|
Name |
Accession |
Description |
Interval |
E-value |
| MopB_ydeP |
cd02767 |
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
59-637 |
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: 1002.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 59 GFDCPGCAWPEKKDT-HTFNFCENGAKAVAFEATSKRVTPEFFATHTVSWLKEQSDFFLEDAGRITDPMRYDAATDKYVP 137
Cdd:cd02767 1 GFDCPGCAWGDPGQKlHGFEFCENGAKALAWETTPKRVTPEFFALHSVSELRTWSDYELEHLGRLTYPMRYDAGSDHYRP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 138 ISWDDAFQLIAKHLQALDhPNEAAFYTSGRTSNEAAFLYQLFVRNFGTNNFPDCSNMCHEATSVGLKDAIGLGKGTVTLD 217
Cdd:cd02767 81 ISWDEAFAEIAARLRALD-PDRAAFYTSGRASNEAAYLYQLFARAYGTNNLPDCSNMCHEPSSVGLKKSIGVGKGTVSLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 218 DFDQADAIFSFGHNPGTNHPRMLATLREVSKRGGTIIAINPLKERGLERFQDPQAPLEMMTnGSTPISRYYFQPKVGGDY 297
Cdd:cd02767 160 DFEHTDLIFFIGQNPGTNHPRMLHYLREAKKRGGKIIVINPLREPGLERFANPQNPESMLT-GGTKIADEYFQVRIGGDI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 298 AIMFGMLKHLDEWDQINlskgkPSVFDRDFIALNTVGFEDMLTEIRNTSWSEIHPHTGLTPEHLEALSKLYLESQRAIFC 377
Cdd:cd02767 239 ALLNGMAKHLIERDDEP-----GNVLDHDFIAEHTSGFEEYVAALRALSWDEIERASGLSREEIEAFAAMYAKSERVVFV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 378 WGMGITQHRHGTVNVHMLANLMLARGHIGRPGAGLAPIRGHSNVQGDRTMGINERPGAKMLDSIDRVFGIQSPREDGLGV 457
Cdd:cd02767 314 WGMGITQHAHGVDNVRAIVNLALLRGNIGRPGAGLMPIRGHSNVQGDRTMGITEKPFPEFLDALEEVFGFTPPRDPGLDT 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 458 VETIKAMAEGQVKVFIGLGGNFAVATPDSDYTQQALRACKLTVHITTKMNRSHLVCGEDALMLPCLGRTEIDTQKHGPQA 537
Cdd:cd02767 394 VEAIEAALEGKVKAFISLGGNFAEAMPDPAATEEALRRLDLTVHVATKLNRSHLVHGEEALILPCLGRTEIDMQAGGAQA 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 538 ISVEDSMSNVHLSAGRNEPISSDLLSEPDIVARIAEATLPDSQIKWRWYVESYDRIRDAISEVF-DEFHDFNQRVYQPGG 616
Cdd:cd02767 474 VTVEDSMSMTHTSRGRLKPASRVLLSEEAIVAGIAGARLGEAKPEWEILVEDYDRIRDEIAAVIyEGFADFNQRGDQPGG 553
|
570 580
....*....|....*....|.
gi 1808832998 617 FHLEHPANQHVWNTPKGKAQF 637
Cdd:cd02767 554 FHLPNGARERKFNTPSGKAQF 574
|
|
| Fdhalpha-like |
TIGR01701 |
oxidoreductase alpha (molybdopterin) subunit; This model represents a well-defined clade of ... |
24-776 |
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: 931.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 24 PAGGWGALLSVARNLKRQETFKKGSISLLNINQPTGFDCPGCAWPEKKDT-HTFNFCENGAKAVAFEATSKRVTPEFFAT 102
Cdd:TIGR01701 1 DAGGWGAVKSVALGKVKPMHIRQTLKLLLTLNKPEGYDCPGCAWGVSPQTlAGLEFCENGAKAIAWETTPRTIDPEFFAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 103 HTVSWLKEQSDFFLEDAGRITDPMRYDAATDKYVPISWDDAFQLIAKHLQALDhPNEAAFYTSGRTSNEAAFLYQLFVRN 182
Cdd:TIGR01701 81 HSVSELRTLDSHELEKLGRLTYPLSLRPGSDHYTPISWDDAYQEIAAKLNSLD-PKQVAFYTSGRTSNEAAYLYQLFARS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 183 FGTNNFPDCSNMCHEATSVGLKDAIGLGKGTVTLDDFDQADAIFSFGHNPGTNHPRMLATLREVSKRGGTIIAINPLKER 262
Cdd:TIGR01701 160 LGSNNLPDCSNMCHEPSSVALKRSIGIGKGSVNLEDFEHTDCLVFIGSNAGTNHPRMLKYLYAAKKRGAKIIAINPLRER 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 263 GLERFQDPQAPLEMMTNGSTPISRYYFQPKVGGDYAIMFGMLKHLDEWDQinlsKGKPSVFDRDFIALNTVGFEDMLTEI 342
Cdd:TIGR01701 240 GLERFWIPQIPESMLTGGGTQISSEYYQVRIGGDIALFNGVMKLLIEAED----AQPGSLIDHEFIANHTNGFDELRRHV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 343 RNTSWSEIHPHTGLTPEHLEALSKLYLESQRAIFCWGMGITQHRHGTVNVHMLANLMLARGHIGRPGAGLAPIRGHSNVQ 422
Cdd:TIGR01701 316 LQLNWNDIERSSGLSQEEILEFAKLLANSRRVVFCWAMGLTQHAHGVDNISQVANLALLRGNIGKPGAGVCPIRGHSNVQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 423 GDRTMGINERPGAKMLDSIDRVFGIQSPREDGLGVVETIKAMAEGQVKVFIGLGGNFAVATPDSDYTQQALRACKLTVHI 502
Cdd:TIGR01701 396 GDRTMGITEKPEEEFLARLSQIYGFTPPDWPGDTTVAMIEAILTGKVRAFICLGGNFLEAMPDTAAIERALRQLDLRVHV 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 503 TTKMNRSHLVCGEDALMLPCLGRTEIDTQKHGPQAISVEDSMSNVHLSAGRNEPISSDLLSEPDIVARIAEATLPDSQIK 582
Cdd:TIGR01701 476 ATKLNRSHVLAKEEALILPVLGRYEQDGQGTGKQAVSVESSMRMVHFSRGILKPRGAELRSEWAIIAEIAKALLPETPVA 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 583 WRWYVESYDRIRDAISEVFDEFHDFNQRVYQPGGFHLEHPA-NQHVWNTPKGKAQFLITPISEVYADKEHQFADTYSkak 661
Cdd:TIGR01701 556 WEILVDTYDQIRDAIAATNPGYDDINHRKRRPDGFQLPGAAlCERKFPTPDGKANFIVIPLPEFRVPTGHEFELVLV--- 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 662 vytlmTTRSHDQYNTTLYGLDDRYRGVFGQRRVLFMNEQDIQEAGFQADQWVDIESIYSDGLKRIVRSFKIVPYNIPRGS 741
Cdd:TIGR01701 633 -----TLRSHDQFNTTIYGEDDRYRGVDGHRRVVFMNETDIKKLGLRNGERVDVYNQYGDGQKRKFDNLRIVFYDTPTGN 707
|
730 740 750
....*....|....*....|....*....|....*
gi 1808832998 742 MAAYYPETNPLVALSSHDKYAKIPASKSIPVILHP 776
Cdd:TIGR01701 708 AAAYYPEANPLLPLDHHDPQSKTPEYKTIPVRLEA 742
|
|
| PRK09939 |
PRK09939 |
acid resistance putative oxidoreductase YdeP; |
17-776 |
0e+00 |
|
acid resistance putative oxidoreductase YdeP;
