|
Name |
Accession |
Description |
Interval |
E-value |
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
10-705 |
0e+00 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 852.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 10 TEVAAVIETQCPFCSVQCKMTVTEGGNGIpgqrraeYKVEGVPNA-ASEGRVCVKGMHAHQHAVHSQRLTNPFIRSNGEL 88
Cdd:COG3383 1 SNPMKKVKTVCPYCGVGCGIDLEVKDGKI-------VKVEGDPDHpVNRGRLCVKGRFGFEFVNSPDRLTTPLIRRGGEF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 89 VPCSWDEAFAVASQHLQGISEQHGPDANAVYGGGSLTNETAYLLGKFARVALGTRHIDYNGRFCMSAAASAGSKTFGIDr 168
Cdd:COG3383 74 REVSWDEALDLVAERLREIQAEHGPDAVAFYGSGQLTNEENYLLQKLARGVLGTNNIDNNARLCMASAVAGLKQSFGSD- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 169 GLTFRLADIPLARCIVLAGTNIAECQPTLLPYFNRAKENGARIIVIDPRKTATAAMADMHLPIRPGTDTVLADVMLKIIM 248
Cdd:COG3383 153 APPNSYDDIEEADVILVIGSNPAEAHPVLARRIKKAKKNGAKLIVVDPRRTETARLADLHLQIKPGTDLALLNGLLHVII 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 249 DEGFIDESFIQARTNGYDELSVYLNSLDLSQAADICGLELGQIREAALAFGEADTGMVLTARGVEQQTDGHLAVRHFLNL 328
Cdd:COG3383 233 EEGLVDEDFIAERTEGFEELKASVAKYTPERVAEITGVPAEDIREAARLIAEAKRAMILWGMGVNQHTQGTDNVNAIINL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 329 VLATGKIGREGCGYGAITGQGNGQGGREHGQKADQLPGYRSIENEKDRAYVASVWGVEAasLPGK-GVSAYEMMELIHQG 407
Cdd:COG3383 313 ALATGNIGRPGTGPFPLTGQNNVQGGRDMGALPNVLPGYRDVTDPEHRAKVADAWGVPP--LPDKpGLTAVEMFDAIADG 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 408 VIKSLFVMGSNPIVSNPNAGLVEEALNKLDFLMVADMFMSETAQLADLVLPVTSYMENEGTLTNLEGRVLLREAGRQAPG 487
Cdd:COG3383 391 EIKALWIIGENPAVSDPDANHVREALEKLEFLVVQDIFLTETAEYADVVLPAASWAEKDGTFTNTERRVQRVRKAVEPPG 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 488 EARHDWMILCSIADMLGKGhyFRFNEPEEVFNELRLASKggiaDYYGITYDRLRREKGVYWPCPSPEEAGAGLLFQQSFA 567
Cdd:COG3383 471 EARPDWEIIAELARRLGYG--FDYDSPEEVFDEIARLTP----DYSGISYERLEALGGVQWPCPSEDHPGTPRLFTGRFP 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 568 HPDGKAVFSimeGTPWKGVTE----EYSLILTNGRVLSHYLTGVQTRRSPSLLARELENFVEIHPITAQRYRIRDGEWVE 643
Cdd:COG3383 545 TPDGKARFV---PVEYRPPAElpdeEYPLVLTTGRLLDQWHTGTRTRRSPRLNKHAPEPFVEIHPEDAARLGIKDGDLVR 621
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2083076315 644 VQSEHGYFTVRARIKDQIREDTLFVPMHWGGvQNVNHATRPELDPFCKMPGFKTSAVRIRPL 705
Cdd:COG3383 622 VSSRRGEVVLRARVTDRVRPGTVFMPFHWGE-GAANALTNDALDPVSKQPEYKACAVRVEKV 682
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
18-582 |
0e+00 |
|
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: 703.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 18 TQCPFCSVQCKMTVTEGGNGIpgqrraeYKVEGVPNA-ASEGRVCVKGMHAHQHAVHSQRLTNPFIRSNG-ELVPCSWDE 95
Cdd:cd02754 2 TTCPYCGVGCGVEIGVKDGKV-------VAVRGDPEHpVNRGRLCIKGLNLHKTLNGPERLTRPLLRRNGgELVPVSWDE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 96 AFAVASQHLQGISEQHGPDANAVYGGGSLTNETAYLLGKFARVALGTRHIDYNGRFCMSAAASAGSKTFGIDrGLTFRLA 175
Cdd:cd02754 75 ALDLIAERFKAIQAEYGPDSVAFYGSGQLLTEEYYAANKLAKGGLGTNNIDTNSRLCMASAVAGYKRSFGAD-GPPGSYD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 176 DIPLARCIVLAGTNIAECQPTLLPYFNRAKEN--GARIIVIDPRKTATAAMADMHLPIRPGTDTVLADVMLKIIMDEGFI 253
Cdd:cd02754 154 DIEHADCFFLIGSNMAECHPILFRRLLDRKKAnpGAKIIVVDPRRTRTADIADLHLPIRPGTDLALLNGLLHVLIEEGLI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 254 DESFIQARTNGYDELSVYLNSLDLSQAADICGLELGQIREAALAFGEADTGMVLTARGVEQQTDGHLAVRHFLNLVLATG 333
Cdd:cd02754 234 DRDFIDAHTEGFEELKAFVADYTPEKVAEITGVPEADIREAARLFGEARKVMSLWTMGVNQSTQGTAANNAIINLHLATG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 334 KIGREGCGYGAITGQGNGQGGREHGQKADQLPGYRSIENEKDRAYVASVWGVEAASLPGK-GVSAYEMMELIHQGVIKSL 412
Cdd:cd02754 314 KIGRPGSGPFSLTGQPNAMGGREVGGLANLLPGHRSVNNPEHRAEVAKFWGVPEGTIPPKpGLHAVEMFEAIEDGEIKAL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 413 FVMGSNPIVSNPNAGLVEEALNKLDFLMVADMF-MSETAQLADLVLPVTSYMENEGTLTNLEGRVLLREAGRQAPGEARH 491
Cdd:cd02754 394 WVMCTNPAVSLPNANRVREALERLEFVVVQDAFaDTETAEYADLVLPAASWGEKEGTMTNSERRVSLLRAAVEPPGEARP 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 492 DWMILCSIADMLGKGHYFRFNEPEEVFNELRLASKGGIADYYGITYDRLRReKGVYWPCPSPEEAGAGLLFQ-QSFAHPD 570
Cdd:cd02754 474 DWWILADVARRLGFGELFPYTSPEEVFEEYRRLSRGRGADLSGLSYERLRD-GGVQWPCPDGPPEGTRRLFEdGRFPTPD 552
|
570
....*....|..
gi 2083076315 571 GKAVFSIMEGTP 582
Cdd:cd02754 553 GRARFVAVPYRP 564
|
|
| Fdh-alpha |
TIGR01591 |
formate dehydrogenase, alpha subunit, archaeal-type; This model describes a subset of formate ... |
18-702 |
0e+00 |
|
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: 579.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 18 TQCPFCSVQCKMTVTEGGNGIpgqRRAEYKVEGVPNaasEGRVCVKGMHAHQHAVHSQRLTNPFIRSNGELVPCSWDEAF 97
Cdd:TIGR01591 1 TVCPYCGVGCSLNLVVKDGKI---VRVEPYQGHKAN---RGHLCVKGYFAWEFINSKDRLTTPLIREGDKFREVSWDEAI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 98 AVASQHLQGISEQHGPDANAVYGGGSLTNETAYLLGKFARVALGTRHIDYNGRFCMSAAASAGSKTFGIDRGlTFRLADI 177
Cdd:TIGR01591 75 SYIAEKLKEIKEKYGPDSIGFIGSSRGTNEENYLLQKLARAVIGTNNVDNCARVCHGPSVAGLKQTVGIGAM-SNTISEI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 178 PLARCIVLAGTNIAECQPTLLPYFNRAKENGARIIVIDPRKTATAAMADMHLPIRPGTDTVLADVMLKIIMDEGFIDESF 257
Cdd:TIGR01591 154 ENADLIVIIGYNPAESHPVVAQYLKNAKRNGAKIIVIDPRKTETAKIADLHIPLKPGTDIALLNAMANVIIEEGLYDKAF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 258 IQARTNGYDELSVYLNSLDLSQAADICGLELGQIREAALAFGEADTGMVLTARGVEQQTDGHLAVRHFLNLVLATGKIGR 337
Cdd:TIGR01591 234 IEKRTEGFEEFREIVKGYTPEYVEDITGVPADLIREAARMYAKAGSAAILWGMGVTQHSQGVETVMALINLAMLTGNIGK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 338 EGCGYGAITGQGNGQGGREHGQKADQLPGYRSIENEKDRAYVASVWGVEaaSLPGK-GVSAYEMMELIHQGVIKSLFVMG 416
Cdd:TIGR01591 314 PGGGVNPLRGQNNVQGACDMGALPDFLPGYQPVSDEEVREKFAKAWGVV--KLPAEpGLRIPEMIDAAADGDVKALYIMG 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 417 SNPIVSNPNAGLVEEALNKLDFLMVADMFMSETAQLADLVLPVTSYMENEGTLTNLEGRVLLREAGRQAPGEARHDWMIL 496
Cdd:TIGR01591 392 EDPLQSDPNTSKVRKALEKLELLVVQDIFMTETAKYADVVLPAAAWLEKEGTFTNAERRIQRFFKAVEPKGESKPDWEII 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 497 CSIADMLG-KGHYfrfNEPEEVFNELRLASKggiaDYYGITYDRLRREKGVYWPCPSPEEAGAGLLFQQSFAHPDGKAVF 575
Cdd:TIGR01591 472 QELANALGlDWNY---NHPQEIMDEIRELTP----LFAGLTYERLDELGSLQWPCNDSDASPTSYLYKDKFATPDGKAKF 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 576 -SIMEGTPWKGVTEEYSLILTNGRVLSHYLTGVQTRRSPSLLARELENFVEIHPITAQRYRIRDGEWVEVQSEHGYFTVR 654
Cdd:TIGR01591 545 iPLEWVAPIEEPDDEYPLILTTGRVLTHYNVGEMTRRVAGLRRLSPEPYVEINTEDAKKLGIKDGDLVKVKSRRGEITLR 624
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 2083076315 655 ARIKDQIREDTLFVPMHWGGVQnVNHATRPELDPFCKMPGFKTSAVRI 702
Cdd:TIGR01591 625 AKVSDRVNKGAIYITMHFWDGA-VNNLTTDDLDPISGTPEYKYTAVRI 671
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
18-705 |
0e+00 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 544.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 18 TQCPFCSVQCKMTVT-EGGNGIpgqrraeyKVEGVPNA-ASEGRVCVKGMHAHQHAVHSQRLTNPFIR----SNGELVPC 91
Cdd:COG0243 26 TTCPGCGVGCGLGVKvEDGRVV--------RVRGDPDHpVNRGRLCAKGAALDERLYSPDRLTYPMKRvgprGSGKFERI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 92 SWDEAFAVASQHLQGISEQHGPDANAVYGGGS----LTNETAYLLGKFARvALGTRHIDYNGRFCMSAAASAGSKTFGID 167
Cdd:COG0243 98 SWDEALDLIAEKLKAIIDEYGPEAVAFYTSGGsagrLSNEAAYLAQRFAR-ALGTNNLDDNSRLCHESAVAGLPRTFGSD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 168 RGlTFRLADIPLARCIVLAGTNIAECQPTLLPYFNRA-KENGARIIVIDPRKTATAAMADMHLPIRPGTDTVLADVMLKI 246
Cdd:COG0243 177 KG-TVSYEDLEHADLIVLWGSNPAENHPRLLRRLREAaKKRGAKIVVIDPRRTETAAIADEWLPIRPGTDAALLLALAHV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 247 IMDEGFIDESFIQARTNGYDELSVYLNSLDLSQAADICGLELGQIREAALAFGEADTGMVLTARGVEQQTDGHLAVRHFL 326
Cdd:COG0243 256 LIEEGLYDRDFLARHTVGFDELAAYVAAYTPEWAAEITGVPAEDIRELAREFATAKPAVILWGMGLQQHSNGTQTVRAIA 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 327 NLVLATGKIGREGCGYGAITGqgngqggrehgqkadqlpgyRSIENEKDRAyvasvwgveaaslpgkgvsayemmelihq 406
Cdd:COG0243 336 NLALLTGNIGKPGGGPFSLTG--------------------EAILDGKPYP----------------------------- 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 407 gvIKSLFVMGSNPIVSNPNAGLVEEALNKLDFLMVADMFMSETAQLADLVLPVTSYMENEGTLTNLE-GRVLLREAGRQA 485
Cdd:COG0243 367 --IKALWVYGGNPAVSAPDTNRVREALRKLDFVVVIDTFLTETARYADIVLPATTWLERDDIVTNSEdRRVHLSRPAVEP 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 486 PGEARHDWMILCSIADMLGKGHYFRF-NEPEEVFNELRLASKGGiadyyGITYDRLRREKGVYWPCPSPEEAGAgllfQQ 564
Cdd:COG0243 445 PGEARSDWEIFAELAKRLGFEEAFPWgRTEEDYLRELLEATRGR-----GITFEELREKGPVQLPVPPEPAFRN----DG 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 565 SFAHPDGKAVFS----IMEGTP--------WKGVTEEYSLILTNGRVLSHYLTgvQTRRSPSLLARELENFVEIHPITAQ 632
Cdd:COG0243 516 PFPTPSGKAEFYsetlALPPLPryappyegAEPLDAEYPLRLITGRSRDQWHS--TTYNNPRLREIGPRPVVEINPEDAA 593
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2083076315 633 RYRIRDGEWVEVQSEHGYFTVRARIKDQIREDTLFVPMHWG------GVQNVNHATRPELDPFCKMPGFKTSAVRIRPL 705
Cdd:COG0243 594 ALGIKDGDLVRVESDRGEVLARAKVTEGIRPGVVFAPHGWWyepaddKGGNVNVLTPDATDPLSGTPAFKSVPVRVEKA 672
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
17-582 |
2.57e-172 |
|
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: 503.28 E-value: 2.57e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 17 ETQCPFCSVQCKMTVTEGGNGIpgqrraeYKVEGVPNA-ASEGRVCVKGMHAHQHAVHSQRLTNPFIRSNGELVPCSWDE 95
Cdd:cd02753 1 KTVCPYCGVGCGLELWVKDNKI-------VGVEPVKGHpVNRGKLCVKGRFGFDFVNSKDRLTKPLIRKNGKFVEASWDE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 96 AFAVASQHLQGISEQHGPDANAVYGGGSLTNETAYLLGKFARVALGTRHIDYNGRFCMSAAASAGSKTFGIDRGlTFRLA 175
Cdd:cd02753 74 ALSLVASRLKEIKDKYGPDAIAFFGSAKCTNEENYLFQKLARAVGGTNNVDHCARLCHSPTVAGLAETLGSGAM-TNSIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 176 DIPLARCIVLAGTNIAECQPTLLPYFNRAKENGARIIVIDPRKTATAAMADMHLPIRPGTDTVLADVMLKIIMDEGFIDE 255
Cdd:cd02753 153 DIEEADVILVIGSNTTEAHPVIARRIKRAKRNGAKLIVADPRRTELARFADLHLQLRPGTDVALLNAMAHVIIEEGLYDE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 256 SFIQARTNGYDELSVYLNSLDLSQAADICGLELGQIREAALAFGEADTGMVLTARGVEQQTDGHLAVRHFLNLVLATGKI 335
Cdd:cd02753 233 EFIEERTEGFEELKEIVEKYTPEYAERITGVPAEDIREAARMYATAKSAAILWGMGVTQHSHGTDNVMALSNLALLTGNI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 336 GREGCGYGAITGQGNGQGGREHGQKADQLPGYrsienekdrayvasvwgveaaslpgkgvsayemmelihqgvIKSLFVM 415
Cdd:cd02753 313 GRPGTGVNPLRGQNNVQGACDMGALPNVLPGY-----------------------------------------VKALYIM 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 416 GSNPIVSNPNAGLVEEALNKLDFLMVADMFMSETAQLADLVLPVTSYMENEGTLTNLEGRVLLREAGRQAPGEARHDWMI 495
Cdd:cd02753 352 GENPALSDPNTNHVRKALESLEFLVVQDIFLTETAELADVVLPAASFAEKDGTFTNTERRVQRVRKAVEPPGEARPDWEI 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 496 LCSIADMLG-KGHYFRfnePEEVFNELRLASKggiaDYYGITYDRLRREKGVYWPCPSPEEAGAGLLFQQSFAHPDGKAV 574
Cdd:cd02753 432 IQELANRLGyPGFYSH---PEEIFDEIARLTP----QYAGISYERLERPGGLQWPCPDEDHPGTPILHTERFATPDGKAR 504
|
....*...
