|
Name |
Accession |
Description |
Interval |
E-value |
| MopB_ydeP |
cd02767 |
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
47-625 |
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: 925.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 47 GFMCVSCAWTKPADH-HPFEFGETGAKATLWELTTRRCTPEFFAKHTVTELRGWKDHDLEQEGRLTHPMRYDRDSDRYVP 125
Cdd:cd02767 1 GFDCPGCAWGDPGQKlHGFEFCENGAKALAWETTPKRVTPEFFALHSVSELRTWSDYELEHLGRLTYPMRYDAGSDHYRP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 126 CGWDEAFSAIGQELKALDPKSVVFYASGRASLETSYLYALFARLYGHNNLPDSSNMCHETTSVGLKKVIGASVGTSVYDD 205
Cdd:cd02767 81 ISWDEAFAEIAARLRALDPDRAAFYTSGRASNEAAYLYQLFARAYGTNNLPDCSNMCHEPSSVGLKKSIGVGKGTVSLED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 206 FSTCDAIFFFGQNTGSNSPRFLHPLQAAVKRGCKIVTFNPVREKGLETMINPQSPTEMLTGkETQISCQYHQVKTGGDIA 285
Cdd:cd02767 161 FEHTDLIFFIGQNPGTNHPRMLHYLREAKKRGGKIIVINPLREPGLERFANPQNPESMLTG-GTKIADEYFQVRIGGDIA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 286 AIMGMCKHVFAKDDeakqQGRNVIDRDFVEQHTSGFHAFEETVRATSWDEIERESGLERAALEAAGQVYVDAERVIGIYG 365
Cdd:cd02767 240 LLNGMAKHLIERDD----EPGNVLDHDFIAEHTSGFEEYVAALRALSWDEIERASGLSREEIEAFAAMYAKSERVVFVWG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 366 MGLTQQVGGFESIAMLVNLLLLKGNIGRDGTGISPVRGHSNVQGQRTVGISEKPELVPLDKLAEMFDFEPPREKGVNTVE 445
Cdd:cd02767 316 MGITQHAHGVDNVRAIVNLALLRGNIGRPGAGLMPIRGHSNVQGDRTMGITEKPFPEFLDALEEVFGFTPPRDPGLDTVE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 446 ACEGIVDGSIRGFVSLGGNFVRAIPDHDVMEAAWTKMRLTVQIATKLNRSHLINGEVAYLLPCLGRSEEDVQEGGPQTVS 525
Cdd:cd02767 396 AIEAALEGKVKAFISLGGNFAEAMPDPAATEEALRRLDLTVHVATKLNRSHLVHGEEALILPCLGRTEIDMQAGGAQAVT 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 526 MEDSLSCIHGSVGKHKPASEHLLSELAIVAGLAKATlPPNPKVKWDEWRGDYGKVRDLIEETYPDKFHDFNKRLFTPGGF 605
Cdd:cd02767 476 VEDSMSMTHTSRGRLKPASRVLLSEEAIVAGIAGAR-LGEAKPEWEILVEDYDRIRDEIAAVIYEGFADFNQRGDQPGGF 554
|
570 580
....*....|....*....|
gi 1148824058 606 YRGNSARERIWKTESGKAEF 625
Cdd:cd02767 555 HLPNGARERKFNTPSGKAQF 574
|
|
| Fdhalpha-like |
TIGR01701 |
oxidoreductase alpha (molybdopterin) subunit; This model represents a well-defined clade of ... |
12-756 |
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 1148824058 12 PAGGWGSVRGIARIFAKELNSPAVADTLRRQNKPGGFMCVSCAW-TKPADHHPFEFGETGAKATLWELTTRRCTPEFFAK 90
Cdd:TIGR01701 1 DAGGWGAVKSVALGKVKPMHIRQTLKLLLTLNKPEGYDCPGCAWgVSPQTLAGLEFCENGAKAIAWETTPRTIDPEFFAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 91 HTVTELRGWKDHDLEQEGRLTHPMRYDRDSDRYVPCGWDEAFSAIGQELKALDPKSVVFYASGRASLETSYLYALFARLY 170
Cdd:TIGR01701 81 HSVSELRTLDSHELEKLGRLTYPLSLRPGSDHYTPISWDDAYQEIAAKLNSLDPKQVAFYTSGRTSNEAAYLYQLFARSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 171 GHNNLPDSSNMCHETTSVGLKKVIGASVGTSVYDDFSTCDAIFFFGQNTGSNSPRFLHPLQAAVKRGCKIVTFNPVREKG 250
Cdd:TIGR01701 161 GSNNLPDCSNMCHEPSSVALKRSIGIGKGSVNLEDFEHTDCLVFIGSNAGTNHPRMLKYLYAAKKRGAKIIAINPLRERG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 251 LETMINPQSPTEMLTGKETQISCQYHQVKTGGDIAAIMGMCKHVFAKDDEAKQqgrNVIDRDFVEQHTSGFHAFEETVRA 330
Cdd:TIGR01701 241 LERFWIPQIPESMLTGGGTQISSEYYQVRIGGDIALFNGVMKLLIEAEDAQPG---SLIDHEFIANHTNGFDELRRHVLQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 331 TSWDEIERESGLERAALEAAGQVYVDAERVIGIYGMGLTQQVGGFESIAMLVNLLLLKGNIGRDGTGISPVRGHSNVQGQ 410
Cdd:TIGR01701 318 LNWNDIERSSGLSQEEILEFAKLLANSRRVVFCWAMGLTQHAHGVDNISQVANLALLRGNIGKPGAGVCPIRGHSNVQGD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 411 RTVGISEKPELVPLDKLAEMFDFEPPREKGVNTVEACEGIVDGSIRGFVSLGGNFVRAIPDHDVMEAAWTKMRLTVQIAT 490
Cdd:TIGR01701 398 RTMGITEKPEEEFLARLSQIYGFTPPDWPGDTTVAMIEAILTGKVRAFICLGGNFLEAMPDTAAIERALRQLDLRVHVAT 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 491 KLNRSHLINGEVAYLLPCLGRSEEDVQEGGPQTVSMEDSLSCIHGSVGKHKPASEHLLSELAIVAGLAKATLPPNPkVKW 570
Cdd:TIGR01701 478 KLNRSHVLAKEEALILPVLGRYEQDGQGTGKQAVSVESSMRMVHFSRGILKPRGAELRSEWAIIAEIAKALLPETP-VAW 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 571 DEWRGDYGKVRDLIEETYPDkFHDFNKRLFTPGGFYRGNSAR-ERIWKTESGKAEFTVPEALSAAGFEDRDGRYRLMTLR 649
Cdd:TIGR01701 557 EILVDTYDQIRDAIAATNPG-YDDINHRKRRPDGFQLPGAALcERKFPTPDGKANFIVIPLPEFRVPTGHEFELVLVTLR 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 650 SNDQFNTTIYGYSDRLRGIEGTRNVLLIDPKEMEKLGLQEGQLVGLQTDIEDGRERKVEGLKVLPFQLPDGCVAGYYPEL 729
Cdd:TIGR01701 636 SHDQFNTTIYGEDDRYRGVDGHRRVVFMNETDIKKLGLRNGERVDVYNQYGDGQKRKFDNLRIVFYDTPTGNAAAYYPEA 715
|
730 740
....*....|....*....|....*..
