|
Name |
Accession |
Description |
Interval |
E-value |
| Fdhalpha-like |
TIGR01701 |
oxidoreductase alpha (molybdopterin) subunit; This model represents a well-defined clade of ... |
10-759 |
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: 898.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 10 AGGWGALKSTAHHLFKSNNVAKNISNLLRTNQDHGFDCPGCAWGEK-HVPGRFRFCENGAKAVNWEATTRRVGGEFFQQY 88
Cdd:TIGR01701 2 AGGWGAVKSVALGKVKPMHIRQTLKLLLTLNKPEGYDCPGCAWGVSpQTLAGLEFCENGAKAIAWETTPRTIDPEFFAEH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 89 SVSWLNKQSDYFLEYQGRLAEPVRYNAETDHYEPISWDDAFALIARHLNQLDnPNQAEFYTSGRASNEAAFLYQLFARRF 168
Cdd:TIGR01701 82 SVSELRTLDSHELEKLGRLTYPLSLRPGSDHYTPISWDDAYQEIAAKLNSLD-PKQVAFYTSGRTSNEAAYLYQLFARSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 169 GTNNFPDCSNMCHEATSVALSRTIGIGKGTVTIDDFEEADAIFLFGQNPGTNHPRMLETLASAYKRGARVVAFNNLKERG 248
Cdd:TIGR01701 161 GSNNLPDCSNMCHEPSSVALKRSIGIGKGSVNLEDFEHTDCLVFIGSNAGTNHPRMLKYLYAAKKRGAKIIAINPLRERG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 249 LERFTNPQNPFEMLSNGSTPTTSDYFMPKLGGDMAAVRGLVKILLGRHEEAQArgeSVFDLAFIEQHTEGLDAYLELVRA 328
Cdd:TIGR01701 241 LERFWIPQIPESMLTGGGTQISSEYYQVRIGGDIALFNGVMKLLIEAEDAQPG---SLIDHEFIANHTNGFDELRRHVLQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 329 TPWEHIEQQSGLSQAELTQAADIYQNANRVIVTWAMGVTQHKHSVATIQELVNLQLLFGQVGKDGAGLCPVRGHSNVQGD 408
Cdd:TIGR01701 318 LNWNDIERSSGLSQEEILEFAKLLANSRRVVFCWAMGLTQHAHGVDNISQVANLALLRGNIGKPGAGVCPIRGHSNVQGD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 409 RTVGINEKPPAALLENIEKALGFTPPKEHGHNVVNALQAMSRGESKVFIGLGGNLVAAAPDTELVAKAMRNCELTVNIAT 488
Cdd:TIGR01701 398 RTMGITEKPEEEFLARLSQIYGFTPPDWPGDTTVAMIEAILTGKVRAFICLGGNFLEAMPDTAAIERALRQLDLRVHVAT 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 489 KLNRSHVNPGKDSLILPCLGRTDVDMQAAGPQKVTVEDSFSMVHASSGRVDMTGEQMRSEPAIIAGMAKATLGDnNPVNW 568
Cdd:TIGR01701 478 KLNRSHVLAKEEALILPVLGRYEQDGQGTGKQAVSVESSMRMVHFSRGILKPRGAELRSEWAIIAEIAKALLPE-TPVAW 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 569 QSMADNYDNIRDLIEDIIPGFTNFNQRIEGPRGFYLGNSARDL-NWKTASGKAQISSNALPQsiIPVETEQLTKkpvFVL 647
Cdd:TIGR01701 557 EILVDTYDQIRDAIAATNPGYDDINHRKRRPDGFQLPGAALCErKFPTPDGKANFIVIPLPE--FRVPTGHEFE---LVL 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 648 QTMRSHDQYNTTVYGFDDRYRGVFGERNVIFMNAKDIDKQGLQAGDLVDIETLWTDDVKRQIIGFKIVAFDIPKGNVAAY 727
Cdd:TIGR01701 632 VTLRSHDQFNTTIYGEDDRYRGVDGHRRVVFMNETDIKKLGLRNGERVDVYNQYGDGQKRKFDNLRIVFYDTPTGNAAAY 711
|
730 740 750
....*....|....*....|....*....|..
gi 521102444 728 FPEANALIPLGSKGDLSDTPTSKSIAVVITPT 759
Cdd:TIGR01701 712 YPEANPLLPLDHHDPQSKTPEYKTIPVRLEAS 743
|
|
| MopB_ydeP |
cd02767 |
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
44-621 |
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: 890.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 44 GFDCPGCAWGE-KHVPGRFRFCENGAKAVNWEATTRRVGGEFFQQYSVSWLNKQSDYFLEYQGRLAEPVRYNAETDHYEP 122
Cdd:cd02767 1 GFDCPGCAWGDpGQKLHGFEFCENGAKALAWETTPKRVTPEFFALHSVSELRTWSDYELEHLGRLTYPMRYDAGSDHYRP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 123 ISWDDAFALIARHLNQLDnPNQAEFYTSGRASNEAAFLYQLFARRFGTNNFPDCSNMCHEATSVALSRTIGIGKGTVTID 202
Cdd:cd02767 81 ISWDEAFAEIAARLRALD-PDRAAFYTSGRASNEAAYLYQLFARAYGTNNLPDCSNMCHEPSSVGLKKSIGVGKGTVSLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 203 DFEEADAIFLFGQNPGTNHPRMLETLASAYKRGARVVAFNNLKERGLERFTNPQNPFEMLSnGSTPTTSDYFMPKLGGDM 282
Cdd:cd02767 160 DFEHTDLIFFIGQNPGTNHPRMLHYLREAKKRGGKIIVINPLREPGLERFANPQNPESMLT-GGTKIADEYFQVRIGGDI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 283 AAVRGLVKILLgrheEAQARGESVFDLAFIEQHTEGLDAYLELVRATPWEHIEQQSGLSQAELTQAADIYQNANRVIVTW 362
Cdd:cd02767 239 ALLNGMAKHLI----ERDDEPGNVLDHDFIAEHTSGFEEYVAALRALSWDEIERASGLSREEIEAFAAMYAKSERVVFVW 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 363 AMGVTQHKHSVATIQELVNLQLLFGQVGKDGAGLCPVRGHSNVQGDRTVGINEKPPAALLENIEKALGFTPPKEHGHNVV 442
Cdd:cd02767 315 GMGITQHAHGVDNVRAIVNLALLRGNIGRPGAGLMPIRGHSNVQGDRTMGITEKPFPEFLDALEEVFGFTPPRDPGLDTV 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 443 NALQAMSRGESKVFIGLGGNLVAAAPDTELVAKAMRNCELTVNIATKLNRSHVNPGKDSLILPCLGRTDVDMQAAGPQKV 522
Cdd:cd02767 395 EAIEAALEGKVKAFISLGGNFAEAMPDPAATEEALRRLDLTVHVATKLNRSHLVHGEEALILPCLGRTEIDMQAGGAQAV 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 523 TVEDSFSMVHASSGRVDMTGEQMRSEPAIIAGMAKATLGdNNPVNWQSMADNYDNIRDLIEDIIP-GFTNFNQRIEGPRG 601
Cdd:cd02767 475 TVEDSMSMTHTSRGRLKPASRVLLSEEAIVAGIAGARLG-EAKPEWEILVEDYDRIRDEIAAVIYeGFADFNQRGDQPGG 553
|
570 580
....*....|....*....|
gi 521102444 602 FYLGNSARDLNWKTASGKAQ 621
Cdd:cd02767 554 FHLPNGARERKFNTPSGKAQ 573
|
|
| PRK09939 |
PRK09939 |
acid resistance putative oxidoreductase YdeP; |
3-759 |
0e+00 |
|
acid resistance putative oxidoreductase YdeP;