gi 2083076315 575 FSIMEGTP 582
Cdd:cd02753 505 FMPVEYRP 512
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
17-503 |
9.15e-108 |
|
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: 332.37 E-value: 9.15e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 17 ETQCPFCSVQCKMTVTEGGNGIpgqrraeYKVEGVPN-AASEGRVCVKGMHAHQHAVHSQRLTNPFIRSN--GELVPCSW 93
Cdd:cd00368 1 PSVCPFCGVGCGILVYVKDGKV-------VRIEGDPNhPVNEGRLCDKGRAGLDGLYSPDRLKYPLIRVGgrGKFVPISW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 94 DEAFAVASQHLQGISEQHGPDANAVYGGGSLTNETAYLLGKFARvALGTRHIDYNGRFCMSAAAsAGSKTFGIDrGLTFR 173
Cdd:cd00368 74 DEALDEIAEKLKEIREKYGPDAIAFYGGGGASNEEAYLLQKLLR-ALGSNNVDSHARLCHASAV-AALKAFGGG-APTNT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 174 LADIPLARCIVLAGTNIAECQPTLLPYFNRAKENGARIIVIDPRKTATAAMADMHLPIRPGTDTVLADVmlkiimdegfi 253
Cdd:cd00368 151 LADIENADLILLWGSNPAETHPVLAARLRRAKKRGAKLIVIDPRRTETAAKADEWLPIRPGTDAALALA----------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 254 desfiqartngydelsvylnsldlSQAADICGLELGQIREAALAFGEADTGMVLTARGVEQQTDGHLAVRHFLNLVLATG 333
Cdd:cd00368 220 ------------------------EWAAEITGVPAETIRALAREFAAAKRAVILWGMGLTQHTNGTQNVRAIANLAALTG 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 334 KIGREGCGYGAitgqgngqggrehgqkadqlpgyrsienekdrayvasvwgveaaslpgkgvsayemmelihqgvikslf 413
Cdd:cd00368 276 NIGRPGGGLGP--------------------------------------------------------------------- 286
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 414 vmGSNPIVSNPNAGLVEEALNKLDFLMVADMFMSETAQLADLVLPVTSYMENEGTLTNLEGRVLLREAGRQAPGEARHDW 493
Cdd:cd00368 287 --GGNPLVSAPDANRVRAALKKLDFVVVIDIFMTETAAYADVVLPAATYLEKEGTYTNTEGRVQLFRQAVEPPGEARSDW 364
|
490
....*....|
gi 2083076315 494 MILCSIADML 503
Cdd:cd00368 365 EILRELAKRL 374
|
|
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
20-572 |
6.35e-83 |
|
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: 271.81 E-value: 6.35e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 20 CPF-CSVQCKMTVTeggngIPGQRRAeyKVEGVP-NAASEGRVCVKGMHAHQHAVHSQRLTNPFIRSN---GELVPCSWD 94
Cdd:cd02766 4 CPLdCPDTCSLLVT-----VEDGRIV--RVEGDPaHPYTRGFICAKGARYVERVYSPDRLLTPLKRVGrkgGQWERISWD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 95 EAFAVASQHLQGISEQHGPDANAVYGGGSLTNETAYLLGKFARVALGTRHIDYNgrFCMSAAASAGSKTFGIDRGLTfrL 174
Cdd:cd02766 77 EALDTIAAKLKEIKAEYGPESILPYSYAGTMGLLQRAARGRFFHALGASELRGT--ICSGAGIEAQKYDFGASLGND--P 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 175 ADIPLARCIVLAGTNIAECQPTLLPYFNRAKENGARIIVIDPRKTATAAMADMHLPIRPGTDTVLADVMLKIIMDEGFID 254
Cdd:cd02766 153 EDMVNADLIVIWGINPAATNIHLMRIIQEARKRGAKVVVIDPYRTATAARADLHIQIRPGTDGALALGVAKVLFREGLYD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 255 ESFIQARTNGYDELSVYLNSLDLSQAADICGLELGQIREAALAFGEADTGMVLTARGVEQQTDGHLAVRHFLNLVLATGK 334
Cdd:cd02766 233 RDFLARHTEGFEELKAHLETYTPEWAAEITGVSAEEIEELARLYGEAKPPSIRLGYGMQRYRNGGQNVRAIDALPALTGN 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 335 IGREGCG--YGaitgqgngqggrehgqkadqlpgyrsienekdrayvasvwgveaaslpgkgvsayemmelIHQGVIKSL 412
Cdd:cd02766 313 IGVPGGGafYS------------------------------------------------------------NSGPPVKAL 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 413 FVMGSNPIVSNPNAGLVEEAL-NKLDFLMVADMFMSETAQLADLVLPVTSYMENEGTLTNLEGR-VLLREAGRQAPGEAR 490
Cdd:cd02766 333 WVYNSNPVAQAPDSNKVRKGLaREDLFVVVHDQFMTDTARYADIVLPATTFLEHEDVYASYWHYyLQYNEPAIPPPGEAR 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 491 HDWMILCSIADMLGKGHYFrFNEPEEVFneLRLASKGGIADYYGITYDRLRRekgvYWPCPSPEEAgaglLFQQSFAHPD 570
Cdd:cd02766 413 SNTEIFRELAKRLGFGEPP-FEESDEEW--LDQALDGTGLPLEGIDLERLLG----PRKAGFPLVA----WEDRGFPTPS 481
|
..
gi 2083076315 571 GK 572
Cdd:cd02766 482 GK 483
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
76-501 |
8.93e-73 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 240.38 E-value: 8.93e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 76 RLTNPFIR-SNGELVPCSWDEAFAVASQHLQGISEQHGPDANAVYG--GGSLTNETAYLLGKFARVALG--TRHIDYNGR 150
Cdd:pfam00384 1 RLKYPMVRrGDGKFVRVSWDEALDLIAKKLKRIIKKYGPDAIAINGgsGGLTDVESLYALKKLLNRLGSknGNTEDHNGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 151 FCMSAAASAGSkTFGIDRGLTFRLADIPLARCIVLAGTNIAECQPTL-LPYFNRAKENGARIIVIDPRKTATaaMADMHL 229
Cdd:pfam00384 81 LCTAAAAAFGS-DLRSNYLFNSSIADIENADLILLIGTNPREEAPILnARIRKAALKGKAKVIVIGPRLDLT--YADEHL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 230 PIRPGTDTVLADVMLKIIMDEGFIDESFiqartngydelsvylnsldlsqaadicglelgqireaalafgeADTGMVLTA 309
Cdd:pfam00384 158 GIKPGTDLALALAGAHVFIKELKKDKDF-------------------------------------------APKPIIIVG 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 310 RGVEQQTDGHLAVRHFLNLVLATGKIGREGCGYGAITgqgNGQG-GREHGQKADQLPgyrsienekdrayvasvwgveaa 388
Cdd:pfam00384 195 AGVLQRQDGEAIFRAIANLADLTGNIGRPGGGWNGLN---ILQGaASPVGALDLGLV----------------------- 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 389 slpgKGVSAYEMMELIHQGVIKSLFVMGSNPIVSNPNAGLVEEALNKLDFLMVADMFM-SETAQLADLVLPVTSYMENEG 467
Cdd:pfam00384 249 ----PGIKSVEMINAIKKGGIKVLYLLGNNPFVTHADENRVVKALQKLDLFVVYDGHHgDKTAKYADVILPAAAYTEKNG 324
|
410 420 430
....*....|....*....|....*....|....
gi 2083076315 468 TLTNLEGRVLLREAGRQAPGEARHDWMILCSIAD 501
Cdd:pfam00384 325 TYVNTEGRVQSTKQAVPPPGEAREDWKILRALSE 358
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
18-508 |
3.51e-72 |
|
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: 244.23 E-value: 3.51e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 18 TQCPFCSVQCKMTVTeggngIPGQRRAeyKVEGVP-NAASEGRVCVKG--MHAHQHavHSQRLTNPFIRSNGELVPCSWD 94
Cdd:cd02762 2 RACILCEANCGLVVT-----VEDGRVA--SIRGDPdDPLSKGYICPKAaaLGDYQN--DPDRLRTPMRRRGGSFEEIDWD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 95 EAFAVASQHLQGISEQHGPDANAVYGGGSLTNEtaYLLGKFARV---ALGTRhidynGRFcmsAAASAGSKT-------- 163
Cdd:cd02762 73 EAFDEIAERLRAIRARHGGDAVGVYGGNPQAHT--HAGGAYSPAllkALGTS-----NYF---SAATADQKPghfwsglm 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 164 FGidRGLTFRLADIPLARCIVLAGTNIAECQ--PTLLPYFNR----AKENGARIIVIDPRKTATAAMADMHLPIRPGTDT 237
Cdd:cd02762 143 FG--HPGLHPVPDIDRTDYLLILGANPLQSNgsLRTAPDRVLrlkaAKDRGGSLVVIDPRRTETAKLADEHLFVRPGTDA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 238 VLADVMLKIIMDEGFIDESFIQARTNGYDELSVYLNSLDLSQAADICGLELGQIREAALAFGEADTGMVLTARGVEQQTD 317
Cdd:cd02762 221 WLLAAMLAVLLAEGLTDRRFLAEHCDGLDEVRAALAEFTPEAYAPRCGVPAETIRRLAREFAAAPSAAVYGRLGVQTQLF 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 318 GHLAvrHFLN--LVLATGKIGREG---CGYGAITGQGN-GQGGREHGQKADQLPGYRSIENEkdrayvasvwgveaasLP 391
Cdd:cd02762 301 GTLC--SWLVklLNLLTGNLDRPGgamFTTPALDLVGQtSGRTIGRGEWRSRVSGLPEIAGE----------------LP 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 392 GKGVSayEMMELIHQGVIKSLFVMGSNPIVSNPNAGLVEEALNKLDFLMVADMFMSETAQLADLVLPVTSYMEN-EGTLT 470
Cdd:cd02762 363 VNVLA--EEILTDGPGRIRAMIVVAGNPVLSAPDGARLEAALGGLEFMVSVDVYMTETTRHADYILPPASQLEKpHATFF 440
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 2083076315 471 NLE---GRVLLREAGRQAPGEARHDWMILC----SIADMLGKGHY 508
Cdd:cd02762 441 NLEfprNAFRYRRPLFPPPPGTLPEWEILArlveALDAVLRAGFY 485
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
17-515 |
9.17e-69 |
|
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: 233.35 E-value: 9.17e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 17 ETQCPFCSVQCKMTVTEGGNGIpgqrraeYKVEGVPN-AASEGRVCVKGMHAHQHAVHSQRLTNPFIRSN----GELVPC 91
Cdd:cd02759 1 KGTCPGCHSGCGVLVYVKDGKL-------VKVEGDPNhPTNKGRLCMRGLAAPEIVYHPDRLLYPLKRVGergeNKWERI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 92 SWDEAFAVASQHLQGISEQHGPDANAVY-GGGSLTNE-TAYLLGKFARVaLGTRHIDYNGRFCMSAAASAGSKTFGIdrG 169
Cdd:cd02759 74 SWDEALDEIAEKLAEIKAEYGPESIATAvGTGRGTMWqDSLFWIRFVRL-FGSPNLFLSGESCYWPRDMAHALTTGF--G 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 170 LTFRLADIPLARCIVLAGTNIAECQPTLLPY-FNRAKENGARIIVIDPRKTATAAMADMHLPIRPGTDTVLADVMLKIIM 248
Cdd:cd02759 151 LGYDEPDWENPECIVLWGKNPLNSNLDLQGHwLVAAMKRGAKLIVVDPRLTWLAARADLWLPIRPGTDAALALGMLNVII 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 249 DEGFIDESFIQARTNGYDELSVYLNSLDLSQAADICGLELGQIREAALAFGEADTGMVLTARGVEQQTDGHLAVRHFLNL 328
Cdd:cd02759 231 NEGLYDKDFVENWCYGFEELAERVQEYTPEKVAEITGVPAEKIRKAARLYATAKPACIQWGLAIDQQKNGTQTSRAIAIL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 329 VlatgkigregcgygAITGQGNGQGGrehgqkadqlpgyrsienekdrayvaSVWGveaaslpgkgvsAYemmelihqgV 408
Cdd:cd02759 311 R--------------AITGNLDVPGG--------------------------NLLI------------PY---------P 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 409 IKSLFVMGSNPIVSNPNAGLVEEALNKLDFLMVADMFMSETAQLADLVLPVTSYMENEGTLTNLEGR--VLLREAGRQAP 486
Cdd:cd02759 330 VKMLIVFGTNPLASYADTAPVLEALKALDFIVVVDLFMTPTAMLADIVLPVAMSLERPGLRGGFEAEnfVQLRQKAVEPY 409
|
490 500 510
....*....|....*....|....*....|.