Pssm-ID: 182156 [Multi-domain] Cd Length: 759 Bit Score: 858.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 17 RIEPYDQPAGGWGALLSVARNLKRQETFKKGSISLLNINQPTGFDCPGCAWPEKKDTHTFNFCENGAKAVAFEATSKRVT 96
Cdd:PRK09939 4 KIESYQGAAGGWGAVKSVANAVRKQMDIRQDVIAMFDMNKPEGFDCPGCAWPDPKHSASFDICENGAKAIAWEVTDKQVN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 97 PEFFATHTVSWLKEQSDFFLEDAGRITDPMRYDAATDKYVPISWDDAFQLIAKHLQALDHPNEAAFYTSGRTSNEAAFLY 176
Cdd:PRK09939 84 ASFFAENTVQSLLTWGDHELEAAGRLTQPLKYDAVSDCYKPLSWQQAFDEIGARLQSYSDPNQVEFYTSGRTSNEAAFLY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 177 QLFVRNFGTNNFPDCSNMCHEATSVGLKDAIGLGKGTVTLDDFDQADAIFSFGHNPGTNHPRMLATLREVSKRGGTIIAI 256
Cdd:PRK09939 164 QLFAREYGSNNFPDCSNMCHEPTSVGLAASIGVGKGTVLLEDFEKCDLVICIGHNPGTNHPRMLTSLRALVKRGAKMIAI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 257 NPLKERGLERFQDPQAPLEMMTNGSTPISRYYFQPKVGGDYAIMFGMLKHLDEWDQINLSKGKPSVFDRDFIALNTVGFE 336
Cdd:PRK09939 244 NPLQERGLERFTAPQNPFEMLTNSETQLASAYYNVRIGGDMALLKGMMRLLIERDDAASAAGRPSLLDDEFIQTHTVGFD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 337 DMLTEIRNTSWSEIHPHTGLTPEHLEALSKLYLESQRAIFCWGMGITQHRHGTVNVHMLANLMLARGHIGRPGAGLAPIR 416
Cdd:PRK09939 324 ELRRDVLNSEWKDIERISGLSQTQIAELADAYAAAERTIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGICPLR 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 417 GHSNVQGDRTMGINERPGAKMLDSIDRVFGIQSPREDGLGVVETIKAMAEGQVKVFIGLGGNFAVATPDSDYTQQALRAC 496
Cdd:PRK09939 404 GHSNVQGDRTVGITEKPSAEFLARLGERYGFTPPHAPGHAAIASMQAICTGQARALICMGGNFALAMPDREASAVPLTQL 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 497 KLTVHITTKMNRSHLVCGEDALMLPCLGRTEIDTQKHGPQAISVEDSMSNVHLSAGRNEPISSDLLSEPDIVARIAEATL 576
Cdd:PRK09939 484 DLAVHVATKLNRSHLLTARHSYILPVLGRSEIDMQKSGAQAVTVEDSMSMIHASRGVLKPAGVMLKSECAVVAGIAQAAL 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 577 PDSQIKWRWYVESYDRIRDAISEVFDEFHDFNQRVYQPGGFHLEHPANQHVWNTPKGKAQFLitPISEVYADKEHQFADT 656
Cdd:PRK09939 564 PQSVVAWEYLVEDYDRIRNDIEAVLPEFADYNQRIRHPGGFHLINAAAERRWMTPSGKANFI--TSKGLLEDPSSAFNSK 641
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 657 yskakvYTLMTTRSHDQYNTTLYGLDDRYRGVFGQRRVLFMNEQDIQEAGFQADQWVDIESIYSDGLK--RIVRSFKIVP 734
Cdd:PRK09939 642 ------LVMATVRSHDQYNTTIYGMDDRYRGVFGQRDVVFMSAKQAKICRVKNGERVNLIALTPDGKRssRRMDRLKVVI 715
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 1808832998 735 YNIPRGSMAAYYPETNPLVALSSHDKYAKIPASKSIPVILHP 776
Cdd:PRK09939 716 YPMADRSLVTYFPESNHMLTLDNHDPLSGIPGYKSIPVELEP 757
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
62-772 |
8.62e-158 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 474.72 E-value: 8.62e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 62 CPGCAWpekkdthtfnFCENGAKAVAFEATskRVTPEffATHTVSWLK-----EQSDFFLEDAGRITDPMRYD--AATDK 134
Cdd:COG0243 28 CPGCGV----------GCGLGVKVEDGRVV--RVRGD--PDHPVNRGRlcakgAALDERLYSPDRLTYPMKRVgpRGSGK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 135 YVPISWDDAFQLIAKHLQAL--DH-PNEAAFYTSG----RTSNEAAFLYQLFVRNFGTNNFPDCSNMCHEATSVGLKDAI 207
Cdd:COG0243 94 FERISWDEALDLIAEKLKAIidEYgPEAVAFYTSGgsagRLSNEAAYLAQRFARALGTNNLDDNSRLCHESAVAGLPRTF 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 208 GLGKGTVTLDDFDQADAIFSFGHNPGTNHPRMLATLRE-VSKRGGTIIAINPLKERglerfqdpqaplemmtngSTPISR 286
Cdd:COG0243 174 GSDKGTVSYEDLEHADLIVLWGSNPAENHPRLLRRLREaAKKRGAKIVVIDPRRTE------------------TAAIAD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 287 YYFQPKVGGDYAIMFGMLKHLDEWDqinlskgkpsVFDRDFIALNTVGFEDMLTEIRNTSWSEIHPHTGLTPEHLEALSK 366
Cdd:COG0243 236 EWLPIRPGTDAALLLALAHVLIEEG----------LYDRDFLARHTVGFDELAAYVAAYTPEWAAEITGVPAEDIRELAR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 367 LYLESQRAIFCWGMGITQHRHGTVNVHMLANLMLARGHIGRPGAGLAPIRGHsnvqgdrtmginerpgakmldsidrvfg 446
Cdd:COG0243 306 EFATAKPAVILWGMGLQQHSNGTQTVRAIANLALLTGNIGKPGGGPFSLTGE---------------------------- 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 447 iqspredglgvvetikAMAEG---QVKVFIGLGGNFAVATPDSDYTQQALRACKLTVHITTKMNRSHLVCgedALMLPCL 523
Cdd:COG0243 358 ----------------AILDGkpyPIKALWVYGGNPAVSAPDTNRVREALRKLDFVVVIDTFLTETARYA---DIVLPAT 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 524 GRTEidtqKHGPqAISVEDSMsnVHLSAGRNEPIsSDLLSEPDIVARIAEATLPDSQIKWRWYVESYdrIRDAISEVFDE 603
Cdd:COG0243 419 TWLE----RDDI-VTNSEDRR--VHLSRPAVEPP-GEARSDWEIFAELAKRLGFEEAFPWGRTEEDY--LRELLEATRGR 488
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 604 ---FHDFNQRvyqpGGFHLEHP-----ANQHVWNTPKGKAQF-----LITPISEVYADKEHqfADTYSKAKVYTLMTTRS 670
Cdd:COG0243 489 gitFEELREK----GPVQLPVPpepafRNDGPFPTPSGKAEFysetlALPPLPRYAPPYEG--AEPLDAEYPLRLITGRS 562
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 671 HDQYNTTLYGLdDRYRGVFGqRRVLFMNEQDIQEAGFQADQWVDIESIYSDglkriVRSFKIVPYNIPRGSMAAYY---- 746
Cdd:COG0243 563 RDQWHSTTYNN-PRLREIGP-RPVVEINPEDAAALGIKDGDLVRVESDRGE-----VLARAKVTEGIRPGVVFAPHgwwy 635
|
730 740 750
....*....|....*....|....*....|...
