|
Name |
Accession |
Description |
Interval |
E-value |
| NuoG |
TIGR01973 |
NADH-quinone oxidoreductase, chain G; This model represents the G subunit (one of 14: A->N) of ... |
39-632 |
0e+00 |
|
NADH-quinone oxidoreductase, chain G; This model represents the G subunit (one of 14: A->N) of the NADH-quinone oxidoreductase complex I which generally couples NADH and ubiquinone oxidation/reduction in bacteria and mammalian mitochondria while translocating protons, but may act on NADPH and/or plastoquinone in cyanobacteria and plant chloroplasts. This model excludes related subunits from formate dehydrogenase complexes. [Energy metabolism, Electron transport]
Pssm-ID: 273904 [Multi-domain] Cd Length: 602 Bit Score: 805.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 39 VFVDDQSVMVAPGTTVLQAAAQVGVEIPRFCYHERLAVAGNCRMCLVEVEKSPKPVAACAMPVMKGWRIKTNSEMTRKAR 118
Cdd:TIGR01973 1 IFIDGKELEVPKGTTVLQACLSAGIEIPRFCYHEKLSIAGNCRMCLVEVEKFPKPVASCATPVTDGMKISTNSEKVKKAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 119 EGVMEFLLMNHPLDCPICDQGGECDLQDQAMAFGSDRSRFtdidHSGKRAVEDKDIGPLVKTIMTRCIHCTRCIRFASEI 198
Cdd:TIGR01973 81 EGVMEFLLINHPLDCPICDQGGECDLQDQAVMYGSDRSRF----REKKRTVENKYLGPLIKTEMTRCIHCTRCVRFANEV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 199 AGVDDLGTTGRGNDMQIGTYVEKLFLSELSGNVIDLCPVGALTNKPYSFVARPWEIRKVESIDVLDAVGSNIIVSTRTGE 278
Cdd:TIGR01973 157 AGVEDLGVIGRGNNVEIGTYEGKTLESELSGNLIDICPVGALTSKPYAFKARPWELKSTPSICVHDSVGCNIRVDERNGE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 279 VLRILPRENEEINEEWLSDKSRFACDGLKRQ-RLIAPMLRNPNGELEAVEWESALITIAQALRSapKGKVAAVAGGLADA 357
Cdd:TIGR01973 237 IMRILPRENDEINEEWLCDKGRFGYDGLNRQdRLTKPLLRNQEGNLLEVSWAEALAIAAEKLKA--SSRIGGIAGPRSSL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 358 EALVALKDLLNRLGSETLCTEQKFPTDGSgTDFRSSYLLNSSIAACEEADLVLLVGTNPRYEAPLLNTRLRKGYVHNEQN 437
Cdd:TIGR01973 315 EELFALKKLVRKLGSENFDLRIRNYEFES-ADLRANYLFNTTLADIEEADLVLLVGADLRQEAPLLNLRLRKAVKKGGAK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 438 IALIGP-KVNLSY-----EYEHLGSDASLVRDIASGNHP-FAKKLKAAKKPLIIVGANQLARKDGAAFVTALHVFANSLQ 510
Cdd:TIGR01973 394 VALIGIeKWNLTYpantnLVFHPGLSPKKLDDIASGAHSdIAAALKAAKKPLIIVGDSAISHLDGAALISAAANIAKVIK 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 511 PADPNWKVWNVLQTNAAQTAALDVGY--TAGADAAIAAEPKVLFLLGAD-----SNAIKKDQLPKDCFIVYQGHHGDAGA 583
Cdd:TIGR01973 474 VRRKEWNGLNILSSGANSVGLLDLGGesTGLDAALNLGAADALFLLGADleralDKTARDALSKADAFIIYQGHHGTETA 553
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1949577332 584 QLAHAILPGAAYTEKQATYVNTEGRAQQTLVAVTPPGLAREDWKILRAL 632
Cdd:TIGR01973 554 EKADVILPGAAFTEKSGTYVNLEGRAQRFEQAVKPPGEAREDWRILRAL 602