gi 2083076315 487 GEARHDWMILCSIADMLG--KGHYFRFNEPE 515
Cdd:cd02759 410 GEAKSDYEIVLELGKRLGpeEAEYYKYEKGL 440
|
|
| MopB_Formate-Dh-Na-like |
cd02752 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
18-533 |
7.44e-67 |
|
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: 232.68 E-value: 7.44e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 18 TQCPFCSVQCKMTV-TEGGNGIpgqrraeyKVEGVP-NAASEGRVCVKGMHAHQHAVHSQRLTNPFIRSNG--ELVPCSW 93
Cdd:cd02752 2 TICPYCSVGCGLIAyVQNGVWV--------HQEGDPdHPVNRGSLCPKGAALRDFVHSPKRLKYPMYRAPGsgKWEEISW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 94 DEAFAVASQHLQGISEQH------------GPDANAVYGGGSLTNETAYLLGKFARvALGTRHIDYNGRFCMSAAASAGS 161
Cdd:cd02752 74 DEALDEIARKMKDIRDASfveknaagvvvnRPDSIAFLGSAKLSNEECYLIRKFAR-ALGTNNLDHQARIUHSPTVAGLA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 162 KTFGidRG-LTFRLADIPLARCIVLAGTNIAECQPTLLPYFNRAKE-NGARIIVIDPRKTATAAMADMHLPIRPGTDTVL 239
Cdd:cd02752 153 NTFG--RGaMTNSWNDIKNADVILVMGGNPAEAHPVSFKWILEAKEkNGAKLIVVDPRFTRTAAKADLYVPIRSGTDIAF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 240 ADVMLKiimdegfidesfiqartngydelsvYLNSLDLSQAADICGLELGQIREAALAF---GEAD-TGMVLTARGVEQQ 315
Cdd:cd02752 231 LGGMIN-------------------------YIIRYTPEEVEDICGVPKEDFLKVAEMFaatGRPDkPGTILYAMGWTQH 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 316 TDGHLAVRHFLNLVLATGKIGREGCGYGAITGQGNGQGGREHGQKADQLPGYRSienekdrayvasvwgveaaslpgkgv 395
Cdd:cd02752 286 TVGSQNIRAMCILQLLLGNIGVAGGGVNALRGHSNVQGATDLGLLSHNLPGYLG-------------------------- 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 396 sayemmelihqgvikslfvmGSNPIVSNPNAGLVEEALNKLDFLMVADMFMSETAQLAD-------------LVLPVTSY 462
Cdd:cd02752 340 --------------------GQNPNSSFPNANKVRRALDKLDWLVVIDPFPTETAAFWKnpgmdpksiqtevFLLPAACQ 399
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 463 MENEGTLTNlEGRVL-LREAGRQAPGEARHDWMILCSIADMLG-----------------KGHYFRFNEPEEVfneLRLA 524
Cdd:cd02752 400 YEKEGSITN-SGRWLqWRYKVVEPPGEAKSDGDILVELAKRLGflyekeggafpepitkwNYGYGDEPTPEEI---AREI 475
|
....*....
gi 2083076315 525 SKGGIADYY 533
Cdd:cd02752 476 NGGALTDGY 484
|
|
| MopB_ydeP |
cd02767 |
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
76-575 |
1.96e-61 |
|
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: 216.02 E-value: 1.96e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 76 RLTNPFIRSNGE--LVPCSWDEAFAVASQHLQGISeqhgPDANAVYGGGSLTNETAYLLGKFARvALGTRHIDYNGRFCM 153
Cdd:cd02767 64 RLTYPMRYDAGSdhYRPISWDEAFAEIAARLRALD----PDRAAFYTSGRASNEAAYLYQLFAR-AYGTNNLPDCSNMCH 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 154 SAAASAGSKTFGIDRGlTFRLADIPLARCIVLAGTNIAECQPTLLPYFNRAKENGARIIVIDPRK--------------- 218
Cdd:cd02767 139 EPSSVGLKKSIGVGKG-TVSLEDFEHTDLIFFIGQNPGTNHPRMLHYLREAKKRGGKIIVINPLRepglerfanpqnpes 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 219 --TATAAMADMHLPIRPGTDTVLADVMLK--IIMDE---GFIDESFIQARTNGYDELSVYLNSLDLSQAADICGLELGQI 291
Cdd:cd02767 218 mlTGGTKIADEYFQVRIGGDIALLNGMAKhlIERDDepgNVLDHDFIAEHTSGFEEYVAALRALSWDEIERASGLSREEI 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 292 REAALAFGEADTGMVLTARGVEQQTDGHLAVRHFLNLVLATGKIGREGCGYGAITGQGNGQGGREHG--QKADQLPgyrs 369
Cdd:cd02767 298 EAFAAMYAKSERVVFVWGMGITQHAHGVDNVRAIVNLALLRGNIGRPGAGLMPIRGHSNVQGDRTMGitEKPFPEF---- 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 370 ieneKDRayVASVWGVEAASLPGKGVSayEMMELIHQGVIKSLFVMGSNPIVSNPNAGLVEEALNKLDFLMVADMFMSET 449
Cdd:cd02767 374 ----LDA--LEEVFGFTPPRDPGLDTV--EAIEAALEGKVKAFISLGGNFAEAMPDPAATEEALRRLDLTVHVATKLNRS 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 450 AQL---ADLVLPVTS--------------YMENEGTLTNL-------EGRVLLREAG------RQAPGEARHDWMILCSI 499
Cdd:cd02767 446 HLVhgeEALILPCLGrteidmqaggaqavTVEDSMSMTHTsrgrlkpASRVLLSEEAivagiaGARLGEAKPEWEILVED 525
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2083076315 500 ADMLgkghyfRfNEPEEVFNElrlaskgGIADYygitYDRLRREKGVYWPCPSPEeagagllfqQSFAHPDGKAVF 575
Cdd:cd02767 526 YDRI------R-DEIAAVIYE-------GFADF----NQRGDQPGGFHLPNGARE---------RKFNTPSGKAQF 574
|
|
| PRK13532 |
PRK13532 |
nitrate reductase catalytic subunit NapA; |
7-702 |
3.95e-56 |
|
nitrate reductase catalytic subunit NapA;
Pssm-ID: 237416 [Multi-domain] Cd Length: 830 Bit Score: 205.90 E-value: 3.95e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 7 AEATEVAAVIETQ-------CPFCSVQCKMTV-TEGGngipgqrraeyKV---EGVPNA-ASEGRVCVKG------MHAH 68
Cdd:PRK13532 27 AVANAVVGSAQTAikwdkapCRFCGTGCGVLVgTKDG-----------RVvatQGDPDApVNRGLNCIKGyflskiMYGK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 69 QhavhsqRLTNPFIR-------SNGELVPCSWDEAFAVASQHLQGISEQHGPDANAVYGGGSLTNETAYLLGKFARVALG 141
Cdd:PRK13532 96 D------RLTQPLLRmkdgkydKEGEFTPVSWDQAFDVMAEKFKKALKEKGPTAVGMFGSGQWTIWEGYAASKLMKAGFR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 142 TRHIDYNGRFCMSAAASAGSKTFGIDR--GLtfrLADIPLARCIVLAGTNIAECQPTLLPYFN--RAKENGARIIVIDPR 217
Cdd:PRK13532 170 SNNIDPNARHCMASAVVGFMRTFGIDEpmGC---YDDIEAADAFVLWGSNMAEMHPILWSRVTdrRLSNPDVKVAVLSTF 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 218 KTATAAMADMHLPIRPGTDTVLADVMLKIIMDEGFIDESFIQARTN--------GY------------------------ 265
Cdd:PRK13532 247 EHRSFELADNGIIFTPQTDLAILNYIANYIIQNNAVNWDFVNKHTNfrkgatdiGYglrpthplekaaknpgtagksepi 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 266 --DELSVYLNSLDLSQAADICGLELGQIREAALAFGEADTGMV-LTARGVEQQTDGHLAVRHFLNLVLATGKIGREGCGY 342
Cdd:PRK13532 327 sfEEFKKFVAPYTLEKTAKMSGVPKEQLEQLAKLYADPNRKVVsFWTMGFNQHTRGVWANNLVYNIHLLTGKISTPGNGP 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 343 GAITGQGNGQG-GREHGQKADQLPGYRSIENEKDRAYVASVWGVEAASLPGK-GVSAYEMMELIHQGVIKSLFVMGSNPI 420
Cdd:PRK13532 407 FSLTGQPSACGtAREVGTFSHRLPADMVVTNPKHREIAEKIWKLPEGTIPPKpGYHAVAQDRMLKDGKLNAYWVMCNNNM 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 421 VSNPNAGlvEEAL----NKLDFLMVADMFMSETAQLADLVLPVTSYMENEGTLTNLEGRVllrEAGRQ---APGEARHD- 492
Cdd:PRK13532 487 QAGPNIN--EERLpgwrNPDNFIVVSDPYPTVSALAADLILPTAMWVEKEGAYGNAERRT---QFWRQqvkAPGEAKSDl 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 493 WMILcsiadMLGKghyfRFnEPEEVFNELRLASKG--------------GIADYYGIT---------------------- 536
Cdd:PRK13532 562 WQLV-----EFSK----RF-KTEEVWPEELLAKKPeyrgktlydvlfanGQVDKFPLSelaegylndeakhfgfyvqkgl 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 537 -----------------YDRLRREKGVYWPCPSPEE--------------AGAGLLFqqsFAHPDGKAV-FSIMEGTPWK 584
Cdd:PRK13532 632 feeyasfgrghghdlapFDTYHKVRGLRWPVVDGKEtlwryregydpyvkAGEGFKF---YGKPDGKAViFALPYEPPAE 708
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 585 GVTEEYSLILTNGRVLSHYLTGVQTRRSPSLLARELENFVEIHPITAQRYRIRDGEWVEVQSEHGYftVRARIKDQIR-- 662
Cdd:PRK13532 709 SPDEEYDLWLSTGRVLEHWHTGSMTRRVPELYRAFPEAVCFMHPEDAKARGLRRGDEVKVVSRRGE--VKSRVETRGRnk 786
|
810 820 830 840
....*....|....*....|....*....|....*....|...
gi 2083076315 663 --EDTLFVPmhW-GGVQNVNHATRPELDPFCKMPGFKTSAVRI 702
Cdd:PRK13532 787 ppRGLVFVP--FfDAAQLINKLTLDATDPLSKQTDFKKCAVKI 827
|
|
| MopB_DmsA-EC |
cd02770 |
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
59-547 |
5.16e-54 |
|
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: 196.39 E-value: 5.16e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 59 RVCVKGMHAHQHAVHSQRLTNPFIRSN----GELVPCSWDEAFAVASQHLQGISEQHGPDANAVYGGGSLTNETAYLLGK 134
Cdd:cd02770 42 RACLRGRSQRKRVYNPDRLKYPMKRVGkrgeGKFVRISWDEALDTIASELKRIIEKYGNEAIYVNYGTGTYGGVPAGRGA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 135 FARV-ALGTRHIDYNGRFCMSAAASAGSKTFGIDrGLTFRLADIPLARCIVLAGTNIAECQPTLLP---YFNRAKENGAR 210
Cdd:cd02770 122 IARLlNLTGGYLNYYGTYSWAQITTATPYTYGAA-ASGSSLDDLKDSKLVVLFGHNPAETRMGGGGstyYYLQAKKAGAK 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 211 IIVIDPRKTATAA-MADMHLPIRPGTDTVLADVMLKIIMDEGFIDESFIQARTNGYDELSV------------YLNSLDL 277
Cdd:cd02770 201 FIVIDPRYTDTAVtLADEWIPIRPGTDAALVAAMAYVMITENLHDQAFLDRYCVGFDAEHLpegappnesykdYVLGTGY 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 278 SQ-------AADICGLELGQIREAALAFGEADTGMVLTARGVEQQTDGHLAVRHFLNLVLATGKIGREGCGYGAitgqgn 350
Cdd:cd02770 281 DGtpktpewASEITGVPAETIRRLAREIATTKPAAILQGWGPQRHANGEQAARAIMMLAAMTGNVGIPGGNTGA------ 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 351 gqggREHGQKAdQLPGYRSIENEKDRAYVASVWgVEAAsLPGKGVSAYEMMeliHQGV------IKSLFVMGSNPIVsNP 424
Cdd:cd02770 355 ----RPGGSAY-NGAGLPAGKNPVKTSIPCFMW-TDAI-ERGEEMTADDGG---VKGAdklksnIKMIWNYAGNTLI-NQ 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 425 NAGL------VEEALNKLDFLMVADMFMSETAQLADLVLPVTSYMENEGTLTN----LEGRVLLREAGRQAPGEARHDWM 494
Cdd:cd02770 424 HSDDnnttraLLDDESKCEFIVVIDNFMTPSARYADILLPDTTELEREDIVLTsnagMMEYLIYSQKAIEPLYECKSDYE 503
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 2083076315 495 ILCSIADMLGKGHYF-RFNEPEEVFNElrLASKGGIADYYGITYDRLrREKGVY 547
Cdd:cd02770 504 ICAELAKRLGVEDQFtEGKTEQEWLEE--LYGQTRAKEPGLPTYEEF-REKGIY 554
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
18-547 |
1.55e-53 |
|
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: 194.75 E-value: 1.55e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 18 TQCPFCsvQCKMTVTEGgngipgqrraeyKVEGV-PNAASEGRVCVKGmHAHQHAVHSQ-RLTNPFIR------------ 83
Cdd:cd02751 2 TACHWG--PFKAHVKDG------------VIVRVePDDTDQPRPCPRG-RSVRDRVYSPdRIKYPMKRvgwlgngpgsre 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 84 --SNGELVPCSWDEAFAVASQHLQGISEQHGPDA--NAVYGG---GSLTNETAyLLGKFARVALGtrHIDYNGRFCMSAA 156
Cdd:cd02751 67 lrGEGEFVRISWDEALDLVASELKRIREKYGNEAifGGSYGWasaGRLHHAQS-LLHRFLNLIGG--YLGSYGTYSTGAA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 157 ASAGSKTFGIDRGL--TFRLADIP-LARCIVLAGTNIAECQP--------TLLPYFNRAKENGARIIVIDPRKTATAA-M 224
Cdd:cd02751 144 QVILPHVVGSDEVYeqGTSWDDIAeHSDLVVLFGANPLKTRQgggggpdhGSYYYLKQAKDAGVRFICIDPRYTDTAAvL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 225 ADMHLPIRPGTDTVLADVMLKIIMDEGFIDESFIQARTNGYDELSVYLNSLDLSQ------AADICGLELGQIREAALAF 298
Cdd:cd02751 224 AAEWIPIRPGTDVALMLAMAHTLITEDLHDQAFLARYTVGFDEFKDYLLGESDGVpktpewAAEITGVPAETIRALAREI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 299 GeADTGMVLTARGVEQQTDGHLAVRHFLNLVLATGKIGREGCGYGAITGQGNGQGGREHGQKADQLP-GYRSIeneKDRA 377
Cdd:cd02751 304 A-SKRTMIAQGWGLQRAHHGEQPAWMLVTLAAMLGQIGLPGGGFGFGYGYSNGGGPPRGGAGGPGLPqGKNPV---KDSI 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 378 YVASVWgvEAASLPGKGVSAyeMMELIHQGVIKSLFVMGSNPIVS-NPNAGLVeEALNKLDFLMVADMFMSETAQLADLV 456
Cdd:cd02751 380 PVARIA--DALLNPGKEFTA--NGKLKTYPDIKMIYWAGGNPLHHhQDLNRLI-KALRKDETIVVHDIFWTASARYADIV 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 457 LPVTSYMENE--GTLTNLEGRVLLreAGRQA--P-GEARHDWMILCSIADMLGKGHYFRFNEPE-----EVFNELRLASK 526
Cdd:cd02751 455 LPATTSLERNdiGLTGNYSNRYLI--AMKQAvePlGEARSDYEIFAELAKRLGVEEEFTEGRDEmewleHLYEETRAKAA 532
|
570 580
....*....|....*....|.