gi 1808832998 747 -------PETNPLVaLSSHDKYAKIPASKSIPV 772
Cdd:COG0243 636 epaddkgGNVNVLT-PDATDPLSGTPAFKSVPV 667
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
115-776 |
1.93e-98 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 320.29 E-value: 1.93e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 115 FLEDAGRITDPM-RYDaatDKYVPISWDDAFQLIAKHLQAL--DH-PNEAAFYTSGRTSNEAAFLYQLFVRN-FGTNNFP 189
Cdd:COG3383 55 FVNSPDRLTTPLiRRG---GEFREVSWDEALDLVAERLREIqaEHgPDAVAFYGSGQLTNEENYLLQKLARGvLGTNNID 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 190 DCSNMCHEATSVGLKDAIGLGKGTVTLDDFDQADAIFSFGHNPGTNHPRMLATLREVSKRGGTIIAINPLKerglerfqd 269
Cdd:COG3383 132 NNARLCMASAVAGLKQSFGSDAPPNSYDDIEEADVILVIGSNPAEAHPVLARRIKKAKKNGAKLIVVDPRR--------- 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 270 pqaplemmtngsTPISRY---YFQPKVGGDYAIMFGMLKHLDEWDQInlskgkpsvfDRDFIALNTVGFEDMLTEIRNTS 346
Cdd:COG3383 203 ------------TETARLadlHLQIKPGTDLALLNGLLHVIIEEGLV----------DEDFIAERTEGFEELKASVAKYT 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 347 WSEIHPHTGLTPEHLEALSKLYLESQRAIFCWGMGITQHRHGTVNVHMLANLMLARGHIGRPGAGLAPIRGHSNVQGDRT 426
Cdd:COG3383 261 PERVAEITGVPAEDIREAARLIAEAKRAMILWGMGVNQHTQGTDNVNAIINLALATGNIGRPGTGPFPLTGQNNVQGGRD 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 427 MGI--NERPGAKMLDS------IDRVFGIQS-PREDGLGVVETIKAMAEGQVKVFIGLGGNFAVATPDSDYTQQALRACK 497
Cdd:COG3383 341 MGAlpNVLPGYRDVTDpehrakVADAWGVPPlPDKPGLTAVEMFDAIADGEIKALWIIGENPAVSDPDANHVREALEKLE 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 498 LTVHI------TTKMnrSHLVcgedalmLPCLGRTEidtqKHGpqaisvedSMSN----VHLSAGRNEPIsSDLLSEPDI 567
Cdd:COG3383 421 FLVVQdiflteTAEY--ADVV-------LPAASWAE----KDG--------TFTNterrVQRVRKAVEPP-GEARPDWEI 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 568 VARIAEAtlpdsqIKWRWYVESYDRIRDAISEVFDEFHDFN-QRVYQPGGFH-----LEHPANQHVW----NTPKGKAQF 637
Cdd:COG3383 479 IAELARR------LGYGFDYDSPEEVFDEIARLTPDYSGISyERLEALGGVQwpcpsEDHPGTPRLFtgrfPTPDGKARF 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 638 LITPISEVyadkehqfADTYSKAKVYTLMTTRSHDQYNT-TLYGLDDRYRGVFGQRRVLfMNEQDIQEAGFQADQWVDIE 716
Cdd:COG3383 553 VPVEYRPP--------AELPDEEYPLVLTTGRLLDQWHTgTRTRRSPRLNKHAPEPFVE-IHPEDAARLGIKDGDLVRVS 623
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1808832998 717 SIYSdglkRIVRSFKIVPyNIPRGS--MAAYYPET--NPLVAlSSHDKYAKIPASKSIPVILHP 776
Cdd:COG3383 624 SRRG----EVVLRARVTD-RVRPGTvfMPFHWGEGaaNALTN-DALDPVSKQPEYKACAVRVEK 681
|
|
| Fdh-alpha |
TIGR01591 |
formate dehydrogenase, alpha subunit, archaeal-type; This model describes a subset of formate ... |
115-772 |
5.21e-75 |
|
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: 257.01 E-value: 5.21e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 115 FLEDAGRITDPMRYDAatDKYVPISWDDAFQLIAKHLQALDH---PNEAAFYTSGRTSNEAAFLYQLFVRN-FGTNNFPD 190
Cdd:TIGR01591 47 FINSKDRLTTPLIREG--DKFREVSWDEAISYIAEKLKEIKEkygPDSIGFIGSSRGTNEENYLLQKLARAvIGTNNVDN 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 191 CSNMCHEATSVGLKDAIGLGKGTVTLDDFDQADAIFSFGHNPGTNHPRMLATLREVSKRGGTIIAINPlKERGLERFQDp 270
Cdd:TIGR01591 125 CARVCHGPSVAGLKQTVGIGAMSNTISEIENADLIVIIGYNPAESHPVVAQYLKNAKRNGAKIIVIDP-RKTETAKIAD- 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 271 qaplemmtngstpisrYYFQPKVGGDYAIMFGMLKHLdewdqinLSKGkpsVFDRDFIALNTVGFEDMLTEIRNTSWSEI 350
Cdd:TIGR01591 203 ----------------LHIPLKPGTDIALLNAMANVI-------IEEG---LYDKAFIEKRTEGFEEFREIVKGYTPEYV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 351 HPHTGLTPEHLEALSKLYLESQRAIFCWGMGITQHRHGTVNVHMLANLMLARGHIGRPGAGLAPIRGHSNVQGDRTMGI- 429
Cdd:TIGR01591 257 EDITGVPADLIREAARMYAKAGSAAILWGMGVTQHSQGVETVMALINLAMLTGNIGKPGGGVNPLRGQNNVQGACDMGAl 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 430 -NERPGAKML------DSIDRVFGIQS-PREDGLGVVETIKAMAEGQVKVFIGLGGNFAVATPDSDYTQQALRACKLTV- 500
Cdd:TIGR01591 337 pDFLPGYQPVsdeevrEKFAKAWGVVKlPAEPGLRIPEMIDAAADGDVKALYIMGEDPLQSDPNTSKVRKALEKLELLVv 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 501 ---HITTKMNRSHLVcgedalmLPCLGRTEidtqKHGpqaiSVEDSMSNVHLSAGRNEPIsSDLLSEPDIVARIAEAtlp 577
Cdd:TIGR01591 417 qdiFMTETAKYADVV-------LPAAAWLE----KEG----TFTNAERRIQRFFKAVEPK-GESKPDWEIIQELANA--- 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 578 dsqIKWRWYVESYDRIRDAISEVFDEFHDFN-QRVYQPGGfhLEHPANQHV-----------WNTPKGKAQFLitPISEV 645
Cdd:TIGR01591 478 ---LGLDWNYNHPQEIMDEIRELTPLFAGLTyERLDELGS--LQWPCNDSDasptsylykdkFATPDGKAKFI--PLEWV 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 646 YADKEhqFADTYSkakvYTLMTTRSHDQYNT-TLYGLDDRYRGVFGQRRVLfMNEQDIQEAGFQADQWVDIESIYSDGLK 724
Cdd:TIGR01591 551 APIEE--PDDEYP----LILTTGRVLTHYNVgEMTRRVAGLRRLSPEPYVE-INTEDAKKLGIKDGDLVKVKSRRGEITL 623
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1808832998 725 RIVRSFKIVP--YNIPrgsMAAYYPETNPLVALSShDKYAKIPASKSIPV 772
Cdd:TIGR01591 624 RAKVSDRVNKgaIYIT---MHFWDGAVNNLTTDDL-DPISGTPEYKYTAV 669
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
115-574 |
3.77e-71 |
|
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: 238.00 E-value: 3.77e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 115 FLEDAGRITDPMRYDAATDKYVPISWDDAFQLIAKHLQAL---DHPNEAAFYTSGRTSNEAAFLYQLFVRNFGTNNFPDC 191
Cdd:cd00368 48 GLYSPDRLKYPLIRVGGRGKFVPISWDEALDEIAEKLKEIrekYGPDAIAFYGGGGASNEEAYLLQKLLRALGSNNVDSH 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 192 SNMCHEATSVGLKdAIGLGKGTVTLDDFDQADAIFSFGHNPGTNHPRMLATLREVSKRGGTIIAINPLKERglerfqdpq 271
Cdd:cd00368 128 ARLCHASAVAALK-AFGGGAPTNTLADIENADLILLWGSNPAETHPVLAARLRRAKKRGAKLIVIDPRRTE--------- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 272 aplemmtngSTPISRYYFQPKVGGDYAIMFGmlkhldEWdqinlskgkpsvfdrdfialntvgfedmlteirntsWSEIh 351
Cdd:cd00368 198 ---------TAAKADEWLPIRPGTDAALALA------EW------------------------------------AAEI- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 352 phTGLTPEHLEALSKLYLESQRAIFCWGMGITQHRHGTVNVHMLANLMLARGHIGRPGAGLAPirghsnvqgdrtmgine 431
Cdd:cd00368 226 --TGVPAETIRALAREFAAAKRAVILWGMGLTQHTNGTQNVRAIANLAALTGNIGRPGGGLGP----------------- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 432 rpgakmldsidrvfgiqspredglgvvetikamaegqvkvfiglGGNFAVATPDSDYTQQALRACKLTVHITTKMNRSHL 511
Cdd:cd00368 287 --------------------------------------------GGNPLVSAPDANRVRAALKKLDFVVVIDIFMTETAA 322
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1808832998 512 VCgedALMLPCLGRTEidtqkhgpqaisVEDSMSNVHLSAGRNEPISS---DLLSEPDIVARIAEA 574
Cdd:cd00368 323 YA---DVVLPAATYLE------------KEGTYTNTEGRVQLFRQAVEppgEARSDWEILRELAKR 373
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
115-637 |
1.97e-66 |
|
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: 229.41 E-value: 1.97e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 115 FLEDAGRITDPMRydAATDKYVPISWDDAFQLIAKHLQALDH---PNEAAFYTSGRTSNEAAFLYQLFVRN-FGTNNFPD 190
Cdd:cd02753 48 FVNSKDRLTKPLI--RKNGKFVEASWDEALSLVASRLKEIKDkygPDAIAFFGSAKCTNEENYLFQKLARAvGGTNNVDH 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 191 CSNMCHEATSVGLKDAIGLGKGTVTLDDFDQADAIFSFGHNPGTNHPRMLATLREVSKRGGTIIAINPlKERGLERFQDp 270
Cdd:cd02753 126 CARLCHSPTVAGLAETLGSGAMTNSIADIEEADVILVIGSNTTEAHPVIARRIKRAKRNGAKLIVADP-RRTELARFAD- 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 271 qaplemmtngstpisrYYFQPKVGGDYAIMFGMLKHLdewdqinLSKGkpsVFDRDFIALNTVGFEDMLTEIRNTSWSEI 350
Cdd:cd02753 204 ----------------LHLQLRPGTDVALLNAMAHVI-------IEEG---LYDEEFIEERTEGFEELKEIVEKYTPEYA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 351 HPHTGLTPEHLEALSKLYLESQRAIFCWGMGITQHRHGTVNVHMLANLMLARGHIGRPGAGLAPIRGHSNVQGDRTMGin 430
Cdd:cd02753 258 ERITGVPAEDIREAARMYATAKSAAILWGMGVTQHSHGTDNVMALSNLALLTGNIGRPGTGVNPLRGQNNVQGACDMG-- 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 431 erpgakmldsidrvfgiqspredglgvveTIKAMAEGQVKVFIGLGGNFAVATPDSDYTQQALRACKLTV----HITTKM 506
Cdd:cd02753 336 -----------------------------ALPNVLPGYVKALYIMGENPALSDPNTNHVRKALESLEFLVvqdiFLTETA 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 507 NRSHLVcgedalmLPCLGRTEidtqKHGpqaiSVEDSMSNVHLSAGRNEPISSdllSEPD--IVARIAEAtlpdsqIKWR 584
Cdd:cd02753 387 ELADVV-------LPAASFAE----KDG----TFTNTERRVQRVRKAVEPPGE---ARPDweIIQELANR------LGYP 442
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1808832998 585 WYVESYDRIRDAISEVFDEFHDFN-QRVYQPGGFH-----LEHPANQHVW----NTPKGKAQF 637
Cdd:cd02753 443 GFYSHPEEIFDEIARLTPQYAGISyERLERPGGLQwpcpdEDHPGTPILHterfATPDGKARF 505
|
|
| MopB_CT_ydeP |
cd02787 |
The MopB_CT_ydeP CD includes a group of related uncharacterized bacterial ... |
663-774 |
8.15e-63 |
|
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: 205.97 E-value: 8.15e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 663 YTLMTTRSHDQYNTTLYGLDDRYRGVFGQRRVLFMNEQDIQEAGFQADQWVDIESIYSDGLKRIVRSFKIVPYNIPRGSM 742
Cdd:cd02787 1 LFLVTTRSHDQFNTTIYGLDDRYRGVFGRRDVVFMNPDDIARLGLKAGDRVDLESAFGDGQGRIVRGFRVVEYDIPRGCL 80
|
90 100 110
....*....|....*....|....*....|..
