|
Name |
Accession |
Description |
Interval |
E-value |
| MopB_ydeP |
cd02767 |
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
60-638 |
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: 961.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 60 GFDCPGCAWPEKKDA-HAFNFCENGAKAVAFEATSKTVTPEYFAGHTVSWLSEQSDFFLEDLGRLTDPVRYDAATDKYVP 138
Cdd:cd02767 1 GFDCPGCAWGDPGQKlHGFEFCENGAKALAWETTPKRVTPEFFALHSVSELRTWSDYELEHLGRLTYPMRYDAGSDHYRP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 139 ISWDDAFKLIAQHLHALDhPDQAAFYTSGRASNEAAFLYQLFVRSFGTNNFPDCSNMCHETTSVGLLDSIGLGKGTVTLE 218
Cdd:cd02767 81 ISWDEAFAEIAARLRALD-PDRAAFYTSGRASNEAAYLYQLFARAYGTNNLPDCSNMCHEPSSVGLKKSIGVGKGTVSLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 219 DFDLADAIFSFGHNPGTNHPRMLGTLREVSKRGGNIIAINPIKERGLERFQDPQAPLEMMTnGSTPISRYYFQPKIGGDY 298
Cdd:cd02767 160 DFEHTDLIFFIGQNPGTNHPRMLHYLREAKKRGGKIIVINPLREPGLERFANPQNPESMLT-GGTKIADEYFQVRIGGDI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 299 ALMLGILKHLHEWDKKalasgKPSVFDRNFIAVNTVGFDEMIAEVERTEWADLYKHSGLSPEHLEKLAKLFLESERSIFC 378
Cdd:cd02767 239 ALLNGMAKHLIERDDE-----PGNVLDHDFIAEHTSGFEEYVAALRALSWDEIERASGLSREEIEAFAAMYAKSERVVFV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 379 WGMGITQHRHGTANVHMLANLLLARGQIGRPGAGLCPVRGHSNVQGDRTMGINELPSPKLLDNIDRVFGIKSPRKNGYGV 458
Cdd:cd02767 314 WGMGITQHAHGVDNVRAIVNLALLRGNIGRPGAGLMPIRGHSNVQGDRTMGITEKPFPEFLDALEEVFGFTPPRDPGLDT 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 459 VETIKAMAEGDIKVFIGLGGNFAVATPDTAYTQEALRKCNLTVHVATKLNRSHLVCGKDALILPCLGRTEIDEQLHGPQA 538
Cdd:cd02767 394 VEAIEAALEGKVKAFISLGGNFAEAMPDPAATEEALRRLDLTVHVATKLNRSHLVHGEEALILPCLGRTEIDMQAGGAQA 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 539 ITVEDSMSNVHLSAGRNTPISKNILSEPDIVARMAEAVLPESQIKWKWYIESYDRIRDSIADVF-DEFHDFNLRVYKPGG 617
Cdd:cd02767 474 VTVEDSMSMTHTSRGRLKPASRVLLSEEAIVAGIAGARLGEAKPEWEILVEDYDRIRDEIAAVIyEGFADFNQRGDQPGG 553
|
570 580
....*....|....*....|.
gi 446292580 618 FHLEHPANQHIWNTKSGKAQF 638
Cdd:cd02767 554 FHLPNGARERKFNTPSGKAQF 574
|
|
| Fdhalpha-like |
TIGR01701 |
oxidoreductase alpha (molybdopterin) subunit; This model represents a well-defined clade of ... |
25-777 |
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: 933.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 25 PAGGWGALLSVARNLKRQDILGKGSITLLNINQPTGFDCPGCAWPEKKDA-HAFNFCENGAKAVAFEATSKTVTPEYFAG 103
Cdd:TIGR01701 1 DAGGWGAVKSVALGKVKPMHIRQTLKLLLTLNKPEGYDCPGCAWGVSPQTlAGLEFCENGAKAIAWETTPRTIDPEFFAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 104 HTVSWLSEQSDFFLEDLGRLTDPVRYDAATDKYVPISWDDAFKLIAQHLHALDhPDQAAFYTSGRASNEAAFLYQLFVRS 183
Cdd:TIGR01701 81 HSVSELRTLDSHELEKLGRLTYPLSLRPGSDHYTPISWDDAYQEIAAKLNSLD-PKQVAFYTSGRTSNEAAYLYQLFARS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 184 FGTNNFPDCSNMCHETTSVGLLDSIGLGKGTVTLEDFDLADAIFSFGHNPGTNHPRMLGTLREVSKRGGNIIAINPIKER 263
Cdd:TIGR01701 160 LGSNNLPDCSNMCHEPSSVALKRSIGIGKGSVNLEDFEHTDCLVFIGSNAGTNHPRMLKYLYAAKKRGAKIIAINPLRER 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 264 GLERFQDPQAPLEMMTNGSTPISRYYFQPKIGGDYALMLGILKHLHEWDKKAlasgKPSVFDRNFIAVNTVGFDEMIAEV 343
Cdd:TIGR01701 240 GLERFWIPQIPESMLTGGGTQISSEYYQVRIGGDIALFNGVMKLLIEAEDAQ----PGSLIDHEFIANHTNGFDELRRHV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 344 ERTEWADLYKHSGLSPEHLEKLAKLFLESERSIFCWGMGITQHRHGTANVHMLANLLLARGQIGRPGAGLCPVRGHSNVQ 423
Cdd:TIGR01701 316 LQLNWNDIERSSGLSQEEILEFAKLLANSRRVVFCWAMGLTQHAHGVDNISQVANLALLRGNIGKPGAGVCPIRGHSNVQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 424 GDRTMGINELPSPKLLDNIDRVFGIKSPRKNGYGVVETIKAMAEGDIKVFIGLGGNFAVATPDTAYTQEALRKCNLTVHV 503
Cdd:TIGR01701 396 GDRTMGITEKPEEEFLARLSQIYGFTPPDWPGDTTVAMIEAILTGKVRAFICLGGNFLEAMPDTAAIERALRQLDLRVHV 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 504 ATKLNRSHLVCGKDALILPCLGRTEIDEQLHGPQAITVEDSMSNVHLSAGRNTPISKNILSEPDIVARMAEAVLPESQIK 583
Cdd:TIGR01701 476 ATKLNRSHVLAKEEALILPVLGRYEQDGQGTGKQAVSVESSMRMVHFSRGILKPRGAELRSEWAIIAEIAKALLPETPVA 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 584 WKWYIESYDRIRDSIADVFDEFHDFNLRVYKPGGFHLEHPA-NQHIWNTKSGKAQFLITPLEEVyadkenqyaaAYTESK 662
Cdd:TIGR01701 556 WEILVDTYDQIRDAIAATNPGYDDINHRKRRPDGFQLPGAAlCERKFPTPDGKANFIVIPLPEF----------RVPTGH 625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 663 VYTLM--TTRSHDQYNTTLYGLDDRYRGVFGQRRVLFMNQADIDEAGFEANQWVDIESVFSDGVKRIVHSFRIVPYNIPR 740
Cdd:TIGR01701 626 EFELVlvTLRSHDQFNTTIYGEDDRYRGVDGHRRVVFMNETDIKKLGLRNGERVDVYNQYGDGQKRKFDNLRIVFYDTPT 705
|
730 740 750
....*....|....*....|....*....|....*..