Pssm-ID: 182156 [Multi-domain] Cd Length: 759 Bit Score: 809.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 3 IKEYTGSAGGWGALKSTAHHLFKSNNVAKNISNLLRTNQDHGFDCPGCAWGEKHVPGRFRFCENGAKAVNWEATTRRVGG 82
Cdd:PRK09939 5 IESYQGAAGGWGAVKSVANAVRKQMDIRQDVIAMFDMNKPEGFDCPGCAWPDPKHSASFDICENGAKAIAWEVTDKQVNA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 83 EFFQQYSVSWLNKQSDYFLEYQGRLAEPVRYNAETDHYEPISWDDAFALIARHLNQLDNPNQAEFYTSGRASNEAAFLYQ 162
Cdd:PRK09939 85 SFFAENTVQSLLTWGDHELEAAGRLTQPLKYDAVSDCYKPLSWQQAFDEIGARLQSYSDPNQVEFYTSGRTSNEAAFLYQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 163 LFARRFGTNNFPDCSNMCHEATSVALSRTIGIGKGTVTIDDFEEADAIFLFGQNPGTNHPRMLETLASAYKRGARVVAFN 242
Cdd:PRK09939 165 LFAREYGSNNFPDCSNMCHEPTSVGLAASIGVGKGTVLLEDFEKCDLVICIGHNPGTNHPRMLTSLRALVKRGAKMIAIN 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 243 NLKERGLERFTNPQNPFEMLSNGSTPTTSDYFMPKLGGDMAAVRGLVKILLGRHEEAQARGE-SVFDLAFIEQHTEGLDA 321
Cdd:PRK09939 245 PLQERGLERFTAPQNPFEMLTNSETQLASAYYNVRIGGDMALLKGMMRLLIERDDAASAAGRpSLLDDEFIQTHTVGFDE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 322 YLELVRATPWEHIEQQSGLSQAELTQAADIYQNANRVIVTWAMGVTQHKHSVATIQELVNLQLLFGQVGKDGAGLCPVRG 401
Cdd:PRK09939 325 LRRDVLNSEWKDIERISGLSQTQIAELADAYAAAERTIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGICPLRG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 402 HSNVQGDRTVGINEKPPAALLENIEKALGFTPPKEHGHNVVNALQAMSRGESKVFIGLGGNLVAAAPDTELVAKAMRNCE 481
Cdd:PRK09939 405 HSNVQGDRTVGITEKPSAEFLARLGERYGFTPPHAPGHAAIASMQAICTGQARALICMGGNFALAMPDREASAVPLTQLD 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 482 LTVNIATKLNRSHVNPGKDSLILPCLGRTDVDMQAAGPQKVTVEDSFSMVHASSGRVDMTGEQMRSEPAIIAGMAKATLg 561
Cdd:PRK09939 485 LAVHVATKLNRSHLLTARHSYILPVLGRSEIDMQKSGAQAVTVEDSMSMIHASRGVLKPAGVMLKSECAVVAGIAQAAL- 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 562 DNNPVNWQSMADNYDNIRDLIEDIIPGFTNFNQRIEGPRGFYLGNSARDLNWKTASGKAQ-ISSNAL---PQSIIPVEte 637
Cdd:PRK09939 564 PQSVVAWEYLVEDYDRIRNDIEAVLPEFADYNQRIRHPGGFHLINAAAERRWMTPSGKANfITSKGLledPSSAFNSK-- 641
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 638 qltkkpvFVLQTMRSHDQYNTTVYGFDDRYRGVFGERNVIFMNAKDIDKQGLQAGDLVDIETLWTDDVK--RQIIGFKIV 715
Cdd:PRK09939 642 -------LVMATVRSHDQYNTTIYGMDDRYRGVFGQRDVVFMSAKQAKICRVKNGERVNLIALTPDGKRssRRMDRLKVV 714
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 521102444 716 AFDIPKGNVAAYFPEANALIPLGSKGDLSDTPTSKSIAVVITPT 759
Cdd:PRK09939 715 IYPMADRSLVTYFPESNHMLTLDNHDPLSGIPGYKSIPVELEPS 758
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
1-758 |
4.57e-161 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 482.04 E-value: 4.57e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 1 MSIKEYTGSAGGWGALKSTAHHLFKSNnvaknisnllrtnqdhgfdCPGCAWGekhvpgrfrfCENGAKAVNWEATtrRV 80
Cdd:COG0243 1 MSLRDFKAAGAGAAALEAAGTKTVKTT-------------------CPGCGVG----------CGLGVKVEDGRVV--RV 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 81 GGEffQQYSVSWLN-----KQSDYFLEYQGRLAEPVRYNAE--TDHYEPISWDDAFALIARHLNQL---DNPNQAEFYTS 150
Cdd:COG0243 50 RGD--PDHPVNRGRlcakgAALDERLYSPDRLTYPMKRVGPrgSGKFERISWDEALDLIAEKLKAIideYGPEAVAFYTS 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 151 G----RASNEAAFLYQLFARRFGTNNFPDCSNMCHEATSVALSRTIGIGKGTVTIDDFEEADAIFLFGQNPGTNHPRMLE 226
Cdd:COG0243 128 GgsagRLSNEAAYLAQRFARALGTNNLDDNSRLCHESAVAGLPRTFGSDKGTVSYEDLEHADLIVLWGSNPAENHPRLLR 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 227 TLASAYK-RGARVVAFNNLKERglerftnpqnpfemlsngsTPTTSDYFMP-KLGGDMAAVRGLVKILLgrheeaqARGe 304
Cdd:COG0243 208 RLREAAKkRGAKIVVIDPRRTE-------------------TAAIADEWLPiRPGTDAALLLALAHVLI-------EEG- 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 305 sVFDLAFIEQHTEGLDAYLELVRATPWEHIEQQSGLSQAELTQAADIYQNANRVIVTWAMGVTQHKHSVATIQELVNLQL 384
Cdd:COG0243 261 -LYDRDFLARHTVGFDELAAYVAAYTPEWAAEITGVPAEDIRELAREFATAKPAVILWGMGLQQHSNGTQTVRAIANLAL 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 385 LFGQVGKDGAGLCPVRGHsnvqgdrtvginekppaALLEniekalGFTPPkehghnvvnalqamsrgeSKVFIGLGGNLV 464
Cdd:COG0243 340 LTGNIGKPGGGPFSLTGE-----------------AILD------GKPYP------------------IKALWVYGGNPA 378
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 465 AAAPDTELVAKAMRNCELTVNIATKLNRSHVNpgkDSLILPCLGRTDVDMQAagpqkVTVEDsfSMVHASSGRVDMTGEq 544
Cdd:COG0243 379 VSAPDTNRVREALRKLDFVVVIDTFLTETARY---ADIVLPATTWLERDDIV-----TNSED--RRVHLSRPAVEPPGE- 447
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 545 MRSEPAIIAGMAKAtLGDNNPVNWQSMADNYdnIRDLIEDIIPGFTNFNQ-RIEGPRGFYLGNSAR---DLNWKTASGKA 620
Cdd:COG0243 448 ARSDWEIFAELAKR-LGFEEAFPWGRTEEDY--LRELLEATRGRGITFEElREKGPVQLPVPPEPAfrnDGPFPTPSGKA 524
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 621 QISSN-----ALPQSIIPVET-EQLTKKPVFVLQTMRSHDQYNTTVYGfDDRYRGVFGeRNVIFMNAKDIDKQGLQAGDL 694
Cdd:COG0243 525 EFYSEtlalpPLPRYAPPYEGaEPLDAEYPLRLITGRSRDQWHSTTYN-NPRLREIGP-RPVVEINPEDAAALGIKDGDL 602
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521102444 695 VDIETLWtddvkRQIIGFKIVAFDIPKGNVAAYF-----------PEANALIPLGSkGDLSDTPTSKSIAVVITP 758