gi 1808832998 743 AAYYPETNPLVALSSHDKYAKIPASKSIPVIL 774
Cdd:cd02787 81 AAYYPEGNVLVPLDHRDPQSKTPAYKSVPVRL 112
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
119-500 |
5.43e-58 |
|
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: 207.46 E-value: 5.43e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 119 AGRITDPMrYDAATDKYVPISWDDAFQLIA---KHLQALDHPNEAAFYTSGRTSNEAAFLYQLFVRNF-GTNNFPDCSNM 194
Cdd:cd02754 52 PERLTRPL-LRRNGGELVPVSWDEALDLIAerfKAIQAEYGPDSVAFYGSGQLLTEEYYAANKLAKGGlGTNNIDTNSRL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 195 CHEATSVGLKDAIGLGKGTVTLDDFDQADAIFSFGHNPGTNHPRMLATLREVSK--RGGTIIAINPLKERglerfqdpqa 272
Cdd:cd02754 131 CMASAVAGYKRSFGADGPPGSYDDIEHADCFFLIGSNMAECHPILFRRLLDRKKanPGAKIIVVDPRRTR---------- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 273 plemmtngSTPISRYYFQPKVGGDYAIMFGMLKHLDEWDQInlskgkpsvfDRDFIALNTVGFEDMLTEIRNTSWSEIHP 352
Cdd:cd02754 201 --------TADIADLHLPIRPGTDLALLNGLLHVLIEEGLI----------DRDFIDAHTEGFEELKAFVADYTPEKVAE 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 353 HTGLTPEHLEALSKLYLESQRAIFCWGMGITQHRHGTVNVHMLANLMLARGHIGRPGAGLAPIRGHSNVQGDRTMG-INE 431
Cdd:cd02754 263 ITGVPEADIREAARLFGEARKVMSLWTMGVNQSTQGTAANNAIINLHLATGKIGRPGSGPFSLTGQPNAMGGREVGgLAN 342
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1808832998 432 RPGAKML-------DSIDRVFGI---QSPREDGLGVVETIKAMAEGQVKVFIGLGGNFAVATPDSDYTQQALRACKLTV 500
Cdd:cd02754 343 LLPGHRSvnnpehrAEVAKFWGVpegTIPPKPGLHAVEMFEAIEDGEIKALWVMCTNPAVSLPNANRVREALERLEFVV 421
|
|
| MopB_Formate-Dh-Na-like |
cd02752 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
115-430 |
1.05e-33 |
|
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate respiration in bacteria such as in the E. coli formate dehydrogenase N (Fdh-N). Fdh-N is a membrane protein that is a complex of three different subunits and is the major electron donor to the nitrate respiratory chain. Also included in this CD is the Desulfovibrio gigas tungsten formate dehydrogenase, DgW-FDH. In contrast to Fdh-N, which is a functional heterotrimer, DgW-FDH is a heterodimer. The DgW-FDH complex is composed of a large subunit carrying the W active site and one [4Fe-4S] center, and a small subunit that harbors a series of three [4Fe-4S] clusters as well as a putative vacant binding site for a fourth cluster. The smaller subunit is not included in this alignment. Members of the MopB_Formate-Dh-Na-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239153 [Multi-domain] Cd Length: 649 Bit Score: 137.92 E-value: 1.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 115 FLEDAGRITDPMRYDAATDKYVPISWDDAFQLIAKHLQAL-----DHPNEA----------AFYTSGRTSNEAAFLYQLF 179
Cdd:cd02752 48 FVHSPKRLKYPMYRAPGSGKWEEISWDEALDEIARKMKDIrdasfVEKNAAgvvvnrpdsiAFLGSAKLSNEECYLIRKF 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 180 VRNFGTNNFPDCSNMCHEATSVGLKDAIGLGKGTVTLDDFDQADAIFSFGHNPGTNHP-RMLATLREVSKRGGTIIAINP 258
Cdd:cd02752 128 ARALGTNNLDHQARIUHSPTVAGLANTFGRGAMTNSWNDIKNADVILVMGGNPAEAHPvSFKWILEAKEKNGAKLIVVDP 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 259 lkergleRFqdpqaplemmtNGSTPISRYYFQPKVGGDYAIMFGMLKHLDEWDqinlskgkPsvfdrdfialntvgfeDM 338
Cdd:cd02752 208 -------RF-----------TRTAAKADLYVPIRSGTDIAFLGGMINYIIRYT--------P----------------EE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 339 LTEIrntswseihphTGLTPEHLEALSKLYLESQRA----IFCWGMGITQHRHGTVNVHMLANLMLARGHIGRPGAGLAP 414
Cdd:cd02752 246 VEDI-----------CGVPKEDFLKVAEMFAATGRPdkpgTILYAMGWTQHTVGSQNIRAMCILQLLLGNIGVAGGGVNA 314
|
330
....*....|....*.
