAGGDAAALKGIAKALLqleeEQGnVLDHAFIAQHTQGFTAFADDLHATRWQDIEQESGLTRESL 348
Cdd:TIGR01591 203 ----------LHIPLKPGTDIALLNAMANVII----EEG-LYDKAFIEKRTEGFEEFREIVKGYTPEYVEDITGVPADLI 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 349 TQVAAAYAKSRATIVTYGMGITQHNKGTSNVRLIADLLLMRGNIGKPGAGICPLRGHSNVQGNRTVG-ISEKPSA----- 422
Cdd:TIGR01591 268 REAARMYAKAGSAAILWGMGVTQHSQGVETVMALINLAMLTGNIGKPGGGVNPLRGQNNVQGACDMGaLPDFLPGyqpvs 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 423 --AFLDSLQRVMGITP-PRHHGHDAVKALEAMIAGEAKALICLGGNFAVAMPDHERAFPAMRGLELSVHVGTKLNRshll 499
Cdd:TIGR01591 348 deEVREKFAKAWGVVKlPAEPGLRIPEMIDAAADGDVKALYIMGEDPLQSDPNTSKVRKALEKLELLVVQDIFMTE---- 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 500 TAKET-FILP--CLGRTELDLQASGRQsitvedsMSMVHassgklKPASPMLRSEP--AIVAGLAKATlpasKVDWQYlv 574
Cdd:TIGR01591 424 TAKYAdVVLPaaAWLEKEGTFTNAERR-------IQRFF------KAVEPKGESKPdwEIIQELANAL----GLDWNY-- 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 575 EDYDRIRDLIEQTIPGFEDYN-QRIRHPGGFRMPLPP----------TERiWPTATGKAMFSVFKGVHENVVVEGEDVMR 643
Cdd:TIGR01591 485 NHPQEIMDEIRELTPLFAGLTyERLDELGSLQWPCNDsdasptsylyKDK-FATPDGKAKFIPLEWVAPIEEPDDEYPLI 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 644 LVTLRSHDQYNTTiyAMDDRYRGVfgRRDV----LFMNEQDMAAQGLEHGDRVDIHTALpGSALTLEDIT-VVAYGIAPG 718
Cdd:TIGR01591 564 LTTGRVLTHYNVG--EMTRRVAGL--RRLSpepyVEINTEDAKKLGIKDGDLVKVKSRR-GEITLRAKVSdRVNKGAIYI 638
|
650 660 670
....*....|....*....|....*....|....
gi 523681045 719 TVGAYYPEANVLVPLNyLDEESGTPSYKSVPVRL 752
Cdd:TIGR01591 639 TMHFWDGAVNNLTTDD-LDPISGTPEYKYTAVRI 671
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
114-487 |
2.73e-71 |
|
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 with the release of a proton and two electrons. It is a component of the anaerobic formate hydrogen lyase complex. The E. coli formate dehydrogenase H (Fdh-H) is a monomer composed of a single polypeptide chain with a Mo active site region and a [4Fe-4S] center. Members of the MopB_Formate-Dh-H CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239154 [Multi-domain] Cd Length: 512 Bit Score: 242.12 E-value: 2.73e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 114 RLTHPLVydRDSDTLRPVAWEQAFARIGKILRGLQ----PDEVEFYTSGRASNEAAWLFQLFARE-YGTNNFPDCSNMCH 188
Cdd:cd02753 54 RLTKPLI--RKNGKFVEASWDEALSLVASRLKEIKdkygPDAIAFFGSAKCTNEENYLFQKLARAvGGTNNVDHCARLCH 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 189 ESTSVGLPQSIGIGKGTVSLDDFDQTELVISIGHNPGTNHPRMMGTLHELSRRGVPIIVFNPlRERALERFADpqnvmem 268
Cdd:cd02753 132 SPTVAGLAETLGSGAMTNSIADIEEADVILVIGSNTTEAHPVIARRIKRAKRNGAKLIVADP-RRTELARFAD------- 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 269 atrrstpiasTYYQVRAGGDAAALKGIAKALLqleeEQGNVlDHAFIAQHTQGFTAFADDLHATRWQDIEQESGLTRESL 348
Cdd:cd02753 204 ----------LHLQLRPGTDVALLNAMAHVII----EEGLY-DEEFIEERTEGFEELKEIVEKYTPEYAERITGVPAEDI 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 349 TQVAAAYAKSRATIVTYGMGITQHNKGTSNVRLIADLLLMRGNIGKPGAGICPLRGHSNVQGNRTVGisekpsaafldsl 428
Cdd:cd02753 269 REAARMYATAKSAAILWGMGVTQHSHGTDNVMALSNLALLTGNIGRPGTGVNPLRGQNNVQGACDMG------------- 335
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 523681045 429 qrvmgitpprhhghdavkALEAMIAGEAKALICLGGNFAVAMPDHERAFPAMRGLELSV 487
Cdd:cd02753 336 ------------------ALPNVLPGYVKALYIMGENPALSDPNTNHVRKALESLEFLV 376
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
66-561 |