Cdd:COG0243 603 VRVESDR-----GEVLARAKVTEGIRPGVVFAPHgwwyepaddkgGNVNVLTPDAT-DPLSGTPAFKSVPVRVEK 671
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
100-758 |
2.44e-87 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 289.86 E-value: 2.44e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 100 FLEYQGRLAEP-VRynaETDHYEPISWDDAFALIARHLNQL---DNPNQAEFYTSGRASNEAAFLYQLFAR-RFGTNNFP 174
Cdd:COG3383 55 FVNSPDRLTTPlIR---RGGEFREVSWDEALDLVAERLREIqaeHGPDAVAFYGSGQLTNEENYLLQKLARgVLGTNNID 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 175 DCSNMCHEATSVALSRTIGIGKGTVTIDDFEEADAIFLFGQNPGTNHPRMLETLASAYKRGARVVAFNnlkerglerftn 254
Cdd:COG3383 132 NNARLCMASAVAGLKQSFGSDAPPNSYDDIEEADVILVIGSNPAEAHPVLARRIKKAKKNGAKLIVVD------------ 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 255 pqnPFEmlsngsTPTT--SDYFMP-KLGGDMAAVRGLVKILLGrheeaqargESVFDLAFIEQHTEGLDAYLELVRATPW 331
Cdd:COG3383 200 ---PRR------TETArlADLHLQiKPGTDLALLNGLLHVIIE---------EGLVDEDFIAERTEGFEELKASVAKYTP 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 332 EHIEQQSGLSQAELTQAADIYQNANRVIVTWAMGVTQHKHSVATIQELVNLQLLFGQVGKDGAGLCPVRGHSNVQGDRTV 411
Cdd:COG3383 262 ERVAEITGVPAEDIREAARLIAEAKRAMILWGMGVNQHTQGTDNVNAIINLALATGNIGRPGTGPFPLTGQNNVQGGRDM 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 412 GI--NEKP-------PAAlLENIEKALGFTP-PKEHGHNVVNALQAMSRGESKVFIGLGGNLVAAAPDTELVAKAMRNCE 481
Cdd:COG3383 342 GAlpNVLPgyrdvtdPEH-RAKVADAWGVPPlPDKPGLTAVEMFDAIADGEIKALWIIGENPAVSDPDANHVREALEKLE 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 482 L----------TVNIAtklnrsHVnpgkdslILPclgrtdvdmqAAG-PQK---VT-VEDSFSMVHASsgrVDMTGEqMR 546
Cdd:COG3383 421 FlvvqdiflteTAEYA------DV-------VLP----------AASwAEKdgtFTnTERRVQRVRKA---VEPPGE-AR 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 547 SEPAIIAGMAKAtLGdnNPVNWQSMADNYDNIRDLiediIPGFTNFN-QRIEGPRGFYLGNSARD---------LNWKTA 616
Cdd:COG3383 474 PDWEIIAELARR-LG--YGFDYDSPEEVFDEIARL----TPDYSGISyERLEALGGVQWPCPSEDhpgtprlftGRFPTP 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 617 SGKAQIssnaLPQSIIPVETEQLTKKPvFVLQTMRSHDQYNT-TVYGFDDRYRGVFGErNVIFMNAKDIDKQGLQAGDLV 695
Cdd:COG3383 547 DGKARF----VPVEYRPPAELPDEEYP-LVLTTGRLLDQWHTgTRTRRSPRLNKHAPE-PFVEIHPEDAARLGIKDGDLV 620
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521102444 696 DIETlwtddvKR-QIIGFKIVAFDIPKGNVAAYF----PEANALIplGSKGD-LSDTPTSKSIAVVITP 758
Cdd:COG3383 621 RVSS------RRgEVVLRARVTDRVRPGTVFMPFhwgeGAANALT--NDALDpVSKQPEYKACAVRVEK 681
|
|
| Fdh-alpha |
TIGR01591 |
formate dehydrogenase, alpha subunit, archaeal-type; This model describes a subset of formate ... |
106-756 |
6.77e-71 |
|
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: 245.07 E-value: 6.77e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 106 RLAEPVRynAETDHYEPISWDDAFALIARHLNQLDN---PNQAEFYTSGRASNEAAFLYQLFARR-FGTNNFPDCSNMCH 181
Cdd:TIGR01591 53 RLTTPLI--REGDKFREVSWDEAISYIAEKLKEIKEkygPDSIGFIGSSRGTNEENYLLQKLARAvIGTNNVDNCARVCH 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 182 EATSVALSRTIGIGKGTVTIDDFEEADAIFLFGQNPGTNHPRMLETLASAYKRGARVVAFNnlkerglERFTnpqnpfem 261
Cdd:TIGR01591 131 GPSVAGLKQTVGIGAMSNTISEIENADLIVIIGYNPAESHPVVAQYLKNAKRNGAKIIVID-------PRKT-------- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 262 lsngSTPTTSDYFMP-KLGGDMAAVRGLVKILLGrheeaqargESVFDLAFIEQHTEGLDAYLELVRATPWEHIEQQSGL 340
Cdd:TIGR01591 196 ----ETAKIADLHIPlKPGTDIALLNAMANVIIE---------EGLYDKAFIEKRTEGFEEFREIVKGYTPEYVEDITGV 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 341 SQAELTQAADIYQNANRVIVTWAMGVTQHKHSVATIQELVNLQLLFGQVGKDGAGLCPVRGHSNVQGDRTVG-INEKPPA 419
Cdd:TIGR01591 263 PADLIREAARMYAKAGSAAILWGMGVTQHSQGVETVMALINLAMLTGNIGKPGGGVNPLRGQNNVQGACDMGaLPDFLPG 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 420 -------ALLENIEKALGFTP-PKEHGHNVVNALQAMSRGESKVFIGLGGNLVAAAPDTELVAKAMRNCELTVNIATKLN 491
Cdd:TIGR01591 343 yqpvsdeEVREKFAKAWGVVKlPAEPGLRIPEMIDAAADGDVKALYIMGEDPLQSDPNTSKVRKALEKLELLVVQDIFMT 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 492 RS----HVnpgkdslILP--CLGRTDVDMQAAgpqkvtvEDSFSMVHASsgrVDMTGEqMRSEPAIIAGMAKAtLGdnnp 565
Cdd:TIGR01591 423 ETakyaDV-------VLPaaAWLEKEGTFTNA-------ERRIQRFFKA---VEPKGE-SKPDWEIIQELANA-LG---- 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 566 VNWQSmaDNYDNIRDLIEDIIPGFTNFN-QRIEGPrgfylGNSARDLNWKTASGKAQISSNALPQS-----IIPVET--- 636
Cdd:TIGR01591 480 LDWNY--NHPQEIMDEIRELTPLFAGLTyERLDEL-----GSLQWPCNDSDASPTSYLYKDKFATPdgkakFIPLEWvap 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 637 -EQLTKKPVFVLQTMRSHDQYNT-TVYGFDDRYRGVFGERNVIfMNAKDIDKQGLQAGDLVDIETlwtddvKRQIIGFKI 714
Cdd:TIGR01591 553 iEEPDDEYPLILTTGRVLTHYNVgEMTRRVAGLRRLSPEPYVE-INTEDAKKLGIKDGDLVKVKS------RRGEITLRA 625
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 521102444 715 VAFDIPKGNVA-----AYFPEANALIPLGSKgDLSDTPTSKSIAVVI 756