gi 446292580 741 GSLAAYYPETNPLVALSSHDKYAKIPASKSVPVILHP 777
Cdd:TIGR01701 706 GNAAAYYPEANPLLPLDHHDPQSKTPEYKTIPVRLEA 742
|
|
| PRK09939 |
PRK09939 |
acid resistance putative oxidoreductase YdeP; |
18-779 |
0e+00 |
|
acid resistance putative oxidoreductase YdeP;
Pssm-ID: 182156 [Multi-domain] Cd Length: 759 Bit Score: 856.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 18 RIEPYSHPAGGWGALLSVARNLKRQDILGKGSITLLNINQPTGFDCPGCAWPEKKDAHAFNFCENGAKAVAFEATSKTVT 97
Cdd:PRK09939 4 KIESYQGAAGGWGAVKSVANAVRKQMDIRQDVIAMFDMNKPEGFDCPGCAWPDPKHSASFDICENGAKAIAWEVTDKQVN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 98 PEYFAGHTVSWLSEQSDFFLEDLGRLTDPVRYDAATDKYVPISWDDAFKLIAQHLHALDHPDQAAFYTSGRASNEAAFLY 177
Cdd:PRK09939 84 ASFFAENTVQSLLTWGDHELEAAGRLTQPLKYDAVSDCYKPLSWQQAFDEIGARLQSYSDPNQVEFYTSGRTSNEAAFLY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 178 QLFVRSFGTNNFPDCSNMCHETTSVGLLDSIGLGKGTVTLEDFDLADAIFSFGHNPGTNHPRMLGTLREVSKRGGNIIAI 257
Cdd:PRK09939 164 QLFAREYGSNNFPDCSNMCHEPTSVGLAASIGVGKGTVLLEDFEKCDLVICIGHNPGTNHPRMLTSLRALVKRGAKMIAI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 258 NPIKERGLERFQDPQAPLEMMTNGSTPISRYYFQPKIGGDYALMLGILKHLHEWDKKALASGKPSVFDRNFIAVNTVGFD 337
Cdd:PRK09939 244 NPLQERGLERFTAPQNPFEMLTNSETQLASAYYNVRIGGDMALLKGMMRLLIERDDAASAAGRPSLLDDEFIQTHTVGFD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 338 EMIAEVERTEWADLYKHSGLSPEHLEKLAKLFLESERSIFCWGMGITQHRHGTANVHMLANLLLARGQIGRPGAGLCPVR 417
Cdd:PRK09939 324 ELRRDVLNSEWKDIERISGLSQTQIAELADAYAAAERTIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGICPLR 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 418 GHSNVQGDRTMGINELPSPKLLDNIDRVFGIKSPRKNGYGVVETIKAMAEGDIKVFIGLGGNFAVATPDTAYTQEALRKC 497
Cdd:PRK09939 404 GHSNVQGDRTVGITEKPSAEFLARLGERYGFTPPHAPGHAAIASMQAICTGQARALICMGGNFALAMPDREASAVPLTQL 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 498 NLTVHVATKLNRSHLVCGKDALILPCLGRTEIDEQLHGPQAITVEDSMSNVHLSAGRNTPISKNILSEPDIVARMAEAVL 577
Cdd:PRK09939 484 DLAVHVATKLNRSHLLTARHSYILPVLGRSEIDMQKSGAQAVTVEDSMSMIHASRGVLKPAGVMLKSECAVVAGIAQAAL 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 578 PESQIKWKWYIESYDRIRDSIADVFDEFHDFNLRVYKPGGFHLEHPANQHIWNTKSGKAQFLitPLEEVYADKENQYaaa 657
Cdd:PRK09939 564 PQSVVAWEYLVEDYDRIRNDIEAVLPEFADYNQRIRHPGGFHLINAAAERRWMTPSGKANFI--TSKGLLEDPSSAF--- 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 658 ytESKVyTLMTTRSHDQYNTTLYGLDDRYRGVFGQRRVLFMNQADIDEAGFEANQWVDIESVFSDGVK--RIVHSFRIVP 735
Cdd:PRK09939 639 --NSKL-VMATVRSHDQYNTTIYGMDDRYRGVFGQRDVVFMSAKQAKICRVKNGERVNLIALTPDGKRssRRMDRLKVVI 715
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 446292580 736 YNIPRGSLAAYYPETNPLVALSSHDKYAKIPASKSVPVILHPGN 779
Cdd:PRK09939 716 YPMADRSLVTYFPESNHMLTLDNHDPLSGIPGYKSIPVELEPSN 759
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
63-773 |
4.95e-162 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 485.89 E-value: 4.95e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 63 CPGCAWpekkdahafnFCENGAKAVAFEATSktVTPEyfAGHTVSWLS-----EQSDFFLEDLGRLTDPVRYD--AATDK 135
Cdd:COG0243 28 CPGCGV----------GCGLGVKVEDGRVVR--VRGD--PDHPVNRGRlcakgAALDERLYSPDRLTYPMKRVgpRGSGK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 136 YVPISWDDAFKLIAQHLHAL--DH-PDQAAFYTSG----RASNEAAFLYQLFVRSFGTNNFPDCSNMCHETTSVGLLDSI 208
Cdd:COG0243 94 FERISWDEALDLIAEKLKAIidEYgPEAVAFYTSGgsagRLSNEAAYLAQRFARALGTNNLDDNSRLCHESAVAGLPRTF 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 209 GLGKGTVTLEDFDLADAIFSFGHNPGTNHPRMLGTLRE-VSKRGGNIIAINPIKERglerfqdpqaplemmtngSTPISR 287
Cdd:COG0243 174 GSDKGTVSYEDLEHADLIVLWGSNPAENHPRLLRRLREaAKKRGAKIVVIDPRRTE------------------TAAIAD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 288 YYFQPKIGGDYALMLGILKHLHEWDkkalasgkpsVFDRNFIAVNTVGFDEMIAEVERTEWADLYKHSGLSPEHLEKLAK 367
Cdd:COG0243 236 EWLPIRPGTDAALLLALAHVLIEEG----------LYDRDFLARHTVGFDELAAYVAAYTPEWAAEITGVPAEDIRELAR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 368 LFLESERSIFCWGMGITQHRHGTANVHMLANLLLARGQIGRPGAGLCPVRGHsnvqgdrtmginelpspklldnidrvfg 447
Cdd:COG0243 306 EFATAKPAVILWGMGLQQHSNGTQTVRAIANLALLTGNIGKPGGGPFSLTGE---------------------------- 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 448 iksprkngygvvetikAMAEGD---IKVFIGLGGNFAVATPDTAYTQEALRKCNLTVHVATKLNRSHLVCgkdALILPCL 524
Cdd:COG0243 358 ----------------AILDGKpypIKALWVYGGNPAVSAPDTNRVREALRKLDFVVVIDTFLTETARYA---DIVLPAT 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 525 GRTEIDEqlhgpQAITVEDSMsnVHLSAGRNTPISkNILSEPDIVARMAEAVLPESQIKWKWYIESY--DRIRDSIADV- 601
Cdd:COG0243 419 TWLERDD-----IVTNSEDRR--VHLSRPAVEPPG-EARSDWEIFAELAKRLGFEEAFPWGRTEEDYlrELLEATRGRGi 490
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 602 -FDEFHD---FNLRVYKPGGFHLEHPanqhiWNTKSGKAQF-----LITPLEEVYADKENQYAAAytESKVYTLMTTRSH 672
Cdd:COG0243 491 tFEELREkgpVQLPVPPEPAFRNDGP-----FPTPSGKAEFysetlALPPLPRYAPPYEGAEPLD--AEYPLRLITGRSR 563
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 673 DQYNTTLYGLdDRYRGVFGqRRVLFMNQADIDEAGFEANQWVDIESVFsdGVkriVHSFRIVPYNIPRGSLAAYY----- 747
Cdd:COG0243 564 DQWHSTTYNN-PRLREIGP-RPVVEINPEDAAALGIKDGDLVRVESDR--GE---VLARAKVTEGIRPGVVFAPHgwwye 636
|
730 740 750
....*....|....*....|....*....|..