7.29e-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: 209.88 E-value: 7.29e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 66 KSTFQFCENGA--KAVTWEATTKRVTPAFLAANTVSSLLAKSDFELEG---YGRLTHPLVYDRDSDTLRPVAWEQAFARI 140
Cdd:cd00368 1 PSVCPFCGVGCgiLVYVKDGKVVRIEGDPNHPVNEGRLCDKGRAGLDGlysPDRLKYPLIRVGGRGKFVPISWDEALDEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 141 GKILRGLQ----PDEVEFYTSGRASNEAAWLFQLFAREYGTNNFPDCSNMCHESTSVGLPQsIGIGKGTVSLDDFDQTEL 216
Cdd:cd00368 81 AEKLKEIRekygPDAIAFYGGGGASNEEAYLLQKLLRALGSNNVDSHARLCHASAVAALKA-FGGGAPTNTLADIENADL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 217 VISIGHNPGTNHPRMMGTLHELSRRGVPIIVFNPLREralerfadpqnvmematrRSTPIASTYYQVRAGGDAAALKGia 296
Cdd:cd00368 160 ILLWGSNPAETHPVLAARLRRAKKRGAKLIVIDPRRT------------------ETAAKADEWLPIRPGTDAALALA-- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 297 kallqleeeqgnvldhafiaqhtqgftafaddlhatrwQDIEQESGLTRESLTQVAAAYAKSRATIVTYGMGITQHNKGT 376
Cdd:cd00368 220 --------------------------------------EWAAEITGVPAETIRALAREFAAAKRAVILWGMGLTQHTNGT 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 377 SNVRLIADLLLMRGNIGKPGAGICPlrghsnvqgnrtvgisekpsaafldslqrvmgitpprhhghdavkaleamiagea 456
Cdd:cd00368 262 QNVRAIANLAALTGNIGRPGGGLGP------------------------------------------------------- 286
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 457 kaliclGGNFAVAMPDHERAFPAMRGLELSVHVGTKLNRSHLLtakETFILPCLGRTEldlqASGrqsiTVEDSMSMVHA 536
Cdd:cd00368 287 ------GGNPLVSAPDANRVRAALKKLDFVVVIDIFMTETAAY---ADVVLPAATYLE----KEG----TYTNTEGRVQL 349
|
490 500
....*....|....*....|....*..
gi 523681045 537 SSgklKPASPM--LRSEPAIVAGLAKA 561
Cdd:cd00368 350 FR---QAVEPPgeARSDWEILRELAKR 373
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
113-487 |
4.35e-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: 210.16 E-value: 4.35e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 113 GRLTHPLVyDRDSDTLRPVAWEQAFARIGKILRGLQ----PDEVEFYTSGRASNEAAWLFQLFAREY-GTNNFPDCSNMC 187
Cdd:cd02754 53 ERLTRPLL-RRNGGELVPVSWDEALDLIAERFKAIQaeygPDSVAFYGSGQLLTEEYYAANKLAKGGlGTNNIDTNSRLC 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 188 HESTSVGLPQSIGIGKGTVSLDDFDQTELVISIGHNPGTNHPRMMGTLHE--LSRRGVPIIVFNPLRERalerfadpqnv 265
Cdd:cd02754 132 MASAVAGYKRSFGADGPPGSYDDIEHADCFFLIGSNMAECHPILFRRLLDrkKANPGAKIIVVDPRRTR----------- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 266 mematrrSTPIASTYYQVRAGGDAAALKGIAKALLqlEEEQgnvLDHAFIAQHTQGFTAFADDLHATRWQDIEQESGLTR 345
Cdd:cd02754 201 -------TADIADLHLPIRPGTDLALLNGLLHVLI--EEGL---IDRDFIDAHTEGFEELKAFVADYTPEKVAEITGVPE 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 346 ESLTQVAAAYAKSRATIVTYGMGITQHNKGTSNVRLIADLLLMRGNIGKPGAGICPLRGHSNVQGNRTVG---------- 415
Cdd:cd02754 269 ADIREAARLFGEARKVMSLWTMGVNQSTQGTAANNAIINLHLATGKIGRPGSGPFSLTGQPNAMGGREVGglanllpghr 348
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 523681045 416 -ISEKPSAAFLDSLQRVMGITPPRHHGHDAVKALEAMIAGEAKALICLGGNFAVAMPDHERAFPAMRGLELSV 487
Cdd:cd02754 349 sVNNPEHRAEVAKFWGVPEGTIPPKPGLHAVEMFEAIEDGEIKALWVMCTNPAVSLPNANRVREALERLEFVV 421
|
|
| MopB_CT_ydeP |
cd02787 |
The MopB_CT_ydeP CD includes a group of related uncharacterized bacterial ... |
642-752 |
3.97e-53 |
|
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: 179.39 E-value: 3.97e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 642 MRLVTLRSHDQYNTTIYAMDDRYRGVFGRRDVLFMNEQDMAAQGLEHGDRVDIHTALP-GSALTLEDITVVAYGIAPGTV 720
Cdd:cd02787 1 LFLVTTRSHDQFNTTIYGLDDRYRGVFGRRDVVFMNPDDIARLGLKAGDRVDLESAFGdGQGRIVRGFRVVEYDIPRGCL 80
|
90 100 110
....*....|....*....|....*....|..