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
36-664 |
0e+00 |
|
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: 592.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 36 LIEVFVDDQSVMVAPGTTVLQAAAQVGVEIPRFCYHERLAVAGNCRMCLVEVEKSPKPVAACAMPVMKGWRIKTNSEMTR 115
Cdd:COG1034 1 MVTITIDGKEVEVPKGTTVLQAAEKAGIEIPRFCYHPKLSIAGACRMCLVEVEGAPKPVASCATPVTDGMVVKTDSPKVK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 116 KAREGVMEFLLMNHPLDCPICDQGGECDLQDQAMAFGSDRSRFTDidhsGKRAVEDKDIGPLVKTIMTRCIHCTRCIRFA 195
Cdd:COG1034 81 KARKGVMEFLLINHPLDCPICDQGGECDLQDQAMEYGVDESRYEE----EKRTVPKKDLGPLILLDMNRCILCTRCVRFC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 196 SEIAGVDDLGTTGRGNDMQIGTYVEKLFLSELSGNVIDLCPVGALTNKPYSFVARPWEIRKVESIDVLDAVGSNIIVSTR 275
Cdd:COG1034 157 DEIAGDPELGVIGRGEHSEIGTYLGKPLDSEFSGNCIDVCPVGALTSKPFRFKARPWELKKTPSICPHCSVGCNIRVDVR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 276 TGEVLRILPRENEEINEEWLSDKSRFACDGLKR-QRLIAPMLRNpNGELEAVEWESALITIAQALRSapkgkvaavaggL 354
Cdd:COG1034 237 GGKVYRVLPRENEAVNEEWLCDKGRFGYDGLNSpDRLTRPLVRK-DGELVEASWEEALAAAAEGLKA------------L 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 355 ADAEalvalkdllNRLGsetlcteqkfptdgsgtdfrssyllnssiaaceeadlVLLVGTNPryeapllntrlrkgyvhn 434
Cdd:COG1034 304 KKAE---------NSVG-------------------------------------AALLGALP------------------ 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 435 eqnialigpkvnlsyeyehlgSDASLVRDIASGnhpfakklkaakkpliivganqlarkdgaafvtalhvfanslqpadp 514
Cdd:COG1034 320 ---------------------DAAAILEAAEAG----------------------------------------------- 331
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 515 nwkvwnvlqtnaaqtaaldvgytagadaaiaaEPKVLFLLGAD----SNAIKKDQLPKDCFIVYQGHHGDAGAQLAHAIL 590
Cdd:COG1034 332 --------------------------------KLKALVLLGADpydlDPAAALAALAKADFVVVLDHFGSATAERADVVL 379
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1949577332 591 PGAAYTEKQATYVNTEGRAQQTLVAVTPPGLAREDWKILRALSEIAGAPLPYDTLDELRSRLEDIAPHLVRYGR 664
Cdd:COG1034 380 PAAAFAEKSGTFVNLEGRVQRFNAAVPPPGEARPDWRVLRALANALGAGLPYDSLEEVRAELAAEAPATVSAEG 453
|
|
| MopB_Res-Cmplx1_Nad11 |
cd02773 |
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone ... |
258-636 |
0e+00 |
|
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: 589.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 258 ESIDVLDAVGSNIIVSTRTGEVLRILPRENEEINEEWLSDKSRFACDGLKRQRLIAPMLRNpNGELEAVEWESALITIAQ 337
Cdd:cd02773 1 ESIDVLDAVGSNIRVDTRGGEVMRILPRLNEDINEEWISDKTRFAYDGLKRQRLDKPYIRK-NGKLKPATWEEALAAIAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 338 ALRSAPKGKVAAVAGGLADAEALVALKDLLNRLGSETLCTEQKFPTDGsgTDFRSSYLLNSSIAACEEADLVLLVGTNPR 417