gi 1148824058 730 NPLIPLSLHERLSQTPASKAVPIRILP 756
Cdd:TIGR01701 716 NPLLPLDHHDPQSKTPEYKTIPVRLEA 742
|
|
| PRK09939 |
PRK09939 |
acid resistance putative oxidoreductase YdeP; |
3-756 |
0e+00 |
|
acid resistance putative oxidoreductase YdeP;
Pssm-ID: 182156 [Multi-domain] Cd Length: 759 Bit Score: 716.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 3 KNETVHYDGPAGGWGSVRGIARIFAKELNSPAVADTLRRQNKPGGFMCVSCAWTKPADHHPFEFGETGAKATLWELTTRR 82
Cdd:PRK09939 2 KKKIESYQGAAGGWGAVKSVANAVRKQMDIRQDVIAMFDMNKPEGFDCPGCAWPDPKHSASFDICENGAKAIAWEVTDKQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 83 CTPEFFAKHTVTELRGWKDHDLEQEGRLTHPMRYDRDSDRYVPCGWDEAFSAIGQELKAL-DPKSVVFYASGRASLETSY 161
Cdd:PRK09939 82 VNASFFAENTVQSLLTWGDHELEAAGRLTQPLKYDAVSDCYKPLSWQQAFDEIGARLQSYsDPNQVEFYTSGRTSNEAAF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 162 LYALFARLYGHNNLPDSSNMCHETTSVGLKKVIGASVGTSVYDDFSTCDAIFFFGQNTGSNSPRFLHPLQAAVKRGCKIV 241
Cdd:PRK09939 162 LYQLFAREYGSNNFPDCSNMCHEPTSVGLAASIGVGKGTVLLEDFEKCDLVICIGHNPGTNHPRMLTSLRALVKRGAKMI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 242 TFNPVREKGLETMINPQSPTEMLTGKETQISCQYHQVKTGGDIAAIMGMCKHVFAKDDEAKQQGR-NVIDRDFVEQHTSG 320
Cdd:PRK09939 242 AINPLQERGLERFTAPQNPFEMLTNSETQLASAYYNVRIGGDMALLKGMMRLLIERDDAASAAGRpSLLDDEFIQTHTVG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 321 FHAFEETVRATSWDEIERESGLERAALEAAGQVYVDAERVIGIYGMGLTQQVGGFESIAMLVNLLLLKGNIGRDGTGISP 400
Cdd:PRK09939 322 FDELRRDVLNSEWKDIERISGLSQTQIAELADAYAAAERTIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGICP 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 401 VRGHSNVQGQRTVGISEKPELVPLDKLAEMFDFEPPREKGVNTVEACEGIVDGSIRGFVSLGGNFVRAIPDHDVMEAAWT 480
Cdd:PRK09939 402 LRGHSNVQGDRTVGITEKPSAEFLARLGERYGFTPPHAPGHAAIASMQAICTGQARALICMGGNFALAMPDREASAVPLT 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 481 KMRLTVQIATKLNRSHLINGEVAYLLPCLGRSEEDVQEGGPQTVSMEDSLSCIHGSVGKHKPASEHLLSELAIVAGLAKA 560
Cdd:PRK09939 482 QLDLAVHVATKLNRSHLLTARHSYILPVLGRSEIDMQKSGAQAVTVEDSMSMIHASRGVLKPAGVMLKSECAVVAGIAQA 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 561 TLpPNPKVKWDEWRGDYGKVRDLIEETYPDkFHDFNKRLFTPGGFYRGNSARERIWKTESGKAEFTVPEALsaagFEDRD 640
Cdd:PRK09939 562 AL-PQSVVAWEYLVEDYDRIRNDIEAVLPE-FADYNQRIRHPGGFHLINAAAERRWMTPSGKANFITSKGL----LEDPS 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 641 GRYR----LMTLRSNDQFNTTIYGYSDRLRGIEGTRNVLLIDPKEMEKLGLQEGQLVGLQTDIEDGRE--RKVEGLKVLP 714
Cdd:PRK09939 636 SAFNsklvMATVRSHDQYNTTIYGMDDRYRGVFGQRDVVFMSAKQAKICRVKNGERVNLIALTPDGKRssRRMDRLKVVI 715
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 1148824058 715 FQLPDGCVAGYYPELNPLIPLSLHERLSQTPASKAVPIRILP 756
Cdd:PRK09939 716 YPMADRSLVTYFPESNHMLTLDNHDPLSGIPGYKSIPVELEP 757
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
89-754 |
2.28e-145 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 441.20 E-value: 2.28e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 89 AKHTVTELRGWK-----DHDLEQEGRLTHPMRYD--RDSDRYVPCGWDEAFSAIGQELKAL----DPKSVVFYASG---- 153
Cdd:COG0243 53 PDHPVNRGRLCAkgaalDERLYSPDRLTYPMKRVgpRGSGKFERISWDEALDLIAEKLKAIideyGPEAVAFYTSGgsag 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 154 RASLETSYLYALFARLYGHNNLPDSSNMCHETTSVGLKKVIGASVGTSVYDDFSTCDAIFFFGQNTGSNSPRFLHPLQAA 233
Cdd:COG0243 133 RLSNEAAYLAQRFARALGTNNLDDNSRLCHESAVAGLPRTFGSDKGTVSYEDLEHADLIVLWGSNPAENHPRLLRRLREA 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 234 VK-RGCKIVTFNPVREKGletminpqsptemltgkeTQISCQYHQVKTGGDIAAIMGMCKHVFAkddeakqqgRNVIDRD 312
Cdd:COG0243 213 AKkRGAKIVVIDPRRTET------------------AAIADEWLPIRPGTDAALLLALAHVLIE---------EGLYDRD 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 313 FVEQHTSGFHAFEETVRATSWDEIERESGLERAALEAAGQVYVDAERVIGIYGMGLTQQVGGFESIAMLVNLLLLKGNIG 392
Cdd:COG0243 266 FLARHTVGFDELAAYVAAYTPEWAAEITGVPAEDIRELAREFATAKPAVILWGMGLQQHSNGTQTVRAIANLALLTGNIG 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 393 RDGTGISPVRGHsnvqgqrtvgisekpelvpldklaEMFDFEPPRekgvntveacegivdgsIRGFVSLGGNFVRAIPDH 472
Cdd:COG0243 346 KPGGGPFSLTGE------------------------AILDGKPYP-----------------IKALWVYGGNPAVSAPDT 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 473 DVMEAAWTKMRLTVQIATKLNRSHLINgevAYLLPCLGRSE-EDVqeggpqTVSMEDslSCIHGSVGKHKPASEhLLSEL 551
Cdd:COG0243 385 NRVREALRKLDFVVVIDTFLTETARYA---DIVLPATTWLErDDI------VTNSED--RRVHLSRPAVEPPGE-ARSDW 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 552 AIVAGLAKAtLPPNPKVKWDEWRGDYgkVRDLIEETYPDK--FHDFNKR-----LFTPGGFYRgnsaRERIWKTESGKAE 624
Cdd:COG0243 453 EIFAELAKR-LGFEEAFPWGRTEEDY--LRELLEATRGRGitFEELREKgpvqlPVPPEPAFR----NDGPFPTPSGKAE 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 625 FTVP-----------EALSAAGFEDRDGRYRLMTLRSNDQFNTTIYGySDRLRGIEGtRNVLLIDPKEMEKLGLQEGQLV 693