gi 523681045 721 GAYYPEANVLVPLNYLDEESGTPSYKSVPVRL 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 |
7.56e-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: 153.32 E-value: 7.56e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 114 RLTHPLVYDRDSDTLRPVAWEQAFARIGKILRGLQ----------------PDEVEFYTSGRASNEAAWLFQLFAREYGT 177
Cdd:cd02752 54 RLKYPMYRAPGSGKWEEISWDEALDEIARKMKDIRdasfveknaagvvvnrPDSIAFLGSAKLSNEECYLIRKFARALGT 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 178 NNFPDCSNMCHESTSVGLPQSIGIGKGTVSLDDFDQTELVISIGHNPGTNHP-RMMGTLHELSRRGVPIIVFNPlreral 256
Cdd:cd02752 134 NNLDHQARIUHSPTVAGLANTFGRGAMTNSWNDIKNADVILVMGGNPAEAHPvSFKWILEAKEKNGAKLIVVDP------ 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 257 eRFadpqnvmemaTRRSTpIASTYYQVRAGGDAAALKGIAKallqleeeqgnvldhafiaqhtqgftafaddlHATRW-- 334
Cdd:cd02752 208 -RF----------TRTAA-KADLYVPIRSGTDIAFLGGMIN--------------------------------YIIRYtp 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 335 QDIEQESGLTRESLTQVAAAYAKS----RATIVTYGMGITQHNKGTSNVRLIADLLLMRGNIGKPGAGICPLRGHSNVQG 410
Cdd:cd02752 244 EEVEDICGVPKEDFLKVAEMFAATgrpdKPGTILYAMGWTQHTVGSQNIRAMCILQLLLGNIGVAGGGVNALRGHSNVQG 323
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
114-494 |
8.82e-28 |
|
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239163 [Multi-domain] Cd Length: 539 Bit Score: 118.65 E-value: 8.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 114 RLTHPLVydRDSDTLRPVAWEQAFARIGKILRGLQ----PDEVEFYTSGRASNEAAWLFQL--FAREYGTNNFPDCS--- 184
Cdd:cd02762 54 RLRTPMR--RRGGSFEEIDWDEAFDEIAERLRAIRarhgGDAVGVYGGNPQAHTHAGGAYSpaLLKALGTSNYFSAAtad 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 185 NMCHESTSVGLPQSigigKGTVSLDDFDQTELVISIGHNPGTNHPRMM------GTLHELSRRGVPIIVFNPLRERALER 258
Cdd:cd02762 132 QKPGHFWSGLMFGH----PGLHPVPDIDRTDYLLILGANPLQSNGSLRtapdrvLRLKAAKDRGGSLVVIDPRRTETAKL 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 259 fadpqnvmematrrstpiASTYYQVRAGGDAAALKGIAKALLQleeeqGNVLDHAFIAQHTQGFTAFADDLHATRWQDIE 338
Cdd:cd02762 208 ------------------ADEHLFVRPGTDAWLLAAMLAVLLA-----EGLTDRRFLAEHCDGLDEVRAALAEFTPEAYA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 339 QESGLTRESLTQVAAAYAKSRATIVTYGMGITQHNKGTSNVRLIADLLLMRGNIGKPGAGIC-----PLRGHSnvqGNRT 413
Cdd:cd02762 265 PRCGVPAETIRRLAREFAAAPSAAVYGRLGVQTQLFGTLCSWLVKLLNLLTGNLDRPGGAMFttpalDLVGQT---SGRT 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 414 VGISEKPSAafLDSLQRVMGITPPrhhghdAVKALEAMIAGEA--KALICLGGNFAVAMPDHERAFPAMRGLELSVHVGT 491
Cdd:cd02762 342 IGRGEWRSR--VSGLPEIAGELPV------NVLAEEILTDGPGriRAMIVVAGNPVLSAPDGARLEAALGGLEFMVSVDV 413
|
...
gi 523681045 492 KLN 494
Cdd:cd02762 414 YMT 416
|
|
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
114-399 |
3.60e-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: 100.79 E-value: 3.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 114 RLTHPLVYD-RDSDTLRPVAWEQAFARIGKILRGLQPdevefytsgRASNEAAWLFQ---------------LFAREYGT 177
Cdd:cd02766 55 RLLTPLKRVgRKGGQWERISWDEALDTIAAKLKEIKA---------EYGPESILPYSyagtmgllqraargrFFHALGAS 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 178 NNFpdcSNMCHESTSVGLPQSIGIGKGtVSLDDFDQTELVISIGHNPGTNHPRMMGTLHELSRRGVPIIVFNPLRERALE 257
Cdd:cd02766 126 ELR---GTICSGAGIEAQKYDFGASLG-NDPEDMVNADLIVIWGINPAATNIHLMRIIQEARKRGAKVVVIDPYRTATAA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 258 RfadpqnvmematrrstpiASTYYQVRAGGDAA-ALkGIAKALLqleEEqgNVLDHAFIAQHTQGFTAFADDLHATRWQD 336
Cdd:cd02766 202 R------------------ADLHIQIRPGTDGAlAL-GVAKVLF---RE--GLYDRDFLARHTEGFEELKAHLETYTPEW 257
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 523681045 337 IEQESGLTRESLTQVAAAYAKSRATIVTYGMGITQHNKGTSNVRLIADLLLMRGNIGKPGAGI 399
Cdd:cd02766 258 AAEITGVSAEEIEELARLYGEAKPPSIRLGYGMQRYRNGGQNVRAIDALPALTGNIGVPGGGA 320
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
114-489 |
5.44e-21 |
|
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. The acetylene hydratase of Pelobacter acetylenicus is a tungsten iron-sulfur protein involved in the fermentation of acetylene to ethanol and acetate. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239160 [Multi-domain] Cd Length: 477 Bit Score: 96.99 E-value: 5.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 114 RLTHPL--VYDRDSDTLRPVAWEQAFARIGKILRGLQ----PDEVEFY-TSGRASNEAAWLFQL-FAREYGTNNFPDCSN 185