Cdd:cd02773 80 ALKGVKPDEIAAIAGDLADVESMVALKDLLNKLGSENLACEQDGPDLP--ADLRSNYLFNTTIAGIEEADAVLLVGTNPR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 418 YEAPLLNTRLRKGYVHNEQNIALIGPKVNLSYEYEHLGSDASLVRDIASGNHPFAKKLKAAKKPLIIVGANQLARKDGAA 497
Cdd:cd02773 158 FEAPVLNARIRKAWLHGGLKVGVIGPPVDLTYDYDHLGTDAKTLQDIASGKHPFSKALKDAKKPMIIVGSGALARKDGAA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 498 FVTALHVFANSLQPADPNWKVWNVLQTNAAQTAALDVGY-TAGADAAIAAEPKVLFLLGADsnAIKKDQLPKDCFIVYQG 576
Cdd:cd02773 238 ILAAVAKLAKKNGVVREGWNGFNVLHRAASRVGALDLGFvPGAGAIRKSGPPKVLYLLGAD--EIDITPIPKDAFVVYQG 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 577 HHGDAGAQLAHAILPGAAYTEKQATYVNTEGRAQQTLVAVTPPGLAREDWKILRALSEIA 636
Cdd:cd02773 316 HHGDRGAQIADVILPGAAYTEKSGTYVNTEGRVQQTRKAVSPPGDAREDWKILRALSEVL 375
|
|
| PRK07860 |
PRK07860 |
NADH dehydrogenase subunit G; Validated |
33-657 |
6.01e-104 |
|
NADH dehydrogenase subunit G; Validated
Pssm-ID: 236118 [Multi-domain] Cd Length: 797 Bit Score: 336.15 E-value: 6.01e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 33 APELIEVFVDDQSVMVAPGTTVLQAAAQVGVEIPRFCYHERLAVAGNCRMCLVEVEKSPKPVAACAMPVMKGWRIKT--N 110
Cdd:PRK07860 1 PPDLVTLTIDGVEVSVPKGTLVIRAAELLGIQIPRFCDHPLLDPVGACRQCLVEVEGQRKPQASCTTTVTDGMVVKTqlT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 111 SEMTRKAREGVMEFLLMNHPLDCPICDQGGECDLQDQAMAFGSDRSRFTDIdhsgKRAVEdKDIgPLVKTIM---TRCIH 187
Cdd:PRK07860 81 SPVADKAQHGVMELLLINHPLDCPVCDKGGECPLQNQAMSNGRAESRFTDV----KRTFP-KPI-NISTQVLldrERCVL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 188 CTRCIRFASEIAGVDDLGTTGRGNDMQIGTYVEKLFLSELSGNVIDLCPVGALTNKPYSFVARPWEIRKVESIDVLDAVG 267
Cdd:PRK07860 155 CARCTRFSDQIAGDPFIDLQERGALQQVGIYEGEPFQSYFSGNTVQICPVGALTGAAYRFRARPFDLVSTPSVCEHCASG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 268 SNIIVSTRTGEVLRILPRENEEINEEWLSDKSRFACD-GLKRQRLIAPMLRNPNGELEAVEWESALITIAQALRSApKGK 346
Cdd:PRK07860 235 CAQRTDHRRGKVLRRLAGDDPEVNEEWNCDKGRWAFTyATQPDRITTPLVRDEDGELEPASWSEALAVAARGLAAA-RGR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 347 VAAVAGGladaealvalkdllnRLGSETLCTEQKFPTDGSGT---DFRS-------SYLLNSSIA---------ACEEAD 407
Cdd:PRK07860 314 VGVLVGG---------------RLTVEDAYAYAKFARVALGTndiDFRArphsaeeADFLAARVAgrglgvtyaDLEKAP 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 408 LVLLVGTNPRYEAPLLNTRLRKGYVHNEQNIALIGPKVNLSYEYEH-------LGSDASLVRDIASGNhPFAKKLKAAKK 480
Cdd:PRK07860 379 AVLLVGFEPEEESPIVFLRLRKAARKHGLKVYSIAPFATRGLEKMGgtllrtaPGGEAAALDALATGA-PDVAELLRTPG 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 481 PLIIVG------------ANQLARKDGAAFV---------TALHVFA-NSLQP-----ADPNWK-----VWNV------- 521