Cdd:TIGR01591 626 KVSDRVNKGAIyitmhFWDGAVNNLTTDDLD-PISGTPEYKYTAVRI 671
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
99-407 |
1.01e-63 |
|
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: 221.70 E-value: 1.01e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 99 YFLEYQGRLAEPVRynAETDHYEPISWDDAFALIARHLNQLD---NPNQAEFYTSGRASNEAAFLYQLFARR-FGTNNFP 174
Cdd:cd02753 47 DFVNSKDRLTKPLI--RKNGKFVEASWDEALSLVASRLKEIKdkyGPDAIAFFGSAKCTNEENYLFQKLARAvGGTNNVD 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 175 DCSNMCHEATSVALSRTIGIGKGTVTIDDFEEADAIFLFGQNPGTNHP----RMLEtlasAYKRGARVVAFNnLKERGLE 250
Cdd:cd02753 125 HCARLCHSPTVAGLAETLGSGAMTNSIADIEEADVILVIGSNTTEAHPviarRIKR----AKRNGAKLIVAD-PRRTELA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 251 RFtnpqnpfemlsngstpttSDYFM-PKLGGDMAAVRGLVKILLGrheeaqargESVFDLAFIEQHTEGLDAYLELVRAT 329
Cdd:cd02753 200 RF------------------ADLHLqLRPGTDVALLNAMAHVIIE---------EGLYDEEFIEERTEGFEELKEIVEKY 252
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521102444 330 PWEHIEQQSGLSQAELTQAADIYQNANRVIVTWAMGVTQHKHSVATIQELVNLQLLFGQVGKDGAGLCPVRGHSNVQG 407
Cdd:cd02753 253 TPEYAERITGVPAEDIREAARMYATAKSAAILWGMGVTQHSHGTDNVMALSNLALLTGNIGRPGTGVNPLRGQNNVQG 330
|
|
| MopB_CT_ydeP |
cd02787 |
The MopB_CT_ydeP CD includes a group of related uncharacterized bacterial ... |
645-756 |
6.44e-55 |
|
The MopB_CT_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative molybdopterin cofactor binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239188 [Multi-domain] Cd Length: 112 Bit Score: 184.02 E-value: 6.44e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 645 FVLQTMRSHDQYNTTVYGFDDRYRGVFGERNVIFMNAKDIDKQGLQAGDLVDIETLWTDDVKRQIIGFKIVAFDIPKGNV 724
Cdd:cd02787 1 LFLVTTRSHDQFNTTIYGLDDRYRGVFGRRDVVFMNPDDIARLGLKAGDRVDLESAFGDGQGRIVRGFRVVEYDIPRGCL 80
|
90 100 110
....*....|....*....|....*....|..
gi 521102444 725 AAYFPEANALIPLGSKGDLSDTPTSKSIAVVI 756
Cdd:cd02787 81 AAYYPEGNVLVPLDHRDPQSKTPAYKSVPVRL 112
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
105-510 |
8.72e-55 |
|
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: 192.93 E-value: 8.72e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 105 GRLAEPVRYNAETDHYEPISWDDAFALIARHLNQL---DNPNQAEFYTSGRASNEAAFLYQLFARRFGTNNFPDCSNMCH 181
Cdd:cd00368 53 DRLKYPLIRVGGRGKFVPISWDEALDEIAEKLKEIrekYGPDAIAFYGGGGASNEEAYLLQKLLRALGSNNVDSHARLCH 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 182 EATSVALSRtIGIGKGTVTIDDFEEADAIFLFGQNPGTNHPRMLETLASAYKRGARVVAFNNlkergleRFTNpqnpfem 261
Cdd:cd00368 133 ASAVAALKA-FGGGAPTNTLADIENADLILLWGSNPAETHPVLAARLRRAKKRGAKLIVIDP-------RRTE------- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 262 lsngsTPTTSDYFMP-KLGGDMAavrglvkillgrheeaqargesvfdLAFIEQhtegldaylelvratpwehIEQQSGL 340
Cdd:cd00368 198 -----TAAKADEWLPiRPGTDAA-------------------------LALAEW-------------------AAEITGV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 341 SQAELTQAADIYQNANRVIVTWAMGVTQHKHSVATIQELVNLQLLFGQVGKDGAGLCPvrghsnvqgdrtvginekppaa 420
Cdd:cd00368 229 PAETIRALAREFAAAKRAVILWGMGLTQHTNGTQNVRAIANLAALTGNIGRPGGGLGP---------------------- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 421 lleniekalgftppkehghnvvnalqamsrgeskvfiglGGNLVAAAPDTELVAKAMRNCELTVNIATKLNRSHVNPgkD 500
Cdd:cd00368 287 ---------------------------------------GGNPLVSAPDANRVRAALKKLDFVVVIDIFMTETAAYA--D 325
|
410
....*....|
gi 521102444 501 sLILPCLGRT 510
Cdd:cd00368 326 -VVLPAATYL 334
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
104-484 |
1.17e-48 |
|
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: 180.88 E-value: 1.17e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 104 QGRLAEP-VRYNaeTDHYEPISWDDAFALIARHLNQL---DNPNQAEFYTSGRASNEAAFLYQLFARRF-GTNNFPDCSN 178
Cdd:cd02754 52 PERLTRPlLRRN--GGELVPVSWDEALDLIAERFKAIqaeYGPDSVAFYGSGQLLTEEYYAANKLAKGGlGTNNIDTNSR 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 179 MCHEATSVALSRTIGIGKGTVTIDDFEEADAIFLFGQNPGTNHP----RMLETLASAykRGARVVAFNnlkerglerftn 254
Cdd:cd02754 130 LCMASAVAGYKRSFGADGPPGSYDDIEHADCFFLIGSNMAECHPilfrRLLDRKKAN--PGAKIIVVD------------ 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 255 pqnPFEmlsngsTPTT--SDYFMP-KLGGDMAAVRGLVKILlgrHEEAQArgesvfDLAFIEQHTEGLDAYLELVRATPW 331
Cdd:cd02754 196 ---PRR------TRTAdiADLHLPiRPGTDLALLNGLLHVL---IEEGLI------DRDFIDAHTEGFEELKAFVADYTP 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 332 EHIEQQSGLSQAELTQAADIYQNANRVIVTWAMGVTQHKHSVATIQELVNLQLLFGQVGKDGAGLCPVRGHSNVQGDRTV 411
Cdd:cd02754 258 EKVAEITGVPEADIREAARLFGEARKVMSLWTMGVNQSTQGTAANNAIINLHLATGKIGRPGSGPFSLTGQPNAMGGREV 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 412 G-INEKPPA-ALLEN------IEKALGFTP---PKEHGHNVVNALQAMSRGESKVFIGLGGNLVAAAPDTELVAKAMRNC 480
Cdd:cd02754 338 GgLANLLPGhRSVNNpehraeVAKFWGVPEgtiPPKPGLHAVEMFEAIEDGEIKALWVMCTNPAVSLPNANRVREALERL 417
|
....