gi 446292580 748 ------PETNPLVaLSSHDKYAKIPASKSVPV 773
Cdd:COG0243 637 paddkgGNVNVLT-PDATDPLSGTPAFKSVPV 667
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
116-777 |
3.58e-98 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 319.52 E-value: 3.58e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 116 FLEDLGRLTDP-VRYDaatDKYVPISWDDAFKLIAQHLHAL--DH-PDQAAFYTSGRASNEAAFLYQLFVRS-FGTNNFP 190
Cdd:COG3383 55 FVNSPDRLTTPlIRRG---GEFREVSWDEALDLVAERLREIqaEHgPDAVAFYGSGQLTNEENYLLQKLARGvLGTNNID 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 191 DCSNMCHETTSVGLLDSIGLGKGTVTLEDFDLADAIFSFGHNPGTNHPRMLGTLREVSKRGGNIIAINPIKerglerfqd 270
Cdd:COG3383 132 NNARLCMASAVAGLKQSFGSDAPPNSYDDIEEADVILVIGSNPAEAHPVLARRIKKAKKNGAKLIVVDPRR--------- 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 271 pqaplemmtngsTPISRY---YFQPKIGGDYALMLGILKHLHEWDKkalasgkpsvFDRNFIAVNTVGFDEMIAEVERTE 347
Cdd:COG3383 203 ------------TETARLadlHLQIKPGTDLALLNGLLHVIIEEGL----------VDEDFIAERTEGFEELKASVAKYT 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 348 WADLYKHSGLSPEHLEKLAKLFLESERSIFCWGMGITQHRHGTANVHMLANLLLARGQIGRPGAGLCPVRGHSNVQGDRT 427
Cdd:COG3383 261 PERVAEITGVPAEDIREAARLIAEAKRAMILWGMGVNQHTQGTDNVNAIINLALATGNIGRPGTGPFPLTGQNNVQGGRD 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 428 MGI--NELPSPKLLDN------IDRVFGIKS-PRKNGYGVVETIKAMAEGDIKVFIGLGGNFAVATPDTAYTQEALRKCN 498
Cdd:COG3383 341 MGAlpNVLPGYRDVTDpehrakVADAWGVPPlPDKPGLTAVEMFDAIADGEIKALWIIGENPAVSDPDANHVREALEKLE 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 499 LTVH---VATKLNR-SHLVcgkdaliLPCLGRTEIDeqlhGpqaiTVEDSMSNVHLS-AGRNTPisKNILSEPDIVARMA 573
Cdd:COG3383 421 FLVVqdiFLTETAEyADVV-------LPAASWAEKD----G----TFTNTERRVQRVrKAVEPP--GEARPDWEIIAELA 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 574 EAVLPEsqikWKWyiesydrirDSIADVFDEF-----------HDfnlRVYKPGGFH-----LEHPANQHIW----NTKS 633
Cdd:COG3383 484 RRLGYG----FDY---------DSPEEVFDEIarltpdysgisYE---RLEALGGVQwpcpsEDHPGTPRLFtgrfPTPD 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 634 GKAQFLITPLEEVyadkenqyAAAYTESKVYTLMTTRSHDQYNT-TLYGLDDRYRGVFGQRRVLfMNQADIDEAGFEANQ 712
Cdd:COG3383 548 GKARFVPVEYRPP--------AELPDEEYPLVLTTGRLLDQWHTgTRTRRSPRLNKHAPEPFVE-IHPEDAARLGIKDGD 618
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446292580 713 WVDIESVFSDGVKRIVHSFRivpynIPRGSLAAY--YPET--NPLVAlSSHDKYAKIPASKSVPVILHP 777
Cdd:COG3383 619 LVRVSSRRGEVVLRARVTDR-----VRPGTVFMPfhWGEGaaNALTN-DALDPVSKQPEYKACAVRVEK 681
|
|
| Fdh-alpha |
TIGR01591 |
formate dehydrogenase, alpha subunit, archaeal-type; This model describes a subset of formate ... |
122-773 |
3.31e-72 |
|
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: 249.69 E-value: 3.31e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 122 RLTDPVRYDAatDKYVPISWDDAFKLIAQHLHALDH---PDQAAFYTSGRASNEAAFLYQLFVRS-FGTNNFPDCSNMCH 197
Cdd:TIGR01591 53 RLTTPLIREG--DKFREVSWDEAISYIAEKLKEIKEkygPDSIGFIGSSRGTNEENYLLQKLARAvIGTNNVDNCARVCH 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 198 ETTSVGLLDSIGLGKGTVTLEDFDLADAIFSFGHNPGTNHPRMLGTLREVSKRGGNIIAINPiKERGLERFQDpqaplem 277
Cdd:TIGR01591 131 GPSVAGLKQTVGIGAMSNTISEIENADLIVIIGYNPAESHPVVAQYLKNAKRNGAKIIVIDP-RKTETAKIAD------- 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 278 mtngstpisrYYFQPKIGGDYALMLGILKHLHEwdkkalasgkPSVFDRNFIAVNTVGFDE--MIAEVERTEWADlyKHS 355
Cdd:TIGR01591 203 ----------LHIPLKPGTDIALLNAMANVIIE----------EGLYDKAFIEKRTEGFEEfrEIVKGYTPEYVE--DIT 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 356 GLSPEHLEKLAKLFLESERSIFCWGMGITQHRHGTANVHMLANLLLARGQIGRPGAGLCPVRGHSNVQGDRTMGI--NEL 433
Cdd:TIGR01591 261 GVPADLIREAARMYAKAGSAAILWGMGVTQHSQGVETVMALINLAMLTGNIGKPGGGVNPLRGQNNVQGACDMGAlpDFL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 434 P------SPKLLDNIDRVFGI-KSPRKNGYGVVETIKAMAEGDIKVFIGLGGNFAVATPDTAYTQEALRKCNLTVHVATK 506
Cdd:TIGR01591 341 PgyqpvsDEEVREKFAKAWGVvKLPAEPGLRIPEMIDAAADGDVKALYIMGEDPLQSDPNTSKVRKALEKLELLVVQDIF 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 507 LNRShlvcGKDA-LILPCLGRTEIDEqlhgpqaiTVEDSMSNVHLSAGRNTPISKnilSEPD--IVARMAEAvlpesqIK 583
Cdd:TIGR01591 421 MTET----AKYAdVVLPAAAWLEKEG--------TFTNAERRIQRFFKAVEPKGE---SKPDweIIQELANA------LG 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 584 WKWYIESYDRIRDSIADVFDEFHDFNLRVYKPGGFhLEHPANQ---------HI--WNTKSGKAQFLitPLEEVYADKEN 652
Cdd:TIGR01591 480 LDWNYNHPQEIMDEIRELTPLFAGLTYERLDELGS-LQWPCNDsdasptsylYKdkFATPDGKAKFI--PLEWVAPIEEP 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 653 qyaaayTESKVYTLMTTRSHDQYNT-TLYGLDDRYRGVFGQRRVLfMNQADIDEAGFEANQWVDIESVFSDGVKRIVHSF 731
Cdd:TIGR01591 557 ------DDEYPLILTTGRVLTHYNVgEMTRRVAGLRRLSPEPYVE-INTEDAKKLGIKDGDLVKVKSRRGEITLRAKVSD 629
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 446292580 732 RIVP--YNIPrgsLAAYYPETNPLVALSShDKYAKIPASKSVPV 773
Cdd:TIGR01591 630 RVNKgaIYIT---MHFWDGAVNNLTTDDL-DPISGTPEYKYTAV 669
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
116-528 |
1.21e-67 |
|
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: 228.75 E-value: 1.21e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 116 FLEDLGRLTDPVRYDAATDKYVPISWDDAFKLIAQHLHAL---DHPDQAAFYTSGRASNEAAFLYQLFVRSFGTNNFPDC 192
Cdd:cd00368 48 GLYSPDRLKYPLIRVGGRGKFVPISWDEALDEIAEKLKEIrekYGPDAIAFYGGGGASNEEAYLLQKLLRALGSNNVDSH 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 193 SNMCHETTSVGLLDsIGLGKGTVTLEDFDLADAIFSFGHNPGTNHPRMLGTLREVSKRGGNIIAINPIKERglerfqdpq 272
Cdd:cd00368 128 ARLCHASAVAALKA-FGGGAPTNTLADIENADLILLWGSNPAETHPVLAARLRRAKKRGAKLIVIDPRRTE--------- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 273 aplemmtngSTPISRYYFQPKIGGDYALMLGilkhlhewdkkalasgkpsvfdrnfiavntvgfdemiaevertEWADly 352
Cdd:cd00368 198 ---------TAAKADEWLPIRPGTDAALALA-------------------------------------------EWAA-- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 353 KHSGLSPEHLEKLAKLFLESERSIFCWGMGITQHRHGTANVHMLANLLLARGQIGRPGAGLCPvrghsnvqgdrtmgine 432
Cdd:cd00368 224 EITGVPAETIRALAREFAAAKRAVILWGMGLTQHTNGTQNVRAIANLAALTGNIGRPGGGLGP----------------- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 433 lpspklldnidrvfgiksprkngygvvetikamaegdikvfiglGGNFAVATPDTAYTQEALRKCNLTVHVATKLNRSHL 512
Cdd:cd00368 287 --------------------------------------------GGNPLVSAPDANRVRAALKKLDFVVVIDIFMTETAA 322
|
410
....*....|....*.