Cdd:PRK07860 458 AVILVGerlatvpgalsaAARLADATGARLAwvprragerGALEAGAlPTLLPggrpvADPAARaevaaAWGVdelpaap 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 522 -------LQTNAA-QTAALDVGytagadaaiAAEPKVLfllgADSNAIkKDQLPKDCFIVYQGHHGDAGAQLAHAILPGA 593
Cdd:PRK07860 538 grdtagiLAAAAAgELGALLVG---------GVEPADL----PDPAAA-LAALDAAGFVVSLELRHSAVTERADVVLPVA 603
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1949577332 594 AYTEKQATYVNTEGRAQQTLVAVTPPGlAREDWKILRALSEIAGAPLPYDTLDELRSRLEDIAP 657
Cdd:PRK07860 604 PVAEKAGTFLNWEGRLRPFEAALRTTG-ALSDLRVLDALADEMGVDLGLPTVAAARAELARLGA 666
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
310-634 |
2.19e-102 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 318.19 E-value: 2.19e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 310 RLIAPMLRNPNGELEAVEWESALITIAQALRSAPK--GK----VAAVAGGLADAEALVALKDLLNRLGSETLCTEQKF-- 381
Cdd:pfam00384 1 RLKYPMVRRGDGKFVRVSWDEALDLIAKKLKRIIKkyGPdaiaINGGSGGLTDVESLYALKKLLNRLGSKNGNTEDHNgd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 382 ----PTDGSGTDFRSSYLLNSSIAACEEADLVLLVGTNPRYEAPLLNTRLRKGYVHNEQNIALIGPKVNLSYEYEHLG-- 455
Cdd:pfam00384 81 lctaAAAAFGSDLRSNYLFNSSIADIENADLILLIGTNPREEAPILNARIRKAALKGKAKVIVIGPRLDLTYADEHLGik 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 456 --SDASLVrdiASGNHPFAKKL----KAAKKPLIIVGANQLARKDGAAFVTALHVFA---NSLQPADPNWKVWNVLQTNA 526
Cdd:pfam00384 161 pgTDLALA---LAGAHVFIKELkkdkDFAPKPIIIVGAGVLQRQDGEAIFRAIANLAdltGNIGRPGGGWNGLNILQGAA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 527 AQTAALDVGYT------AGADAAIAAEPKVLFLLG-------ADSNAIKKDQLPKDCFIVYQGHHGDAGAQLAHAILPGA 593
Cdd:pfam00384 238 SPVGALDLGLVpgiksvEMINAIKKGGIKVLYLLGnnpfvthADENRVVKALQKLDLFVVYDGHHGDKTAKYADVILPAA 317
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1949577332 594 AYTEKQATYVNTEGRAQQTLVAVTPPGLAREDWKILRALSE 634
Cdd:pfam00384 318 AYTEKNGTYVNTEGRVQSTKQAVPPPGEAREDWKILRALSE 358
|
|
| NADH-G_4Fe-4S_3 |
smart00929 |
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region; |
118-158 |
3.91e-17 |
|
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region;
Pssm-ID: 214918 [Multi-domain] Cd Length: 41 Bit Score: 75.31 E-value: 3.91e-17
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1949577332 118 REGVMEFLLMNHPLDCPICDQGGECDLQDQAMAFGSDRSRF 158
Cdd:smart00929 1 RKTILELLLANHPLDCPVCDKNGECELQDLAYELGVDEQRY 41
|
|
| NADH_dhqG_C |
pfam09326 |
NADH-ubiquinone oxidoreductase subunit G, C-terminal; Members of this family of are found at ... |
673-716 |
2.23e-09 |
|
NADH-ubiquinone oxidoreductase subunit G, C-terminal; Members of this family of are found at the C-terminus of NADH dehydrogenases subunit G or NADH-ubiquinone oxidoreductase subunit G. EC:1.6.99.5.