gi 521102444 481 ELTV 484
Cdd:cd02754 418 EFVV 421
|
|
| MopB_Formate-Dh-Na-like |
cd02752 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
106-407 |
3.21e-31 |
|
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: 130.21 E-value: 3.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 106 RLAEPVRYNAETDHYEPISWDDAFALIARHLNQLDNPNQAE---------------FYTSGRASNEAAFLYQLFARRFGT 170
Cdd:cd02752 54 RLKYPMYRAPGSGKWEEISWDEALDEIARKMKDIRDASFVEknaagvvvnrpdsiaFLGSAKLSNEECYLIRKFARALGT 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 171 NNFPDCSNMCHEATSVALSRTIGIGKGTVTIDDFEEADAIFLFGQNPGTNHP-RMLETLASAYKRGARVVAFNnlkergl 249
Cdd:cd02752 134 NNLDHQARIUHSPTVAGLANTFGRGAMTNSWNDIKNADVILVMGGNPAEAHPvSFKWILEAKEKNGAKLIVVD------- 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 250 ERFTNpqnpfemlsngsTPTTSDYFMP-KLGGDMAAVRGLVKILLgrheeaqargesvfdlafieqhtegldaylelvRA 328
Cdd:cd02752 207 PRFTR------------TAAKADLYVPiRSGTDIAFLGGMINYII---------------------------------RY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 329 TPwEHIEQQSGLSQAELTQAADIYQNANRV----IVTWAMGVTQHKHSVATIQELVNLQLLFGQVGKDGAGLCPVRGHSN 404
Cdd:cd02752 242 TP-EEVEDICGVPKEDFLKVAEMFAATGRPdkpgTILYAMGWTQHTVGSQNIRAMCILQLLLGNIGVAGGGVNALRGHSN 320
|
...
gi 521102444 405 VQG 407
Cdd:cd02752 321 VQG 323
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
98-558 |
3.29e-18 |
|
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: 88.61 E-value: 3.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 98 DYFLEYQGRLAEPVRynAETDHYEPISWDDAFALIARHLNQL---DNPNQAEFYTSGRASNEAA-------FLYQLFARR 167
Cdd:cd02762 46 GDYQNDPDRLRTPMR--RRGGSFEEIDWDEAFDEIAERLRAIrarHGGDAVGVYGGNPQAHTHAggayspaLLKALGTSN 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 168 FGTNNFPDcsNMCHEATSVALsrtIGIGkGTVTIDDFEEADAIFLFGQNPGTNH------PRMLETLASAYKRGARVVAf 241
Cdd:cd02762 124 YFSAATAD--QKPGHFWSGLM---FGHP-GLHPVPDIDRTDYLLILGANPLQSNgslrtaPDRVLRLKAAKDRGGSLVV- 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 242 nnlkerglerfTNPQNPfemlsngSTPTTSDYFMP-KLGGDMAAVRGLVKILLgrheeaqarGESVFDLAFIEQHTEGLD 320
Cdd:cd02762 197 -----------IDPRRT-------ETAKLADEHLFvRPGTDAWLLAAMLAVLL---------AEGLTDRRFLAEHCDGLD 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 321 AYLELVRATPWEHIEQQSGLSQAELTQAADIYQNANRVIVTWAMGVTQHKHSVATiQELVN-LQLLFGQVGKDGAGLCPV 399
Cdd:cd02762 250 EVRAALAEFTPEAYAPRCGVPAETIRRLAREFAAAPSAAVYGRLGVQTQLFGTLC-SWLVKlLNLLTGNLDRPGGAMFTT 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 400 -------------RGHSNVQgDRTVG----INEKPPAALLENIEKAlgftppkehGHNVVNALqamsrgeskvfIGLGGN 462
Cdd:cd02762 329 paldlvgqtsgrtIGRGEWR-SRVSGlpeiAGELPVNVLAEEILTD---------GPGRIRAM-----------IVVAGN 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 463 LVAAAPDTELVAKAMRNCELTVNIATKLNRS--HVNpgkdsLILPclgrtdvdmqAAGPQKVTVEDSFSM------VHAS 534
Cdd:cd02762 388 PVLSAPDGARLEAALGGLEFMVSVDVYMTETtrHAD-----YILP----------PASQLEKPHATFFNLefprnaFRYR 452
|
490 500
....*....|....*....|....