Cdd:COG0243 526 FYSEtlalpplpryaPPYEGAEPLDAEYPLRLITGRSRDQWHSTTYN-NPRLREIGP-RPVVEINPEDAAALGIKDGDLV 603
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1148824058 694 GLQTDIedGRerkVEGLKVLPFQLPDGCVA---GYYPEL--------NPLIPlSLHERLSQTPASKAVPIRI 754
Cdd:COG0243 604 RVESDR--GE---VLARAKVTEGIRPGVVFaphGWWYEPaddkggnvNVLTP-DATDPLSGTPAFKSVPVRV 669
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
97-756 |
2.38e-88 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 292.17 E-value: 2.38e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 97 RGWKDHD-LEQEGRLTHPMRydRDSDRYVPCGWDEAFSAIGQELKAL----DPKSVVFYASGRASLETSYLYALFARLY- 170
Cdd:COG3383 48 KGRFGFEfVNSPDRLTTPLI--RRGGEFREVSWDEALDLVAERLREIqaehGPDAVAFYGSGQLTNEENYLLQKLARGVl 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 171 GHNNLPDSSNMCHETTSVGLKKVIGASVGTSVYDDFSTCDAIFFFGQNTGSNSPRFLHPLQAAVKRGCKIVTFNPVRekg 250
Cdd:COG3383 126 GTNNIDNNARLCMASAVAGLKQSFGSDAPPNSYDDIEEADVILVIGSNPAEAHPVLARRIKKAKKNGAKLIVVDPRR--- 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 251 letminpqspTEMltgkeTQISCQYHQVKTGGDIAAIMGMCKHVFAkddeakqqgRNVIDRDFVEQHTSGFHAFEETVRA 330
Cdd:COG3383 203 ----------TET-----ARLADLHLQIKPGTDLALLNGLLHVIIE---------EGLVDEDFIAERTEGFEELKASVAK 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 331 TSWDEIERESGLERAALEAAGQVYVDAERVIGIYGMGLTQQVGGFESIAMLVNLLLLKGNIGRDGTGISPVRGHSNVQGQ 410
Cdd:COG3383 259 YTPERVAEITGVPAEDIREAARLIAEAKRAMILWGMGVNQHTQGTDNVNAIINLALATGNIGRPGTGPFPLTGQNNVQGG 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 411 RTVGIseKPELVP----------LDKLAEMFDFEP-PREKGVNTVEACEGIVDGSIRGFVSLGGNFVRAIPDHDVMEAAW 479
Cdd:COG3383 339 RDMGA--LPNVLPgyrdvtdpehRAKVADAWGVPPlPDKPGLTAVEMFDAIADGEIKALWIIGENPAVSDPDANHVREAL 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 480 TKMRL----------TVQIAtklnrsHLIngevaylLPCLGRSEEDvqegGPQTvSMEDSLSCIHGSVgkhkPASEHLLS 549
Cdd:COG3383 417 EKLEFlvvqdiflteTAEYA------DVV-------LPAASWAEKD----GTFT-NTERRVQRVRKAV----EPPGEARP 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 550 ELAIVAGLAKA---TLP-PNPKVKWDEWR---GDYGKVR-DLIEET------YPDKFHDFNKRLFTpGGFYrgnsareri 615
Cdd:COG3383 475 DWEIIAELARRlgyGFDyDSPEEVFDEIArltPDYSGISyERLEALggvqwpCPSEDHPGTPRLFT-GRFP--------- 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 616 wkTESGKAEFTVPEALSAAGFEDRDGRYRLMTLRSNDQFNT-TIYGYSDRLRGIEGtRNVLLIDPKEMEKLGLQEGQLVG 694
Cdd:COG3383 545 --TPDGKARFVPVEYRPPAELPDEEYPLVLTTGRLLDQWHTgTRTRRSPRLNKHAP-EPFVEIHPEDAARLGIKDGDLVR 621
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 695 LQTdiEDGR--------ERKVEGLKVLPFQLPDGCVagyypelNPLIPlSLHERLSQTPASKAVPIRILP 756
Cdd:COG3383 622 VSS--RRGEvvlrarvtDRVRPGTVFMPFHWGEGAA-------NALTN-DALDPVSKQPEYKACAVRVEK 681
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
109-409 |
1.64e-57 |
|
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: 204.37 E-value: 1.64e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 109 RLTHPMRydRDSDRYVPCGWDEAFSAIGQELKAL----DPKSVVFYASGRASLETSYLYALFAR-LYGHNNLPDSSNMCH 183
Cdd:cd02753 54 RLTKPLI--RKNGKFVEASWDEALSLVASRLKEIkdkyGPDAIAFFGSAKCTNEENYLFQKLARaVGGTNNVDHCARLCH 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 184 ETTSVGLKKVIGASVGTSVYDDFSTCDAIFFFGQNTGSNSPRFLHPLQAAVKRGCKIVTFNPVRekgletminpqspTEM 263
Cdd:cd02753 132 SPTVAGLAETLGSGAMTNSIADIEEADVILVIGSNTTEAHPVIARRIKRAKRNGAKLIVADPRR-------------TEL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 264 ltgkeTQISCQYHQVKTGGDIAAIMGMCkHVFAKddeakqqgRNVIDRDFVEQHTSGFHAFEETVRATSWDEIERESGLE 343
Cdd:cd02753 199 -----ARFADLHLQLRPGTDVALLNAMA-HVIIE--------EGLYDEEFIEERTEGFEELKEIVEKYTPEYAERITGVP 264
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1148824058 344 RAALEAAGQVYVDAERVIGIYGMGLTQQVGGFESIAMLVNLLLLKGNIGRDGTGISPVRGHSNVQG 409
Cdd:cd02753 265 AEDIREAARMYATAKSAAILWGMGVTQHSHGTDNVMALSNLALLTGNIGRPGTGVNPLRGQNNVQG 330
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
84-560 |
1.53e-53 |
|
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: 189.46 E-value: 1.53e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 84 TPEFFAKHTVTELRGWKDHDleqegRLTHPMRYDRDSDRYVPCGWDEAFSAIGQELKAL----DPKSVVFYASGRASLET 159
Cdd:cd00368 34 NEGRLCDKGRAGLDGLYSPD-----RLKYPLIRVGGRGKFVPISWDEALDEIAEKLKEIrekyGPDAIAFYGGGGASNEE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 160 SYLYALFARLYGHNNLPDSSNMCHETTSVGLKkVIGASVGTSVYDDFSTCDAIFFFGQNTGSNSPRFLHPLQAAVKRGCK 239
Cdd:cd00368 109 AYLLQKLLRALGSNNVDSHARLCHASAVAALK-AFGGGAPTNTLADIENADLILLWGSNPAETHPVLAARLRRAKKRGAK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 240 IVTFNPVREKGletminpqsptemltgkeTQISCQYHQVKTGGDIAAIMGmckhvfakddeakqqgrnvidrdfveqhts 319