Pssm-ID: 462757 Cd Length: 41 Bit Score: 53.38 E-value: 2.23e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1949577332 673 QAEEMLRNAAVHFDGAKVEVPqksLQDFFMTDPITRASPTMAKC 716
Cdd:pfam09326 1 ALVLALAGAKGKLSGAPLKSP---IEDFYMTDPISRASATMAKC 41
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| NuoG |
TIGR01973 |
NADH-quinone oxidoreductase, chain G; This model represents the G subunit (one of 14: A->N) of ... |
39-632 |
0e+00 |
|
NADH-quinone oxidoreductase, chain G; This model represents the G subunit (one of 14: A->N) of the NADH-quinone oxidoreductase complex I which generally couples NADH and ubiquinone oxidation/reduction in bacteria and mammalian mitochondria while translocating protons, but may act on NADPH and/or plastoquinone in cyanobacteria and plant chloroplasts. This model excludes related subunits from formate dehydrogenase complexes. [Energy metabolism, Electron transport]
Pssm-ID: 273904 [Multi-domain] Cd Length: 602 Bit Score: 805.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 39 VFVDDQSVMVAPGTTVLQAAAQVGVEIPRFCYHERLAVAGNCRMCLVEVEKSPKPVAACAMPVMKGWRIKTNSEMTRKAR 118
Cdd:TIGR01973 1 IFIDGKELEVPKGTTVLQACLSAGIEIPRFCYHEKLSIAGNCRMCLVEVEKFPKPVASCATPVTDGMKISTNSEKVKKAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 119 EGVMEFLLMNHPLDCPICDQGGECDLQDQAMAFGSDRSRFtdidHSGKRAVEDKDIGPLVKTIMTRCIHCTRCIRFASEI 198
Cdd:TIGR01973 81 EGVMEFLLINHPLDCPICDQGGECDLQDQAVMYGSDRSRF----REKKRTVENKYLGPLIKTEMTRCIHCTRCVRFANEV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 199 AGVDDLGTTGRGNDMQIGTYVEKLFLSELSGNVIDLCPVGALTNKPYSFVARPWEIRKVESIDVLDAVGSNIIVSTRTGE 278
Cdd:TIGR01973 157 AGVEDLGVIGRGNNVEIGTYEGKTLESELSGNLIDICPVGALTSKPYAFKARPWELKSTPSICVHDSVGCNIRVDERNGE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 279 VLRILPRENEEINEEWLSDKSRFACDGLKRQ-RLIAPMLRNPNGELEAVEWESALITIAQALRSapKGKVAAVAGGLADA 357
Cdd:TIGR01973 237 IMRILPRENDEINEEWLCDKGRFGYDGLNRQdRLTKPLLRNQEGNLLEVSWAEALAIAAEKLKA--SSRIGGIAGPRSSL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 358 EALVALKDLLNRLGSETLCTEQKFPTDGSgTDFRSSYLLNSSIAACEEADLVLLVGTNPRYEAPLLNTRLRKGYVHNEQN 437
Cdd:TIGR01973 315 EELFALKKLVRKLGSENFDLRIRNYEFES-ADLRANYLFNTTLADIEEADLVLLVGADLRQEAPLLNLRLRKAVKKGGAK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 438 IALIGP-KVNLSY-----EYEHLGSDASLVRDIASGNHP-FAKKLKAAKKPLIIVGANQLARKDGAAFVTALHVFANSLQ 510
Cdd:TIGR01973 394 VALIGIeKWNLTYpantnLVFHPGLSPKKLDDIASGAHSdIAAALKAAKKPLIIVGDSAISHLDGAALISAAANIAKVIK 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 511 PADPNWKVWNVLQTNAAQTAALDVGY--TAGADAAIAAEPKVLFLLGAD-----SNAIKKDQLPKDCFIVYQGHHGDAGA 583
Cdd:TIGR01973 474 VRRKEWNGLNILSSGANSVGLLDLGGesTGLDAALNLGAADALFLLGADleralDKTARDALSKADAFIIYQGHHGTETA 553
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1949577332 584 QLAHAILPGAAYTEKQATYVNTEGRAQQTLVAVTPPGLAREDWKILRAL 632