gi 521102444 535 SGRVDMTGEQMrSEPAIIAGMAKA 558
Cdd:cd02762 453 RPLFPPPPGTL-PEWEILARLVEA 475
|
|
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
106-484 |
4.14e-18 |
|
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: 88.07 E-value: 4.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 106 RLAEP-VRYNAETDHYEPISWDDAFALIARHLNQLDNPNQAEFYTSGRASNEAAFLYQLFARRF----GTNNFPDcsNMC 180
Cdd:cd02766 55 RLLTPlKRVGRKGGQWERISWDEALDTIAAKLKEIKAEYGPESILPYSYAGTMGLLQRAARGRFfhalGASELRG--TIC 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 181 HEATSVALSRTIGIGKGtVTIDDFEEADAIFLFGQNPGTNHPRMLETLASAYKRGARVVAFNNLKERGLERftnpqnpfe 260
Cdd:cd02766 133 SGAGIEAQKYDFGASLG-NDPEDMVNADLIVIWGINPAATNIHLMRIIQEARKRGAKVVVIDPYRTATAAR--------- 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 261 mlsngstpttSD-YFMPKLGGDMAAVRGLVKILL--GRHeeaqargesvfDLAFIEQHTEGLDAYLELVRATPWEHIEQQ 337
Cdd:cd02766 203 ----------ADlHIQIRPGTDGALALGVAKVLFreGLY-----------DRDFLARHTEGFEELKAHLETYTPEWAAEI 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 338 SGLSQAELTQAADIYQNANRVIVTWAMGVTQHKHSVATIQELVNLQLLFGQVGKDGAGlcpvrghsnvqgdrtvginekp 417
Cdd:cd02766 262 TGVSAEEIEELARLYGEAKPPSIRLGYGMQRYRNGGQNVRAIDALPALTGNIGVPGGG---------------------- 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521102444 418 paalleniekalgftppkehghnvvnALQAMSRGESKVFIGLGGNLVAAAPDTELVAKAM-RNCELTV 484
Cdd:cd02766 320 --------------------------AFYSNSGPPVKALWVYNSNPVAQAPDSNKVRKGLaREDLFVV 361
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
120-486 |
9.42e-16 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 79.75 E-value: 9.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 120 YEPISWDDAFALIARHLNQL-----DNPNQAEFYTSGRASNEAAFLYQLFARRFGTNNF---PDCSNMCHEATSVALSRT 191
Cdd:pfam00384 14 FVRVSWDEALDLIAKKLKRIikkygPDAIAINGGSGGLTDVESLYALKKLLNRLGSKNGnteDHNGDLCTAAAAAFGSDL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 192 IGIGKGTVTIDDFEEADAIFLFGQNPGTNHP-RMLETLASAYKRGARVVAFnnlkerglerftnpqnpfemlsngSTPTT 270
Cdd:pfam00384 94 RSNYLFNSSIADIENADLILLIGTNPREEAPiLNARIRKAALKGKAKVIVI------------------------GPRLD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 271 SDYFMPKLGGDMAAVRGLVkiLLGRHeeaqargesvfdlAFIEqhtegldaylELVRATPWehieqqsglsqaeltqaad 350
Cdd:pfam00384 150 LTYADEHLGIKPGTDLALA--LAGAH-------------VFIK----------ELKKDKDF------------------- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 351 iyqnANRVIVTWAMGVTQHKHSVATIQELVNLQLLFGQVGKDGAGlcpVRGHSNVQGDRTvginekpPAALLEniekaLG 430
Cdd:pfam00384 186 ----APKPIIIVGAGVLQRQDGEAIFRAIANLADLTGNIGRPGGG---WNGLNILQGAAS-------PVGALD-----LG 246
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 521102444 431 FTPPKEhghnVVNALQAMSRGESKVFIGLGGNLVAAAPDTELVAKAMRNCELTVNI 486
Cdd:pfam00384 247 LVPGIK----SVEMINAIKKGGIKVLYLLGNNPFVTHADENRVVKALQKLDLFVVY 298
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
120-398 |
1.62e-15 |
|
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: 79.65 E-value: 1.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 120 YEPISWDDAFALIARHLNQLDNPNQAEFYTSGRASNEAAFLYQLFARRFGTNNFPDCSNMCHEATSVALSRTIGIGkGTV 199
Cdd:cd02755 71 FREASWDEALQYIASKLKEIKEQHGPESVLFGGHGGCYSPFFKHFAAAFGSPNIFSHESTCLASKNLAWKLVIDSF-GGE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 200 TIDDFEEADAIFLFGQN--PGTNHPRMLEtLASAYKRGARVVAFNnlkerglERFTNpqnpfemlsngsTPTTSDYFMP- 276
Cdd:cd02755 150 VNPDFENARYIILFGRNlaEAIIVVDARR-LMKALENGAKVVVVD-------PRFSE------------LASKADEWIPi 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 277 KLGGDMAAVRGLVKILLgrheeaqarGESVFDLAFIEQHTEGLDAYLELVRATPWEHIEQQSGLSQAELTQAA-DIYQNA 355
Cdd:cd02755 210 KPGTDLAFVLALIHVLI---------SENLYDAAFVEKYTNGFELLKAHVKPYTPEWAAQITDIPADTIRRIArEFAAAA 280
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 521102444 356 NRVIV------TWAMGVTQHKHSVATIQELVnlqllfGQVGKDGaGLCP 398
Cdd:cd02755 281 PHAVVdpgwrgTFYSNSFQTRRAIAIINALL------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 ... |
116-484 |
1.67e-15 |
|
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: 79.74 E-value: 1.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 116 ETDHYEPISWDDAFALIARHLNQLDNpnQAEFYTSGRASNEAAFLYQLFARRF-GTNNFpDCSNMCHEATSVALSRTIgi 194
Cdd:cd02771 62 RGGTLVPVSWNEALDVAAARLKEAKD--KVGGIGSPRASNESNYALQKLVGAVlGTNNV-DHRARRLIAEILRNGPIY-- 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 195 gkgTVTIDDFEEADAIFLFGQNPGTNHPRMLETLASAYKRgaRVVAFNNLKERGLERFTNPQNPFEMLSNGSTPTTSDyf 274
Cdd:cd02771 137 ---IPSLRDIESADAVLVLGEDLTQTAPRIALALRQAARR--KAVELAALSGIPKWQDAAVRNIAQGAKSPLFIVNAL-- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 275 mpklggdmaavrgLVKILLGRHEEAQArgeSVFDLAFIeqhTEGLDaylelvRATPWEHIEQQSGLSQAELTQAADIYQN 354
Cdd:cd02771 210 -------------ATRLDDIAAESIRA---SPGGQARL---GAALA------RAVDASAAGVSGLAPKEKAARIAARLTG 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 355 ANRVIVTWAmgvtQHKHSVATIQELVNLQLLFGQVGKDgAGLCPVRGHSNVQGdrtvginekppaallenieKALGFTPP 434
Cdd:cd02771 265 AKKPLIVSG----TLSGSLELIKAAANLAKALKRRGEN-AGLTLAVEEGNSPG-------------------LLLLGGHV 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 521102444 435 KEHGHNVVNALQAMSRGESKVFIGLGGNLVAAAPDTELVAkAMRNCELTV 484