Cdd:cd00368 188 LIVIDPRRTET------------------AAKADEWLPIRPGTDAALALA------------------------------ 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 320 gfhafeetvratswDEIERESGLERAALEAAGQVYVDAERVIGIYGMGLTQQVGGFESIAMLVNLLLLKGNIGRDGTGIS 399
Cdd:cd00368 220 --------------EWAAEITGVPAETIRALAREFAAAKRAVILWGMGLTQHTNGTQNVRAIANLAALTGNIGRPGGGLG 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 400 PvrghsnvqgqrtvgisekpelvpldklaemfdfepprekgvntveacegivdgsirgfvslGGNFVRAIPDHDVMEAAW 479
Cdd:cd00368 286 P-------------------------------------------------------------GGNPLVSAPDANRVRAAL 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 480 TKMRLTVQIATKLNRSHlingEVA-YLLPCLGRSEEdvqeggpqtvsmEDSLSCIHGSVGKHKPASE---HLLSELAIVA 555
Cdd:cd00368 305 KKLDFVVVIDIFMTETA----AYAdVVLPAATYLEK------------EGTYTNTEGRVQLFRQAVEppgEARSDWEILR 368
|
....*
gi 1148824058 556 GLAKA 560
Cdd:cd00368 369 ELAKR 373
|
|
| MopB_CT_ydeP |
cd02787 |
The MopB_CT_ydeP CD includes a group of related uncharacterized bacterial ... |
643-754 |
6.66e-51 |
|
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: 172.85 E-value: 6.66e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 643 YRLMTLRSNDQFNTTIYGYSDRLRGIEGTRNVLLIDPKEMEKLGLQEGQLVGLQTDIEDGRERKVEGLKVLPFQLPDGCV 722
Cdd:cd02787 1 LFLVTTRSHDQFNTTIYGLDDRYRGVFGRRDVVFMNPDDIARLGLKAGDRVDLESAFGDGQGRIVRGFRVVEYDIPRGCL 80
|
90 100 110
....*....|....*....|....*....|..
gi 1148824058 723 AGYYPELNPLIPLSLHERLSQTPASKAVPIRI 754
Cdd:cd02787 81 AAYYPEGNVLVPLDHRDPQSKTPAYKSVPVRL 112
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
107-625 |
1.83e-45 |
|
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: 171.64 E-value: 1.83e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 107 EGRLTHPMrYDRDSDRYVPCGWDEAFSAIGQELKAL----DPKSVVFYASGRASLETSYLYALFARLY-GHNNLPDSSNM 181
Cdd:cd02754 52 PERLTRPL-LRRNGGELVPVSWDEALDLIAERFKAIqaeyGPDSVAFYGSGQLLTEEYYAANKLAKGGlGTNNIDTNSRL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 182 CHETTSVGLKKVIGASVGTSVYDDFSTCDAIFFFGQNTGSnsprfLHP-----LQAAVK--RGCKIVTFNPVRekgletm 254
Cdd:cd02754 131 CMASAVAGYKRSFGADGPPGSYDDIEHADCFFLIGSNMAE-----CHPilfrrLLDRKKanPGAKIIVVDPRR------- 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 255 inpqSPTemltgkeTQISCQYHQVKTGGDIAAIMGMCKHVFAKDdeakqqgrnVIDRDFVEQHTSGFHAFEETVRATSWD 334
Cdd:cd02754 199 ----TRT-------ADIADLHLPIRPGTDLALLNGLLHVLIEEG---------LIDRDFIDAHTEGFEELKAFVADYTPE 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 335 EIERESGLERAALEAAGQVYVDAERVIGIYGMGLTQQVGGFESIAMLVNLLLLKGNIGRDGTGISPVRGHSNVQGQRTVG 414
Cdd:cd02754 259 KVAEITGVPEADIREAARLFGEARKVMSLWTMGVNQSTQGTAANNAIINLHLATGKIGRPGSGPFSLTGQPNAMGGREVG 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 415 ----------ISEKPELVplDKLAEMFDFEP---PREKGVNTVEACEGIVDGSIRGFVSLGGNFVRAIPD-HDVMEAAWT 480
Cdd:cd02754 339 glanllpghrSVNNPEHR--AEVAKFWGVPEgtiPPKPGLHAVEMFEAIEDGEIKALWVMCTNPAVSLPNaNRVREALER 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 481 KMRLTVQIATKLNRShlinGEVAYL-LPCLGRSEEDvqegGPQTvSMEDSLSCIHGSVgkhKPASEhLLSELAIVAGLAK 559
Cdd:cd02754 417 LEFVVVQDAFADTET----AEYADLvLPAASWGEKE----GTMT-NSERRVSLLRAAV---EPPGE-ARPDWWILADVAR 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 560 A-----TLP-PNPKVKWDEWRG------------DYGKVRDL-IEETYPDKFHDFNKRLFTPGGFYrgnsareriwkTES 620
Cdd:cd02754 484 RlgfgeLFPyTSPEEVFEEYRRlsrgrgadlsglSYERLRDGgVQWPCPDGPPEGTRRLFEDGRFP-----------TPD 552
|
....*
gi 1148824058 621 GKAEF 625
Cdd:cd02754 553 GRARF 557
|
|
| MopB_Formate-Dh-Na-like |
cd02752 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
109-415 |
6.15e-27 |
|
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: 116.73 E-value: 6.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 109 RLTHPMRYDRDSDRYVPCGWDEAFSAIGQELKAL----------------DPKSVVFYASGRASLETSYLYALFARLYGH 172
Cdd:cd02752 54 RLKYPMYRAPGSGKWEEISWDEALDEIARKMKDIrdasfveknaagvvvnRPDSIAFLGSAKLSNEECYLIRKFARALGT 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 173 NNLPDSSNMCHETTSVGLKKVIGASVGTSVYDDFSTCDAIFFFGQNTGSNSP-RFLHPLQAAVKRGCKIVTFNPVREKgl 251
Cdd:cd02752 134 NNLDHQARIUHSPTVAGLANTFGRGAMTNSWNDIKNADVILVMGGNPAEAHPvSFKWILEAKEKNGAKLIVVDPRFTR-- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 252 etminpqsptemltgkeTQISCQYH-QVKTGGDIAAIMGMCKHVFAKDDEakqqgrNVidrdfveqhtsgfhafeETVRA 330
Cdd:cd02752 212 -----------------TAAKADLYvPIRSGTDIAFLGGMINYIIRYTPE------EV-----------------EDICG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 331 TSwdeierESGLERAALEAAGQVYVDAERVIgIYGMGLTQQVGGFESI-AMLVNLLLLkGNIGRDGTGISPVRGHSNVQG 409
Cdd:cd02752 252 VP------KEDFLKVAEMFAATGRPDKPGTI-LYAMGWTQHTVGSQNIrAMCILQLLL-GNIGVAGGGVNALRGHSNVQG 323
|
....*.