gi 446292580 513 VCgkdALILPCLGRTE 528
Cdd:cd00368 323 YA---DVVLPAATYLE 335
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
116-501 |
9.76e-67 |
|
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: 230.56 E-value: 9.76e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 116 FLEDLGRLTDPVRydAATDKYVPISWDDAFKLIAQHLHALDH---PDQAAFYTSGRASNEAAFLYQLFVRS-FGTNNFPD 191
Cdd:cd02753 48 FVNSKDRLTKPLI--RKNGKFVEASWDEALSLVASRLKEIKDkygPDAIAFFGSAKCTNEENYLFQKLARAvGGTNNVDH 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 192 CSNMCHETTSVGLLDSIGLGKGTVTLEDFDLADAIFSFGHNPGTNHPRMLGTLREVSKRGGNIIAINPiKERGLERFQDp 271
Cdd:cd02753 126 CARLCHSPTVAGLAETLGSGAMTNSIADIEEADVILVIGSNTTEAHPVIARRIKRAKRNGAKLIVADP-RRTELARFAD- 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 272 qaplemmtngstpisrYYFQPKIGGDYALMLGILKHL--HEWdkkalasgkpsvFDRNFIAVNTVGFDEMIAEVERTEWA 349
Cdd:cd02753 204 ----------------LHLQLRPGTDVALLNAMAHVIieEGL------------YDEEFIEERTEGFEELKEIVEKYTPE 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 350 DLYKHSGLSPEHLEKLAKLFLESERSIFCWGMGITQHRHGTANVHMLANLLLARGQIGRPGAGLCPVRGHSNVQGDRTMG 429
Cdd:cd02753 256 YAERITGVPAEDIREAARMYATAKSAAILWGMGVTQHSHGTDNVMALSNLALLTGNIGRPGTGVNPLRGQNNVQGACDMG 335
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446292580 430 I--NELPspklldnidrvfgiksprknGYgvvetIKAMaegdikvFIgLGGNFAVATPDTAYTQEALRKCNLTV 501
Cdd:cd02753 336 AlpNVLP--------------------GY-----VKAL-------YI-MGENPALSDPNTNHVRKALESLEFLV 376
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
121-501 |
2.47e-61 |
|
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: 217.09 E-value: 2.47e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 121 GRLTDP-VRYDaaTDKYVPISWDDAFKLIAQHLHAL--DH-PDQAAFYTSGRASNEAAFLYQLFVRSF-GTNNFPDCSNM 195
Cdd:cd02754 53 ERLTRPlLRRN--GGELVPVSWDEALDLIAERFKAIqaEYgPDSVAFYGSGQLLTEEYYAANKLAKGGlGTNNIDTNSRL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 196 CHETTSVGLLDSIGLGKGTVTLEDFDLADAIFSFGHNPGTNHPRMLGTLREVSK--RGGNIIAINPikerglerfqdpqa 273
Cdd:cd02754 131 CMASAVAGYKRSFGADGPPGSYDDIEHADCFFLIGSNMAECHPILFRRLLDRKKanPGAKIIVVDP-------------- 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 274 plemMTNGSTPISRYYFQPKIGGDYALMLGILKHLHEWDKkalasgkpsvFDRNFIAVNTVGFDEMIAEVERTEWADLYK 353
Cdd:cd02754 197 ----RRTRTADIADLHLPIRPGTDLALLNGLLHVLIEEGL----------IDRDFIDAHTEGFEELKAFVADYTPEKVAE 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 354 HSGLSPEHLEKLAKLFLESERSIFCWGMGITQHRHGTANVHMLANLLLARGQIGRPGAGLCPVRGHSNVQGDRTMG--IN 431
Cdd:cd02754 263 ITGVPEADIREAARLFGEARKVMSLWTMGVNQSTQGTAANNAIINLHLATGKIGRPGSGPFSLTGQPNAMGGREVGglAN 342
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446292580 432 ELPSPKLLDN------IDRVFGIKS---PRKNGYGVVETIKAMAEGDIKVFIGLGGNFAVATPDTAYTQEALRKCNLTV 501
Cdd:cd02754 343 LLPGHRSVNNpehraeVAKFWGVPEgtiPPKPGLHAVEMFEAIEDGEIKALWVMCTNPAVSLPNANRVREALERLEFVV 421
|
|
| MopB_CT_ydeP |
cd02787 |
The MopB_CT_ydeP CD includes a group of related uncharacterized bacterial ... |
664-775 |
4.93e-61 |
|
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: 201.35 E-value: 4.93e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 664 YTLMTTRSHDQYNTTLYGLDDRYRGVFGQRRVLFMNQADIDEAGFEANQWVDIESVFSDGVKRIVHSFRIVPYNIPRGSL 743
Cdd:cd02787 1 LFLVTTRSHDQFNTTIYGLDDRYRGVFGRRDVVFMNPDDIARLGLKAGDRVDLESAFGDGQGRIVRGFRVVEYDIPRGCL 80
|
90 100 110
....*....|....*....|....*....|..
gi 446292580 744 AAYYPETNPLVALSSHDKYAKIPASKSVPVIL 775
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 ... |
122-501 |
1.31e-35 |
|
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: 143.69 E-value: 1.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 122 RLTDPVRYDAATDKYVPISWDDAFKLIAQHLHAL---------------DHPDQAAFYTSGRASNEAAFLYQLFVRSFGT 186
Cdd:cd02752 54 RLKYPMYRAPGSGKWEEISWDEALDEIARKMKDIrdasfveknaagvvvNRPDSIAFLGSAKLSNEECYLIRKFARALGT 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 187 NNFPDCSNMCHETTSVGLLDSIGLGKGTVTLEDFDLADAIFSFGHNPGTNHP-RMLGTLREVSKRGGNIIAINPikergl 265
Cdd:cd02752 134 NNLDHQARIUHSPTVAGLANTFGRGAMTNSWNDIKNADVILVMGGNPAEAHPvSFKWILEAKEKNGAKLIVVDP------ 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 266 eRFqdpqaplemmtNGSTPISRYYFQPKIGGDYALMLGILKHLHEWDkkalasgkPsvfdrnfiavntvgfdEMIAEVer 345
Cdd:cd02752 208 -RF-----------TRTAAKADLYVPIRSGTDIAFLGGMINYIIRYT--------P----------------EEVEDI-- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 346 tewadlykhSGLSPEHLEKLAKLFLESER----SIFCWGMGITQHRHGTANVHMLANLLLARGQIGRPGAGLCPVRGHSN 421
Cdd:cd02752 250 ---------CGVPKEDFLKVAEMFAATGRpdkpGTILYAMGWTQHTVGSQNIRAMCILQLLLGNIGVAGGGVNALRGHSN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 422 VQGDRTMGI--NELPspklldnidrvfgiksprknGYgvvetikamaegdikvfigLGG-NFAVATPDTAYTQEALRKCN 498
Cdd:cd02752 321 VQGATDLGLlsHNLP--------------------GY-------------------LGGqNPNSSFPNANKVRRALDKLD 361
|
...
gi 446292580 499 LTV 501
Cdd:cd02752 362 WLV 364
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
114-575 |
2.48e-27 |
|
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239163 [Multi-domain] Cd Length: 539 Bit Score: 117.11 E-value: 2.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 114 DFFLEDLGRLTDPVRYDAatDKYVPISWDDAFKLIAQHLHAL---DHPDQAAFYTSGRASNEAAFLYQL--FVRSFGTNN 188
Cdd:cd02762 46 GDYQNDPDRLRTPMRRRG--GSFEEIDWDEAFDEIAERLRAIrarHGGDAVGVYGGNPQAHTHAGGAYSpaLLKALGTSN 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 189 FPDCS---NMCHETTSVGLLDSIGLGkgtvTLEDFDLADAIFSFGHNPGTNH------PRMLGTLREVSKRGGNIIAINP 259
Cdd:cd02762 124 YFSAAtadQKPGHFWSGLMFGHPGLH----PVPDIDRTDYLLILGANPLQSNgslrtaPDRVLRLKAAKDRGGSLVVIDP 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 260 IKERGLERfqdpqaplemmtngstpiSRYYFQPKIGGDYALMLGILKHLhewdkkaLASGkpsVFDRNFIAVNTVGFDEM 339
Cdd:cd02762 200 RRTETAKL------------------ADEHLFVRPGTDAWLLAAMLAVL-------LAEG---LTDRRFLAEHCDGLDEV 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 340 IAEVERTEWADLYKHSGLSPEHLEKLAKLFlESERSIFCWG-MGITQHRHGTANvHMLANLL-LARGQIGRPGAGLCP-- 415
Cdd:cd02762 252 RAALAEFTPEAYAPRCGVPAETIRRLAREF-AAAPSAAVYGrLGVQTQLFGTLC-SWLVKLLnLLTGNLDRPGGAMFTtp 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 416 -VRGHSNVQGDRTMG-------------INELPSPKLLDNIDRVfgiksprkngygvvetikamAEGDIKVFIGLGGNFA 481
Cdd:cd02762 330 aLDLVGQTSGRTIGRgewrsrvsglpeiAGELPVNVLAEEILTD--------------------GPGRIRAMIVVAGNPV 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 482 VATPDTAYTQEALRKCNLTVHVATKLNRShlvcGKDA-LILPCLGRTEIDE-QLHGPQAitvedSMSNVHLSAgRNTPIS 559
Cdd:cd02762 390 LSAPDGARLEAALGGLEFMVSVDVYMTET----TRHAdYILPPASQLEKPHaTFFNLEF-----PRNAFRYRR-PLFPPP 459
|
490
....*....|....*.