Cdd:cd02771 321 TEPGLDLDGALAALEDGSADALIVLGNDLYRSAPERRVEA-ALDAAEFVV 369
|
|
| MopB_NADH-Q-OR-NuoG2 |
cd02768 |
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone ... |
98-253 |
1.17e-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: 76.55 E-value: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 98 DYFLEYQgRLAEP-VRynaETDHYEPISWDDAFALIARHLNQLdNPNQAEFYTSGRASNEAAFLYQLFARRFGTNNFpDC 176
Cdd:cd02768 47 DGLNSRQ-RLTQPlIK---KGGKLVPVSWEEALKTVAEGLKAV-KGDKIGGIAGPRADLESLFLLKKLLNKLGSNNI-DH 120
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521102444 177 SNMCHEATSVALSRTIGIGkgTVTIDDFEEADAIFLFGQNPGTNHPRMLETLASAYKR-GARVVAFNNLKERGLERFT 253
Cdd:cd02768 121 RLRQSDLPADNRLRGNYLF--NTSIAEIEEADAVLLIGSNLRKEAPLLNARLRKAVKKkGAKIAVIGPKDTDLIADLT 196
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
106-367 |
3.51e-10 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 63.53 E-value: 3.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 106 RLAEPVRYNAE--TDHYEPISWDDAFALIARHLNQLDNPNQAE--FYTSGRASNEAAFLYqlFARRFGT-NNFPDCSNmC 180
Cdd:PRK15488 98 RIVKPLKRVGErgEGKWQEISWDEAYQEIAAKLNAIKQQHGPEsvAFSSKSGSLSSHLFH--LATAFGSpNTFTHAST-C 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 181 HEATSVALSRTIGigkGTVTIdDFEEADAIFLFGQN--PGTNHPRMLETLASAYKRGARVVAFnnlkerglerftNPQnp 258
Cdd:PRK15488 175 PAGYAIAAKVMFG---GKLKR-DLANSKYIINFGHNlyEGINMSDTRGLMTAQMEKGAKLVVF------------EPR-- 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 259 FEMLSNGSTpttsDYFMPKLGGDMAAVRGLVKILLgrheeaqarGESVFDLAFIEQHTEGLDAYLELVRATPWEHIEQQS 338
Cdd:PRK15488 237 FSVVASKAD----EWHAIRPGTDLAVVLALCHVLI---------EENLYDKAFVERYTSGFEELAASVKEYTPEWAEAIS 303
|
250 260 270
....*....|....*....|....*....|
gi 521102444 339 GLSQAELTQ-AADIYQNANRVIVTWAMGVT 367
Cdd:PRK15488 304 DVPADDIRRiARELAAAAPHAIVDFGHRAT 333
|
|
| MopB_Arsenate-R |
cd02757 |
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ... |
120-401 |
4.85e-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: 62.84 E-value: 4.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 120 YEPISWDDAFALIARHLNQLDNPNQA-EF-YTSGRASNEAAFLYQLFARRFGTNNFPDCSNMCHEATSVALSRTIGiGKG 197
Cdd:cd02757 76 FVPISWDEALDTIADKIRALRKENEPhKImLHRGRYGHNNSILYGRFTKMIGSPNNISHSSVCAESEKFGRYYTEG-GWD 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 198 TVTIdDFEEADAIFLFGQNP-GTNHP-----RMLETLASaykrGARVVAFNnlkerglERFTNpqnpfemlsngsTPTTS 271
Cdd:cd02757 155 YNSY-DYANAKYILFFGADPlESNRQnphaqRIWGGKMD----QAKVVVVD-------PRLSN------------TAAKA 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 272 DYFMP-KLGGDMAAVRGLVKILL----------GRHEEAQAR---GESVFDLAFIEQHTEGLDAYL--ELVRATPwEHIE 335
Cdd:cd02757 211 DEWLPiKPGEDGALALAIAHVILteglwdkdfvGDFVDGKNYfkaGETVDEESFKEKSTEGLVKWWnlELKDYTP-EWAA 289
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521102444 336 QQSGLSQAELTQAADIYQNANRVIVTWAM-GVTQHKHSVATIQELVNLQLLFGQVGKDGaGLCPVRG 401
Cdd:cd02757 290 KISGIPAETIERVAREFATAAPAAAAFTWrGATMQNRGSYNSMACHALNGLVGSIDSKG-GLCPNMG 355
|
|
| MopB_CT |
cd02775 |
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a ... |
652-750 |
1.04e-09 |
|
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: 56.17 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 652 SHDQYNTTVYGFDDRYRGVFGErNVIFMNAKDIDKQGLQAGDLVDIETLWtddvkRQIIGFKIVAFDIPKGNVAAYFP-- 729
Cdd:cd02775 1 LRDHFHSGTRTRNPWLRELAPE-PVVEINPEDAAALGIKDGDLVRVESRR-----GSVVLRAKVTDGVPPGVVFLPHGwg 74
|
90 100
....*....|....*....|....*...
gi 521102444 730 -------EANALIPLGSKgDLSDTPTSK 750
Cdd:cd02775 75 hrggrggNANVLTPDALD-PPSGGPAYK 101
|
|
| MopB_2 |
cd02763 |
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
106-393 |
1.01e-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: 58.69 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 106 RLAEPVRYNAE--TDHYEPISWDDAFALIARHLNQL--DNPNQAEFYTsGRASNEAafLYQLFARRFGTNNFPDCSNMCH 181
Cdd:cd02763 54 RLTKPLLRKGPrgSGQFEEIEWEEAFSIATKRLKAAraTDPKKFAFFT-GRDQMQA--LTGWFAGQFGTPNYAAHGGFCS 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 182 EATSVALSRTIGIGKGTVTIDDFEEADAIFLFGQNPGTNHPRMLETLASAYKRGARVVAFNNLKerglerftnpqnpfem 261
Cdd:cd02763 131 VNMAAGGLYSIGGSFWEFGGPDLEHTKYFMMIGVAEDHHSNPFKIGIQKLKRRGGKFVAVNPVR---------------- 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 262 lsNGSTPTTSDYFMPKLGGDMAAVRGLVKILLgrheEAQArgesvFDLAFIEQHTEGldayLELVRATPwEHIEQQSGLS 341
Cdd:cd02763 195 --TGYAAIADEWVPIKPGTDGAFILALAHELL----KAGL-----IDWEFLKRYTNA----AELVDYTP-EWVEKITGIP 258
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521102444 342 -------QAELTQAAdiYQNANRVIVTW-------------------AM-GVTQHKHSVATIQELVNLQLLFGQVGKDG 393
Cdd:cd02763 259 adtirriAKELGVTA--RDQPIELPIAWtdvwgrkhekitgrpvsfhAMrGIAAHSNGFQTIRALFVLMMLLGTIDRPG 335
|
|
| Molydop_binding |
pfam01568 |
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
645-753 |
1.31e-07 |
|
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: 50.35 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 645 FVLQTMRSHDQYNTTVYGFDDRYRGVFgERNVIFMNAKDIDKQGLQAGDLVDIETlwtddvKR-QIIGFKIVAFDIPKGN 723
Cdd:pfam01568 1 LYLITGRVLGQYHSQTRTRRVLRLAKP-EPEVVEIHPEDAAALGIKDGDLVEVTS------RRgSVVVRAKVTDRVRPGV 73
|
90 100 110
....*....|....*....|....*....|....*...