Cdd:cd02759 54 RLLYPLkrVGERGENKWERISWDEALDEIAEKLAEIKaeygPESIATAvGTGRGTMWQDSLFWIrFVRLFGSPNLFLSGE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 186 MCHESTSVGLPQSIGIGkGTVSLDDFDQTELVISIGHNPG-TNHPRMMGTLHELSRRGVPIIVFNPLREralerfadpqn 264
Cdd:cd02759 134 SCYWPRDMAHALTTGFG-LGYDEPDWENPECIVLWGKNPLnSNLDLQGHWLVAAMKRGAKLIVVDPRLT----------- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 265 vmEMATRrstpiASTYYQVRAGGDAAALKGIAKALLqlEEEqgnVLDHAFIAQHTQGFTAFAD---DLHATRWQDIeqeS 341
Cdd:cd02759 202 --WLAAR-----ADLWLPIRPGTDAALALGMLNVII--NEG---LYDKDFVENWCYGFEELAErvqEYTPEKVAEI---T 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 342 GLTRESLTQVAAAYAKSRATIVTYGMGITQHNKGTSNVRLIADLLLMRGNIGKPGAGIcplrghsnvqgnrtvgisekps 421
Cdd:cd02759 267 GVPAEKIRKAARLYATAKPACIQWGLAIDQQKNGTQTSRAIAILRAITGNLDVPGGNL---------------------- 324
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 523681045 422 aafldslqrvmgITPPRhhghdavkaleamiageAKALICLGGNFAVAMPDHERAFPAMRGLELSVHV 489
Cdd:cd02759 325 ------------LIPYP-----------------VKMLIVFGTNPLASYADTAPVLEALKALDFIVVV 363
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
113-401 |
6.14e-20 |
|
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and other related proteins. Thiosulfate reductase catalyzes the cleavage of sulfur-sulfur bonds in thiosulfate. Polysulfide reductase is a membrane-bound enzyme that catalyzes the reduction of polysulfide using either hydrogen or formate as the electron donor. Members of the MopB_Thiosulfate-R-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239156 [Multi-domain] Cd Length: 454 Bit Score: 93.52 E-value: 6.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 113 GRLTHPL--VYDRDSDTLRPVAWEQAFARIGKILRGLQPDEV-EFYTSGRASNEAAWLFQLFAREYGTNNFPDCSNMCHE 189
Cdd:cd02755 54 DRLKKPLirVGERGEGKFREASWDEALQYIASKLKEIKEQHGpESVLFGGHGGCYSPFFKHFAAAFGSPNIFSHESTCLA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 190 STSVGLPQSIGIGkGTVSLDDFDQTELVISIGHN--PGTNHPRMMGTLHELsRRGVPIIVFNPlreraleRFAdpqnvmE 267
Cdd:cd02755 134 SKNLAWKLVIDSF-GGEVNPDFENARYIILFGRNlaEAIIVVDARRLMKAL-ENGAKVVVVDP-------RFS------E 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 268 MATrrstpIASTYYQVRAGGDAAALKGIAKALLqleeeQGNVLDHAFIAQHTQGFTAFADDLHATRWQDIEQESGLTRES 347
Cdd:cd02755 199 LAS-----KADEWIPIKPGTDLAFVLALIHVLI-----SENLYDAAFVEKYTNGFELLKAHVKPYTPEWAAQITDIPADT 268
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 523681045 348 LTQVA--AAYAKSRATIVTYGMGITQHNKgTSNVRLIADLLLMRGNIGKPGaGICP 401
Cdd:cd02755 269 IRRIAreFAAAAPHAVVDPGWRGTFYSNS-FQTRRAIAIINALLGNIDKRG-GLYY 322
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
114-508 |
1.29e-18 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 88.23 E-value: 1.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 114 RLTHPLVyDRDSDTLRPVAWEQAFARIGKILRGLQPD------EVEFYTSGRASNEAAWLFQLFAREYGTNNF---PDCS 184
Cdd:pfam00384 1 RLKYPMV-RRGDGKFVRVSWDEALDLIAKKLKRIIKKygpdaiAINGGSGGLTDVESLYALKKLLNRLGSKNGnteDHNG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 185 NMCHESTSVGLPQSIGIGKGTVSLDDFDQTELVISIGHNPGTNHPRMMGTLH-ELSRRGVPIIVFNPlreralerfadpq 263
Cdd:pfam00384 80 DLCTAAAAAFGSDLRSNYLFNSSIADIENADLILLIGTNPREEAPILNARIRkAALKGKAKVIVIGP------------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 264 nvmematRRSTPIASTYYQVRAGGDAAALKGIAkallqleeeqgnvldHAFIAQhtqgftafaddlhatrwqdieqesgl 343
Cdd:pfam00384 147 -------RLDLTYADEHLGIKPGTDLALALAGA---------------HVFIKE-------------------------- 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 344 tresltqvaAAYAKSRAT--IVTYGMGITQHNKGTSNVRLIADLLLMRGNIGKPGAGICPLRghsNVQGNRTvgisekps 421
Cdd:pfam00384 179 ---------LKKDKDFAPkpIIIVGAGVLQRQDGEAIFRAIANLADLTGNIGRPGGGWNGLN---ILQGAAS-------- 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 422 aafldslqRVMGITPPRHHGHDAVKALEAMIAGEAKALICLGGNFAVAMPDHERAFPAMRGLELSV----HVGTKL-NRS 496
Cdd:pfam00384 239 --------PVGALDLGLVPGIKSVEMINAIKKGGIKVLYLLGNNPFVTHADENRVVKALQKLDLFVvydgHHGDKTaKYA 310
|
410
....*....|..