gi 446292580 560 KNILSEPDIVARMAEA 575
Cdd:cd02762 460 PGTLPEWEILARLVEA 475
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
122-501 |
4.13e-23 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 101.71 E-value: 4.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 122 RLTDP-VRYDAatDKYVPISWDDAFKLIAQHLHAL-----DHPDQAAFYTSGRASNEAAFLYQLFVRSFGTNNF---PDC 192
Cdd:pfam00384 1 RLKYPmVRRGD--GKFVRVSWDEALDLIAKKLKRIikkygPDAIAINGGSGGLTDVESLYALKKLLNRLGSKNGnteDHN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 193 SNMCHETTSVGLLDSIGLGKGTVTLEDFDLADAIFSFGHNPGTNHPrMLGT--LREVSKRGGNIIAINPIKERGLERFqd 270
Cdd:pfam00384 79 GDLCTAAAAAFGSDLRSNYLFNSSIADIENADLILLIGTNPREEAP-ILNAriRKAALKGKAKVIVIGPRLDLTYADE-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 271 pqaplemmtngstpisryYFQPKIGGDYALMLGiLKHLhewdkkalasgkpsvfdrnFIAVNtvgfdemiaevertewad 350
Cdd:pfam00384 156 ------------------HLGIKPGTDLALALA-GAHV-------------------FIKEL------------------ 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 351 lykhsglspehleKLAKLFleSERSIFCWGMGITQHRHGTANVHMLANLLLARGQIGRPGAGlcpVRGHSNVQGDRT-MG 429
Cdd:pfam00384 180 -------------KKDKDF--APKPIIIVGAGVLQRQDGEAIFRAIANLADLTGNIGRPGGG---WNGLNILQGAASpVG 241
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446292580 430 INELPSPKlldnidrvfgiksprknGYGVVETIKAMAEGDIKVFIGLGGNFAVATPDTAYTQEALRKCNLTV 501
Cdd:pfam00384 242 ALDLGLVP-----------------GIKSVEMINAIKKGGIKVLYLLGNNPFVTHADENRVVKALQKLDLFV 296
|
|
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
122-412 |
1.88e-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: 101.94 E-value: 1.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 122 RLTDP-VRYDAATDKYVPISWDDAFKLIAQHLHAL--DHPDQAAFYTSGraSNEAAFLYQLFVRSF----GTNNF--PDC 192
Cdd:cd02766 55 RLLTPlKRVGRKGGQWERISWDEALDTIAAKLKEIkaEYGPESILPYSY--AGTMGLLQRAARGRFfhalGASELrgTIC 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 193 SNMCHETTSVGLLDSIGlgkgtVTLEDFDLADAIFSFGHNPGTNHPRMLGTLREVSKRGGNIIAINPIKERGLERfqdpq 272
Cdd:cd02766 133 SGAGIEAQKYDFGASLG-----NDPEDMVNADLIVIWGINPAATNIHLMRIIQEARKRGAKVVVIDPYRTATAAR----- 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 273 aplemmtngstpiSRYYFQPKIGGDYALMLGILKHLHEwdkKALAsgkpsvfDRNFIAVNTVGFDEMIAEVERTEWADLY 352
Cdd:cd02766 203 -------------ADLHIQIRPGTDGALALGVAKVLFR---EGLY-------DRDFLARHTEGFEELKAHLETYTPEWAA 259
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 353 KHSGLSPEHLEKLAKLFLESERSIFCWGMGITQHRHGTANVHMLANLLLARGQIGRPGAG 412
Cdd:cd02766 260 EITGVSAEEIEELARLYGEAKPPSIRLGYGMQRYRNGGQNVRAIDALPALTGNIGVPGGG 319
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
134-496 |
4.99e-21 |
|
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: 98.07 E-value: 4.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 134 DKYVPISWDDAFKLIAQHL----HAldHPDQAAFYTSG---------RASNEAAFLYQL---FVRSFGTNNfpdcsnmcH 197
Cdd:cd02751 71 GEFVRISWDEALDLVASELkrirEK--YGNEAIFGGSYgwasagrlhHAQSLLHRFLNLiggYLGSYGTYS--------T 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 198 ETTSVGL---LDSIGLGKGTVTLED-FDLADAIFSFGHNPGTN--------HPRMLGTLREVSKRGGNIIAINPIKERGL 265
Cdd:cd02751 141 GAAQVILphvVGSDEVYEQGTSWDDiAEHSDLVVLFGANPLKTrqgggggpDHGSYYYLKQAKDAGVRFICIDPRYTDTA 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 266 ERFQDPQAPlemmtngstpisryyfqPKIGGDYALMLGILkhlHEWDKKALasgkpsvFDRNFIAVNTVGFDEMIA---- 341
Cdd:cd02751 221 AVLAAEWIP-----------------IRPGTDVALMLAMA---HTLITEDL-------HDQAFLARYTVGFDEFKDyllg 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 342 ---EVERT-EWADlyKHSGLSPEHLEKLAKLFlESERSIFCWGMGITQHRHGTANVHMLANLLLARGQIGRPGAGLCPVR 417
Cdd:cd02751 274 esdGVPKTpEWAA--EITGVPAETIRALAREI-ASKRTMIAQGWGLQRAHHGEQPAWMLVTLAAMLGQIGLPGGGFGFGY 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 418 GHSNVQGDRTMGINELPSPKLLDNIDRVFgiksprkNGYGVVETI----KAM-AEG------DIKVFIGLGGNFAVATPD 486
Cdd:cd02751 351 GYSNGGGPPRGGAGGPGLPQGKNPVKDSI-------PVARIADALlnpgKEFtANGklktypDIKMIYWAGGNPLHHHQD 423
|
410
....*....|
gi 446292580 487 TAYTQEALRK 496
Cdd:cd02751 424 LNRLIKALRK 433
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
134-503 |
2.28e-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: 2.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 134 DKYVPISWDDAFKLIAQHLHAL---DHPDQAAFY-TSGRASNEAAFLYQL-FVRSFGTNNFPDCSNMC--HETTSVGLLD 206
Cdd:cd02759 68 NKWERISWDEALDEIAEKLAEIkaeYGPESIATAvGTGRGTMWQDSLFWIrFVRLFGSPNLFLSGESCywPRDMAHALTT 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 207 SIGLGKGTVTLEDfdlADAIFSFGHNPGTNHPRMLG-TLREVSKRGGNIIAInpikerglerfqDPQAplemmtNGSTPI 285
Cdd:cd02759 148 GFGLGYDEPDWEN---PECIVLWGKNPLNSNLDLQGhWLVAAMKRGAKLIVV------------DPRL------TWLAAR 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 286 SRYYFQPKIGGDYALMLGILKHLHEWDkkalasgkpsVFDRNFIAVNTVGFDEMIAEVER--TEWADlyKHSGLSPEHLE 363
Cdd:cd02759 207 ADLWLPIRPGTDAALALGMLNVIINEG----------LYDKDFVENWCYGFEELAERVQEytPEKVA--EITGVPAEKIR 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 364 KLAKLFLESERSIFCWGMGITQHRHGTANVHMLANLLLARGQIGRPGAGLCpvrghsnvqgdrtmgineLPSPklldnid 443
Cdd:cd02759 275 KAARLYATAKPACIQWGLAIDQQKNGTQTSRAIAILRAITGNLDVPGGNLL------------------IPYP------- 329
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 444 rvfgiksprkngygvvetikamaegdIKVFIGLGGNFAVATPDTAYTQEALRKCNLTVHV 503
Cdd:cd02759 330 --------------------------VKMLIVFGTNPLASYADTAPVLEALKALDFIVVV 363
|
|
| MopB_DMSOR-BSOR-TMAOR |
cd02769 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
134-412 |
3.28e-14 |
|
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: 76.53 E-value: 3.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 134 DKYVPISWDDAFKLIAQHLH--ALDHPDQAAFYTS------GRASNEAAFLYQL------FVRSFGtnnfpDCSN----- 194
Cdd:cd02769 71 EEFVRVSWDEALDLVAAELKrvRKTYGNEAIFGGSygwssaGRFHHAQSLLHRFlnlaggYVGSVG-----DYSTgaaqv 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 195 -MCHettSVGLLDSIgLGKGT---VTLEDFDLadaIFSFGHNP---------GTNHPRMLGTLREVSKRGGNIIAINPIK 261
Cdd:cd02769 146 iLPH---VVGSMEVY-TEQQTswpVIAEHTEL---VVAFGADPlknaqiawgGIPDHQAYSYLKALKDRGIRFISISPLR 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 262 ERGLERFQDPQAPLEMMTngstpisryyfqpkiggDYALMLGILKHLHEWDKkalasgkpsvFDRNFIAVNTVGFDEMIA 341
Cdd:cd02769 219 DDTAAELGAEWIAIRPGT-----------------DVALMLALAHTLVTEGL----------HDKAFLARYTVGFDKFLP 271