Cdd:TIGR01973 554 EKADVILPGAAFTEKSGTYVNLEGRAQRFEQAVKPPGEAREDWRILRAL 602
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
36-664 |
0e+00 |
|
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: 592.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 36 LIEVFVDDQSVMVAPGTTVLQAAAQVGVEIPRFCYHERLAVAGNCRMCLVEVEKSPKPVAACAMPVMKGWRIKTNSEMTR 115
Cdd:COG1034 1 MVTITIDGKEVEVPKGTTVLQAAEKAGIEIPRFCYHPKLSIAGACRMCLVEVEGAPKPVASCATPVTDGMVVKTDSPKVK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 116 KAREGVMEFLLMNHPLDCPICDQGGECDLQDQAMAFGSDRSRFTDidhsGKRAVEDKDIGPLVKTIMTRCIHCTRCIRFA 195
Cdd:COG1034 81 KARKGVMEFLLINHPLDCPICDQGGECDLQDQAMEYGVDESRYEE----EKRTVPKKDLGPLILLDMNRCILCTRCVRFC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 196 SEIAGVDDLGTTGRGNDMQIGTYVEKLFLSELSGNVIDLCPVGALTNKPYSFVARPWEIRKVESIDVLDAVGSNIIVSTR 275
Cdd:COG1034 157 DEIAGDPELGVIGRGEHSEIGTYLGKPLDSEFSGNCIDVCPVGALTSKPFRFKARPWELKKTPSICPHCSVGCNIRVDVR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 276 TGEVLRILPRENEEINEEWLSDKSRFACDGLKR-QRLIAPMLRNpNGELEAVEWESALITIAQALRSapkgkvaavaggL 354
Cdd:COG1034 237 GGKVYRVLPRENEAVNEEWLCDKGRFGYDGLNSpDRLTRPLVRK-DGELVEASWEEALAAAAEGLKA------------L 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 355 ADAEalvalkdllNRLGsetlcteqkfptdgsgtdfrssyllnssiaaceeadlVLLVGTNPryeapllntrlrkgyvhn 434
Cdd:COG1034 304 KKAE---------NSVG-------------------------------------AALLGALP------------------ 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 435 eqnialigpkvnlsyeyehlgSDASLVRDIASGnhpfakklkaakkpliivganqlarkdgaafvtalhvfanslqpadp 514
Cdd:COG1034 320 ---------------------DAAAILEAAEAG----------------------------------------------- 331
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 515 nwkvwnvlqtnaaqtaaldvgytagadaaiaaEPKVLFLLGAD----SNAIKKDQLPKDCFIVYQGHHGDAGAQLAHAIL 590
Cdd:COG1034 332 --------------------------------KLKALVLLGADpydlDPAAALAALAKADFVVVLDHFGSATAERADVVL 379
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1949577332 591 PGAAYTEKQATYVNTEGRAQQTLVAVTPPGLAREDWKILRALSEIAGAPLPYDTLDELRSRLEDIAPHLVRYGR 664
Cdd:COG1034 380 PAAAFAEKSGTFVNLEGRVQRFNAAVPPPGEARPDWRVLRALANALGAGLPYDSLEEVRAELAAEAPATVSAEG 453
|
|
| MopB_Res-Cmplx1_Nad11 |
cd02773 |
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone ... |
258-636 |
0e+00 |
|
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: 589.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 258 ESIDVLDAVGSNIIVSTRTGEVLRILPRENEEINEEWLSDKSRFACDGLKRQRLIAPMLRNpNGELEAVEWESALITIAQ 337
Cdd:cd02773 1 ESIDVLDAVGSNIRVDTRGGEVMRILPRLNEDINEEWISDKTRFAYDGLKRQRLDKPYIRK-NGKLKPATWEEALAAIAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 338 ALRSAPKGKVAAVAGGLADAEALVALKDLLNRLGSETLCTEQKFPTDGsgTDFRSSYLLNSSIAACEEADLVLLVGTNPR 417