gi 1808832998 415 IRGHSNVQGDRTMGIN 430
Cdd:cd02752 315 LRGHSNVQGATDLGLL 330
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
113-574 |
5.27e-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: 119.42 E-value: 5.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 113 DFFLEDAGRITDPMRYDAatDKYVPISWDDAFQLIAKHLQAL---DHPNEAAFYTSGRTSNEAA-------FLYQLFVRN 182
Cdd:cd02762 46 GDYQNDPDRLRTPMRRRG--GSFEEIDWDEAFDEIAERLRAIrarHGGDAVGVYGGNPQAHTHAggayspaLLKALGTSN 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 183 FGTNNFPDcsNMCHEATSVGLkdaIGLGkGTVTLDDFDQADAIFSFGHNPGTNHPRMLAT------LREVSKRGGTIIAI 256
Cdd:cd02762 124 YFSAATAD--QKPGHFWSGLM---FGHP-GLHPVPDIDRTDYLLILGANPLQSNGSLRTApdrvlrLKAAKDRGGSLVVI 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 257 NPLKERGLERfqdpqaplemmtngstpiSRYYFQPKVGGDYAIMFGMLkhldewdQINLSKGkpsVFDRDFIALNTVGFE 336
Cdd:cd02762 198 DPRRTETAKL------------------ADEHLFVRPGTDAWLLAAML-------AVLLAEG---LTDRRFLAEHCDGLD 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 337 DMLTEIRNTSWSEIHPHTGLTPEHLEALSKlYLESQRAIFCWG-MGITQHRHGTVNvHMLANLM-LARGHIGRPGAGLAP 414
Cdd:cd02762 250 EVRAALAEFTPEAYAPRCGVPAETIRRLAR-EFAAAPSAAVYGrLGVQTQLFGTLC-SWLVKLLnLLTGNLDRPGGAMFT 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 415 ---IRGHSNVQGDRTMGINERPGAKMLDSIDRVFGIQSpredglgVVETIKAMAEGQVKVFIGLGGNFAVATPDSDYTQQ 491
Cdd:cd02762 328 tpaLDLVGQTSGRTIGRGEWRSRVSGLPEIAGELPVNV-------LAEEILTDGPGRIRAMIVVAGNPVLSAPDGARLEA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 492 ALRACKLTVHITTKMNRS----HLVcgedalmLPC---LGRTEIDTqkHGPQAisvedSMSNVHLSAGRNEPiSSDLLSE 564
Cdd:cd02762 401 ALGGLEFMVSVDVYMTETtrhaDYI-------LPPasqLEKPHATF--FNLEF-----PRNAFRYRRPLFPP-PPGTLPE 465
|
490
....*....|
gi 1808832998 565 PDIVARIAEA 574
Cdd:cd02762 466 WEILARLVEA 475
|
|
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
121-411 |
2.50e-26 |
|
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins
Pssm-ID: 239167 [Multi-domain] Cd Length: 501 Bit Score: 113.88 E-value: 2.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 121 RITDPMRYD-AATDKYVPISWDDAFQLIAKHLQAL--DHPNEAAFYTSGrtSNEAAFLYQLFVRNF----GTNNF--PDC 191
Cdd:cd02766 55 RLLTPLKRVgRKGGQWERISWDEALDTIAAKLKEIkaEYGPESILPYSY--AGTMGLLQRAARGRFfhalGASELrgTIC 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 192 SNMCHEATSVGLKDAIGlgkgtVTLDDFDQADAIFSFGHNPGTNHPRMLATLREVSKRGGTIIAINPLKERGLERfqdpq 271
Cdd:cd02766 133 SGAGIEAQKYDFGASLG-----NDPEDMVNADLIVIWGINPAATNIHLMRIIQEARKRGAKVVVIDPYRTATAAR----- 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 272 aplemmtngstpiSRYYFQPKVGGDYAIMFGMLKHLdewdqinLSKGkpsVFDRDFIALNTVGFEDMLTEIRNTSWSEIH 351
Cdd:cd02766 203 -------------ADLHIQIRPGTDGALALGVAKVL-------FREG---LYDRDFLARHTEGFEELKAHLETYTPEWAA 259
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 352 PHTGLTPEHLEALSKLYLESQRAIFCWGMGITQHRHGTVNVHMLANLMLARGHIGRPGAG 411
Cdd:cd02766 260 EITGVSAEEIEELARLYGEAKPPSIRLGYGMQRYRNGGQNVRAIDALPALTGNIGVPGGG 319
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
121-512 |
1.77e-22 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 99.78 E-value: 1.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 121 RITDPMrYDAATDKYVPISWDDAFQLIAKHLQAL-----DHPNEAAFYTSGRTSNEAAFLYQLFVRNFGTNNF---PDCS 192
Cdd:pfam00384 1 RLKYPM-VRRGDGKFVRVSWDEALDLIAKKLKRIikkygPDAIAINGGSGGLTDVESLYALKKLLNRLGSKNGnteDHNG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 193 NMCHEATSVGLKDAIGLGKGTVTLDDFDQADAIFSFGHNPGTNHPRMLATLREVSKRGGT-IIAINPLKERGLErfqdpq 271
Cdd:pfam00384 80 DLCTAAAAAFGSDLRSNYLFNSSIADIENADLILLIGTNPREEAPILNARIRKAALKGKAkVIVIGPRLDLTYA------ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 272 aplemmtngstpisryyfqpkvggdyaimfgmlkhlDEWdqinlskgkpsvfdrdfIALNTVGFEDMLTEIRNTSWSEIH 351
Cdd:pfam00384 154 ------------------------------------DEH-----------------LGIKPGTDLALALAGAHVFIKELK 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 352 PHTGLTPehlealsklylesqRAIFCWGMGITQHRHGTVNVHMLANLMLARGHIGRPGAGLAPIRGHSNVqgdrtmgiNE 431
Cdd:pfam00384 181 KDKDFAP--------------KPIIIVGAGVLQRQDGEAIFRAIANLADLTGNIGRPGGGWNGLNILQGA--------AS 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 432 RPGAKMLdsidrvfgiqsPREDGLGVVETIKAMAEGQVKVFIGLGGNFAVATPDSDYTQQALRACKLTV-----HITTKM 506
Cdd:pfam00384 239 PVGALDL-----------GLVPGIKSVEMINAIKKGGIKVLYLLGNNPFVTHADENRVVKALQKLDLFVvydghHGDKTA 307
|
....*.
gi 1808832998 507 NRSHLV 512
Cdd:pfam00384 308 KYADVI 313
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
121-416 |
2.01e-16 |
|
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: 82.74 E-value: 2.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 121 RITDPMRY--DAATDKYVPISWDDAFQLIAKHLQAL---DHPNEAAFY-TSGRTSNEAAFLYQL-FVRNFGTNNFPDCSN 193
Cdd:cd02759 54 RLLYPLKRvgERGENKWERISWDEALDEIAEKLAEIkaeYGPESIATAvGTGRGTMWQDSLFWIrFVRLFGSPNLFLSGE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 194 MC--HEATSVGLKDAIGLGKGTVtldDFDQADAIFSFGHNPG-TNHPRMLATLREVSKRGGTIIAInplkerglerfqDP 270
Cdd:cd02759 134 SCywPRDMAHALTTGFGLGYDEP---DWENPECIVLWGKNPLnSNLDLQGHWLVAAMKRGAKLIVV------------DP 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 271 QAplemmtNGSTPISRYYFQPKVGGDYAIMFGMLKHLdewdqINlskgkPSVFDRDFIALNTVGFEDMLTEIRNTSWSEI 350
Cdd:cd02759 199 RL------TWLAARADLWLPIRPGTDAALALGMLNVI-----IN-----EGLYDKDFVENWCYGFEELAERVQEYTPEKV 262
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1808832998 351 HPHTGLTPEHLEALSKLYLESQRAIFCWGMGITQHRHGTVNVHMLANLMLARGHIGRPGAGLA---PIR 416
Cdd:cd02759 263 AEITGVPAEKIRKAARLYATAKPACIQWGLAIDQQKNGTQTSRAIAILRAITGNLDVPGGNLLipyPVK 331
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
133-430 |
2.61e-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: 83.05 E-value: 2.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 133 DKYVPISWDDAFQLIAKHLQ--ALDHPNEAAFYTSG---------RTSNEAAFLYQL---FVRNFGTNNfpdcsnmcHEA 198
Cdd:cd02751 71 GEFVRISWDEALDLVASELKriREKYGNEAIFGGSYgwasagrlhHAQSLLHRFLNLiggYLGSYGTYS--------TGA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 199 TSVGLKDAIG----LGKGTvTLDD-FDQADAIFSFGHNPGTN--------HPRMLATLREVSKRGGTIIAINPLKERGLE 265
Cdd:cd02751 143 AQVILPHVVGsdevYEQGT-SWDDiAEHSDLVVLFGANPLKTrqgggggpDHGSYYYLKQAKDAGVRFICIDPRYTDTAA 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 266 RFQDPQAPlemmtngstpisryyfqPKVGGDYAIMFGMLKHLdewdqinLSKGKpsvFDRDFIALNTVGFEDMLTEIRNT 345
Cdd:cd02751 222 VLAAEWIP-----------------IRPGTDVALMLAMAHTL-------ITEDL---HDQAFLARYTVGFDEFKDYLLGE 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 346 S--------W-SEIhphTGLTPEHLEALSKLYlESQRAIFCWGMGITQHRHGTVNVHMLANLMLARGHIGRPGAGLAPIR 416
Cdd:cd02751 275 SdgvpktpeWaAEI---TGVPAETIRALAREI-ASKRTMIAQGWGLQRAHHGEQPAWMLVTLAAMLGQIGLPGGGFGFGY 350
|
330
....*....|....