gi 1148824058 410 QRTVGI 415
Cdd:cd02752 324 ATDLGL 329
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
93-516 |
3.92e-23 |
|
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: 104.02 E-value: 3.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 93 VTELRGWKDHDLEQ----------------EGRLTHPMRydRDSDRYVPCGWDEAFSAIGQELKAL----DPKSVVFY-- 150
Cdd:cd02762 22 VASIRGDPDDPLSKgyicpkaaalgdyqndPDRLRTPMR--RRGGSFEEIDWDEAFDEIAERLRAIrarhGGDAVGVYgg 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 151 -ASGRASLETSYLYALFARLYGHNNLPDSS--NMCHETTSVGLkkviGASVGTSVYDDFSTCDAIFFFGQNT-GSNS--- 223
Cdd:cd02762 100 nPQAHTHAGGAYSPALLKALGTSNYFSAATadQKPGHFWSGLM----FGHPGLHPVPDIDRTDYLLILGANPlQSNGslr 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 224 --PRFLHPLQAAVKRGCKIVTFNPVRekgletminpqspTEmlTGKetqISCQYHQVKTGGDIAAIMGMCKHVFAKddea 301
Cdd:cd02762 176 taPDRVLRLKAAKDRGGSLVVIDPRR-------------TE--TAK---LADEHLFVRPGTDAWLLAAMLAVLLAE---- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 302 kqqgrNVIDRDFVEQHTSGFHAFEETVRATSWDEIERESGLERAALEAAGQVYVDAERVIgIYG-MGLTQQVGGFESiAM 380
Cdd:cd02762 234 -----GLTDRRFLAEHCDGLDEVRAALAEFTPEAYAPRCGVPAETIRRLAREFAAAPSAA-VYGrLGVQTQLFGTLC-SW 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 381 LVNLL-LLKGNIGRDGT---------GISPVRGHSNVQGQRTVGISEKPE---LVPLDKLAEMFDFEPPrekgvntveac 447
Cdd:cd02762 307 LVKLLnLLTGNLDRPGGamfttpaldLVGQTSGRTIGRGEWRSRVSGLPEiagELPVNVLAEEILTDGP----------- 375
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1148824058 448 egivdGSIRGFVSLGGNFVRAIPDHDVMEAAWTKMRLTVQIATKLNrshlingEVA----YLLPCLGRSEEDV 516
Cdd:cd02762 376 -----GRIRAMIVVAGNPVLSAPDGARLEAALGGLEFMVSVDVYMT-------ETTrhadYILPPASQLEKPH 436
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
67-395 |
3.76e-17 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 85.87 E-value: 3.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 67 GETGAKATLWELTTRRCTPE---------F-----FAKHTVTEL--RGWKDHD-LEQEGRLTHPMRY--DRDSDRYVPCG 127
Cdd:PRK15488 39 GKTKLTPSICEMCSTRCPIEarvvngknvFiqgnpKAKSFGTKVcaRGGSGHSlLYDPQRIVKPLKRvgERGEGKWQEIS 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 128 WDEAFSAIGQELKALD----PKSVVFYA-SGraslETSYLYALFARLYGHNNLpdssnMCHETTSVGlKKVIGASV--GT 200
Cdd:PRK15488 119 WDEAYQEIAAKLNAIKqqhgPESVAFSSkSG----SLSSHLFHLATAFGSPNT-----FTHASTCPA-GYAIAAKVmfGG 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 201 SVYDDFSTCDAIFFFGQN--TGSNSPRFLHPLQAAVKRGCKIVTFNP----VREKGLEtminpqsptemltgketqiscq 274
Cdd:PRK15488 189 KLKRDLANSKYIINFGHNlyEGINMSDTRGLMTAQMEKGAKLVVFEPrfsvVASKADE---------------------- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 275 YHQVKTGGDIAAIMGMCkHVFAKDdeakqqgrNVIDRDFVEQHTSGFHAFEETVRATSWDEIERESG-----LERAALEa 349
Cdd:PRK15488 247 WHAIRPGTDLAVVLALC-HVLIEE--------NLYDKAFVERYTSGFEELAASVKEYTPEWAEAISDvpaddIRRIARE- 316
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1148824058 350 agqVYVDAERVIGIYGMGLTQQVGGFESIAMLVNLLLLKGNIGRDG 395
Cdd:PRK15488 317 ---LAAAAPHAIVDFGHRATFTPEEFDMRRAIFAANVLLGNIERKG 359
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
107-395 |
5.09e-17 |
|
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: 84.27 E-value: 5.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 107 EGRLTHPMR--YDRDSDRYVPCGWDEAFSAIGQELKAL----DPKSVVFyaSGRASLETSYLYAlFARLYGHNNLPDSSN 180
Cdd:cd02755 53 PDRLKKPLIrvGERGEGKFREASWDEALQYIASKLKEIkeqhGPESVLF--GGHGGCYSPFFKH-FAAAFGSPNIFSHES 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 181 MCHETTSVGLKKVIGaSVGTSVYDDFSTCDAIFFFGQN--TGSNSPRfLHPLQAAVKRGCKIVTFNPvREkgletminpq 258
Cdd:cd02755 130 TCLASKNLAWKLVID-SFGGEVNPDFENARYIILFGRNlaEAIIVVD-ARRLMKALENGAKVVVVDP-RF---------- 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 259 spTEMltgkeTQISCQYHQVKTGGDIAAIMGMCkHVFAkddeakqqGRNVIDRDFVEQHTSGFHAFEETVRATSWDEIER 338
Cdd:cd02755 197 --SEL-----ASKADEWIPIKPGTDLAFVLALI-HVLI--------SENLYDAAFVEKYTNGFELLKAHVKPYTPEWAAQ 260
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1148824058 339 ESG-----LERAALEAAGQvyvdAERVI---GIYGMGLTQQVGGFESIAMlVNLLLlkGNIGRDG 395
Cdd:cd02755 261 ITDipadtIRRIAREFAAA----APHAVvdpGWRGTFYSNSFQTRRAIAI-INALL--GNIDKRG 318
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
109-395 |
8.55e-17 |
|