gi 2083076315 527 GGIADYygITYDRLrREKGVY 547
Cdd:cd02751 533 GPGPEL--PSFEEF-WEKGIV 550
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
20-528 |
3.97e-53 |
|
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: 190.20 E-value: 3.97e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 20 CPFCSVQCKMTV-TEGGNGIpgqrraeyKVEGVP-NAASEGRVCVKGMHAHQHAVHSQRLTNPFIRS----NGELVPCSW 93
Cdd:cd02755 5 CEMCSSRCGILArVEDGRVV--------KIDGNPlSPLSRGKLCARGNAGIQLLYDPDRLKKPLIRVgergEGKFREASW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 94 DEAFAVASQHLQGISEQHGPDAnAVYGGGSLTNETayLLGKFARvALGTRHIDYNGRFCMSAAASAGSKTFGIDRGLTfr 173
Cdd:cd02755 77 DEALQYIASKLKEIKEQHGPES-VLFGGHGGCYSP--FFKHFAA-AFGSPNIFSHESTCLASKNLAWKLVIDSFGGEV-- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 174 LADIPLARCIVLAGTNIAEC-QPTLLPYFNRAKENGARIIVIDPRKTATAAMADMHLPIRPGTDTVLADVMLKIIMDEGF 252
Cdd:cd02755 151 NPDFENARYIILFGRNLAEAiIVVDARRLMKALENGAKVVVVDPRFSELASKADEWIPIKPGTDLAFVLALIHVLISENL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 253 IDESFIQARTNGYDELSVYLNSLDLSQAADICGLELGQIREAALAFGEADTGMVLtargveqqtdghlavrhflnlvlat 332
Cdd:cd02755 231 YDAAFVEKYTNGFELLKAHVKPYTPEWAAQITDIPADTIRRIAREFAAAAPHAVV------------------------- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 333 gkigregcgygaITGQgngqggreHGQKADQlpgyrsiENEKDRAYVA-----SVWGVEAASLPGKGVSAYEmmelihqg 407
Cdd:cd02755 286 ------------DPGW--------RGTFYSN-------SFQTRRAIAIinallGNIDKRGGLYYAGSAKPYP-------- 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 408 vIKSLFVMGSNPIVSNPNAGLVEEALNKLDFLMVADMFMSETAQLADLVLPVTSYMENEGTLTNLEG---RVLLREAGRQ 484
Cdd:cd02755 331 -IKALFIYRTNPFHSMPDRARLIKALKNLDLVVAIDILPSDTALYADVILPEATYLERDEPFSDKGGpapAVATRQRAIE 409
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 2083076315 485 APGEARHDWMILCSIADMLGkghyfRFNEPE---EVFNeLRLASKGG 528
Cdd:cd02755 410 PLYDTRPGWDILKELARRLG-----LFGTPSgkiELYS-PILAKAGY 450
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
20-675 |
1.94e-51 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 191.42 E-value: 1.94e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 20 CPFCSVQCKMTV-TEGGNGIpgqrraeyKVEGVPNAAS-EGRVCVKGMHAHQHAVHSQRLTNPFIRS----NGELVPCSW 93
Cdd:PRK15488 48 CEMCSTRCPIEArVVNGKNV--------FIQGNPKAKSfGTKVCARGGSGHSLLYDPQRIVKPLKRVgergEGKWQEISW 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 94 DEAFAVASQHLQGISEQHGPDANAVyggGSLTNETAYLLGKFARvALGTRHIDYNGRFCMSAAASAGSKTFGIDRGLtfr 173
Cdd:PRK15488 120 DEAYQEIAAKLNAIKQQHGPESVAF---SSKSGSLSSHLFHLAT-AFGSPNTFTHASTCPAGYAIAAKVMFGGKLKR--- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 174 laDIPLARCIV------LAGTNIAECQPtllpYFNRAKENGARIIVIDPRKTATAAMADMHLPIRPGTDTVLADVMLKII 247
Cdd:PRK15488 193 --DLANSKYIInfghnlYEGINMSDTRG----LMTAQMEKGAKLVVFEPRFSVVASKADEWHAIRPGTDLAVVLALCHVL 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 248 MDEGFIDESFIQARTNGYDELSVYLNSLDLSQAADICGLELGQIREAALAFGEA------DTGMVLTARGVEQQTDGHLA 321
Cdd:PRK15488 267 IEENLYDKAFVERYTSGFEELAASVKEYTPEWAEAISDVPADDIRRIARELAAAaphaivDFGHRATFTPEEFDMRRAIF 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 322 VrhfLNLVLatGKIGREGCGYGAITGQGNGQGGREhgQKADQL-----PGYRSIENEK-DRA-----YVASVWGV----E 386
Cdd:PRK15488 347 A---ANVLL--GNIERKGGLYFGKNASVYNKLAGE--KVAPTLakpgvKGMPKPTAKRiDLVgeqfkYIAAGGGVvqsiI 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 387 AASLPGKgvsAYEmmelihqgvIKSLFVMGSNPIVSNPNAGLVEEALNKLDFLMVADMFMSETAQLADLVLPVTSYMENE 466
Cdd:PRK15488 420 DATLTQK---PYQ---------IKGWVMSRHNPMQTVTDRADVVKALKKLDLVVVCDVYLSESAAYADVVLPESTYLERD 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 467 GTLTNLEGRV---LLREAGRQAPGEARHDWMILCSIADMLGKGHYFrfnePEEVFNELRLASKGGIADYYG-------IT 536
Cdd:PRK15488 488 EEISDKSGKNpayALRQRVVEPIGDTKPSWQIFKELGEKMGLGQYY----PWQDMETLQLYQVNGDHALLKelkkkgyVS 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 537 YDR--LRREKG------VYWPCPSPEEAGAGLLFQQSFAHPDGK-AVFS--IMEGTPWKGV--------TEEYSLILTNG 597
Cdd:PRK15488 564 FGVplLLREPKmvakfvARYPNAKAVDEDGTYGSQLKFKTPSGKiELFSakLEALAPGYGVpryrdvalKKEDELYFIQG 643
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2083076315 598 RVLSHylTGVQTRRSPSLLARELENFVEIHPITAQRYRIRDGEWVEVQSEHGYFTVRARIKDQIREDTLFVPMHWGGV 675
Cdd:PRK15488 644 KVAVH--TNGATQNVPLLANLMSDNAVWIHPQTAGKLGIKNGDEIRLENSVGKEKGKALVTPGIRPDTLFAYMGFGSK 719
|
|
| 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 ... |
20-505 |
2.74e-51 |
|
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: 185.67 E-value: 2.74e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 20 CPFCSVQCkmtvteggNGIPGQRRAEYK-VEG-VPNAASEGRVCVKGMHAHQHAVHSQRLTNPFIRSNGELVPCSWDEAF 97
Cdd:cd02771 4 CHHCSVGC--------NISLGERYGELRrVENrYNGAVNHYFLCDRGRFGYGYVNSRDRLTQPLIRRGGTLVPVSWNEAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 98 AVASQHLQGISeqhgpDANAVYGGGSLTNETAYLLGKFARVALGTRHIDYNGRfcMSAAASAgsKTFGIDRGltfRLADI 177
Cdd:cd02771 76 DVAAARLKEAK-----DKVGGIGSPRASNESNYALQKLVGAVLGTNNVDHRAR--RLIAEIL--RNGPIYIP---SLRDI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 178 PLARCIVLAGTNIAECQPTLLPYFNRAKENGARIIVIDPRKTATAAMADMHLPIRPGTDTVLADVMLKIIMDegfIDESF 257
Cdd:cd02771 144 ESADAVLVLGEDLTQTAPRIALALRQAARRKAVELAALSGIPKWQDAAVRNIAQGAKSPLFIVNALATRLDD---IAAES 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 258 IQARTNGYDELSVYLNSLDLSQAADICGLELgqiREAALAFGEADTG--MVLTARGVEQQTDGhlAVRHFLNLVLATGKI 335
Cdd:cd02771 221 IRASPGGQARLGAALARAVDASAAGVSGLAP---KEKAARIAARLTGakKPLIVSGTLSGSLE--LIKAAANLAKALKRR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 336 GrEGCGYGAITGQGNgqggrehgqkadqLPGYRSIENEKDRAyvasvwgveaaslpgkGVSAYEMMELIHQGVIKSLFVM 415
Cdd:cd02771 296 G-ENAGLTLAVEEGN-------------SPGLLLLGGHVTEP----------------GLDLDGALAALEDGSADALIVL 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 416 GSNPIVSNPNAGlVEEALNKLDFLMVADMFMSETAQLADLVLPVTSYMENEGTLTNLEGRV-LLREAGRQAPGEARHDWM 494
Cdd:cd02771 346 GNDLYRSAPERR-VEAALDAAEFVVVLDHFLTETAERADVVLPAASFAEKSGTFVNYEGRAqRFFKAYDDPAGDARSDWR 424
|
490
....*....|.
gi 2083076315 495 ILCSIADMLGK 505
Cdd:cd02771 425 WLHALAAKLGG 435
|
|
| MopB_4 |
cd02765 |
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
21-575 |
3.06e-49 |
|
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: 181.91 E-value: 3.06e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 21 PFCSVQCKMTVTEGGNGIpgqrraeYKVE-GVPNAASEGRVCVKGMHAHQHAVHSQRLTNPFIR----SNGELVPCSWDE 95
Cdd:cd02765 6 PNCGGRCPLKCHVRDGKI-------VKVEpNEWPDKTYKRGCTRGLSHLQRVYSPDRLKYPMKRvgerGEGKFERITWDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 96 AFAVASQHLQGISEQHGPDANAVYGGGSLTNETAYLLGkfaRVALGTRHIDYNGRFCMSAAASAGSKTFGIDRGLTFRLA 175
Cdd:cd02765 79 ALDTIADKLTEAKREYGGKSILWMSSSGDGAILSYLRL---ALLGGGLQDALTYGIDTGVGQGFNRVTGGGFMPPTNEIT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 176 DIPLARCIVLAGTNIAECQPTLLPYFNRAKENGARIIVIDPRKTATAAMADMHLPIRPGTDTVLADVMLKIIMDEGFIDE 255
Cdd:cd02765 156 DWVNAKTIIIWGSNILETQFQDAEFFLDARENGAKIVVIDPVYSTTAAKADQWVPIRPGTDPALALGMINYILEHNWYDE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 256 SFIQARTN--------------------------------------------------------------GYDELSVYLN 273
Cdd:cd02765 236 AFLKSNTSapflvredngtllrqadvtatpaedgyvvwdtnsdspepvaatninpalegeytingvkvhtVLTALREQAA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 274 SLDLSQAADICGLELGQIREAALAFGEADTGMVLTARGVEQQTDGHLAVRHFLNLVLATGKIGREGCGygaitgqgngqg 353
Cdd:cd02765 316 SYPPKAAAEICGLEEAIIETLAEWYATGKPSGIWGFGGVDRYYHSHVFGRTAAILAALTGNIGRVGGG------------ 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 354 greHGQkadqlpgyrsienekdrayvasvwgveaaslpgkgvsayemmelihqgvIKSLFVMGSNPIVSNPNAGLVEEAL 433
Cdd:cd02765 384 ---VGQ-------------------------------------------------IKFMYFMGSNFLGNQPDRDRWLKVM 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 434 NKLDFLMVADMFMSETAQLADLVLPVTSYMENEGTLTNLEGR--VLLREAGRQAPGEARHDWMILCSIADMLGKGHYFRf 511
Cdd:cd02765 412 KNLDFIVVVDIFHTPTVRYADIVLPAAHWFEVEDLLVRYTTHphVLLQQKAIEPLFESKSDFEIEKGLAERLGLGDYFP- 490
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2083076315 512 NEPEEVfneLRLASKGGIADYYGITYDRLrREKGVYWPCPSPEEAGAGLLfQQSFAHPDGKAVF 575
Cdd:cd02765 491 KTPEDY---VRAFMNSDDPALDGITWEAL-KEEGIIMRLATPEDPYVAYL-DQKFGTPSGKLEF 549
|
|
| MopB_CT_Fdh-Nap-like |
cd00508 |
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and ... |
588-704 |
8.21e-45 |
|
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and other related proteins. Formate dehydrogenase H is a component of the anaerobic formate hydrogen lyase complex and catalyzes the reversible oxidation of formate to CO2 with the release of a proton and two electrons. Formate dehydrogenase N (alpha subunit) is the major electron donor to the bacterial nitrate respiratory chain and nitrate reductases, Nap and Nas, catalyze the reduction of nitrate to nitrite. This CD (MopB_CT_Fdh-Nap-like) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 238282 [Multi-domain] Cd Length: 120 Bit Score: 156.13 E-value: 8.21e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 588 EEYSLILTNGRVLSHYLTGVQTRRSPSLLARELENFVEIHPITAQRYRIRDGEWVEVQSEHGYFTVRARIKDQIREDTLF 667
Cdd:cd00508 1 EEYPLVLTTGRLLEHWHTGTMTRRSPRLAALAPEPFVEIHPEDAARLGIKDGDLVRVSSRRGSVVVRARVTDRVRPGTVF 80
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2083076315 668 VPMHWGGV---QNVNHATRPELDPFCKMPGFKTSAVRIRP 704
Cdd:cd00508 81 MPFHWGGEvsgGAANALTNDALDPVSGQPEFKACAVRIEK 120
|
|
| MopB_Arsenite-Ox |
cd02756 |
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the ... |
36-586 |
1.59e-39 |
|
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: 155.33 E-value: 1.59e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 36 NGIPGQRRAEYKVEGVPNAAS---EGRVCVKG------MHAHQHAVHSQRLTNPFIRSNGELVPCSWDEAFAVASQHLQG 106
Cdd:cd02756 68 YVVVTQDGREVYIVIVPDKECpvnSGNYSTRGgtnaerIWSPDNRVGETRLTTPLVRRGGQLQPTTWDDAIDLVARVIKG 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 107 ISEQHGPDANAV-----YGGGSLTNETAYLLGKFARVALGTRHIDYNGRFCMSAAASAgSKTFGIDRgLTFRLADIPLAR 181
Cdd:cd02756 148 ILDKDGNDDAVFasrfdHGGGGGGFENNWGVGKFFFMALQTPFVRIHNRPAYNSEVHA-TREMGVGE-LNNSYEDARLAD 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 182 CIVLAGTNIAECQPT-----LLPYF--------NRAKENG-----ARIIVIDPRKTATAAMAD--------MHLPIRPGT 235
Cdd:cd02756 226 TIVLWGNNPYETQTVyflnhWLPNLrgatvsekQQWFPPGepvppGRIIVVDPRRTETVHAAEaaagkdrvLHLQVNPGT 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 236 DTVLADVMLKIIMDegfidesfiqartnGYDELsvylnsldLSQAADICGLELGQIREAALAFGEADTG------MVLTA 309
Cdd:cd02756 306 DTALANAIARYIYE--------------SLDEV--------LAEAEQITGVPRAQIEKAADWIAKPKEGgyrkrvMFEYE 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 310 RGVEQQTDGHLAVRHFLNLVLATGKIGREGCGYGAitgqgngQGGREHGQKADQLPGYRSIENEKDRAYVAsvwgveaas 389
Cdd:cd02756 364 KGIIWGNDNYRPIYSLVNLAIITGNIGRPGTGCVR-------QGGHQEGYVRPPPPPPPWYPQYQYAPYID--------- 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 390 lpgkgvsayemmELIHQGVIKSLFVMGSNPIVSNPNAGLVEEALNKLD-------------------------------- 437
Cdd:cd02756 428 ------------QLLISGKGKVLWVIGCDPYKTTPNAQRLRETINHRSklvtdaveaalyagtydreamvcligdaiqpg 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 438 --FLMVADMFMSETAQLADLVLPVTSYME-NEGTLTNLEGRVLLREAGRQAPGEARHDWMILCSIADML-------GKGH 507
Cdd:cd02756 496 glFIVVQDIYPTKLAEDAHVILPAAANGEmNETSMNGHERRLRLYEKFMDPPGEAMPDWWIAAMIANRIyelyqeeGKGG 575
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 508 Y-------FRFNEPEEVF----NELRL-------ASKGGIADYYGITYDRLRR--EKGVYWPC----PSPEEAGAGLLFQ 563
Cdd:cd02756 576 SaqyqffgFIWKTEEDNFmdgsQEFADggefsedYYVLGQERYEGVTYNRLKAvgVNGIQLPVttdtVTKILVTNVLRTE 655
|
650 660
....*....|....*....|...