gi 523681045 497 HLltaketfILP 508
Cdd:pfam00384 311 DV-------ILP 315
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
189-417 |
4.64e-16 |
|
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: 82.28 E-value: 4.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 189 ESTSVGLPQSIG---IGKGTVSLDD-FDQTELVISIGHNPGTNhpRM---MGTLH-------ELSRRGVPIIVFNPLRER 254
Cdd:cd02751 141 GAAQVILPHVVGsdeVYEQGTSWDDiAEHSDLVVLFGANPLKT--RQgggGGPDHgsyyylkQAKDAGVRFICIDPRYTD 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 255 ALERFADPQnvmematrrstpIAstyyqVRAGGDAAALKGIAKALLqleEEqgNVLDHAFIAQHTQGFTAFADDLHAT-- 332
Cdd:cd02751 219 TAAVLAAEW------------IP-----IRPGTDVALMLAMAHTLI---TE--DLHDQAFLARYTVGFDEFKDYLLGEsd 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 333 ------RWQdiEQESGLTRESLTQVAAAYAKSRATIVTyGMGITQHNKGTSNVRLIADLLLMRGNIGKPGAGICPLRGHS 406
Cdd:cd02751 277 gvpktpEWA--AEITGVPAETIRALAREIASKRTMIAQ-GWGLQRAHHGEQPAWMLVTLAAMLGQIGLPGGGFGFGYGYS 353
|
250
....*....|.
gi 523681045 407 NVQGNRTVGIS 417
Cdd:cd02751 354 NGGGPPRGGAG 364
|
|
| Molydop_binding |
pfam01568 |
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
642-749 |
1.22e-14 |
|
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: 70.38 E-value: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 642 MRLVTLRSHDQYNTTIYAMDDRYRGVFgRRDVLFMNEQDMAAQGLEHGDRVDIHTALpGSALTledITVVAYGIAPGTVG 721
Cdd:pfam01568 1 LYLITGRVLGQYHSQTRTRRVLRLAKP-EPEVVEIHPEDAAALGIKDGDLVEVTSRR-GSVVV---RAKVTDRVRPGVVF 75
|
90 100 110
....*....|....*....|....*....|....*.
gi 523681045 722 AYYPE--------ANVLVPLnYLDEESGTPSYKSVP 749
Cdd:pfam01568 76 MPFGWwyeprggnANALTDD-ATDPLSGGPEFKTCA 110
|
|
| MopB_CT |
cd02775 |
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a ... |
649-746 |
5.66e-13 |
|
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: 65.42 E-value: 5.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 649 SHDQYNTTIYAMDDRYRGVFgRRDVLFMNEQDMAAQGLEHGDRVDIHTalPGSALTLedITVVAYGIAPGTVGAYYP--- 725
Cdd:cd02775 1 LRDHFHSGTRTRNPWLRELA-PEPVVEINPEDAAALGIKDGDLVRVES--RRGSVVL--RAKVTDGVPPGVVFLPHGwgh 75
|
90 100
....*....|....*....|....*..
gi 523681045 726 ------EANVLVPLnYLDEESGTPSYK 746
Cdd:cd02775 76 rggrggNANVLTPD-ALDPPSGGPAYK 101
|
|
| MopB_DmsA-EC |
cd02770 |
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
207-466 |
3.44e-12 |
|
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic dimethylsulfoxide reductase (DMSOR) of Escherichia coli and other related DMSOR-like enzymes. Unlike other DMSOR-like enzymes, this group has a predicted N-terminal iron-sulfur [4Fe-4S] cluster binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239171 [Multi-domain] Cd Length: 617 Bit Score: 69.66 E-value: 3.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 207 SLDDFDQTELVISIGHNPGTNHPRMMGTLHELS---RRGVPIIVFNPlreraleRFADpqnvmEMATRrstpiASTYYQV 283
Cdd:cd02770 160 SLDDLKDSKLVVLFGHNPAETRMGGGGSTYYYLqakKAGAKFIVIDP-------RYTD-----TAVTL-----ADEWIPI 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 284 RAGGDAAALKGIAKALLqleeeQGNVLDHAFIAQHTQGFTA--------------------FADDLHAT-RWQdiEQESG 342
Cdd:cd02770 223 RPGTDAALVAAMAYVMI-----TENLHDQAFLDRYCVGFDAehlpegappnesykdyvlgtGYDGTPKTpEWA--SEITG 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 343 LTRESLTQVAAAYAKSRATIVTYGMGITQHNKGTSNVRLIADLLLMRGNIGKPGAGICPLRGHSNVQGNRTVGISEK--- 419
Cdd:cd02770 296 VPAETIRRLAREIATTKPAAILQGWGPQRHANGEQAARAIMMLAAMTGNVGIPGGNTGARPGGSAYNGAGLPAGKNPvkt 375
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 523681045 420 --PSAAFLDSLQRVMGITPPRHHGHDAVKaLEAMIageaKALICLGGNF 466
Cdd:cd02770 376 siPCFMWTDAIERGEEMTADDGGVKGADK-LKSNI----KMIWNYAGNT 419
|
|
| MopB_2 |
cd02763 |
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
114-396 |
4.75e-12 |
|
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins
Pssm-ID: 239164 [Multi-domain] Cd Length: 679 Bit Score: 69.48 E-value: 4.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 114 RLTHPL--VYDRDSDTLRPVAWEQAFA----RIGKIlRGLQPDEVEFYTsGRASNEAawLFQLFAREYGTNNFPDCSNMC 187