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. The acetylene hydratase of Pelobacter acetylenicus is a tungsten iron-sulfur protein involved in the fermentation of acetylene to ethanol and acetate. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239160 [Multi-domain] Cd Length: 477 Bit Score: 83.89 E-value: 8.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 109 RLTHPMRY--DRDSDRYVPCGWDEAFSAIGQELKALD----PKSVVFY-ASGR-ASLETSYLYALFARLYGHNNLPDSSN 180
Cdd:cd02759 54 RLLYPLKRvgERGENKWERISWDEALDEIAEKLAEIKaeygPESIATAvGTGRgTMWQDSLFWIRFVRLFGSPNLFLSGE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 181 MCHETTSVGLKKVIGASVGtsvYD--DFSTCDAIFFFGQN-TGSNSPRFLHPLQAAVKRGCKIVTFNPvREKGLETMinp 257
Cdd:cd02759 134 SCYWPRDMAHALTTGFGLG---YDepDWENPECIVLWGKNpLNSNLDLQGHWLVAAMKRGAKLIVVDP-RLTWLAAR--- 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 258 qsptemltgketqiSCQYHQVKTGGDIAAIMGMCkHVFAKDDeakqqgrnVIDRDFVEQHTSGFHAFEETVRATSWDEIE 337
Cdd:cd02759 207 --------------ADLWLPIRPGTDAALALGML-NVIINEG--------LYDKDFVENWCYGFEELAERVQEYTPEKVA 263
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1148824058 338 RESGLERAALEAAGQVYVDAeRVIGIY-GMGLTQQVGGFESIAMLVNLLLLKGNIGRDG 395
Cdd:cd02759 264 EITGVPAEKIRKAARLYATA-KPACIQwGLAIDQQKNGTQTSRAIAILRAITGNLDVPG 321
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
109-486 |
7.24e-15 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 76.67 E-value: 7.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 109 RLTHPMrYDRDSDRYVPCGWDEAFSAIGQELKALDPKS------VVFYASGRASLETSYLYALFARLYGHNNL-PDSSNM 181
Cdd:pfam00384 1 RLKYPM-VRRGDGKFVRVSWDEALDLIAKKLKRIIKKYgpdaiaINGGSGGLTDVESLYALKKLLNRLGSKNGnTEDHNG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 182 --CHETTSVGLKKVIGASVGTSVYDDFSTCDAIFFFGQNtgsnsPRFLHPL------QAAVKRGCKIVTFNPVrekglet 253
Cdd:pfam00384 80 dlCTAAAAAFGSDLRSNYLFNSSIADIENADLILLIGTN-----PREEAPIlnarirKAALKGKAKVIVIGPR------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 254 minpqsptemltgKETQISCQYHQVKTGGDIAAIMGMCkHVFAKDdeakqqgrNVIDRDFveqhtsgfhafeetvratsw 333
Cdd:pfam00384 148 -------------LDLTYADEHLGIKPGTDLALALAGA-HVFIKE--------LKKDKDF-------------------- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 334 deieresgleraaleaagqvyvdAERVIGIYGMGLTQQVGGFESIAMLVNLLLLKGNIGRDGTGISPVRghsNVQGQRtv 413
Cdd:pfam00384 186 -----------------------APKPIIIVGAGVLQRQDGEAIFRAIANLADLTGNIGRPGGGWNGLN---ILQGAA-- 237
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1148824058 414 gisekpELVPLDKLaemfdfepPREKGVNTVEACEGIVDGSIRGFVSLGGNFVRAIPDHDVMEAAWTKMRLTV 486
Cdd:pfam00384 238 ------SPVGALDL--------GLVPGIKSVEMINAIKKGGIKVLYLLGNNPFVTHADENRVVKALQKLDLFV 296
|
|
| MopB_NADH-Q-OR-NuoG2 |
cd02768 |
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone ... |
104-245 |
8.88e-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: 73.86 E-value: 8.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 104 LEQEGRLTHPMRydRDSDRYVPCGWDEAFSAIGQELKALDPKSVVFYASGRASLETSYLYALFARLYGhnnlpdSSNMCH 183
Cdd:cd02768 49 LNSRQRLTQPLI--KKGGKLVPVSWEEALKTVAEGLKAVKGDKIGGIAGPRADLESLFLLKKLLNKLG------SNNIDH 120
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1148824058 184 E--TTSVGLKKV-IGASVGTSVYDDFSTCDAIFFFGQNtgsnsPRFLHPL------QAAVKRGCKIVTFNP 245
Cdd:cd02768 121 RlrQSDLPADNRlRGNYLFNTSIAEIEEADAVLLIGSN-----LRKEAPLlnarlrKAVKKKGAKIAVIGP 186
|
|
| MopB_2 |
cd02763 |
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
82-395 |
2.07e-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: 64.08 E-value: 2.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 82 RCTPEFFAKH-TVTELRGWKDHDLEQ----------------EGRLTHPMRY--DRDSDRYVPCGWDEAFSAIGQELKAL 142
Cdd:cd02763 10 RCGIRVHLRDgKVRYIKGNPDHPLNKgvicakgssgimkqysPARLTKPLLRkgPRGSGQFEEIEWEEAFSIATKRLKAA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 143 ---DPKSVVFYaSGRASLETsyLYALFARLYGHNNLPDSSNMCHETTSVGLKKVIGASVGTSVYDDFSTCDAIFFFGQNT 219
Cdd:cd02763 90 ratDPKKFAFF-TGRDQMQA--LTGWFAGQFGTPNYAAHGGFCSVNMAAGGLYSIGGSFWEFGGPDLEHTKYFMMIGVAE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 220 GSNSPRFLHPLQAAVKRGCKIVTFNPVRekgletminpqsptemlTGKETqISCQYHQVKTGGDIAAIMGMCKHVFAKdd 299
Cdd:cd02763 167 DHHSNPFKIGIQKLKRRGGKFVAVNPVR-----------------TGYAA-IADEWVPIKPGTDGAFILALAHELLKA-- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 300 eakqqgrNVIDRDFVEQHTSGFHAFE------ETVRATSWDEIERESG-LERAALEAAGQV---YVDA-----ERVIG-- 362
Cdd:cd02763 227 -------GLIDWEFLKRYTNAAELVDytpewvEKITGIPADTIRRIAKeLGVTARDQPIELpiaWTDVwgrkhEKITGrp 299
|
330 340 350
....*....|....*....|....*....|....*.