gi 2083076315 564 QSFAHPDGKAVFsiMEGTPWKGV 586
Cdd:cd02756 656 GVFDTEDGKAYV--IDLAPWPGL 676
|
|
| MopB_NADH-Q-OR-NuoG2 |
cd02768 |
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone ... |
17-503 |
1.68e-38 |
|
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: 147.43 E-value: 1.68e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 17 ETQCPFCSVQCKMTVTEGGNGIpgqRRAEYKVEGVPNaasEGRVCVKGMHAHQHAVHSQRLTNPFIRSNGELVPCSWDEA 96
Cdd:cd02768 1 ESIDVHDALGSNIRVDVRGGEV---MRILPRENEAIN---EEWISDKGRFGYDGLNSRQRLTQPLIKKGGKLVPVSWEEA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 97 FAVASQHLQGISeqhgPDANAVYGGGSLTNETAYLLGKFARvALGTRHIDYNGRFcMSAAASAGSKTFGIdrgLTFRLAD 176
Cdd:cd02768 75 LKTVAEGLKAVK----GDKIGGIAGPRADLESLFLLKKLLN-KLGSNNIDHRLRQ-SDLPADNRLRGNYL---FNTSIAE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 177 IPLARCIVLAGTNIAECQPTLlpyfN-----RAKENGARIIVIDPRktataamadmhlpirpgtdtvladvmlkiiMDEG 251
Cdd:cd02768 146 IEEADAVLLIGSNLRKEAPLL----NarlrkAVKKKGAKIAVIGPK------------------------------DTDL 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 252 FIDESFIqartngydelsVYLNSLDLSQAADIcgLELGQIREAALAFGEADTGMVLTARGVeQQTDGHLAVRHFLNLVLA 331
Cdd:cd02768 192 IADLTYP-----------VSPLGASLATLLDI--AEGKHLKPFAKSLKKAKKPLIILGSSA-LRKDGAAILKALANLAAK 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 332 TGKIGREGCGYGAITGQGNGQGGRehgqkadqlpgyrsienekdrayvasvwGVEAASLPGKGVSAYemmelihqgvikS 411
Cdd:cd02768 258 LGTGAGLWNGLNVLNSVGARLGGA----------------------------GLDAGLALLEPGKAK------------L 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 412 LFVMGSNPIVSNPNAGLveeALNKLDFLMVADMFMSETAQLADLVLPVTSYMENEGTLTNLEGRVLLREAGRQAPGEARH 491
Cdd:cd02768 298 LLLGEDELDRSNPPAAV---ALAAADAFVVYQGHHGDTGAQADVILPAAAFTEKSGTYVNTEGRVQRFKKAVSPPGDARE 374
|
490
....*....|..
gi 2083076315 492 DWMILCSIADML 503
Cdd:cd02768 375 DWKILRALSNLL 386
|
|
| MopB_DMSOR-BSOR-TMAOR |
cd02769 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
50-515 |
1.55e-37 |
|
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide reductase (BSOR), trimethylamine N-oxide reductase (TMAOR) and other related proteins. DMSOR always catalyzes the reduction of DMSO to dimethylsulfide, but its cellular location and oligomerization state are organism-dependent. For example, in Rhodobacter sphaeriodes and Rhodobacter capsulatus, it is an 82-kDa monomeric soluble protein found in the periplasmic space; in E. coli, it is membrane-bound and exists as a heterotrimer. BSOR catalyzes the reduction of biotin sulfixode to biotin, and is unique among Mo enzymes because no additional auxiliary proteins or cofactors are required. TMAOR is similar to DMSOR, but its only natural substrate is TMAO. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239170 [Multi-domain] Cd Length: 609 Bit Score: 148.56 E-value: 1.55e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 50 GVPNAA-SEGRV---CV-KGMHAHQHAVHSQRltnpfiRSNGELVPCSWDEAFAVASQHLQGISEQHGPDAnaVYGG--- 121
Cdd:cd02769 36 GVPDAVySPTRIkypMVrRGWLEKGPGSDRSL------RGKEEFVRVSWDEALDLVAAELKRVRKTYGNEA--IFGGsyg 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 122 ----GSLTNETAyLLGKFARVALG-TRHI-DYngrfcmSAAASA-------GSKTFGIDRGLTFRLAdIPLARCIVLAGT 188
Cdd:cd02769 108 wssaGRFHHAQS-LLHRFLNLAGGyVGSVgDY------STGAAQvilphvvGSMEVYTEQQTSWPVI-AEHTELVVAFGA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 189 NIAECQPT---------LLPYFNRAKENGARIIVIDPRKTATAAMADM-HLPIRPGTDTVLadvMLKI---IMDEGFIDE 255
Cdd:cd02769 180 DPLKNAQIawggipdhqAYSYLKALKDRGIRFISISPLRDDTAAELGAeWIAIRPGTDVAL---MLALahtLVTEGLHDK 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 256 SFIQARTNGYDELSVYLNSLDLSQ------AADICGLELGQIREAALAFGEADTgMVLTARGVEQQTDGHLAvrHFLNLV 329
Cdd:cd02769 257 AFLARYTVGFDKFLPYLLGESDGVpktpewAAAICGIPAETIRELARRFASKRT-MIMAGWSLQRAHHGEQP--HWMAVT 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 330 LAT--GKIGREGCGYGAITGQGNGQGGREHGQKADQLP-GYRSIeneKDRAYVASVwgVEAASLPGKgvsayemmELIHQ 406
Cdd:cd02769 334 LAAmlGQIGLPGGGFGFGYHYSNGGGPPRGAAPPPALPqGRNPV---SSFIPVARI--ADMLLNPGK--------PFDYN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 407 GV------IKSLFVMGSNPIVSNPNAGLVEEALNKLDFLMVADMFMSETAQLADLVLPVTSYME-NEGTLTNLEGRVLlr 479
Cdd:cd02769 401 GKkltypdIKLVYWAGGNPFHHHQDLNRLIRAWQKPETVIVHEPFWTATARHADIVLPATTSLErNDIGGSGDNRYIV-- 478
|
490 500 510
....*....|....*....|....*....|....*....
gi 2083076315 480 eAGRQA--P-GEARHDWMILCSIADMLGKGHYFRFNEPE 515
Cdd:cd02769 479 -AMKQVvePvGEARDDYDIFADLAERLGVEEQFTEGRDE 516
|
|
| MopB_CT_Formate-Dh_H |
cd02790 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
588-704 |
6.30e-36 |
|
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. This CD (MopB_CT_Formate-Dh_H) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239191 [Multi-domain] Cd Length: 116 Bit Score: 131.21 E-value: 6.30e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 588 EEYSLILTNGRVLSHYLTGVQTRRSPSLLARELENFVEIHPITAQRYRIRDGEWVEVQSEHGYFTVRARIKDQIREDTLF 667
Cdd:cd02790 1 EEYPLVLTTGRVLYHYHTGTMTRRAEGLDAIAPEEYVEINPEDAKRLGIEDGEKVRVSSRRGSVEVRARVTDRVPEGVVF 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 2083076315 668 VPMHWgGVQNVNHATRPELDPFCKMPGFKTSAVRIRP 704
Cdd:cd02790 81 MPFHF-AEAAANLLTNAALDPVAKIPEFKVCAVRVEK 116
|
|
| MopB_Arsenate-R |
cd02757 |
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ... |
16-516 |
7.85e-36 |
|
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: 142.19 E-value: 7.85e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 16 IETQCPFCSVQCkmtvteggnGIPGQRRAE--YKVEGVPNA-ASEGRVCVKGMHAHQHAVHSQRLTNPFIRSN------- 85
Cdd:cd02757 2 VPSTCQGCTAWC---------GLQAYVEDGrvTKVEGNPLHpGSRGRLCAKGHLGLQQVYDPDRILYPMKRTNprkgrdv 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 86 -GELVPCSWDEAFAVASQHLQGISEQHGPDANAV-YGGGSLTNETAYllGKFARvALGTRHIDYNGRFCMSAAASAGSKT 163
Cdd:cd02757 73 dPKFVPISWDEALDTIADKIRALRKENEPHKIMLhRGRYGHNNSILY--GRFTK-MIGSPNNISHSSVCAESEKFGRYYT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 164 fgiDRGLTFRLADIPLARCIVLAGTNIAECQpTLLPYFNR---AKENGARIIVIDPRKTATAAMADMHLPIRPGTDTVLA 240
Cdd:cd02757 150 ---EGGWDYNSYDYANAKYILFFGADPLESN-RQNPHAQRiwgGKMDQAKVVVVDPRLSNTAAKADEWLPIKPGEDGALA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 241 DVMLKIIMDEGFIDESFIQARTNG--------------YDELSVY-----LNsLDLSQ-----AADICGLELGQIREAAL 296
Cdd:cd02757 226 LAIAHVILTEGLWDKDFVGDFVDGknyfkagetvdeesFKEKSTEglvkwWN-LELKDytpewAAKISGIPAETIERVAR 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 297 AFGEADT-GMVLTARGVEQQTDGHLAVR--HFLNLVlaTGKIGREGcgyGAITGQGNGQggrehgqkadqlpgyrsiene 373
Cdd:cd02757 305 EFATAAPaAAAFTWRGATMQNRGSYNSMacHALNGL--VGSIDSKG---GLCPNMGVPK--------------------- 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 374 kdrayvasvwgveaaslpgkgvsayemmelihqgvIKSLFVMGSNPIVSNPNAGLVEEALNKLDFLMVADMFMSETAQLA 453
Cdd:cd02757 359 -----------------------------------IKVYFTYLDNPVFSNPDGMSWEEALAKIPFHVHLSPFMSETTYFA 403
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2083076315 454 DLVLPVTSYMENEGTL---TNLEGRVLLREAGRQAPGEARHDWMILCSIADML-GKGH-------YFRFNEPEE 516
Cdd:cd02757 404 DIVLPDGHHFERWDVMsqeNNLHPWLSIRQPVVKSLGEVREETEILIELAKKLdPKGSdgmkryaPGQFKDPET 477
|
|
| MopB_Nitrate-R-NarG-like |
cd02750 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
49-500 |
4.83e-34 |
|
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under anaerobic conditions in the presence of nitrate, E. coli synthesizes the cytoplasmic membrane-bound quinol-nitrate oxidoreductase (NarGHI), which reduces nitrate to nitrite and forms part of a redox loop generating a proton-motive force. Found in prokaryotes and some archaea, NarGHI usually functions as a heterotrimer. The alpha chain contains the molybdenum cofactor-containing Mo-bisMGD catalytic subunit. Members of the MopB_Nitrate-R-NarG-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239151 [Multi-domain] Cd Length: 461 Bit Score: 135.91 E-value: 4.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 49 EGVPNAasEGRVCVKGMHAHQHAVHSQRLTNPFIRS----NGELVPCSWDEAFAVASQHLQGISEQHGPDANAVYGGGSL 124
Cdd:cd02750 41 PDLPDY--NPRGCQRGASFSWYLYSPDRVKYPLKRVgargEGKWKRISWDEALELIADAIIDTIKKYGPDRVIGFSPIPA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 125 TNETAYllgkfarvALGTRHIDYNGRFCMSAAA------SAGSKTFGiDRGLTFRLADIPLARCIVLAGTNIAECQPTLL 198
Cdd:cd02750 119 MSMVSY--------AAGSRFASLIGGVSLSFYDwygdlpPGSPQTWG-EQTDVPESADWYNADYIIMWGSNVPVTRTPDA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 199 PYFNRAKENGARIIVIDPRKTATAAMADMHLPIRPGTDTVLADVMLKIIMDEGFIDESFIQARTNgyDELSVYlnslDLS 278
Cdd:cd02750 190 HFLTEARYNGAKVVVVSPDYSPSAKHADLWVPIKPGTDAALALAMAHVIIKEKLYDEDYLKEYTD--LPFLVY----TPA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 279 QAADICGLELGQIREAALAFGEADTGMVLTARGVEQQTDGHLAVRHFLNLVLATGKIGRegcgygaitgqgngqggrehg 358
Cdd:cd02750 264 WQEAITGVPRETVIRLAREFATNGRSMIIVGAGINHWYHGDLCYRALILLLALTGNEGK--------------------- 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 359 qkadqlpgyrsienekdrayvasvwgveaaslPGKGVSAYEmmelihqGVIKSLFVMGSNPIVSNPNAG-LVEEALN-KL 436
Cdd:cd02750 323 --------------------------------NGGGWAHYV-------GQPRVLFVWRGNLFGSSGKGHeYFEDAPEgKL 363
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2083076315 437 DFLMVADMFMSETAQLADLVLP-VTSYMENEGTLTNLEGRVLLREAGRQAPGEARHDWMILCSIA 500
Cdd:cd02750 364 DLIVDLDFRMDSTALYSDIVLPaATWYEKHDLSTTDMHPFIHPFSPAVDPLWEAKSDWEIFKALA 428
|
|
| MopB_CT_Nitrate-R-NapA-like |
cd02791 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
588-704 |
5.79e-34 |
|
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. This CD (MopB_CT_Nitrate-R-Nap) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs
Pssm-ID: 239192 [Multi-domain] Cd Length: 122 Bit Score: 125.76 E-value: 5.79e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 588 EEYSLILTNGRVLSHYLTGVQTRRSPSLLARELENFVEIHPITAQRYRIRDGEWVEVQSEHGYFTVRARIKDQIREDTLF 667
Cdd:cd02791 1 AEYPLWLNTGRVRDQWHTMTRTGRVPRLNAHVPEPYVEIHPEDAARLGLKEGDLVRVTSRRGEVVLRVRVTDRVRPGEVF 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2083076315 668 VPMHWGGVQN----VNHATRPELDPFCKMPGFKTSAVRIRP 704
Cdd:cd02791 81 VPMHWGDQFGrsgrVNALTLDATDPVSGQPEFKHCAVRIEK 121
|
|
| Molydop_binding |
pfam01568 |
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
592-699 |
1.24e-32 |
|
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: 121.61 E-value: 1.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 592 LILTNGRVLSHYLTGVQTRRSPSLLARElENFVEIHPITAQRYRIRDGEWVEVQSEHGYFTVRARIKDQIREDTLFVPMH 671
Cdd:pfam01568 1 LYLITGRVLGQYHSQTRTRRVLRLAKPE-PEVVEIHPEDAAALGIKDGDLVEVTSRRGSVVVRAKVTDRVRPGVVFMPFG 79
|
90 100 110
....*....|....*....|....*....|.