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446292580 342 -------EVERT-EWADlyKHSGLSPEHLEKLAKLFlESERSIFCWGMGITQHRHGTANVHMLANLLLARGQIGRPGAG 412
Cdd:cd02769 272 yllgesdGVPKTpEWAA--AICGIPAETIRELARRF-ASKRTMIMAGWSLQRAHHGEQPHWMAVTLAAMLGQIGLPGGG 347
|
|
| MopB_NADH-Q-OR-NuoG2 |
cd02768 |
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone ... |
108-257 |
4.32e-14 |
|
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: 75.01 E-value: 4.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 108 WLSEQSDFFLEDLG---RLTDP-VRYDaatDKYVPISWDDAFKLIAQHLHALDhPDQAAFYTSGRASNEAAFLYQLFVRS 183
Cdd:cd02768 37 WISDKGRFGYDGLNsrqRLTQPlIKKG---GKLVPVSWEEALKTVAEGLKAVK-GDKIGGIAGPRADLESLFLLKKLLNK 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446292580 184 FGTNNFpDCSNMCHETTSVGLLDSIGLgkGTVTLEDFDLADAIFSFGHNPGTNHPRMLGTLREVSKRGGNIIAI 257
Cdd:cd02768 113 LGSNNI-DHRLRQSDLPADNRLRGNYL--FNTSIAEIEEADAVLLIGSNLRKEAPLLNARLRKAVKKKGAKIAV 183
|
|
| MopB_DmsA-EC |
cd02770 |
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
134-496 |
1.47e-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: 71.20 E-value: 1.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 134 DKYVPISWDDAFKLIAQHLHAL--DHPDQAAFYTSGRASNEAAFLYQlfvrsfgtNNFPDCSNMC------HETTSVG-- 203
Cdd:cd02770 73 GKFVRISWDEALDTIASELKRIieKYGNEAIYVNYGTGTYGGVPAGR--------GAIARLLNLTggylnyYGTYSWAqi 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 204 --LLDSIGLGKGTVTLEDfDLADA--IFSFGHNPGTNhpRMLGT-----LREVSKRGGNIIAINPIKERGLERFQDPQAP 274
Cdd:cd02770 145 ttATPYTYGAAASGSSLD-DLKDSklVVLFGHNPAET--RMGGGgstyyYLQAKKAGAKFIVIDPRYTDTAVTLADEWIP 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 275 LemmtngstpisryyfQPkiGGDYALMLGIlkhlhewdkkALASGKPSVFDRNFIAVNTVGFDE--MIA----------- 341
Cdd:cd02770 222 I---------------RP--GTDAALVAAM----------AYVMITENLHDQAFLDRYCVGFDAehLPEgappnesykdy 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 342 -------EVERT-EWADlyKHSGLSPEHLEKLAKLFLESERSIFCWGMGITQHRHGTANVHMLANLLLARGQIGRPGAGL 413
Cdd:cd02770 275 vlgtgydGTPKTpEWAS--EITGVPAETIRRLAREIATTKPAAILQGWGPQRHANGEQAARAIMMLAAMTGNVGIPGGNT 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 414 CPVRGHSNVQGDRT-MGIN----ELPSPKLLDNIDRVfGIKSPRKNGYGVVETIKAmaegDIKVFIGLGGNFAV-ATPDT 487
Cdd:cd02770 353 GARPGGSAYNGAGLpAGKNpvktSIPCFMWTDAIERG-EEMTADDGGVKGADKLKS----NIKMIWNYAGNTLInQHSDD 427
|
....*....
gi 446292580 488 AYTQEALRK 496
Cdd:cd02770 428 NNTTRALLD 436
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
135-415 |
2.40e-12 |
|
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: 70.02 E-value: 2.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 135 KYVPISWDDAFKLIAQHLHAL--DHPDQAAFYTSGRASNEAAFlyQLFVRSFGTNNFPDCSNMCHETTSVGLLDSIGLGk 212
Cdd:cd02755 70 KFREASWDEALQYIASKLKEIkeQHGPESVLFGGHGGCYSPFF--KHFAAAFGSPNIFSHESTCLASKNLAWKLVIDSF- 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 213 GTVTLEDFDLADAIFSFGHN--PGTNHPRM--LGTLREvskRGGNIIAInpikerglerfqDPQAPlEMMTNGST--PIs 286
Cdd:cd02755 147 GGEVNPDFENARYIILFGRNlaEAIIVVDArrLMKALE---NGAKVVVV------------DPRFS-ELASKADEwiPI- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 287 ryyfqpKIGGDYALMLGILKHLHEWDkkalasgkpsVFDRNFIAVNTVGFDEMIAEVERT--EWADlyKHSGLSPEHLEK 364
Cdd:cd02755 210 ------KPGTDLAFVLALIHVLISEN----------LYDAAFVEKYTNGFELLKAHVKPYtpEWAA--QITDIPADTIRR 271
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 446292580 365 LAKLFLESERSIFcWGMGitqhRHGTANVH--------MLANLLLarGQIGRPGaGLCP 415
Cdd:cd02755 272 IAREFAAAAPHAV-VDPG----WRGTFYSNsfqtrraiAIINALL--GNIDKRG-GLYY 322
|
|
| 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 ... |
122-275 |
1.23e-10 |
|
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: 64.72 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 122 RLTDP-VRYDAAtdkYVPISWDDAFKLIAQHLHALDhpDQAAFYTSGRASNEAAFLYQLFVRSF-GTNNFpDCSNMCHet 199
Cdd:cd02771 54 RLTQPlIRRGGT---LVPVSWNEALDVAAARLKEAK--DKVGGIGSPRASNESNYALQKLVGAVlGTNNV-DHRARRL-- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 200 tsvgLLDSIGLGKG-TVTLEDFDLADAIFSFGHNPGTNHPRMLGTLREVSKRGGNIIAINPIKERGL-----ERFQDPQA 273
Cdd:cd02771 126 ----IAEILRNGPIyIPSLRDIESADAVLVLGEDLTQTAPRIALALRQAARRKAVELAALSGIPKWQdaavrNIAQGAKS 201
|
..
gi 446292580 274 PL 275
Cdd:cd02771 202 PL 203
|
|
| MopB_Arsenate-R |
cd02757 |
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ... |
103-660 |
2.81e-10 |
|
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: 63.61 E-value: 2.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 103 GHTVSWLSEQSDFFLEDLGRlTDPVRYDAATDKYVPISWDDAFKLIAQHLHALDHPDQAA--FYTSGRASNEAAFLYQLF 180
Cdd:cd02757 44 GHLGLQQVYDPDRILYPMKR-TNPRKGRDVDPKFVPISWDEALDTIADKIRALRKENEPHkiMLHRGRYGHNNSILYGRF 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 181 VRSFGTNNFPDCSNMCHETTSVG--LLDSiGLGKgtvtlEDFDLADA--IFSFGHNP-GTNH--PRMLGTLREVSKRgGN 253
Cdd:cd02757 123 TKMIGSPNNISHSSVCAESEKFGryYTEG-GWDY-----NSYDYANAkyILFFGADPlESNRqnPHAQRIWGGKMDQ-AK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 254 IIAINPikergleRFqdpqaplemmtNGSTPISRYYFQPKIGGDYALMLGIlKH--LHE--WDKK----------ALASG 319
Cdd:cd02757 196 VVVVDP-------RL-----------SNTAAKADEWLPIKPGEDGALALAI-AHviLTEglWDKDfvgdfvdgknYFKAG 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 320 KPsVFDRNFIAVNTVGFDEMI-AEV-ERT-EWADlyKHSGLSPEHLEKLAKLFLESERSIFCW-GMGITQHRHGTANVHM 395
Cdd:cd02757 257 ET-VDEESFKEKSTEGLVKWWnLELkDYTpEWAA--KISGIPAETIERVAREFATAAPAAAAFtWRGATMQNRGSYNSMA 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 396 LANLLLARGQIGRPGaGLCPvrghsnvqgdrtmginelpspklldnidrvfgiksprkngygvvetikAMAEGDIKVFIG 475
Cdd:cd02757 334 CHALNGLVGSIDSKG-GLCP------------------------------------------------NMGVPKIKVYFT 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 476 LGGNFAVATPDTAYTQEALRKCNLTVHVATKLNR-SHLVcgkdALILPclgrteideQLHGPQAITVEDSMSNVHLSAGR 554
Cdd:cd02757 365 YLDNPVFSNPDGMSWEEALAKIPFHVHLSPFMSEtTYFA----DIVLP---------DGHHFERWDVMSQENNLHPWLSI 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 555 NTPISKNILSEpdivarMAEAVLPeSQIKWKWYIESYDRIRDSIadvFDEFHDfnLRVYKPGGFHLEhpanqHIWNTKSG 634
Cdd:cd02757 432 RQPVVKSLGEV------REETEIL-IELAKKLDPKGSDGMKRYA---PGQFKD--PETGKNNRWEFE-----NVFPTETG 494
|
570 580
....*....|....*....|....*.