gi 1148824058 363 --IYGM-GLTQQVGGFESIAMLVNLLLLKGNIGRDG 395
Cdd:cd02763 300 vsFHAMrGIAAHSNGFQTIRALFVLMMLLGTIDRPG 335
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
109-409 |
3.95e-09 |
|
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: 59.93 E-value: 3.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 109 RLTHPM------------RYDRDSDRYVPCGWDEAFSAIGQELK----ALDPKSV-VFYASGRASLETSYLYALFARL-- 169
Cdd:cd02751 47 RIKYPMkrvgwlgngpgsRELRGEGEFVRISWDEALDLVASELKrireKYGNEAIfGGSYGWASAGRLHHAQSLLHRFln 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 170 -----YGHNNlPDSSnmchETTSVGLKKVIGASV----GTSVYDDFSTCDAIFFFG----QNTGSNSPRFLHP----LQA 232
Cdd:cd02751 127 liggyLGSYG-TYST----GAAQVILPHVVGSDEvyeqGTSWDDIAEHSDLVVLFGanplKTRQGGGGGPDHGsyyyLKQ 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 233 AVKRGCKIVTFNPVREKGLETMinpqsptemltgketqiSCQYHQVKTGGDIAAIMGMCkHVFAKDdeakqqgrNVIDRD 312
Cdd:cd02751 202 AKDAGVRFICIDPRYTDTAAVL-----------------AAEWIPIRPGTDVALMLAMA-HTLITE--------DLHDQA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 313 FVEQHTSGFHAFEETVRATSwDEIEREsgLERAAlEAAGqvyVDAERVIG------------IYGMGLTQQVGGFESIAM 380
Cdd:cd02751 256 FLARYTVGFDEFKDYLLGES-DGVPKT--PEWAA-EITG---VPAETIRAlareiaskrtmiAQGWGLQRAHHGEQPAWM 328
|
330 340
....*....|....*....|....*....
gi 1148824058 381 LVNLLLLKGNIGRDGTGISPVRGHSNVQG 409
Cdd:cd02751 329 LVTLAAMLGQIGLPGGGFGFGYGYSNGGG 357
|
|
| 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 ... |
104-236 |
1.24e-08 |
|
MopB_NDH-1_NuoG2-N7: The second domain of the NuoG subunit (with a [4Fe-4S] cluster, N7) of the NADH-quinone oxidoreductase/NADH dehydrogenase-1 (NDH-1) found in various bacteria. The NDH-1 is the first energy-transducting complex in the respiratory chain and functions as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. In Escherichia coli NDH-1, the largest subunit is encoded by the nuoG gene, and is part of the 14 distinct subunits constituting the functional enzyme. The NuoG subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Unique to this group, compared to the other prokaryotic and eukaryotic groups in this domain protein family (NADH-Q-OR-NuoG2), is an N-terminal [4Fe-4S] cluster (N7/N1c) present in the second domain. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain belongs to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239172 [Multi-domain] Cd Length: 472 Bit Score: 58.17 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 104 LEQEGRLTHPMRydRDSDRYVPCGWDEAFSAIGQELKALDPKSVVFyASGRASLETSYLYALFARLY-GHNNLPDSSNMc 182
Cdd:cd02771 49 VNSRDRLTQPLI--RRGGTLVPVSWNEALDVAAARLKEAKDKVGGI-GSPRASNESNYALQKLVGAVlGTNNVDHRARR- 124
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1148824058 183 hetTSVGLKKVIGASVGTsvYDDFSTCDAIFFFGQNTGSNSPRFLHPLQAAVKR 236
Cdd:cd02771 125 ---LIAEILRNGPIYIPS--LRDIESADAVLVLGEDLTQTAPRIALALRQAARR 173
|
|
| MopB_Arsenite-Ox |
cd02756 |
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the ... |
96-404 |
3.37e-08 |
|
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: 57.11 E-value: 3.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 96 LRGWKDHDLEQEGRLTHPMRydRDSDRYVPCGWDEAFSAIGQELKA-LDPK----SVVFYAS----GRASLETS------ 160
Cdd:cd02756 104 ERIWSPDNRVGETRLTTPLV--RRGGQLQPTTWDDAIDLVARVIKGiLDKDgnddAVFASRFdhggGGGGFENNwgvgkf 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 161 YLYAL---FARLygHNNlPDSSNMCHETTSVGlkkvIGASvgTSVYDDFSTCDAIFFFGQNTGSNSPRF-----LHPLQA 232
Cdd:cd02756 182 FFMALqtpFVRI--HNR-PAYNSEVHATREMG----VGEL--NNSYEDARLADTIVLWGNNPYETQTVYflnhwLPNLRG 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 233 AVKrGCKIVTFNP--VREKGLETMINPQsPTEMLTGKETQISCQ---YHQVKTGGDIAAIMGMCKHVFAKDDEAKQQGRN 307
Cdd:cd02756 253 ATV-SEKQQWFPPgePVPPGRIIVVDPR-RTETVHAAEAAAGKDrvlHLQVNPGTDTALANAIARYIYESLDEVLAEAEQ 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 308 V--IDRDFVEqhtsgfhafeetvRATSWDEIERESGLERaaleaagqvyvdaeRVIGIYGMGLTQQVGGFESIAMLVNLL 385
Cdd:cd02756 331 ItgVPRAQIE-------------KAADWIAKPKEGGYRK--------------RVMFEYEKGIIWGNDNYRPIYSLVNLA 383
|
330
....*....|....*....