gi 521102444 724 VAAYFPE--------ANALIPLGSKgDLSDTPTSKSIA 753
Cdd:pfam01568 74 VFMPFGWwyeprggnANALTDDATD-PLSGGPEFKTCA 110
|
|
| PRK07860 |
PRK07860 |
NADH dehydrogenase subunit G; Validated |
106-251 |
4.11e-06 |
|
NADH dehydrogenase subunit G; Validated
Pssm-ID: 236118 [Multi-domain] Cd Length: 797 Bit Score: 50.33 E-value: 4.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 106 RLAEP-VRynAETDHYEPISWDDAFALIARHLNQLDNPnqAEFYTSGRASNEAAFLYQLFAR-RFGTNNFpDCSNMCH-- 181
Cdd:PRK07860 278 RITTPlVR--DEDGELEPASWSEALAVAARGLAAARGR--VGVLVGGRLTVEDAYAYAKFARvALGTNDI-DFRARPHsa 352
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521102444 182 -EATSVAlSRTIGIGKGtVTIDDFEEADAIFLFGQNPGTNHPRMLETLASAY-KRGARVVAFNNLKERGLER 251
Cdd:PRK07860 353 eEADFLA-ARVAGRGLG-VTYADLEKAPAVLLVGFEPEEESPIVFLRLRKAArKHGLKVYSIAPFATRGLEK 422
|
|
| MopB_Res-Cmplx1_Nad11 |
cd02773 |
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone ... |
92-217 |
4.86e-06 |
|
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone oxidoreductase/respiratory complex I/NADH dehydrogenase-1(NDH-1) of eukaryotes and the Nqo3/G subunit of alphaproteobacteria NDH-1. The NADH-quinone oxidoreductase is the first energy-transducting complex in the respiratory chains of many prokaryotes and eukaryotes. Mitochondrial complex I and its bacterial counterpart, NDH-1, function as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. The nad11 gene codes for the largest (75 kDa) subunit of the mitochondrial NADH:ubiquinone oxidoreductase, it constitutes the electron input part of the enzyme, or the so-called NADH dehydrogenase fragment. In Paracoccus denitrificans, this subunit is encoded by the nqo3 gene, and is part of the 14 distinct subunits constituting the 'minimal' functional enzyme. The Nad11/Nqo3 subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain belongs to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239174 [Multi-domain] Cd Length: 375 Bit Score: 49.57 E-value: 4.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 92 WLNKQSDYF---LEYQgRLAEP-VRynaETDHYEPISWDDAFALIARHLNQLdNPNQAEFYTSGRASNEAAFLYQLFARR 167
Cdd:cd02773 37 WISDKTRFAydgLKRQ-RLDKPyIR---KNGKLKPATWEEALAAIAKALKGV-KPDEIAAIAGDLADVESMVALKDLLNK 111
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 521102444 168 FGtnnfpdCSNMCHEATSVALSRTIGIGK-GTVTIDDFEEADAIFLFGQNP 217
Cdd:cd02773 112 LG------SENLACEQDGPDLPADLRSNYlFNTTIAGIEEADAVLLVGTNP 156
|
|
| PRK13532 |
PRK13532 |
nitrate reductase catalytic subunit NapA; |
99-395 |
1.93e-05 |
|
nitrate reductase catalytic subunit NapA;
Pssm-ID: 237416 [Multi-domain] Cd Length: 830 Bit Score: 48.36 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 99 YFLE---Y-QGRLAEPV------RYNAETDhYEPISWDDAFALIARH----LNQLDnPNQAEFYTSGR--------ASne 156
Cdd:PRK13532 86 YFLSkimYgKDRLTQPLlrmkdgKYDKEGE-FTPVSWDQAFDVMAEKfkkaLKEKG-PTAVGMFGSGQwtiwegyaAS-- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 157 aaflyQLFARRFGTNNFPDCSNMCHEATSVALSRTIGIGKGTVTIDDFEEADAIFLFGQNPGTNHP----RMLETLASAy 232
Cdd:PRK13532 162 -----KLMKAGFRSNNIDPNARHCMASAVVGFMRTFGIDEPMGCYDDIEAADAFVLWGSNMAEMHPilwsRVTDRRLSN- 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 233 kRGARVVAfnnlkergLERFTNpqNPFEMLSNGS--TPTTsdyfmpklggDMAAVRGLVKILLGRHEeaqargesvFDLA 310
Cdd:PRK13532 236 -PDVKVAV--------LSTFEH--RSFELADNGIifTPQT----------DLAILNYIANYIIQNNA---------VNWD 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 311 FIEQHTE----------GL------------------------DAYLELVRATPWEHIEQQSGLSQAELTQAADIYQNAN 356
Cdd:PRK13532 286 FVNKHTNfrkgatdigyGLrpthplekaaknpgtagksepisfEEFKKFVAPYTLEKTAKMSGVPKEQLEQLAKLYADPN 365
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 521102444 357 RVIVT-WAMGVTQHKHSVATIQELVNLQLLFGQVGKDGAG 395
Cdd:PRK13532 366 RKVVSfWTMGFNQHTRGVWANNLVYNIHLLTGKISTPGNG 405
|
|
| MopB_DmsA-EC |
cd02770 |
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
118-407 |
1.59e-03 |
|
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: 41.92 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 118 DHYEPISWDDAFALIARHLNQLDNP--NQAEFYTSGRASNEAAFLYQLFARR----FG--TNNFPDCSNMCheaTSVALS 189
Cdd:cd02770 73 GKFVRISWDEALDTIASELKRIIEKygNEAIYVNYGTGTYGGVPAGRGAIARllnlTGgyLNYYGTYSWAQ---ITTATP 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 190 RTIGIGKGTVTIDDFEEADAIFLFGQNPGtnhprmlETLASAykrGARVVAFNNLKERGLE------RFTNpqnpfemls 263
Cdd:cd02770 150 YTYGAAASGSSLDDLKDSKLVVLFGHNPA-------ETRMGG---GGSTYYYLQAKKAGAKfividpRYTD--------- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 264 ngSTPTTSDYFMPKL-GGDMAAVRGLVKILLgrheeaqarGESVFDLAFIEQHTEGLDA---------------YLELVR 327
Cdd:cd02770 211 --TAVTLADEWIPIRpGTDAALVAAMAYVMI---------TENLHDQAFLDRYCVGFDAehlpegappnesykdYVLGTG 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 328 A-----TP-W-EHIeqqSGLSQAELTQAADIYQNANRVIVTWAMGVTQHKHSVATIQELVNLQLLFGQVGKDGAGLCPVR 400
Cdd:cd02770 280 YdgtpkTPeWaSEI---TGVPAETIRRLAREIATTKPAAILQGWGPQRHANGEQAARAIMMLAAMTGNVGIPGGNTGARP 356
|
....*..
gi 521102444 401 GHSNVQG 407
Cdd:cd02770 357 GGSAYNG 363
|
|
| MopB_4 |
cd02765 |
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
120-293 |
2.03e-03 |
|
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: 41.31 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 120 YEPISWDDAFALIARHLNQLDN---PNQAEFYTSgraSNEAAFLYQLFARRFGTNNFPDCSNMCHEATSVALSRTIGIG- 195
Cdd:cd02765 71 FERITWDEALDTIADKLTEAKReygGKSILWMSS---SGDGAILSYLRLALLGGGLQDALTYGIDTGVGQGFNRVTGGGf 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521102444 196 -KGTVTIDDFEEADAIFLFGQNPGTNHPRMLETLASAYKRGARVVAFNnlkerglERFTNpqnpfemlsngsTPTTSDYF 274
Cdd:cd02765 148 mPPTNEITDWVNAKTIIIWGSNILETQFQDAEFFLDARENGAKIVVID-------PVYST------------TAAKADQW 208
|
170 180
....*....|....*....|
gi 521102444 275 MP-KLGGDMAAVRGLVKILL 293
Cdd:cd02765 209 VPiRPGTDPALALGMINYIL 228
|
|
| |