gi 2083076315 672 WGGV---QNVNHATRPELDPFCKMPGFKTSA 699
Cdd:pfam01568 80 WWYEprgGNANALTDDATDPLSGGPEFKTCA 110
|
|
| MopB_CT_Formate-Dh-Na-like |
cd02792 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
588-704 |
2.66e-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. This CD (MopB_CT_Formate-Dh-Na-like) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239193 [Multi-domain] Cd Length: 122 Bit Score: 118.48 E-value: 2.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 588 EEYSLILTNGRVLSHYLTGVQTRRSPSLLARELENFVEIHPITAQRYRIRDGEWVEVQSEHGYFTVRARIKDQIREDTLF 667
Cdd:cd02792 1 EEFPLVLTTGRLTEHFHGGNMTRNSPYLAELQPEMFVEISPELAAERGIKNGDMVWVSSPRGKIKVKALVTDRVKPHEVG 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2083076315 668 VPMHWGGV-----QNVNHATRPELDPFCKMPGFKTSAVRIRP 704
Cdd:cd02792 81 IPYHWGGMglvigDSANTLTPYVGDPNTQTPEYKAFLVNIEK 122
|
|
| PRK07860 |
PRK07860 |
NADH dehydrogenase subunit G; Validated |
61-676 |
5.46e-30 |
|
NADH dehydrogenase subunit G; Validated
Pssm-ID: 236118 [Multi-domain] Cd Length: 797 Bit Score: 126.60 E-value: 5.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 61 CVKGMHAHQHAVHSQRLTNPFIR-SNGELVPCSWDEAFAVASQHLQGISEQHGpdanaVYGGGSLTNETAYLLGKFARVA 139
Cdd:PRK07860 263 CDKGRWAFTYATQPDRITTPLVRdEDGELEPASWSEALAVAARGLAAARGRVG-----VLVGGRLTVEDAYAYAKFARVA 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 140 LGTRHIDYNGRfcmsaAASAGSKTF------GIDRGLTFrlADIPLARCIVLAGTNIAECQPTLlpyFNR----AKENGA 209
Cdd:PRK07860 338 LGTNDIDFRAR-----PHSAEEADFlaarvaGRGLGVTY--ADLEKAPAVLLVGFEPEEESPIV---FLRlrkaARKHGL 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 210 RIIVIDPrkTATAAMADMH---LPIRPGTDtvlADVMLKIIMDEGFIDESFiqaRTNGydelSVYLnsldlsqaadicgl 286
Cdd:PRK07860 408 KVYSIAP--FATRGLEKMGgtlLRTAPGGE---AAALDALATGAPDVAELL---RTPG----AVIL-------------- 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 287 eLGQiREAALAFGeadtgmvLTArgveqqtdghlAVRhflnLVLATGK----IGREGCGYGAItgqgngqggrEHGQKAD 362
Cdd:PRK07860 462 -VGE-RLATVPGA-------LSA-----------AAR----LADATGArlawVPRRAGERGAL----------EAGALPT 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 363 QLPGYRSIENEKDRAYVASVWGVeaASLPGK-GVSAYEMMELIHQGVIKSLFVMGSNPI-VSNPNAglVEEALNKLDFLM 440
Cdd:PRK07860 508 LLPGGRPVADPAARAEVAAAWGV--DELPAApGRDTAGILAAAAAGELGALLVGGVEPAdLPDPAA--ALAALDAAGFVV 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 441 VADMFMSETAQLADLVLPVTSYMENEGTLTNLEGRVLLREAGRQAPGeARHDWMILCSIADMLGKghYFRFNEPEEVFNE 520
Cdd:PRK07860 584 SLELRHSAVTERADVVLPVAPVAEKAGTFLNWEGRLRPFEAALRTTG-ALSDLRVLDALADEMGV--DLGLPTVAAARAE 660
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 521 LrlaskggiadyygityDRLRREKGVYWPCPSPEEAGAgllfqqsfAHPD-GKAVFSimegtPWKgvteeysLILTNGRV 599
Cdd:PRK07860 661 L----------------ARLGAWDGARAAAPAVPAAAP--------PQPGaGEAVLA-----TWR-------MLLDDGRL 704
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2083076315 600 L--SHYLTGvqTRRSPSllarelenfVEIHPITAQRYRIRDGEWVEVQSEHGYFTVRARIKDqIREDTLFVPMHWGGVQ 676
Cdd:PRK07860 705 QdgEPHLAG--TARPPV---------ARLSAATAAEIGVADGDAVTVSTERGSITLPLAITD-MPDRVVWLPLNSPGST 771
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
388-521 |
2.79e-28 |
|
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production and conversion]; NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) is part of the Pathway/BioSystem: NADH dehydrogenase
Pssm-ID: 440657 [Multi-domain] Cd Length: 453 Bit Score: 118.79 E-value: 2.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 388 ASLPGKGVSAYEMMELIHQGVIKSLFVMGSNPIVSNPNAglVEEALNKLDFLMVADMFMSETAQLADLVLPVTSYMENEG 467
Cdd:COG1034 312 AALLGALPDAAAILEAAEAGKLKALVLLGADPYDLDPAA--ALAALAKADFVVVLDHFGSATAERADVVLPAAAFAEKSG 389
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2083076315 468 TLTNLEGRVLLREAGRQAPGEARHDWMILCSIADMLGKGhyFRFNEPEEVFNEL 521
Cdd:COG1034 390 TFVNLEGRVQRFNAAVPPPGEARPDWRVLRALANALGAG--LPYDSLEEVRAEL 441
|
|
| MopB_NDH-1_NuoG2 |
cd02772 |
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase ... |
73-496 |
3.36e-28 |
|
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase/NADH dehydrogenase-1 (NDH-1), found in beta- and gammaproteobacteria. The NDH-1 is the first energy-transducting complex in the respiratory chain and functions as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. In Escherichia coli NDH-1, the largest subunit is encoded by the nuoG gene, and is part of the 14 distinct subunits constituting the functional enzyme. The NuoG subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain belongs to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239173 [Multi-domain] Cd Length: 414 Bit Score: 117.84 E-value: 3.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 73 HSQRLTNPFIRSNGELVPCSWDEAFAVASQHLQGISEQHGPDANAVYGGGSLTNETAYLLGKFARvALGTRHIDYNGRfc 152
Cdd:cd02772 51 SEDRLTKPMIKKDGQWQEVDWETALEYVAEGLSAIIKKHGADQIGALASPHSTLEELYLLQKLAR-GLGSDNIDHRLR-- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 153 mSAAASAGSKtFGIDRGLTFRLADIPLARCIVLAGTNIAECQPTLLPYFNRAKENGARIIVIDPrktataAMADMHLPIr 232
Cdd:cd02772 128 -QSDFRDDAK-ASGAPWLGMPIAEISELDRVLVIGSNLRKEHPLLAQRLRQAVKKGAKLSAINP------ADDDFLFPL- 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 233 PGTDTVLADVMLKIimdegfidesfiqartngydelsvylnsldLSQAADICGLELGQIREAALAFGEADTgmvlTARGV 312
Cdd:cd02772 199 SGKAIVAPSALANA------------------------------LAQVAKALAEEKGLAVPDEDAKVEASE----EARKI 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 313 EQQTD---------GHLAVRH-----FLNLVLATGKIgrEGCGYGAITGQGNGQGGREHGqkadqlpgyrsienekdray 378
Cdd:cd02772 245 AASLVsaeraavflGNLAQNHpqaatLRALAQEIAKL--TGATLGVLGEGANSVGAYLAG-------------------- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 379 vasvwgveaaSLPGKGVSAYEMMElihQGvIKSLFVMGSNPIVSNPNAGLVEEALNKLDFLMVADMFMSETAQ-LADLVL 457
Cdd:cd02772 303 ----------ALPHGGLNAAAMLE---QP-RKAYLLLNVEPELDCANPAQALAALNQAEFVVALSAFASAALLdYADVLL 368
|
410 420 430
....*....|....*....|....*....|....*....
gi 2083076315 458 PVTSYMENEGTLTNLEGRVLLREAGRQAPGEARHDWMIL 496
Cdd:cd02772 369 PIAPFTETSGTFVNLEGRVQSFKGVVKPLGEARPAWKVL 407
|
|
| PRK09939 |
PRK09939 |
acid resistance putative oxidoreductase YdeP; |
76-704 |
2.39e-27 |
|
acid resistance putative oxidoreductase YdeP;
Pssm-ID: 182156 [Multi-domain] Cd Length: 759 Bit Score: 118.22 E-value: 2.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 76 RLTNP--FIRSNGELVPCSWDEAFAVASQHLQGISEqhgPDANAVYGGGSLTNETAYLLGKFARvALGTRHIDYNGRFCM 153
Cdd:PRK09939 108 RLTQPlkYDAVSDCYKPLSWQQAFDEIGARLQSYSD---PNQVEFYTSGRTSNEAAFLYQLFAR-EYGSNNFPDCSNMCH 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 154 SAAASAGSKTFGIDRGlTFRLADIPLARCIVLAGTNIAECQPTLLPYFNRAKENGARIIVIDP-------RKTA------ 220
Cdd:PRK09939 184 EPTSVGLAASIGVGKG-TVLLEDFEKCDLVICIGHNPGTNHPRMLTSLRALVKRGAKMIAINPlqergleRFTApqnpfe 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 221 -----TAAMADMHLPIRPGTDTVLADVMLKIIMDE----------GFIDESFIQARTNGYDELSVYLNSLDLSQAADICG 285
Cdd:PRK09939 263 mltnsETQLASAYYNVRIGGDMALLKGMMRLLIERddaasaagrpSLLDDEFIQTHTVGFDELRRDVLNSEWKDIERISG 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 286 LELGQIREAALAFGEADTGMVLTARGVEQQTDGHLAVRHFLNLVLATGKIGREGCGYGAITGQGNGQGGREHGqkADQLP 365
Cdd:PRK09939 343 LSQTQIAELADAYAAAERTIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGICPLRGHSNVQGDRTVG--ITEKP 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 366 GYRSIenekdrAYVASVWGVEAASLPGKgvSAYEMMELIHQGVIKSLFVMGSNPIVSNPNAGLVEEALNKLDFLMVADMF 445
Cdd:PRK09939 421 SAEFL------ARLGERYGFTPPHAPGH--AAIASMQAICTGQARALICMGGNFALAMPDREASAVPLTQLDLAVHVATK 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 446 MSETAQLA---DLVLPVTSYMEnegtltnlegrVLLREAGRQApgearhdwmilCSIADMLGKGHYFR-FNEPEEVFNEL 521
Cdd:PRK09939 493 LNRSHLLTarhSYILPVLGRSE-----------IDMQKSGAQA-----------VTVEDSMSMIHASRgVLKPAGVMLKS 550
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 522 RLASKGGIA-----------DYYGITYDRLRREKGVYWPCPSP------EEAGAGLL---FQQSFAHPDGKAVFsimegT 581
Cdd:PRK09939 551 ECAVVAGIAqaalpqsvvawEYLVEDYDRIRNDIEAVLPEFADynqrirHPGGFHLInaaAERRWMTPSGKANF-----I 625
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 582 PWKGVTEEYS------LILTNGRVLSHYLT---GVQTRRSPSLLARELenfVEIHPITAQRYRIRDGEWVEVQSEHGYFT 652
Cdd:PRK09939 626 TSKGLLEDPSsafnskLVMATVRSHDQYNTtiyGMDDRYRGVFGQRDV---VFMSAKQAKICRVKNGERVNLIALTPDGK 702
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 2083076315 653 VRARIKDQIRedTLFVPMHWGGV----QNVNHA-TRPELDPFCKMPGFKTSAVRIRP 704
Cdd:PRK09939 703 RSSRRMDRLK--VVIYPMADRSLvtyfPESNHMlTLDNHDPLSGIPGYKSIPVELEP 757
|
|
| MopB_CT |
cd02775 |
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a ... |
599-696 |
2.69e-25 |
|
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: 100.47 E-value: 2.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 599 VLSHYLTGVQTRrSPSLLARELENFVEIHPITAQRYRIRDGEWVEVQSEHGYFTVRARIKDQIREDTLFVPMHWGGV--- 675
Cdd:cd02775 1 LRDHFHSGTRTR-NPWLRELAPEPVVEINPEDAAALGIKDGDLVRVESRRGSVVLRAKVTDGVPPGVVFLPHGWGHRggr 79
|
90 100
....*....|....*....|..