Cdd:cd02763 54 RLTKPLlrKGPRGSGQFEEIEWEEAFSiatkRLKAA-RATDPKKFAFFT-GRDQMQA--LTGWFAGQFGTPNYAAHGGFC 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 188 HESTSVGLPQSIGIGKGTVSLDDFDQTELVISIGHNPGTNHPRMMGTLHELSRRGVPIIVFNPLREralerfadpqnvme 267
Cdd:cd02763 130 SVNMAAGGLYSIGGSFWEFGGPDLEHTKYFMMIGVAEDHHSNPFKIGIQKLKRRGGKFVAVNPVRT-------------- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 268 matrRSTPIASTYYQVRAGGDAAALKGIAKALLqleeeQGNVLDHAFIAQHT-------------QGFTAFADD------ 328
Cdd:cd02763 196 ----GYAAIADEWVPIKPGTDGAFILALAHELL-----KAGLIDWEFLKRYTnaaelvdytpewvEKITGIPADtirria 266
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 523681045 329 ---LHATRWQDIE------QESGLTRESLTQVAAAYAKSRativtygmGITQHNKGTSNVRLIADLLLMRGNIGKPG 396
Cdd:cd02763 267 kelGVTARDQPIElpiawtDVWGRKHEKITGRPVSFHAMR--------GIAAHSNGFQTIRALFVLMMLLGTIDRPG 335
|
|
| PRK13532 |
PRK13532 |
nitrate reductase catalytic subunit NapA; |
112-398 |
2.95e-10 |
|
nitrate reductase catalytic subunit NapA;
Pssm-ID: 237416 [Multi-domain] Cd Length: 830 Bit Score: 63.76 E-value: 2.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 112 YG--RLTHPL------VYDRDSDtLRPVAWEQAF----ARIGKILRGLQPDEVEFYTSGRasneaaWLFQ-------LFA 172
Cdd:PRK13532 93 YGkdRLTQPLlrmkdgKYDKEGE-FTPVSWDQAFdvmaEKFKKALKEKGPTAVGMFGSGQ------WTIWegyaaskLMK 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 173 REYGTNNFPDCSNMCHESTSVGLPQSIGIGKGTVSLDDFDQTELVISIGHNPGTNHPrmmgtlhelsrrgvpiIVFNPLR 252
Cdd:PRK13532 166 AGFRSNNIDPNARHCMASAVVGFMRTFGIDEPMGCYDDIEAADAFVLWGSNMAEMHP----------------ILWSRVT 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 253 ERaleRFADPQ---NVMEMATRRSTPIASTYYQVRAGGDAAALKGIAKALLqleeeQGNVLDHAFIAQHTQGFTAFAD-- 327
Cdd:PRK13532 230 DR---RLSNPDvkvAVLSTFEHRSFELADNGIIFTPQTDLAILNYIANYII-----QNNAVNWDFVNKHTNFRKGATDig 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 328 ----DLH-----------ATRWQDIEQE-----------------SGLTRESLTQVAAAYAKSRATIVTY-GMGITQHNK 374
Cdd:PRK13532 302 yglrPTHplekaaknpgtAGKSEPISFEefkkfvapytlektakmSGVPKEQLEQLAKLYADPNRKVVSFwTMGFNQHTR 381
|
330 340
....*....|....*....|....
gi 523681045 375 GTSNVRLIADLLLMRGNIGKPGAG 398
Cdd:PRK13532 382 GVWANNLVYNIHLLTGKISTPGNG 405
|
|
| 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 |
1.12e-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: 58.17 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 114 RLTHPLVydRDSDTLRPVAWEQAFARIGKILRGLQpDEVEFYTSGRASNEAAWLFQLFAREY-GTNNFpDCSNMCHests 192
Cdd:cd02771 54 RLTQPLI--RRGGTLVPVSWNEALDVAAARLKEAK-DKVGGIGSPRASNESNYALQKLVGAVlGTNNV-DHRARRL---- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 193 vgLPQSIGIGKG-TVSLDDFDQTELVISIGHNPGTNHPRMMGTLHELSRR---------GVPIIVFNPLRERAlERFADP 262
Cdd:cd02771 126 --IAEILRNGPIyIPSLRDIESADAVLVLGEDLTQTAPRIALALRQAARRkavelaalsGIPKWQDAAVRNIA-QGAKSP 202
|
170 180 190
....*....|....*....|....*....|....*..
gi 523681045 263 QNVMEMATRRSTPIASTYYQVRAGGDAAALKGIAKAL 299
Cdd:cd02771 203 LFIVNALATRLDDIAAESIRASPGGQARLGAALARAV 239
|
|
| MopB_Arsenite-Ox |
cd02756 |
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the ... |
105-405 |
1.20e-07 |
|
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: 55.18 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 105 SDFELEGYGRLTHPLVydRDSDTLRPVAWEQAFARIGKILRGL-----QPDEVEFYTS-------GRASNEAAWLFQL-- 170
Cdd:cd02756 108 SPDNRVGETRLTTPLV--RRGGQLQPTTWDDAIDLVARVIKGIldkdgNDDAVFASRFdhgggggGFENNWGVGKFFFma 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 171 ----FAReygTNNFPDCSNMCHEStsvglpQSIGIGKGTVSLDDFDQTELVISIGHNP---GTNH------PRMMG-TLH 236
Cdd:cd02756 186 lqtpFVR---IHNRPAYNSEVHAT------REMGVGELNNSYEDARLADTIVLWGNNPyetQTVYflnhwlPNLRGaTVS 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 237 ELSRRGVP--------IIVFNPLRE---RALERFADPQNVMEMatrrstpiastyyQVRAGGDAAALKGIAKALLQLEEE 305
Cdd:cd02756 257 EKQQWFPPgepvppgrIIVVDPRRTetvHAAEAAAGKDRVLHL-------------QVNPGTDTALANAIARYIYESLDE 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 306 qgnVLDHAfiaqhtqgftafaddlhatrwqdiEQESGLTRESLTQVAAAYAKSRA------TIVTYGMGITQHNKGTSNV 379
Cdd:cd02756 324 ---VLAEA------------------------EQITGVPRAQIEKAADWIAKPKEggyrkrVMFEYEKGIIWGNDNYRPI 376
|
330 340
....*....|....*....|....*.