gi 446292580 635 KAQFLITPLEEVYADKENQYAAAYTE 660
Cdd:cd02757 495 KFEFYSETLKKYLQNHADKKKVSWDE 520
|
|
| MopB_FmdB-FwdB |
cd02761 |
The MopB_FmdB-FwdB CD contains the molybdenum/tungsten formylmethanofuran dehydrogenases, ... |
137-424 |
3.12e-10 |
|
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: 63.12 E-value: 3.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 137 VPISWDDAFKLIAQHLHALDHPdqaAFYTSGRASNEA-AFLYQLFVRSFGTnnFPDCSNMCHETTSVGLLDSiglGKGTV 215
Cdd:cd02761 52 KPVSLEEAIEKAAEILKEAKRP---LFYGLGTTVCEAqRAGIELAEKLGAI--IDHAASVCHGPNLLALQDS---GWPTT 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 216 TL-EDFDLADAIFSFGHNPGTNHPRMLgtlrevSKRggniiAINPikeRGLERFQDPQA-------PLEMMTNGstpISR 287
Cdd:cd02761 124 TLgEVKNRADVIVYWGTNPMHAHPRHM------SRY-----SVFP---RGFFREGGREDrtlivvdPRKSDTAK---LAD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 288 YYFQPKIGGDYALMLGILkhlhewdkkALASGKPSVFDrnfiavnTVGfdemiaevertewadlykhsGLSPEHLEKLAK 367
Cdd:cd02761 187 IHLQIDPGSDYELLAALR---------ALLRGAGLVPD-------EVA--------------------GIPAETILELAE 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 446292580 368 LFLESERSIFCWGMGITQHRHGTANVHMLANLLLARGQIGRpgAGLCPVRGHSNVQG 424
Cdd:cd02761 231 RLKNAKFGVIFWGLGLLPSRGAHRNIEAAIRLVKALNEYTK--FALLPLRGHYNVRG 285
|
|
| MopB_2 |
cd02763 |
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
122-410 |
6.90e-10 |
|
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: 62.54 E-value: 6.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 122 RLTDPVRY--DAATDKYVPISWDDAFKLIAQHLHAL--DHPDQAAFYTsGRASNEAafLYQLFVRSFGTNNFPDCSNMCH 197
Cdd:cd02763 54 RLTKPLLRkgPRGSGQFEEIEWEEAFSIATKRLKAAraTDPKKFAFFT-GRDQMQA--LTGWFAGQFGTPNYAAHGGFCS 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 198 ETTSVGLLDSIGLGKGTVTLEDFDLADAIFSFG----HNpgtNHPRMLGtLREVSKRGGNIIAINPIKerglerfqdpqa 273
Cdd:cd02763 131 VNMAAGGLYSIGGSFWEFGGPDLEHTKYFMMIGvaedHH---SNPFKIG-IQKLKRRGGKFVAVNPVR------------ 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 274 plemmtNGSTPISRYYFQPKIGGDYALMLGILKHLHEWDkkalasgkpsVFDRNFIavntVGFDEMIAEVERT-EWADly 352
Cdd:cd02763 195 ------TGYAAIADEWVPIKPGTDGAFILALAHELLKAG----------LIDWEFL----KRYTNAAELVDYTpEWVE-- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 353 KHSGLSPEHLEKLAKLFLESERS---------IFCWGM----------------GITQHRHGTANVHMLANLLLARGQIG 407
Cdd:cd02763 253 KITGIPADTIRRIAKELGVTARDqpielpiawTDVWGRkhekitgrpvsfhamrGIAAHSNGFQTIRALFVLMMLLGTID 332
|
...
gi 446292580 408 RPG 410
Cdd:cd02763 333 RPG 335
|
|
| MopB_Arsenite-Ox |
cd02756 |
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the ... |
122-419 |
2.59e-09 |
|
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the electrons obtained from the oxidation of arsenite towards the soluble periplasmic electron carriers cytochrome c and/or amicyanin. Arsenite oxidase is a heterodimeric enzyme containing a large and a small subunit. The large catalytic subunit harbors the molybdopterin cofactor and the [3Fe-4S] cluster; and the small subunit belongs to the structural class of the Rieske proteins. The small subunit is not included in this alignment. Members of MopB_Arsenite-Ox CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239157 [Multi-domain] Cd Length: 676 Bit Score: 60.57 E-value: 2.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 122 RLTDPVRYdaATDKYVPISWDDAFKLIAQHLHAL---DHPDQAAFYT--------SGRASNEAA---FLYQLFVRSFGTN 187
Cdd:cd02756 117 RLTTPLVR--RGGQLQPTTWDDAIDLVARVIKGIldkDGNDDAVFASrfdhggggGGFENNWGVgkfFFMALQTPFVRIH 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 188 NFPDCSNMCHETTSVglldsiGLGKGTVTLEDFDLADAIFSFGHNP---GTNH--PRMLGTLR--EVSKR---------- 250
Cdd:cd02756 195 NRPAYNSEVHATREM------GVGELNNSYEDARLADTIVLWGNNPyetQTVYflNHWLPNLRgaTVSEKqqwfppgepv 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 251 -GGNIIAINPIKERGLERFQDPQAPLEMMtngstpisryYFQPKIGGDYALMLGILKHLHEwdkkalasgkpsvfdrnfi 329
Cdd:cd02756 269 pPGRIIVVDPRRTETVHAAEAAAGKDRVL----------HLQVNPGTDTALANAIARYIYE------------------- 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 330 avntvGFDEMIAEVERTewadlykhSGLSPEHLEKLAKLFLESE------RSIFCWGMGITQHRHGTANVHMLANLLLAR 403
Cdd:cd02756 320 -----SLDEVLAEAEQI--------TGVPRAQIEKAADWIAKPKeggyrkRVMFEYEKGIIWGNDNYRPIYSLVNLAIIT 386
|
330
....*....|....*.
gi 446292580 404 GQIGRPGAGLCPVRGH 419
Cdd:cd02756 387 GNIGRPGTGCVRQGGH 402
|
|
| PRK15102 |
PRK15102 |
trimethylamine-N-oxide reductase TorA; |
297-413 |
3.18e-09 |
|
trimethylamine-N-oxide reductase TorA;
Pssm-ID: 237909 [Multi-domain] Cd Length: 825 Bit Score: 60.46 E-value: 3.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 297 DYALMLGILkhlHEWDKKALasgkpsvFDRNFIAVNTVGFDEMIA-------EVERT-EWADlyKHSGLSPEHLEKLAKL 368
Cdd:PRK15102 283 DVPLMLALA---HTLYSENL-------YDKKFIDNYCLGFEQFLPyllgekdGVPKTpEWAE--KICGIDAETIRELARQ 350
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 446292580 369 fLESERSIFCWGMGITQHRHGTANVHMLANLLLARGQIGRPGAGL 413
Cdd:PRK15102 351 -MAKGRTQIIAGWCIQRQQHGEQPYWMGAVLAAMLGQIGLPGGGI 394
|
|
| PRK13532 |
PRK13532 |
nitrate reductase catalytic subunit NapA; |
122-412 |
1.09e-08 |
|
nitrate reductase catalytic subunit NapA;
Pssm-ID: 237416 [Multi-domain] Cd Length: 830 Bit Score: 58.76 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 122 RLTDPV------RYDAaTDKYVPISWDDAFKLIAQHL-HALDH--PDQAAFYTSGR--------ASneaaflyQLFVRSF 184
Cdd:PRK13532 97 RLTQPLlrmkdgKYDK-EGEFTPVSWDQAFDVMAEKFkKALKEkgPTAVGMFGSGQwtiwegyaAS-------KLMKAGF 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 185 GTNNFPDCSNMCHETTSVGLLDSIGLGKGTVTLEDFDLADAIFSFGHNPGTNHP----RMlgTLREVSKRGGNIIAINPI 260
Cdd:PRK13532 169 RSNNIDPNARHCMASAVVGFMRTFGIDEPMGCYDDIEAADAFVLWGSNMAEMHPilwsRV--TDRRLSNPDVKVAVLSTF 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 261 KERGLER------FQdPQAPLEMMTNgstpISRYYFQP-KIGGDYalmlgILKHL----------------HEWDKKALA 317
Cdd:PRK13532 247 EHRSFELadngiiFT-PQTDLAILNY----IANYIIQNnAVNWDF-----VNKHTnfrkgatdigyglrptHPLEKAAKN 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 318 SGKPSvfdrnfiAVNTVGFDEMIAEVERTEWADLYKHSGLSPEHLEKLAKLFLESERSIFC-WGMGITQHRHGT-ANvHM 395
Cdd:PRK13532 317 PGTAG-------KSEPISFEEFKKFVAPYTLEKTAKMSGVPKEQLEQLAKLYADPNRKVVSfWTMGFNQHTRGVwAN-NL 388
|
330
....*....|....*..