gi 2083076315 676 -QNVNHATRPELDPFCKMPGFK 696
Cdd:cd02775 80 gGNANVLTPDALDPPSGGPAYK 101
|
|
| PRK14990 |
PRK14990 |
anaerobic dimethyl sulfoxide reductase subunit A; Provisional |
59-657 |
5.03e-23 |
|
anaerobic dimethyl sulfoxide reductase subunit A; Provisional
Pssm-ID: 184952 [Multi-domain] Cd Length: 814 Bit Score: 104.73 E-value: 5.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 59 RVCVKGMHAHQHAVHSQRLTNPF----IRSNGELVPCSWDEAFAVASQHLQGISEQHGPDANAV-YG----GGSLTNE-- 127
Cdd:PRK14990 102 RACLRGRSMRRRVYNPDRLKYPMkrvgARGEGKFERISWEEAYDIIATNMQRLIKEYGNESIYLnYGtgtlGGTMTRSwp 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 128 -TAYLLGKFARVALGtrHIDYNGRFCMSAAASAGSKTFG--IDRGLTfrlADIPLARCIVLAGTNIAECQPT---LLPYF 201
Cdd:PRK14990 182 pGNTLVARLMNCCGG--YLNHYGDYSSAQIAEGLNYTYGgwADGNSP---SDIENSKLVVLFGNNPGETRMSgggVTYYL 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 202 NRAKE-NGARIIVIDPRKTATAA-MADMHLPIRPGTDTVLADVMLKIIMDEGFIDESFIQARTNGYDELSV--------Y 271
Cdd:PRK14990 257 EQARQkSNARMIIIDPRYTDTGAgREDEWIPIRPGTDAALVNGLAYVMITENLVDQPFLDKYCVGYDEKTLpasapkngH 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 272 LNSLDLSQAAD-----------ICGLELGQIREAALAFGEADTGMVLTARGVEQQTDGHLAVRHFLNLVLATGKIGREGc 340
Cdd:PRK14990 337 YKAYILGEGPDgvaktpewasqITGVPADKIIKLAREIGSTKPAFISQGWGPQRHANGEIATRAISMLAILTGNVGING- 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 341 gygaitgqGNgQGGREHGQKadqLPGYR--SIENEKDRAYVASVW------GVEAASLPgKGVSAYEMMELihqgVIKSL 412
Cdd:PRK14990 416 --------GN-SGAREGSYS---LPFVRmpTLENPIQTSISMFMWtdaierGPEMTALR-DGVRGKDKLDV----PIKMI 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 413 FVMGSNPIVS-NPNAGLVEEALN---KLDFLMVADMFMSETAQLADLVLPVTSYMEN-----EGTLTNLEgRVLLREAGR 483
Cdd:PRK14990 479 WNYAGNCLINqHSEINRTHEILQddkKCELIVVIDCHMTSSAKYADILLPDCTASEQmdfalDASCGNMS-YVIFNDQVI 557
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 484 QAPGEARHDWMILCSIADMLGKGHYF-RFNEPEEVFNELRLASKGGIADYygITYDRLRREkGVYW-------------- 548
Cdd:PRK14990 558 KPRFECKTIYEMTSELAKRLGVEQQFtEGRTQEEWMRHLYAQSREAIPEL--PTFEEFRKQ-GIFKkrdpqghhvaykaf 634
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 549 ---PCPSPEEAGAGL--LFQQSFAH-------PDGKAVFSIMEGTPW-----KGVTEEYSLILTNgrvlSHYLTGVQ-TR 610
Cdd:PRK14990 635 redPQANPLTTPSGKieIYSQALADiaatwelPEGDVIDPLPIYTPGfesyqDPLNKQYPLQLTG----FHYKSRVHsTY 710
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 2083076315 611 RSPSLLARELENFVEIHPITAQRYRIRDGEWVEVQSEHGYFTVRARI 657
Cdd:PRK14990 711 GNVDVLKAACRQEMWINPLDAQKRGINNGDKVRIFNDRGEVHIEAKV 757
|
|
| MopB_Tetrathionate-Ra |
cd02758 |
The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other ... |
58-531 |
2.40e-21 |
|
The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other related proteins. The Salmonella enterica tetrathionate reductase catalyses the reduction of trithionate but not sulfur or thiosulfate. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239159 [Multi-domain] Cd Length: 735 Bit Score: 99.34 E-value: 2.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 58 GRVCVKGMHAHQHAVHSQRLTNPFIR----SNGELVPCSWDEAF-AVASQ-------HLQG----------ISEQH---G 112
Cdd:cd02758 65 ATACARGNAGLQYLYDPYRVLQPLKRvgprGSGKWKPISWEQLIeEVVEGgdlfgegHVEGlkairdldtpIDPDHpdlG 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 113 PDANAVYGGGSLTNETAYLLGKFARVALGTRHIDYNGRFC---MSAAASAGSKTFGidrGLTFRLADIPLARCIVLAGTN 189
Cdd:cd02758 145 PKANQLLYTFGRDEGRTPFIKRFANQAFGTVNFGGHGSYCglsYRAGNGALMNDLD---GYPHVKPDFDNAEFALFIGTS 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 190 IAECQPTLLP----YFNRAKENGARIIVIDPRKTATAAMADMH---LPIRPGTDTVLADVMLKIIMDEGFIDESFIQ--- 259
Cdd:cd02758 222 PAQAGNPFKRqarrLAEARTEGNFKYVVVDPVLPNTTSAAGENirwVPIKPGGDGALAMAMIRWIIENERYNAEYLSips 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 260 ---ARTNGYDELS--VYL-----------------NSLDLSQAADICGLELGQIREAALAFGEADTGMVLTARGVEQQTD 317
Cdd:cd02758 302 keaAKAAGEPSWTnaTHLvitvrvksalqllkeeaFSYSLEEYAEICGVPEAKIIELAKEFTSHGRAAAVVHHGGTMHSN 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 318 GHLAVRHFLNLVLATGKIGREGcgyGAITGQG----NGQGGR------------------EHGQKADQLPGYRSIENEKD 375
Cdd:cd02758 382 GFYNAYAIRMLNALIGNLNWKG---GLLMSGGgfadNSAGPRydfkkffgevkpwgvpidRSKKAYEKTSEYKRKVAAGE 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 376 RAYVAsvwgvEAASLPGKGVSAYEMMELIHQGV---IKSLFVMGSNPIVSNPnaGL---VEEALN---KLDFLMVADMFM 446
Cdd:cd02758 459 NPYPA-----KRPWYPLTPELYTEVIASAAEGYpykLKALILWMANPVYGAP--GLvkqVEEKLKdpkKLPLFIAIDAFI 531
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 447 SETAQLADLVLPVTSYMENEGTLTNLEGRVLLREAGRQ----------APGEARHDWMILCSIADMLG------------ 504
Cdd:cd02758 532 NETSAYADYIVPDTTYYESWGFSTPWGGVPTKASTARWpviapltektANGHPVSMESFLIDLAKALGlpgfgpnaikdg 611
|
570 580 590
....*....|....*....|....*....|.
gi 2083076315 505 KGHYFRFNEPEE----VFNELRLASKGGIAD 531
Cdd:cd02758 612 QGNKFPLNRAEDyylrVAANIAYDGKAPVPD 642
|
|
| MopB_2 |
cd02763 |
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
18-473 |
8.02e-18 |
|
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: 87.96 E-value: 8.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 18 TQCPFCSVQCKMTVTeggngipgQRRAEYK-VEGVPN-AASEGRVCVKGMHAHQHAVHSQRLTNPFIRS----NGELVPC 91
Cdd:cd02763 2 TTCYMCACRCGIRVH--------LRDGKVRyIKGNPDhPLNKGVICAKGSSGIMKQYSPARLTKPLLRKgprgSGQFEEI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 92 SWDEAFAVASQHLQGISeQHGPDANAVYGGgslTNETAYLLGKFARvALGTRHIDYNGRFCMSAAASAGSKTFGiDRGLT 171
Cdd:cd02763 74 EWEEAFSIATKRLKAAR-ATDPKKFAFFTG---RDQMQALTGWFAG-QFGTPNYAAHGGFCSVNMAAGGLYSIG-GSFWE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 172 FRLADIPLARCIVLAGTNIAECQPTLLPYFNRAKENGARIIVIDPRKTATAAMADMHLPIRPGTDTVLADVMLKIIMDEG 251
Cdd:cd02763 148 FGGPDLEHTKYFMMIGVAEDHHSNPFKIGIQKLKRRGGKFVAVNPVRTGYAAIADEWVPIKPGTDGAFILALAHELLKAG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 252 FIDESFIQARTNgydelSVYLNSLDLSQAADICGLELGQIREAALAFG----------------------EADTGMVLT- 308
Cdd:cd02763 228 LIDWEFLKRYTN-----AAELVDYTPEWVEKITGIPADTIRRIAKELGvtardqpielpiawtdvwgrkhEKITGRPVSf 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 309 --ARGVEQQTDGHLAVRHFLNLVLATGKIGREG--------------CGYGAITGQGNGQGGREHG------QKADQLpg 366
Cdd:cd02763 303 haMRGIAAHSNGFQTIRALFVLMMLLGTIDRPGgfrhkppyprhippLPKPPKIPSADKPFTPLYGpplgwpASPDDL-- 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 367 yrSIENEK-----DRAYvasVWgveaaSLPgkgVSAYEMMelihQGVIKSLFVMGSNPI------------VSNPNAGLV 429
Cdd:cd02763 381 --LVDEDGnplriDKAY---SW-----EYP---LAAHGCM----QNVITNAWRGDPYPIdtlmiymanmawNSSMNTPEV 443
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 2083076315 430 EEALN--------KLDFLMVADMFMSETAQLADLVLPVTSYMENEGTLTNLE 473
Cdd:cd02763 444 REMLTdkdasgnyKIPFIIVCDAFYSEMVAFADLVLPDTTYLERHDAMSLLD 495
|
|
| MopB_FmdB-FwdB |
cd02761 |
The MopB_FmdB-FwdB CD contains the molybdenum/tungsten formylmethanofuran dehydrogenases, ... |
20-478 |
2.97e-15 |
|
The MopB_FmdB-FwdB CD contains the molybdenum/tungsten formylmethanofuran dehydrogenases, subunit B (FmdB/FwdB), and other related proteins. Formylmethanofuran dehydrogenase catalyzes the first step in methane formation from CO2 in methanogenic archaea and some eubacteria. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239162 [Multi-domain] Cd Length: 415 Bit Score: 78.53 E-value: 2.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 20 CPFCSVQCK-MTVTEGGNGIPGQRRAeykvegvpnaasegrvCVKGMHAHQHAVHsqRLTNPFIRSngelVPCSWDEAFA 98
Cdd:cd02761 4 CPFCGLLCDdIEVEVEDNKITKVRNA----------------CRIGAAKFARYER--RITTPRIDG----KPVSLEEAIE 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 99 VASQHLQgisEQHGPdanAVYGGGSLTNE---TAYLLGKfarvALGTrHIDYNGRFCMSAAASAGsktfgIDRGLTF-RL 174
Cdd:cd02761 62 KAAEILK---EAKRP---LFYGLGTTVCEaqrAGIELAE----KLGA-IIDHAASVCHGPNLLAL-----QDSGWPTtTL 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 175 ADIP-LARCIVLAGTNIAECQPTLLP---YFNRAKE-NGAR----IIVIDPRKTATAAMADMHLPIRPGTDTVLADVMLK 245
Cdd:cd02761 126 GEVKnRADVIVYWGTNPMHAHPRHMSrysVFPRGFFrEGGRedrtLIVVDPRKSDTAKLADIHLQIDPGSDYELLAALRA 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 246 IIMDEGFIDEsfiqARTNGYDElsvylnsldlsqaadicglelgQIREAALAFGEADTGMVLTARGVEQQTDGHLAVRHF 325
Cdd:cd02761 206 LLRGAGLVPD----EVAGIPAE----------------------TILELAERLKNAKFGVIFWGLGLLPSRGAHRNIEAA 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 326 LNLVLATGKIGREGCgyGAITGQGNGQGgreHGQKADQLPGYrsienekdrayvasVWGVEAASLPGKGvSAYEMM--EL 403
Cdd:cd02761 260 IRLVKALNEYTKFAL--LPLRGHYNVRG---FNQVLTWLTGY--------------PFRVDFSRGYPRY-NPGEFTavDL 319
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2083076315 404 IHQGVIKSLFVMGSNPIVSNPnAGLVEEALNKLdfLMVADMFMSETAQLADLVLPV-TSYMENEGTLTNLEGRVLL 478
Cdd:cd02761 320 LAEGEADALLIIASDPPAHFP-QSAVKHLAEIP--VIVIDPPPTPTTRVADVVIPVaIPGIEAGGTAYRMDGVVVL 392
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
16-237 |
6.18e-15 |
|
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production and conversion]; NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) is part of the Pathway/BioSystem: NADH dehydrogenase
Pssm-ID: 440657 [Multi-domain] Cd Length: 453 Bit Score: 77.96 E-value: 6.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 16 IETQCPFCSVQCKMTVTEGGNGIpgqrraeYKVEGVPNAA-SEGRVCVKGMHAHQHAVHSQRLTNPFIRSNGELVPCSWD 94
Cdd:COG1034 218 TPSICPHCSVGCNIRVDVRGGKV-------YRVLPRENEAvNEEWLCDKGRFGYDGLNSPDRLTRPLVRKDGELVEASWE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 95 EAFAVASQHLQGISeqhgpDANAVYGggsltnetAYLLGKFARVAlgtrhidyngrfCMSAAASAGSktfgidrgltfrl 174
Cdd:COG1034 291 EALAAAAEGLKALK-----KAENSVG--------AALLGALPDAA------------AILEAAEAGK------------- 332
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2083076315 175 adiplARCIVLAGTNIAECQPTLLpyfNRAKENGARIIVIDPRKTATAAMADMHLPIRPGTDT 237
Cdd:COG1034 333 -----LKALVLLGADPYDLDPAAA---LAALAKADFVVVLDHFGSATAERADVVLPAAAFAEK 387
|
|
| MopB_Phenylacetyl-CoA-OR |
cd02760 |
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large ... |
18-263 |
2.24e-14 |
|
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large subunit (PadB2), and other related proteins. The phenylacetyl-CoA:acceptor oxidoreductase has been characterized as a membrane-bound molybdenum-iron-sulfur enzyme involved in anaerobic metabolism of phenylalanine in the denitrifying bacterium Thauera aromatica. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239161 [Multi-domain] Cd Length: 760 Bit Score: 76.93 E-value: 2.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 18 TQCPFCSVQCKMTVTEGGNGIPGQRRAEYKVEGVPNAasEGRVCVKGMHAHQHAVHSQRLTNPFIRSNGE--------LV 89
Cdd:cd02760 2 TYCYNCVAGPDFMAVKVVDGVATEIEPNFAAEDIHPA--RGRVCVKAYGLVQKTYNPNRVLQPMKRTNPKkgrnedpgFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 90 PCSWDEAFAVASQHLQGISEQHGPD-------ANAVYGGGSLTNETAYLLGKFArvALGTrhIDYN----GRFCMSAAAS 158
Cdd:cd02760 80 PISWDEALDLVAAKLRRVREKGLLDekglprlAATFGHGGTPAMYMGTFPAFLA--AWGP--IDFSfgsgQGVKCVHSEH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 159 AGSKTFgiDRGLTFrLADIPLARCIVLAGTNI-AECQPTLLPYFNRAKENGARIIVIDPRKTATAAMADMHLPIRPGTDT 237
Cdd:cd02760 156 LYGEFW--HRAFTV-AADTPLANYVISFGSNVeASGGPCAVTRHADARVRGYKRVQVEPHLSVTGACSAEWVPIRPKTDP 232
|
250 260
....*....|....*....|....*....