gi 1808832998 417 GHSNVQGDRTMGIN 430
Cdd:cd02751 351 GYSNGGGPPRGGAG 364
|
|
| MopB_NADH-Q-OR-NuoG2 |
cd02768 |
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone ... |
121-264 |
2.62e-16 |
|
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: 81.56 E-value: 2.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 121 RITDPMRYDaaTDKYVPISWDDAFQLIAKHLQALDhPNEAAFYTSGRTSNEAAFLYQLFVRNFGTNNFpdCSNMCHEATS 200
Cdd:cd02768 54 RLTQPLIKK--GGKLVPVSWEEALKTVAEGLKAVK-GDKIGGIAGPRADLESLFLLKKLLNKLGSNNI--DHRLRQSDLP 128
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1808832998 201 VGLKDAIGLGKGTvTLDDFDQADAIFSFGHNPGTNHPRMLATLREVSKRGGT-IIAINPLKERGL 264
Cdd:cd02768 129 ADNRLRGNYLFNT-SIAEIEEADAVLLIGSNLRKEAPLLNARLRKAVKKKGAkIAVIGPKDTDLI 192
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
118-409 |
1.15e-14 |
|
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: 77.34 E-value: 1.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 118 DAGRITDPMRYDAA--TDKYVPISWDDAFQLIAKHLQAL--DHPNEAAFYTSGRTSNEAAFlyQLFVRNFGTNNFPDCSN 193
Cdd:cd02755 52 DPDRLKKPLIRVGErgEGKFREASWDEALQYIASKLKEIkeQHGPESVLFGGHGGCYSPFF--KHFAAAFGSPNIFSHES 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 194 MCHEATSVGLKDAIGLGkGTVTLDDFDQADAIFSFGHN--PGTNHPRMLAtLREVSKRGGTIIAInplkerglerfqDPQ 271
Cdd:cd02755 130 TCLASKNLAWKLVIDSF-GGEVNPDFENARYIILFGRNlaEAIIVVDARR-LMKALENGAKVVVV------------DPR 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 272 APlEMMTNGST--PIsryyfqpKVGGDYAIMFGMLKHL-DEwdqiNLskgkpsvFDRDFIALNTVGFEDMLTEIRNTS-- 346
Cdd:cd02755 196 FS-ELASKADEwiPI-------KPGTDLAFVLALIHVLiSE----NL-------YDAAFVEKYTNGFELLKAHVKPYTpe 256
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1808832998 347 WSEihPHTGLTPEHLEALS-KLYLESQRAIFCWGMGITQHRHGTVNVHMLANLMLARGHIGRPG 409
Cdd:cd02755 257 WAA--QITDIPADTIRRIArEFAAAAPHAVVDPGWRGTFYSNSFQTRRAIAIINALLGNIDKRG 318
|
|
| 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 ... |
121-274 |
4.45e-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: 68.95 E-value: 4.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 121 RITDPMRYDaaTDKYVPISWDDAFQLIAKHLQALDhpNEAAFYTSGRTSNEAAFLYQLFVRNF-GTNNFPdcsnmcHEAT 199
Cdd:cd02771 54 RLTQPLIRR--GGTLVPVSWNEALDVAAARLKEAK--DKVGGIGSPRASNESNYALQKLVGAVlGTNNVD------HRAR 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 200 SVGLKDAIGLGKGTVTLDDFDQADAIFSFGHNPGTNHPRMLATLREVSKRGGTIIAINP-----LKERGLERFQDPQAPL 274
Cdd:cd02771 124 RLIAEILRNGPIYIPSLRDIESADAVLVLGEDLTQTAPRIALALRQAARRKAVELAALSgipkwQDAAVRNIAQGAKSPL 203
|
|
| MopB_FmdB-FwdB |
cd02761 |
The MopB_FmdB-FwdB CD contains the molybdenum/tungsten formylmethanofuran dehydrogenases, ... |
121-423 |
7.55e-12 |
|
The MopB_FmdB-FwdB CD contains the molybdenum/tungsten formylmethanofuran dehydrogenases, subunit B (FmdB/FwdB), and other related proteins. Formylmethanofuran dehydrogenase catalyzes the first step in methane formation from CO2 in methanogenic archaea and some eubacteria. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239162 [Multi-domain] Cd Length: 415 Bit Score: 68.13 E-value: 7.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 121 RITDPMRydaatdKYVPISWDDAFQLIAKHLQALDHPneaAFYTSGRTSNEA-AFLYQLFVRNFGTnnFPDCSNMCHEAT 199
Cdd:cd02761 43 RITTPRI------DGKPVSLEEAIEKAAEILKEAKRP---LFYGLGTTVCEAqRAGIELAEKLGAI--IDHAASVCHGPN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 200 SVGLKDAiglGKGTVTLDDF-DQADAIFSFGHNPGTNHPRMLatlrevSKRggtiiAINPlkeRGLERFQDPQA------ 272
Cdd:cd02761 112 LLALQDS---GWPTTTLGEVkNRADVIVYWGTNPMHAHPRHM------SRY-----SVFP---RGFFREGGREDrtlivv 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 273 -PLEMMTNGstpISRYYFQPKVGGDYAIMFGMLkhldewdqiNLSKGKPSVFDRDfialntvgfedmlteirntswseih 351
Cdd:cd02761 175 dPRKSDTAK---LADIHLQIDPGSDYELLAALR---------ALLRGAGLVPDEV------------------------- 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1808832998 352 phTGLTPEHLEALSKLYLESQRAIFCWGMGITQHRHGTVNVHMLANLMLARGHIGRpgAGLAPIRGHSNVQG 423
Cdd:cd02761 218 --AGIPAETILELAERLKNAKFGVIFWGLGLLPSRGAHRNIEAAIRLVKALNEYTK--FALLPLRGHYNVRG 285
|
|
| MopB_DmsA-EC |
cd02770 |
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
133-479 |
5.20e-11 |
|
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: 66.19 E-value: 5.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 133 DKYVPISWDDAFQLIAKHLQAL--DHPNEAAFYTSG--------RTSNEAAFLYQLFVRNFGTNNFPDCSNMCHEATSVG 202
Cdd:cd02770 73 GKFVRISWDEALDTIASELKRIieKYGNEAIYVNYGtgtyggvpAGRGAIARLLNLTGGYLNYYGTYSWAQITTATPYTY 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 203 LKDAIGlgkgtVTLDDFDQADAIFSFGHNPGTNHPRMLAT---LREVSKRGGTIIAINPlkergleRFQDPQAPLEmmtN 279
Cdd:cd02770 153 GAAASG-----SSLDDLKDSKLVVLFGHNPAETRMGGGGStyyYLQAKKAGAKFIVIDP-------RYTDTAVTLA---D 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 280 GSTPIsryyfQPkvGGDYAIMFGMLkhldeWDQINlskgkPSVFDRDFIALNTVGF-EDMLTE----------------- 341
Cdd:cd02770 218 EWIPI-----RP--GTDAALVAAMA-----YVMIT-----ENLHDQAFLDRYCVGFdAEHLPEgappnesykdyvlgtgy 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 342 ---IRNTSW-SEIhphTGLTPEHLEALSKLYLESQRAIFCWGMGITQHRHGTVNVHMLANLMLARGHIGRPGAGLAPIRG 417
Cdd:cd02770 281 dgtPKTPEWaSEI---TGVPAETIRRLAREIATTKPAAILQGWGPQRHANGEQAARAIMMLAAMTGNVGIPGGNTGARPG 357
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1808832998 418 HSNVQGDRTMGINER-----PGAKMLDSIDRVfGIQSPREDGLGVVETIKAmaegQVKVFIGLGGNF 479
Cdd:cd02770 358 GSAYNGAGLPAGKNPvktsiPCFMWTDAIERG-EEMTADDGGVKGADKLKS----NIKMIWNYAGNT 419
|
|
| MopB_DMSOR-BSOR-TMAOR |
cd02769 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
115-411 |
1.65e-10 |
|
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: 64.59 E-value: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 115 FLEDAGRITDPMRYDaatDKYVPISWDDAFQLIAKHLQ--ALDHPNEAAFYTS------GRTSNEAAFLYQL------FV 180
Cdd:cd02769 56 WLEKGPGSDRSLRGK---EEFVRVSWDEALDLVAAELKrvRKTYGNEAIFGGSygwssaGRFHHAQSLLHRFlnlaggYV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 181 RNFGTNNfpdcsnmcHEATSVGLKDAIG----LGKGTVTLDDF-DQADAIFSFGHNP---------GTNHPRMLATLREV 246
Cdd:cd02769 133 GSVGDYS--------TGAAQVILPHVVGsmevYTEQQTSWPVIaEHTELVVAFGADPlknaqiawgGIPDHQAYSYLKAL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 247 SKRGGTIIAINPLKERGLERFQDPQAPLEMMTngstpisryyfqpkvggDYAIMFGMLKHLdewdqinLSKGKpsvFDRD 326
Cdd:cd02769 205 KDRGIRFISISPLRDDTAAELGAEWIAIRPGT-----------------DVALMLALAHTL-------VTEGL---HDKA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 327 FIALNTVGFEDMLTEIRNTS--------W-SEIhphTGLTPEHLEALSKLyLESQRAIFCWGMGITQHRHGTVNVHMLAN 397
Cdd:cd02769 258 FLARYTVGFDKFLPYLLGESdgvpktpeWaAAI---CGIPAETIRELARR-FASKRTMIMAGWSLQRAHHGEQPHWMAVT 333
|
330
....*....|....