gi 523681045 380 RLIADLLLMRGNIGKPGAGICPLRGH 405
Cdd:cd02756 377 YSLVNLAIITGNIGRPGTGCVRQGGH 402
|
|
| MopB_DMSOR-BSOR-TMAOR |
cd02769 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
214-399 |
1.30e-07 |
|
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: 54.96 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 214 TELVISIGHNP---------GTNHPRMMGTLHELSRRGVPIIVFNPLRERALERFadpqnvmematrrstpiASTYYQVR 284
Cdd:cd02769 171 TELVVAFGADPlknaqiawgGIPDHQAYSYLKALKDRGIRFISISPLRDDTAAEL-----------------GAEWIAIR 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 285 AGGDAAALKGIAKALlqLEEeqgNVLDHAFIAQHTQGFTAFADDL--------HATRWQdiEQESGLTRESLTQVAAAYA 356
Cdd:cd02769 234 PGTDVALMLALAHTL--VTE---GLHDKAFLARYTVGFDKFLPYLlgesdgvpKTPEWA--AAICGIPAETIRELARRFA 306
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 523681045 357 KSRaTIVTYGMGITQHNKGTSNVRLIADLLLMRGNIGKPGAGI 399
Cdd:cd02769 307 SKR-TMIMAGWSLQRAHHGEQPHWMAVTLAAMLGQIGLPGGGF 348
|
|
| MopB_Res-Cmplx1_Nad11 |
cd02773 |
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone ... |
104-224 |
4.99e-07 |
|
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: 52.65 E-value: 4.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 104 KSDFELEG--YGRLTHPLVydRDSDTLRPVAWEQAFARIGKILRGLQPDEVEFYTSGRASNEAAWLFQLFAREYGtnnfp 181
Cdd:cd02773 41 KTRFAYDGlkRQRLDKPYI--RKNGKLKPATWEEALAAIAKALKGVKPDEIAAIAGDLADVESMVALKDLLNKLG----- 113
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 523681045 182 dCSNMCHESTSVGLPQSIGIGK-GTVSLDDFDQTELVISIGHNP 224
Cdd:cd02773 114 -SENLACEQDGPDLPADLRSNYlFNTTIAGIEEADAVLLVGTNP 156
|
|
| MopB_Nitrate-R-NarG-like |
cd02750 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
273-399 |
5.85e-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: 52.71 E-value: 5.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 273 STPIASTYYQVRAGGDAAALKGIAKALLQleeeqGNVLDHAFIAQHTqgftafadDL----HATRWQdiEQESGLTRESL 348
Cdd:cd02750 212 SAKHADLWVPIKPGTDAALALAMAHVIIK-----EKLYDEDYLKEYT--------DLpflvYTPAWQ--EAITGVPRETV 276
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 523681045 349 TQVAAAYAKSRATIVTYGMGITQHNKGTSNVRLIADLLLMRGNIGKPGAGI 399
Cdd:cd02750 277 IRLAREFATNGRSMIIVGAGINHWYHGDLCYRALILLLALTGNEGKNGGGW 327
|
|
| MopB_CT_Fdh-Nap-like |
cd00508 |
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and ... |
673-753 |
7.03e-06 |
|
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: 45.96 E-value: 7.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 673 VLFMNEQDMAAQGLEHGDRVDIHTAlPGSALTledITVVAYGIAPGTVGAYY--------PEANVLVPLNYlDEESGTPS 744
Cdd:cd00508 36 FVEIHPEDAARLGIKDGDLVRVSSR-RGSVVV---RARVTDRVRPGTVFMPFhwggevsgGAANALTNDAL-DPVSGQPE 110
|
....*....
gi 523681045 745 YKSVPVRLT 753
Cdd:cd00508 111 FKACAVRIE 119
|
|
| FwdD |
COG1153 |
Formylmethanofuran dehydrogenase subunit D [Energy production and conversion]; |
673-750 |
1.56e-05 |
|
Formylmethanofuran dehydrogenase subunit D [Energy production and conversion];
Pssm-ID: 440767 [Multi-domain] Cd Length: 127 Bit Score: 44.84 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 673 VLFMNEQDMAAQGLEHGDRVdihtalpgsALTLEDITVV-----AYGIAPGTV----GayyPEANVLVPLNylDEESGTP 743
Cdd:COG1153 32 VCELNPEDMKKLGIKEGDKV---------KVTSEYGEVVvkakeSEDLHPGLVfipmG---PWANAVVPPE--THSTGMP 97
|
....*..