gi 2083076315 238 VLADVMLKIIMDE---GFIDESFIQARTN 263
Cdd:cd02760 233 AFMFAMIHVMVHEqglGKLDVPFLRDRTS 261
|
|
| MopB_Res-Cmplx1_Nad11 |
cd02773 |
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone ... |
58-503 |
3.13e-14 |
|
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: 74.99 E-value: 3.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 58 GRVCVKGMHahqhavhSQRLTNPFIRSNGELVPCSWDEAFAVASQHLQGIseqhGPDANAVYGGGSLTNETAYLLGKFAR 137
Cdd:cd02773 42 TRFAYDGLK-------RQRLDKPYIRKNGKLKPATWEEALAAIAKALKGV----KPDEIAAIAGDLADVESMVALKDLLN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 138 vALGTRHIDYNGRFCMSAAASAGSKTFGIdrgltfRLADIPLARCIVLAGTNIA-ECqptllPYFNrakengARIividp 216
Cdd:cd02773 111 -KLGSENLACEQDGPDLPADLRSNYLFNT------TIAGIEEADAVLLVGTNPRfEA-----PVLN------ARI----- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 217 RKTATAAMADMHLpIRPGTDTvladvmlkiimdegfidesfiqarTNGYDELSVylnslDLSQAADICGlelGQIrEAAL 296
Cdd:cd02773 168 RKAWLHGGLKVGV-IGPPVDL------------------------TYDYDHLGT-----DAKTLQDIAS---GKH-PFSK 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 297 AFGEADTGMVLTARGVEQQTDGhlavrhflNLVLATgkIGREGCGYGAITGQGNGQggrehgqkadqlpgyrsieNEKDR 376
Cdd:cd02773 214 ALKDAKKPMIIVGSGALARKDG--------AAILAA--VAKLAKKNGVVREGWNGF-------------------NVLHR 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 377 AyVASVWGVEAASLPGKGvsayemmELIHQGVIKSLFVMGSNPIVsnpnaglvEEALNKLDFLMVADMFMSETAQLADLV 456
Cdd:cd02773 265 A-ASRVGALDLGFVPGAG-------AIRKSGPPKVLYLLGADEID--------ITPIPKDAFVVYQGHHGDRGAQIADVI 328
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2083076315 457 LPVTSYMENEGTLTNLEGRVLLREAGRQAPGEARHDWMILCSIADML 503
Cdd:cd02773 329 LPGAAYTEKSGTYVNTEGRVQQTRKAVSPPGDAREDWKILRALSEVL 375
|
|
| MopB_CT_Acetylene-hydratase |
cd02781 |
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related ... |
589-676 |
2.55e-13 |
|
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. The acetylene hydratase of Pelobacter acetylenicus is a tungsten iron-sulfur protein involved in the fermentation of acetylene to ethanol and acetate. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239182 [Multi-domain] Cd Length: 130 Bit Score: 67.33 E-value: 2.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 589 EYSLILTNG-RVLSHylTGVQTRRSPSLLARELENFVEIHPITAQRYRIRDGEWVEVQSEHGYFTVRARIKDQIREDTLF 667
Cdd:cd02781 1 EYPLILTTGaRSYYY--FHSEHRQLPSLRELHPDPVAEINPETAAKLGIADGDWVWVETPRGRARQKARLTPGIRPGVVR 78
|
90
....*....|
gi 2083076315 668 VPM-HWGGVQ 676
Cdd:cd02781 79 AEHgWWYPER 88
|
|
| MopB_CT_Thiosulfate-R-like |
cd02778 |
The MopB_CT_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, ... |
621-673 |
6.48e-13 |
|
The MopB_CT_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. Also included in this CD is the phenylacetyl-CoA:acceptor oxidoreductase, large subunit (PadB2), which has been characterized as a membrane-bound molybdenum-iron-sulfur enzyme involved in anaerobic metabolism of phenylalanine in the denitrifying bacterium Thauera aromatica. The MopB_CT_Thiosulfate-R-like CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239179 [Multi-domain] Cd Length: 123 Bit Score: 65.76 E-value: 6.48e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2083076315 621 ENFVEIHPITAQRYRIRDGEWVEVQSEHGYFTVRARIKDQIREDTLFVPMHWG 673
Cdd:cd02778 29 ENTLWINPETAARLGIKDGDRVEVSSARGKVTGKARLTEGIRPDTVFMPHGFG 81
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|
| Molybdop_Fe4S4 |
pfam04879 |
Molybdopterin oxidoreductase Fe4S4 domain; This domain is found in formate dehydrogenase H for ... |
15-70 |
8.15e-11 |
|
Molybdopterin oxidoreductase Fe4S4 domain; This domain is found in formate dehydrogenase H for which the structure is known. This first domain (residues 1 to 60) of PDB:1aa6 is an Fe4S4 cluster just below the protein surface.
Pssm-ID: 428168 [Multi-domain] Cd Length: 55 Bit Score: 57.69 E-value: 8.15e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2083076315 15 VIETQCPFCSVQCKMTVTEGGNGIpgqrraeYKVEGVPNA-ASEGRVCVKGMHAHQH 70
Cdd:pfam04879 3 VVKTICPYCGVGCGLEVHVKDGKI-------VKVEGDPDHpVNEGRLCVKGRFGYER 52
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|
| MopB_PHLH |
cd02764 |
The MopB_PHLH CD includes a group of related uncharacterized putative hydrogenase-like ... |
47-467 |
2.80e-10 |
|
The MopB_PHLH CD includes a group of related uncharacterized putative hydrogenase-like homologs (PHLH) of molybdopterin binding (MopB) proteins. This CD is of the PHLH region homologous to the catalytic molybdopterin-binding subunit of MopB homologs.
Pssm-ID: 239165 [Multi-domain] Cd Length: 524 Bit Score: 63.28 E-value: 2.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 47 KVEGVP-NAASEGrvcvkGMHAH-QHAVHS----QRLTNPFIRS-NGELVPCSWDEAFA-VASQHLQGiseqHGPDANAV 118
Cdd:cd02764 69 KIEGNPdHPASLG-----GTSARaQASVLSlydpDRAQGPLRRGiDGAYVASDWADFDAkVAEQLKAV----KDGGKLAV 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 119 YGGGSLTNETAYLLGKFARVALGTRHIDYNGrfcMSA--AASAGSKTFGIDRGLTFrlaDIPLARCIVLAGTNIAECQPT 196
Cdd:cd02764 140 LSGNVNSPTTEALIGDFLKKYPGAKHVVYDP---LSAedVNEAWQASFGKDVVPGY---DFDKAEVIVSIDADFLGSWIS 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 197 LLPYFN--------RAKENGARIIVIDPRKTATAAMADMHLPIRPGTDTVLADVMLKIIMDEGFIDESFIQARTNGYDEL 268
Cdd:cd02764 214 AIRHRHdfaakrrlGAEEPMSRLVAAESVYTLTGANADVRLAIRPSQEKAFALGLAHKLIKKGAGSSLPDFFRALNLAFK 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 269 SVYLNSL--DLSQAadicglelgqIREAALAFGEADTGMVLTargveqqtdghlavrhflnlvlatgkigregcgyGAIT 346
Cdd:cd02764 294 PAKVAELtvDLDKA----------LAALAKALAAAGKSLVVA----------------------------------GSEL 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 347 GQGNGqggrehgqKADQLPGYRSieNEKDRAYVASVwGVEAASLPGKGVSAYEMMEL---IHQGVIKSLFVMGSNPIVSN 423
Cdd:cd02764 330 SQTAG--------ADTQVAVNAL--NSLLGNDGKTV-DHARPIKGGELGNQQDLKALasrINAGKVSALLVYDVNPVYDL 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2083076315 424 PNAGLVEEALNKLDFLMVADMFMSETAQLADLVLPVTSYMENEG 467
Cdd:cd02764 399 PQGLGFAKALEKVPLSVSFGDRLDETAMLCDWVAPMSHGLESWG 442
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|
| Molybdop_Fe4S4 |
smart00926 |
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is ... |
15-73 |
2.79e-09 |
|
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is found in a number of reductase/dehydrogenase families, which include the periplasmic nitrate reductase precursor and the formate dehydrogenase alpha chain.
Pssm-ID: 197994 [Multi-domain] Cd Length: 55 Bit Score: 53.41 E-value: 2.79e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 15 VIETQCPFCSVQCKMTVTEGGNGIpgqrraeYKVEGVPN-AASEGRVCVKGMHAHQHAVH 73
Cdd:smart00926 3 WVPTVCPLCGVGCGLLVEVKDGRV-------VRVRGDPDhPVNRGRLCPKGRAGLEQVYS 55
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|
| MopB_CT_3 |
cd02786 |
The MopB_CT_3 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
612-686 |
6.72e-08 |
|
The MopB_CT_3 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239187 [Multi-domain] Cd Length: 116 Bit Score: 51.51 E-value: 6.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 612 SPSLLARELENFVEIHPITAQRYRIRDGEWVEVQSEHGYFTVRARIKDQIREDTLFVPMHW-----GGVQNVNHATRPEL 686
Cdd:cd02786 21 LPELRAKEGEPTLLIHPADAAARGIADGDLVVVFNDRGSVTLRAKVTDDVPPGVVVAEGGWwrehsPDGRGVNALTSARL 100
|
|
| MopB_CT_Arsenite-Ox |
cd02779 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of Arsenite oxidase ... |
590-703 |
1.36e-07 |
|
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of Arsenite oxidase (Arsenite-Ox) and related proteins. Arsenite oxidase 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.
Pssm-ID: 239180 [Multi-domain] Cd Length: 115 Bit Score: 50.53 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 590 YSLILTNGRVLSHYLTGVQTRRSPSLLARELENFVEIHPITAQRYRIRDGEWVEVQSEHGYFTVRARIKDQIREDTLFVP 669
Cdd:cd02779 1 YKYWVNNGRANIIWQTAYHDQNNSEIAERVPLPYIEVNPEDAKREGLKNGDLVEVYNDYGSTTAMAYVTNTVKPGQTFML 80
|
90 100 110
....*....|....*....|....*....|....*
gi 2083076315 670 M-HWGGvqNVNHATRPELDPFCKMPGFKTSAVRIR 703
Cdd:cd02779 81 MaHPRP--GANGLVTPYVDPETIIPYYKGTWANIR 113
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| MopB_CT_Tetrathionate_Arsenate-R |
cd02780 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate ... |
590-673 |
2.19e-07 |
|
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate reductase, subunit A, (TtrA); respiratory arsenate As(V) reductase, catalytic subunit (ArrA); and other related proteins.
Pssm-ID: 239181 [Multi-domain] Cd Length: 143 Bit Score: 50.76 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 590 YSLILTN--GRVLSHYLTGvqtrrSPSLLARELENFVEIHPITAQRYRIRDGEWVEVQSEHGYFTVRARIKDQIREDTLF 667
Cdd:cd02780 1 YPFILVTfkSNLNSHRSAN-----APWLKEIKPENPVWINPEDAAKLGIKTGDRVRVVTPGGSVVGKAKVTEGVRPGVVA 75
|
....*.
gi 2083076315 668 VPMHWG 673
Cdd:cd02780 76 IEHGYG 81
|
|
| PRK15102 |
PRK15102 |
trimethylamine-N-oxide reductase TorA; |
200-464 |
9.34e-07 |
|
trimethylamine-N-oxide reductase TorA;
Pssm-ID: 237909 [Multi-domain] Cd Length: 825 Bit Score: 52.37 E-value: 9.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 200 YFNRAKENGA----RIIVIDPRKTATAA-MADMHLPIRPGTDTVLadvMLKI---IMDEGFIDESFIQARTNGYDELSVY 271
Cdd:PRK15102 242 YLAQLKEKVAkgeiNVISIDPVVTKTQNyLGCEHLYVNPQTDVPL---MLALahtLYSENLYDKKFIDNYCLGFEQFLPY 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 272 LN------SLDLSQAADICGLELGQIREAALAFGEADTGMVLtarGVEQQTDGHLAVRHFLNLVLAT--GKIGREGCGY- 342
Cdd:PRK15102 319 LLgekdgvPKTPEWAEKICGIDAETIRELARQMAKGRTQIIA---GWCIQRQQHGEQPYWMGAVLAAmlGQIGLPGGGIs 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 343 --------GAITGQGNGQGGREHGQKADQLPGYrsiENEKDRAYVASV----WgVEAASLPGKGVSA---------YEMM 401
Cdd:PRK15102 396 yghhysgiGVPSSGGAIPGGFPGNLDTGQKPKH---DNSDYKGYSSTIpvarF-IDAILEPGKTINWngkkvtlppLKMM 471
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2083076315 402 elihqgvikslFVMGSNPIVSNPNAGLVEEALNKLDFLMVADMFMSETAQLADLVLPVTSYME 464
Cdd:PRK15102 472 -----------IFSGTNPWHRHQDRNRMKEAFRKLETVVAIDNQWTATCRFADIVLPACTQFE 523
|
|
| MopB_CT_4 |
cd02785 |
The MopB_CT_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
618-688 |
1.19e-06 |
|
The MopB_CT_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. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239186 [Multi-domain] Cd Length: 124 Bit Score: 48.13 E-value: 1.19e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2083076315 618 REL--ENFVEIHPITAQRYRIRDGEWVEVQSEHGYFTVRARIKDQIREDTLFVPMHW------GGvqNVNHATRPELDP 688
Cdd:cd02785 26 LELqpEPRVKINPIDAAARGIAHGDLVEVYNDRGSVVCKAKVDDGIQPGVVTAEQGWwsryfqEG--SLQDLTSPFVNP 102
|
|
| MopB_CT_Nitrate-R-NarG-like |
cd02776 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
624-706 |
1.01e-04 |
|
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under anaerobic conditions in the presence of nitrate, E. coli synthesizes the cytoplasmic membrane-bound quinol-nitrate oxidoreductase (NarGHI), which reduces nitrate to nitrite and forms part of a redox loop generating a proton-motive force. Found in prokaryotes and some archaea, NarGHI usually functions as a heterotrimer. The alpha chain contains the molybdenum cofactor-containing Mo-bisMGD catalytic subunit. This CD (MopB_CT_Nitrate-R-NarG-like) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239177 [Multi-domain] Cd Length: 141 Bit Score: 42.75 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 624 VEIHPITAQRYRIRDGEWVEVQSEHGYFTVRARIKDQIREDTLFvpMHWGGVQNVNHATRPELDPfcKMPGFKT-SAVRI 702
Cdd:cd02776 33 VWMNPKDAAELGIKDNDWVEVFNDNGVVVARAKVSPRIPRGTVF--MYHAQERHVNVPGSKLTGK--RGGIHNSvTRVRI 108
|
....
gi 2083076315 703 RPLH 706
Cdd:cd02776 109 KPTH 112
|
|
| MopB_CT_1 |
cd02782 |
The MopB_CT_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
609-705 |
4.64e-04 |
|
The MopB_CT_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239183 [Multi-domain] Cd Length: 129 Bit Score: 40.84 E-value: 4.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 609 TRRSPSLLARELENFVEIHPITAQRYRIRDGEWVEVQSEHGYFTVRARIKDQIREDTLFVPMHWG-------------GV 675
Cdd:cd02782 20 LHNDPRLVKGRNRCTLRIHPDDAAALGLADGDKVRVTSAAGSVEAEVEVTDDMMPGVVSLPHGWGhdypgvsgagsrpGV 99
|
90 100 110
....*....|....*....|....*....|.
gi 2083076315 676 qNVNHATRPE-LDPFCKMPGFKTSAVRIRPL 705
Cdd:cd02782 100 -NVNDLTDDTqRDPLSGNAAHNGVPVRLARV 129
|
|
| MopB_CT_2 |
cd02783 |
The MopB_CT_2 CD includes a group of related uncharacterized bacterial and archaeal ... |
621-668 |
5.58e-04 |
|
The MopB_CT_2 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. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239184 [Multi-domain] Cd Length: 156 Bit Score: 40.91 E-value: 5.58e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2083076315 621 ENFVEIHPITAQRYRIRDGEWVEVQSEHGYFTVRARIKDQIREDTLFV 668
Cdd:cd02783 31 RNYLYMHPKTAKELGIKDGDWVWVESVNGRVKGQARFTETVEPGTVWT 78
|
|
| MopB_CT_FmdC-FwdD |
cd02789 |
The MopB_FmdC-FwdD CD includes the C-terminus of subunit C of molybdenum formylmethanofuran ... |
622-702 |
4.41e-03 |
|
The MopB_FmdC-FwdD CD includes the C-terminus of subunit C of molybdenum formylmethanofuran dehydrogenase (FmdC) and subunit D of tungsten formylmethanofuran dehydrogenase (FwdD), and other related proteins. Formylmethanofuran dehydrogenase catalyzes the first step in methane formation from CO2 in methanogenic archaea and some eubacteria. Members of this CD belong to the molybdopterin_binding superfamily of proteins. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239190 [Multi-domain] Cd Length: 106 Bit Score: 37.41 E-value: 4.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083076315 622 NFVEIHPITAQRYRIRDGEWVEVQSEHGYFTVRARIKDQIREDTLFVPMH-WGgvqnvNHATRPELDPfCKMPGFKTSAV 700
Cdd:cd02789 31 AYCEINPEDYKLLGKPEGDKVKVTSEFGEVVVFAKENEGVPEGMVFIPMGpWA-----NVVVDPYTDS-TGSPIFKGVPV 104
|
..
gi 2083076315 701 RI 702
Cdd:cd02789 105 YI 106
|
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