gi 1808832998 398 LMLARGHIGRPGAG 411
Cdd:cd02769 334 LAAMLGQIGLPGGG 347
|
|
| MopB_Arsenate-R |
cd02757 |
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ... |
118-417 |
5.86e-09 |
|
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other related proteins. These members belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239158 [Multi-domain] Cd Length: 523 Bit Score: 59.38 E-value: 5.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 118 DAGRITDPMR------YDAATDKYVPISWDDAFQLIAKHLQAL---DHPNEAAfYTSGRTSNEAAFLYQLFVRNFGTNNF 188
Cdd:cd02757 53 DPDRILYPMKrtnprkGRDVDPKFVPISWDEALDTIADKIRALrkeNEPHKIM-LHRGRYGHNNSILYGRFTKMIGSPNN 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 189 PDCSNMCHEATSVGlKDAIGLGKGTVTLdDFDQADAIFSFGHNP-GTNH--PRMLATLREVSKRgGTIIAINPlkergle 265
Cdd:cd02757 132 ISHSSVCAESEKFG-RYYTEGGWDYNSY-DYANAKYILFFGADPlESNRqnPHAQRIWGGKMDQ-AKVVVVDP------- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 266 RFqdpqaplemmtNGSTPISRYYFQPKVGGDYAIMFGMLKHL---DEWDQ---------INLSKGKPSVFDRDFIALNTV 333
Cdd:cd02757 202 RL-----------SNTAAKADEWLPIKPGEDGALALAIAHVIlteGLWDKdfvgdfvdgKNYFKAGETVDEESFKEKSTE 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 334 GFEDMLTEI---RNTSWSEihPHTGLTPEHLEALSKLYLESQRAIFCW-GMGITQHRHGTVNVHMLANLMLARGHIGRPG 409
Cdd:cd02757 271 GLVKWWNLElkdYTPEWAA--KISGIPAETIERVAREFATAAPAAAAFtWRGATMQNRGSYNSMACHALNGLVGSIDSKG 348
|
....*...
gi 1808832998 410 aGLAPIRG 417
Cdd:cd02757 349 -GLCPNMG 355
|
|
| MopB_2 |
cd02763 |
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
137-409 |
2.13e-08 |
|
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: 57.92 E-value: 2.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 137 PISWDDAFQLIAKHLQAL--DHPNEAAFYTsGRTSNEAafLYQLFVRNFGTNNFPDCSNMCHEATSVGLKDAIGLGKGTV 214
Cdd:cd02763 72 EIEWEEAFSIATKRLKAAraTDPKKFAFFT-GRDQMQA--LTGWFAGQFGTPNYAAHGGFCSVNMAAGGLYSIGGSFWEF 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 215 TLDDFDQADAIFSFGHNPGTNHPRMLATLREVSKRGGTIIAINPLKerglerfqdpqaplemmtNGSTPISRYYFQPKVG 294
Cdd:cd02763 149 GGPDLEHTKYFMMIGVAEDHHSNPFKIGIQKLKRRGGKFVAVNPVR------------------TGYAAIADEWVPIKPG 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 295 GDYAIMFGMLKHLDEWDqinlskgkpsVFDRDFIalntvgfedmlteIRNTSWSEIhphTGLTPEHLEALSKLYLESQRA 374
Cdd:cd02763 211 TDGAFILALAHELLKAG----------LIDWEFL-------------KRYTNAAEL---VDYTPEWVEKITGIPADTIRR 264
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1808832998 375 IF--------------------CWGM----------------GITQHRHGTVNVHMLANLMLARGHIGRPG 409
Cdd:cd02763 265 IAkelgvtardqpielpiawtdVWGRkhekitgrpvsfhamrGIAAHSNGFQTIRALFVLMMLLGTIDRPG 335
|
|
| PRK13532 |
PRK13532 |
nitrate reductase catalytic subunit NapA; |
121-411 |
2.32e-08 |
|
nitrate reductase catalytic subunit NapA;
Pssm-ID: 237416 [Multi-domain] Cd Length: 830 Bit Score: 57.60 E-value: 2.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 121 RITDPM------RYDAaTDKYVPISWDDAFQLIAKHL-QALDH--PNEAAFYTSGR-TSNEAAFLYQLFVRNFGTNNFPD 190
Cdd:PRK13532 97 RLTQPLlrmkdgKYDK-EGEFTPVSWDQAFDVMAEKFkKALKEkgPTAVGMFGSGQwTIWEGYAASKLMKAGFRSNNIDP 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 191 CSNMCHEATSVGLKDAIGLGKGTVTLDDFDQADAIFSFGHNPGTNHP----RMlaTLREVSKRGGTIIAINPLKERGLEr 266
Cdd:PRK13532 176 NARHCMASAVVGFMRTFGIDEPMGCYDDIEAADAFVLWGSNMAEMHPilwsRV--TDRRLSNPDVKVAVLSTFEHRSFE- 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 267 fqdpQAPLEMMtngstpisryyFQPkvGGDYAIMFGMLKHLDEWDQINlskgkpsvfdRDFIALNTV---GFEDMLTEIR 343
Cdd:PRK13532 253 ----LADNGII-----------FTP--QTDLAILNYIANYIIQNNAVN----------WDFVNKHTNfrkGATDIGYGLR 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 344 NTS--------------WSEI---------HPHT--------GLTPEHLEALSKLYLESQRAIFC-WGMGITQHRHGT-V 390
Cdd:PRK13532 306 PTHplekaaknpgtagkSEPIsfeefkkfvAPYTlektakmsGVPKEQLEQLAKLYADPNRKVVSfWTMGFNQHTRGVwA 385
|
330 340
....*....|....*....|.
gi 1808832998 391 NvHMLANLMLARGHIGRPGAG 411
Cdd:PRK13532 386 N-NLVYNIHLLTGKISTPGNG 405
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
116-386 |
5.71e-08 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 56.60 E-value: 5.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 116 LEDAGRITDPMRY--DAATDKYVPISWDDAFQLIAKHLQAL--DHPNEAAFYTSGRTSNEAAFLYqlFVRNFGT-NNFPD 190
Cdd:PRK15488 93 LYDPQRIVKPLKRvgERGEGKWQEISWDEAYQEIAAKLNAIkqQHGPESVAFSSKSGSLSSHLFH--LATAFGSpNTFTH 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 191 CSNmCHEATSVGLKDAIGlgkGTVTLdDFDQADAIFSFGHN--PGTNHPRMLATLREVSKRGGTIIAINPlkergleRFQ 268
Cdd:PRK15488 171 AST-CPAGYAIAAKVMFG---GKLKR-DLANSKYIINFGHNlyEGINMSDTRGLMTAQMEKGAKLVVFEP-------RFS 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 269 dpqapleMMTNGSTPisryYFQPKVGGDYAIMFGMLkHLdeWDQINLskgkpsvFDRDFIALNTVGFEDMLTEIRNTS-- 346
Cdd:PRK15488 239 -------VVASKADE----WHAIRPGTDLAVVLALC-HV--LIEENL-------YDKAFVERYTSGFEELAASVKEYTpe 297
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1808832998 347 WSEIhpHTGLTPEHLEALSK-LYLESQRAIFCWGmgitqHR 386
Cdd:PRK15488 298 WAEA--ISDVPADDIRRIAReLAAAAPHAIVDFG-----HR 331
|
|
| MopB_NDH-1_NuoG2 |
cd02772 |
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase ... |
121-261 |
6.54e-08 |
|
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase/NADH dehydrogenase-1 (NDH-1), found in beta- and gammaproteobacteria. The NDH-1 is the first energy-transducting complex in the respiratory chain and functions as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. In Escherichia coli NDH-1, the largest subunit is encoded by the nuoG gene, and is part of the 14 distinct subunits constituting the functional enzyme. The NuoG subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain belongs to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239173 [Multi-domain] Cd Length: 414 Bit Score: 55.82 E-value: 6.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 121 RITDPMRydAATDKYVPISWDDAFQLIAKHLQAL--DH-PNEAAFYTSGRTSNEAAFLYQLFVRNFGTNNFPDCSNMCHE 197
Cdd:cd02772 54 RLTKPMI--KKDGQWQEVDWETALEYVAEGLSAIikKHgADQIGALASPHSTLEELYLLQKLARGLGSDNIDHRLRQSDF 131
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1808832998 198 ATSVGLKDAIGLGkgtVTLDDFDQADAIFSFGHNPGTNHPRMLATLREVSKRGGTIIAINPLKE 261
Cdd:cd02772 132 RDDAKASGAPWLG---MPIAEISELDRVLVIGSNLRKEHPLLAQRLRQAVKKGAKLSAINPADD 192
|
|
| Molydop_binding |
pfam01568 |
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
663-771 |
1.45e-06 |
|
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - containing oxidoreductases and tungsten formylmethanofuran dehydrogenase subunit d (FwdD) and molybdenum formylmethanofuran dehydrogenase subunit (FmdD); where the domain constitutes almost the entire subunit. The formylmethanofuran dehydrogenase catalyzes the first step in methane formation from CO2 in methanogenic archaea and has a molybdopterin dinucleotide cofactor. This domain corresponds to the C-terminal domain IV in dimethyl sulfoxide (DMSO)reductase which interacts with the 2-amino pyrimidone ring of both molybdopterin guanine dinucleotide molecules.