gi 523681045 744 SYKSVPV 750
Cdd:COG1153 98 DFKGVPV 104
|
|
| MopB_CT_1 |
cd02782 |
The MopB_CT_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
648-753 |
5.49e-05 |
|
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: 43.54 E-value: 5.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 648 RSHDQYNTTIYAMDDRYRGVfGRRDVLFMNEQDMAAQGLEHGDRVDIHTALPGSALTLEditvVAYGIAPGTV------G 721
Cdd:cd02782 10 RRHLRSNNSWLHNDPRLVKG-RNRCTLRIHPDDAAALGLADGDKVRVTSAAGSVEAEVE----VTDDMMPGVVslphgwG 84
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 523681045 722 AYYP-----------EANVLVPLNYLDEESGTPSYKSVPVRLT 753
Cdd:cd02782 85 HDYPgvsgagsrpgvNVNDLTDDTQRDPLSGNAAHNGVPVRLA 127
|
|
| PRK14991 |
PRK14991 |
tetrathionate reductase subunit TtrA; |
618-721 |
8.72e-05 |
|
tetrathionate reductase subunit TtrA;
Pssm-ID: 237883 [Multi-domain] Cd Length: 1031 Bit Score: 46.14 E-value: 8.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 618 ATGKAMFSVFKgvhenvvvEGEDVMRLVTLRSHDQYNTTIyaMDDRYRGVFGRRDVLfMNEQDMAAQGLEHGDRVDIHTa 697
Cdd:PRK14991 873 ADGTPLREQFP--------ESQWPLLLISFKSNLMSSMSI--ASPRLRQVKPANPVA-LNPQDAARLGIQHGDRVRIST- 940
|
90 100
....*....|....*....|....
gi 523681045 698 lPGSALTLEdITVVAyGIAPGTVG 721
Cdd:PRK14991 941 -PGGSVVAQ-ASVLN-GVMPGVIA 961
|
|
| MopB_CT_Tetrathionate_Arsenate-R |
cd02780 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate ... |
671-724 |
1.20e-04 |
|
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate reductase, subunit A, (TtrA); respiratory arsenate As(V) reductase, catalytic subunit (ArrA); and other related proteins.
Pssm-ID: 239181 [Multi-domain] Cd Length: 143 Bit Score: 42.67 E-value: 1.20e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 523681045 671 RDVLFMNEQDMAAQGLEHGDRVDIHTalPGSAltLEDITVVAYGIAPGTVGAYY 724
Cdd:cd02780 29 ENPVWINPEDAAKLGIKTGDRVRVVT--PGGS--VVGKAKVTEGVRPGVVAIEH 78
|
|
| MopB_CT_Formate-Dh-Na-like |
cd02792 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
676-753 |
6.66e-04 |
|
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. This CD (MopB_CT_Formate-Dh-Na-like) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239193 [Multi-domain] Cd Length: 122 Bit Score: 40.28 E-value: 6.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 676 MNEQDMAAQGLEHGDRVDIHTAlPGSALTledITVVAYGIAPGTVGAYY----------PEANVLVPLNYlDEESGTPSY 745
Cdd:cd02792 39 ISPELAAERGIKNGDMVWVSSP-RGKIKV---KALVTDRVKPHEVGIPYhwggmglvigDSANTLTPYVG-DPNTQTPEY 113
|
....*...
gi 523681045 746 KSVPVRLT 753
Cdd:cd02792 114 KAFLVNIE 121
|
|
| MopB_CT_Acetylene-hydratase |
cd02781 |
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related ... |
673-751 |
2.88e-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: 38.44 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 673 VLFMNEQDMAAQGLEHGDRVDIHTalPGSALTLEdiTVVAYGIAPGTV----GAYYPE---------------ANVLVPL 733
Cdd:cd02781 34 VAEINPETAAKLGIADGDWVWVET--PRGRARQK--ARLTPGIRPGVVraehGWWYPEreagepalggvwesnANALTSD 109
|
90
....*....|....*...
gi 523681045 734 NYLDEESGTPSYKSVPVR 751
Cdd:cd02781 110 DWNDPVSGSSPLRSMLCK 127
|
|
| PRK07860 |
PRK07860 |
NADH dehydrogenase subunit G; Validated |
114-304 |
4.08e-03 |
|
NADH dehydrogenase subunit G; Validated
Pssm-ID: 236118 [Multi-domain] Cd Length: 797 Bit Score: 40.70 E-value: 4.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 114 RLTHPLVYDRDsDTLRPVAWEQAFARIGkilRGLQP--DEVEFYTSGRASNEAAWLFQLFAR-EYGTNNFpDCSNMCHES 190
Cdd:PRK07860 278 RITTPLVRDED-GELEPASWSEALAVAA---RGLAAarGRVGVLVGGRLTVEDAYAYAKFARvALGTNDI-DFRARPHSA 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523681045 191 TSVGLPQSIGIGKG-TVSLDDFDQTELVISIGHNPGTNHPrmmgtlhelsrrgvpiIVFNPLRERALERFADPQNVMEMA 269
Cdd:PRK07860 353 EEADFLAARVAGRGlGVTYADLEKAPAVLLVGFEPEEESP----------------IVFLRLRKAARKHGLKVYSIAPFA 416
|
170 180 190
....*....|....*....|....*....|....*
gi 523681045 270 TRRSTPIASTYYQVRAGGDAAALKGIAKALLQLEE 304
Cdd:PRK07860 417 TRGLEKMGGTLLRTAPGGEAAALDALATGAPDVAE 451
|
|
| |