gi 1148824058 386 LLKGNIGRDGTGISPVRGH 404
Cdd:cd02756 384 IITGNIGRPGTGCVRQGGH 402
|
|
| MopB_DmsA-EC |
cd02770 |
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
109-409 |
5.81e-07 |
|
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: 53.10 E-value: 5.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 109 RLTHPMRY--DRDSDRYVPCGWDEAFSAIGQELKAL----DPKSVVF-YASGRASLETSYLyALFARLY----GHNNLPD 177
Cdd:cd02770 59 RLKYPMKRvgKRGEGKFVRISWDEALDTIASELKRIiekyGNEAIYVnYGTGTYGGVPAGR-GAIARLLnltgGYLNYYG 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 178 SSNMCHETTsvGLKKVIGASVGTSVYDDFSTCDAIFFFGQNTGSNSPRFLHP---LQAAVKRGCKIVtfnpvrekgletM 254
Cdd:cd02770 138 TYSWAQITT--ATPYTYGAAASGSSLDDLKDSKLVVLFGHNPAETRMGGGGStyyYLQAKKAGAKFI------------V 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 255 INPQSpTEMLTGKETqiscQYHQVKTGGDIAAIMGMCkHVFAKDdeakqqgrNVIDRDFVEQHTSGF---HAFEETVRAT 331
Cdd:cd02770 204 IDPRY-TDTAVTLAD----EWIPIRPGTDAALVAAMA-YVMITE--------NLHDQAFLDRYCVGFdaeHLPEGAPPNE 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 332 SW-DEI--ERESGLERAALEAAGQVYVDAERVIG-------------IYGMGLTQQVGGFESIAMLVNLLLLKGNIGRDG 395
Cdd:cd02770 270 SYkDYVlgTGYDGTPKTPEWASEITGVPAETIRRlareiattkpaaiLQGWGPQRHANGEQAARAIMMLAAMTGNVGIPG 349
|
330
....*....|....
gi 1148824058 396 TGISPVRGHSNVQG 409
Cdd:cd02770 350 GNTGARPGGSAYNG 363
|
|
| MopB_Res-Cmplx1_Nad11 |
cd02773 |
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone ... |
109-230 |
1.49e-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: 51.11 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 109 RLTHPMRydRDSDRYVPCGWDEAFSAIGQELKALDPKSVVFYASGRASLETSY-LYALFARLyghnnlpDSSNMCHETTS 187
Cdd:cd02773 53 RLDKPYI--RKNGKLKPATWEEALAAIAKALKGVKPDEIAAIAGDLADVESMVaLKDLLNKL-------GSENLACEQDG 123
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1148824058 188 VGLKKVIGAS-VGTSVYDDFSTCDAIFFFGQNtgsnsPRFLHPL 230
Cdd:cd02773 124 PDLPADLRSNyLFNTTIAGIEEADAVLLVGTN-----PRFEAPV 162
|
|
| Molydop_binding |
pfam01568 |
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
643-751 |
1.96e-05 |
|
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: 44.19 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 643 YRLMTLRSNDQFNTTIYGYSDRLRGIEGtRNVLLIDPKEMEKLGLQEGQLVGLQTDIedGR--------ERKVEGLKVLP 714
Cdd:pfam01568 1 LYLITGRVLGQYHSQTRTRRVLRLAKPE-PEVVEIHPEDAAALGIKDGDLVEVTSRR--GSvvvrakvtDRVRPGVVFMP 77
|
90 100 110
....*....|....*....|....*....|....*..
gi 1148824058 715 FQLPDGCVAGyypELNPLIPLSLHErLSQTPASKAVP 751
Cdd:pfam01568 78 FGWWYEPRGG---NANALTDDATDP-LSGGPEFKTCA 110
|
|
| PRK13532 |
PRK13532 |
nitrate reductase catalytic subunit NapA; |
109-397 |
3.05e-05 |
|
nitrate reductase catalytic subunit NapA;
Pssm-ID: 237416 [Multi-domain] Cd Length: 830 Bit Score: 47.59 E-value: 3.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 109 RLTHPM------RYDRDSDrYVPCGWDEAFSAIGQE----LKALDPKSVVFYASGRASLETSYLYA-LFARLYGHNNLPD 177
Cdd:PRK13532 97 RLTQPLlrmkdgKYDKEGE-FTPVSWDQAFDVMAEKfkkaLKEKGPTAVGMFGSGQWTIWEGYAASkLMKAGFRSNNIDP 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 178 SSNMCHETTSVGLKKVIGASVGTSVYDDFSTCDAIFFFGQNTGSNSP---------RFLHPlqaavkrGCKIVTFNPVRE 248
Cdd:PRK13532 176 NARHCMASAVVGFMRTFGIDEPMGCYDDIEAADAFVLWGSNMAEMHPilwsrvtdrRLSNP-------DVKVAVLSTFEH 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 249 KGLE----TMI-NPQSptemltgketqiscqyhqvktggDIAAIMGMCKHVFakddeakQQGRnvIDRDFVEQHT----- 318
Cdd:PRK13532 249 RSFEladnGIIfTPQT-----------------------DLAILNYIANYII-------QNNA--VNWDFVNKHTnfrkg 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 319 -----------------------------SGFHAFEETVRATSWDEIERESGLERAALEAAGQVYVDAER-VIGIYGMGL 368
Cdd:PRK13532 297 atdigyglrpthplekaaknpgtagksepISFEEFKKFVAPYTLEKTAKMSGVPKEQLEQLAKLYADPNRkVVSFWTMGF 376
|
330 340
....*....|....*....|....*....
gi 1148824058 369 TQQVGGFESIAMLVNLLLLKGNIGRDGTG 397
Cdd:PRK13532 377 NQHTRGVWANNLVYNIHLLTGKISTPGNG 405
|
|
| PRK07860 |
PRK07860 |
NADH dehydrogenase subunit G; Validated |
106-254 |
9.55e-05 |
|
NADH dehydrogenase subunit G; Validated
Pssm-ID: 236118 [Multi-domain] Cd Length: 797 Bit Score: 46.09 E-value: 9.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148824058 106 QEGRLTHPMRYDRDsDRYVPCGWDEAFSAIGQEL-KALDPKSVVfyASGRASLETSYLYALFARLYGHNNLPDSSNMCH- 183
Cdd:PRK07860 275 QPDRITTPLVRDED-GELEPASWSEALAVAARGLaAARGRVGVL--VGGRLTVEDAYAYAKFARVALGTNDIDFRARPHs 351
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90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1148824058 184 --ETTSVGlKKVIGASVGTSvYDDFSTCDAIFFFGQNTGSNSP-RFLHPLQAAVKRGCKIVTFNPVREKGLETM 254
Cdd:PRK07860 352 aeEADFLA-ARVAGRGLGVT-YADLEKAPAVLLVGFEPEEESPiVFLRLRKAARKHGLKVYSIAPFATRGLEKM 423
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|
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