Pssm-ID: 426328 [Multi-domain] Cd Length: 110 Bit Score: 47.65 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 663 YTLMTTRSHDQYNTTLYGLDDRYRGVFGQRRVLfMNEQDIQEAGFQADQWVDIESIYSDGLKRIVRSfkivpYNIPRGSM 742
Cdd:pfam01568 1 LYLITGRVLGQYHSQTRTRRVLRLAKPEPEVVE-IHPEDAAALGIKDGDLVEVTSRRGSVVVRAKVT-----DRVRPGVV 74
|
90 100 110
....*....|....*....|....*....|....*..
gi 1808832998 743 AAYYPE--------TNPLVALSShDKYAKIPASKSIP 771
Cdd:pfam01568 75 FMPFGWwyeprggnANALTDDAT-DPLSGGPEFKTCA 110
|
|
| MopB_CT |
cd02775 |
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a ... |
670-768 |
2.94e-06 |
|
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a large, diverse, heterogeneous superfamily of enzymes that, in general, bind molybdopterin as a cofactor. The MopB domain is found in a wide variety of molybdenum- and tungsten-containing enzymes, including formate dehydrogenase-H (Fdh-H) and -N (Fdh-N), several forms of nitrate reductase (Nap, Nas, NarG), dimethylsulfoxide reductase (DMSOR), thiosulfate reductase, formylmethanofuran dehydrogenase, and arsenite oxidase. Molybdenum is present in most of these enzymes in the form of molybdopterin, a modified pterin ring with a dithiolene side chain, which is responsible for ligating the Mo. In many bacterial and archaeal species, molybdopterin is in the form of a dinucleotide, with two molybdopterin dinucleotide units per molybdenum. These proteins can function as monomers, heterodimers, or heterotrimers, depending on the protein and organism. Also included in the MopB superfamily is the eukaryotic/eubacterial protein domain family of the 75-kDa subunit/Nad11/NuoG (second domain) of respiratory complex 1/NADH-quinone oxidoreductase which is postulated to have lost an ancestral formate dehydrogenase activity and only vestigial sequence evidence remains of a molybdopterin binding site. This hierarchy is of the conserved MopB_CT domain present in many, but not all, MopB homologs.
Pssm-ID: 239176 [Multi-domain] Cd Length: 101 Bit Score: 46.54 E-value: 2.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 670 SHDQYNTTLYGLDDRYRGVFGqRRVLFMNEQDIQEAGFQADQWVDIESIYSDGLKRIVRSFKIVPYNI----PRGSMAAY 745
Cdd:cd02775 1 LRDHFHSGTRTRNPWLRELAP-EPVVEINPEDAAALGIKDGDLVRVESRRGSVVLRAKVTDGVPPGVVflphGWGHRGGR 79
|
90 100
....*....|....*....|...
gi 1808832998 746 YPETNPLVAlSSHDKYAKIPASK 768
Cdd:cd02775 80 GGNANVLTP-DALDPPSGGPAYK 101
|
|
| MopB_4 |
cd02765 |
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
116-444 |
9.27e-06 |
|
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins
Pssm-ID: 239166 [Multi-domain] Cd Length: 567 Bit Score: 49.01 E-value: 9.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 116 LEDAGRITDPMRY--DAATDKYVPISWDDAFQLIAKHLQALDH---PNEAAFYTSgrtSNEAAFLYQLFVRNFGTNNFPD 190
Cdd:cd02765 50 VYSPDRLKYPMKRvgERGEGKFERITWDEALDTIADKLTEAKReygGKSILWMSS---SGDGAILSYLRLALLGGGLQDA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 191 CSNMCHEATSVGLKDAIGLG--KGTVTLDDFDQADAIFSFGHNPGTNHPRMLATLREVSKRGGTIIAINPlkergleRFQ 268
Cdd:cd02765 127 LTYGIDTGVGQGFNRVTGGGfmPPTNEITDWVNAKTIIIWGSNILETQFQDAEFFLDARENGAKIVVIDP-------VYS 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 269 DPQAPLEMMtngsTPIsryyfqpKVGGDYAIMFGMLKHL--DEW------------------------DQINLSKGKPS- 321
Cdd:cd02765 200 TTAAKADQW----VPI-------RPGTDPALALGMINYIleHNWydeaflksntsapflvredngtllRQADVTATPAEd 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 322 ---VFDRDFIALNTV----------------------GFEDMLTEIRNTSWSEIHPHTGLTPEHLEALSKLYLESQRAIF 376
Cdd:cd02765 269 gyvVWDTNSDSPEPVaatninpalegeytingvkvhtVLTALREQAASYPPKAAAEICGLEEAIIETLAEWYATGKPSGI 348
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1808832998 377 CWGMGITQHRHGTVNVHMLANLMLARGHIGRPGAGLAPIRG----HSNVQGdrtMGINERPGAKMLDSIDRV 444
Cdd:cd02765 349 WGFGGVDRYYHSHVFGRTAAILAALTGNIGRVGGGVGQIKFmyfmGSNFLG---NQPDRDRWLKVMKNLDFI 417
|
|
| MopB_Res-Cmplx1_Nad11 |
cd02773 |
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone ... |
121-255 |
1.15e-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: 48.41 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 121 RITDPMRYDAatDKYVPISWDDAFQLIAKHLQALDhPNEAAFYTSGRTSNEAAFLYQLFVRNFGtnnfpdCSNMCHEAts 200
Cdd:cd02773 53 RLDKPYIRKN--GKLKPATWEEALAAIAKALKGVK-PDEIAAIAGDLADVESMVALKDLLNKLG------SENLACEQ-- 121
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1808832998 201 VGLKDAIGLGKGTV---TLDDFDQADAIFSFGHNPGTNHPRMLATLREVSKRGGTIIA 255
Cdd:cd02773 122 DGPDLPADLRSNYLfntTIAGIEEADAVLLVGTNPRFEAPVLNARIRKAWLHGGLKVG 179
|
|
| PRK07860 |
PRK07860 |
NADH dehydrogenase subunit G; Validated |
121-266 |
2.00e-05 |
|
NADH dehydrogenase subunit G; Validated
Pssm-ID: 236118 [Multi-domain] Cd Length: 797 Bit Score: 48.40 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 121 RITDPMRYDAaTDKYVPISWDDAFQLIAKHL-QALDHpneAAFYTSGRTSNEAAFLYQLFVR-NFGTNNFpDCSNMCHEA 198
Cdd:PRK07860 278 RITTPLVRDE-DGELEPASWSEALAVAARGLaAARGR---VGVLVGGRLTVEDAYAYAKFARvALGTNDI-DFRARPHSA 352
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 199 TSVGLKDAIGLGKG-TVTLDDFDQADAIFSFGHNPGTNHPRMLATLRE-VSKRGGTIIAINPLKERGLER 266
Cdd:PRK07860 353 EEADFLAARVAGRGlGVTYADLEKAPAVLLVGFEPEEESPIVFLRLRKaARKHGLKVYSIAPFATRGLEK 422
|
|
| PRK15102 |
PRK15102 |
trimethylamine-N-oxide reductase TorA; |
323-412 |
2.09e-03 |
|
trimethylamine-N-oxide reductase TorA;
Pssm-ID: 237909 [Multi-domain] Cd Length: 825 Bit Score: 41.58 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808832998 323 FDRDFIALNTVGFEDMLTEIRNTS--------WSEihPHTGLTPEHLEALSKLyLESQRAIFCWGMGITQHRHGTVNVHM 394
Cdd:PRK15102 300 YDKKFIDNYCLGFEQFLPYLLGEKdgvpktpeWAE--KICGIDAETIRELARQ-MAKGRTQIIAGWCIQRQQHGEQPYWM 376
|
90
....*....|....*...
gi 1808832998 395 LANLMLARGHIGRPGAGL 412
Cdd:PRK15102 377 GAVLAAMLGQIGLPGGGI 394
|
|
| |