gi 446292580 396 LANLLLARGQIGRPGAG 412
Cdd:PRK13532 389 VYNIHLLTGKISTPGNG 405
|
|
| MopB_NDH-1_NuoG2 |
cd02772 |
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase ... |
108-262 |
6.49e-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: 6.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 108 WLSEQSDFFLEDLG---RLTDP-VRYDaatDKYVPISWDDAFKLIAQHLHAL--DH-PDQAAFYTSGRASNEAAFLYQLF 180
Cdd:cd02772 37 WLSDRDRFSYEGLNsedRLTKPmIKKD---GQWQEVDWETALEYVAEGLSAIikKHgADQIGALASPHSTLEELYLLQKL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 181 VRSFGTNNFP------DCSnmchetTSVGLLDSIGLGkgtVTLEDFDLADAIFSFGHNPGTNHPRMLGTLREVSKRGGNI 254
Cdd:cd02772 114 ARGLGSDNIDhrlrqsDFR------DDAKASGAPWLG---MPIAEISELDRVLVIGSNLRKEHPLLAQRLRQAVKKGAKL 184
|
....*...
gi 446292580 255 IAINPIKE 262
Cdd:cd02772 185 SAINPADD 192
|
|
| MopB_CT |
cd02775 |
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a ... |
671-769 |
3.52e-07 |
|
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: 48.86 E-value: 3.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 671 SHDQYNTTLYGLDDRYRGVFGqRRVLFMNQADIDEAGFEANQWVDIESVFSDGVKRIVHSFRivpynIPRGSLAAYYP-- 748
Cdd:cd02775 1 LRDHFHSGTRTRNPWLRELAP-EPVVEINPEDAAALGIKDGDLVRVESRRGSVVLRAKVTDG-----VPPGVVFLPHGwg 74
|
90 100
....*....|....*....|....*...
gi 446292580 749 -------ETNPLVAlSSHDKYAKIPASK 769
Cdd:cd02775 75 hrggrggNANVLTP-DALDPPSGGPAYK 101
|
|
| Molydop_binding |
pfam01568 |
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
664-772 |
2.67e-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: 46.88 E-value: 2.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 664 YTLMTTRSHDQYNTTLYGLDDRYRGVFGQRRVLfMNQADIDEAGFEANQWVDIESVFSDgVKRIVhsfrIVPYNIPRGSL 743
Cdd:pfam01568 1 LYLITGRVLGQYHSQTRTRRVLRLAKPEPEVVE-IHPEDAAALGIKDGDLVEVTSRRGS-VVVRA----KVTDRVRPGVV 74
|
90 100 110
....*....|....*....|....*....|....*..
gi 446292580 744 AAYYPE--------TNPLVALSShDKYAKIPASKSVP 772
Cdd:pfam01568 75 FMPFGWwyeprggnANALTDDAT-DPLSGGPEFKTCA 110
|
|
| MopB_Res-Cmplx1_Nad11 |
cd02773 |
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone ... |
108-233 |
1.29e-04 |
|
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone oxidoreductase/respiratory complex I/NADH dehydrogenase-1(NDH-1) of eukaryotes and the Nqo3/G subunit of alphaproteobacteria NDH-1. The NADH-quinone oxidoreductase is the first energy-transducting complex in the respiratory chains of many prokaryotes and eukaryotes. Mitochondrial complex I and its bacterial counterpart, NDH-1, function as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. The nad11 gene codes for the largest (75 kDa) subunit of the mitochondrial NADH:ubiquinone oxidoreductase, it constitutes the electron input part of the enzyme, or the so-called NADH dehydrogenase fragment. In Paracoccus denitrificans, this subunit is encoded by the nqo3 gene, and is part of the 14 distinct subunits constituting the 'minimal' functional enzyme. The Nad11/Nqo3 subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain belongs to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239174 [Multi-domain] Cd Length: 375 Bit Score: 44.95 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 108 WLSEQSDFFLEDLG--RLTDP-VRydaATDKYVPISWDDAFKLIAQHLHALDhPDQAAFYTSGRASNEAAFLYQLFVRSF 184
Cdd:cd02773 37 WISDKTRFAYDGLKrqRLDKPyIR---KNGKLKPATWEEALAAIAKALKGVK-PDEIAAIAGDLADVESMVALKDLLNKL 112
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 446292580 185 GTNNFpdcsnMCHETTSVGLLDSIGLGKGTVTLEDFDLADAIFSFGHNP 233
Cdd:cd02773 113 GSENL-----ACEQDGPDLPADLRSNYLFNTTIAGIEEADAVLLVGTNP 156
|
|
| PRK07860 |
PRK07860 |
NADH dehydrogenase subunit G; Validated |
122-267 |
1.99e-04 |
|
NADH dehydrogenase subunit G; Validated
Pssm-ID: 236118 [Multi-domain] Cd Length: 797 Bit Score: 44.94 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 122 RLTDP-VRYDaaTDKYVPISWDDAFKLIAQHLHALDhpDQAAFYTSGRASNEAAFLYQLFVR-SFGTNNFpDCSNMCHET 199
Cdd:PRK07860 278 RITTPlVRDE--DGELEPASWSEALAVAARGLAAAR--GRVGVLVGGRLTVEDAYAYAKFARvALGTNDI-DFRARPHSA 352
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 200 TSVGLLDSIGLGKG-TVTLEDFDLADAIFSFGHNPGTNHPRMLGTLRE-VSKRGGNIIAINPIKERGLER 267
Cdd:PRK07860 353 EEADFLAARVAGRGlGVTYADLEKAPAVLLVGFEPEEESPIVFLRLRKaARKHGLKVYSIAPFATRGLEK 422
|
|
| MopB_Phenylacetyl-CoA-OR |
cd02760 |
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large ... |
121-325 |
7.87e-04 |
|
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large subunit (PadB2), and other related proteins. The phenylacetyl-CoA:acceptor oxidoreductase has been characterized as a membrane-bound molybdenum-iron-sulfur enzyme involved in anaerobic metabolism of phenylalanine in the denitrifying bacterium Thauera aromatica. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239161 [Multi-domain] Cd Length: 760 Bit Score: 43.03 E-value: 7.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 121 GRLTDPvrydaatdKYVPISWDDAFKLIAQHLHALDH---------PDQAAFYTSGRASNEAAFLYQLFVRSFGTNNFPD 191
Cdd:cd02760 71 GRNEDP--------GFVPISWDEALDLVAAKLRRVREkglldekglPRLAATFGHGGTPAMYMGTFPAFLAAWGPIDFSF 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 192 CSNMCHETTSVGLLDSIGLGKGTVTLEDFDLADAIFSFGHNPgtnhprmlgtlrEVSKRGGNIIAINPIKERGLERFQdp 271
Cdd:cd02760 143 GSGQGVKCVHSEHLYGEFWHRAFTVAADTPLANYVISFGSNV------------EASGGPCAVTRHADARVRGYKRVQ-- 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446292580 272 qapLEMMTNGSTPISRYYFQPKIGGDYALMLGILK-HLHEW----------------------DKKAL---ASGKPSVFD 325
Cdd:cd02760 209 ---VEPHLSVTGACSAEWVPIRPKTDPAFMFAMIHvMVHEQglgkldvpflrdrtsspylvgpDGLYLrdaATGKPLVWD 285
|
|
| |