Cdd:cd02773 80 ALKGVKPDEIAAIAGDLADVESMVALKDLLNKLGSENLACEQDGPDLP--ADLRSNYLFNTTIAGIEEADAVLLVGTNPR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 418 YEAPLLNTRLRKGYVHNEQNIALIGPKVNLSYEYEHLGSDASLVRDIASGNHPFAKKLKAAKKPLIIVGANQLARKDGAA 497
Cdd:cd02773 158 FEAPVLNARIRKAWLHGGLKVGVIGPPVDLTYDYDHLGTDAKTLQDIASGKHPFSKALKDAKKPMIIVGSGALARKDGAA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 498 FVTALHVFANSLQPADPNWKVWNVLQTNAAQTAALDVGY-TAGADAAIAAEPKVLFLLGADsnAIKKDQLPKDCFIVYQG 576
Cdd:cd02773 238 ILAAVAKLAKKNGVVREGWNGFNVLHRAASRVGALDLGFvPGAGAIRKSGPPKVLYLLGAD--EIDITPIPKDAFVVYQG 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 577 HHGDAGAQLAHAILPGAAYTEKQATYVNTEGRAQQTLVAVTPPGLAREDWKILRALSEIA 636
Cdd:cd02773 316 HHGDRGAQIADVILPGAAYTEKSGTYVNTEGRVQQTRKAVSPPGDAREDWKILRALSEVL 375
|
|
| MopB_NADH-Q-OR-NuoG2 |
cd02768 |
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone ... |
258-635 |
4.07e-138 |
|
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: 411.29 E-value: 4.07e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 258 ESIDVLDAVGSNIIVSTRTGEVLRILPRENEEINEEWLSDKSRFACDGLK-RQRLIAPMLRNpNGELEAVEWESALITIA 336
Cdd:cd02768 1 ESIDVHDALGSNIRVDVRGGEVMRILPRENEAINEEWISDKGRFGYDGLNsRQRLTQPLIKK-GGKLVPVSWEEALKTVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 337 QALRSAPKGKVAAVAGGLADAEALVALKDLLNRLGSETLCTEQKFPTDGSGTDFRSSYLLNSSIAACEEADLVLLVGTNP 416
Cdd:cd02768 80 EGLKAVKGDKIGGIAGPRADLESLFLLKKLLNKLGSNNIDHRLRQSDLPADNRLRGNYLFNTSIAEIEEADAVLLIGSNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 417 RYEAPLLNTRLRKGYVHNEQNIALIGPK-----VNLSYEYEHLGSDASLVRDIASGNH--PFAKKLKAAKKPLIIVGANq 489
Cdd:cd02768 160 RKEAPLLNARLRKAVKKKGAKIAVIGPKdtdliADLTYPVSPLGASLATLLDIAEGKHlkPFAKSLKKAKKPLIILGSS- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 490 LARKDGAAFVTALHVFANSLQPADPNWKVWNVLQTNAAQTAA--LDVGYTAGADAAIAaepkvLFLLGAD----SNAIKK 563
Cdd:cd02768 239 ALRKDGAAILKALANLAAKLGTGAGLWNGLNVLNSVGARLGGagLDAGLALLEPGKAK-----LLLLGEDeldrSNPPAA 313
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1949577332 564 DQL-PKDCFIVYQGHHGDAGAQlAHAILPGAAYTEKQATYVNTEGRAQQTLVAVTPPGLAREDWKILRALSEI 635
Cdd:cd02768 314 VALaAADAFVVYQGHHGDTGAQ-ADVILPAAAFTEKSGTYVNTEGRVQRFKKAVSPPGDAREDWKILRALSNL 385
|
|
| PRK07860 |
PRK07860 |
NADH dehydrogenase subunit G; Validated |
33-657 |
6.01e-104 |
|
NADH dehydrogenase subunit G; Validated
Pssm-ID: 236118 [Multi-domain] Cd Length: 797 Bit Score: 336.15 E-value: 6.01e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 33 APELIEVFVDDQSVMVAPGTTVLQAAAQVGVEIPRFCYHERLAVAGNCRMCLVEVEKSPKPVAACAMPVMKGWRIKT--N 110
Cdd:PRK07860 1 PPDLVTLTIDGVEVSVPKGTLVIRAAELLGIQIPRFCDHPLLDPVGACRQCLVEVEGQRKPQASCTTTVTDGMVVKTqlT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 111 SEMTRKAREGVMEFLLMNHPLDCPICDQGGECDLQDQAMAFGSDRSRFTDIdhsgKRAVEdKDIgPLVKTIM---TRCIH 187
Cdd:PRK07860 81 SPVADKAQHGVMELLLINHPLDCPVCDKGGECPLQNQAMSNGRAESRFTDV----KRTFP-KPI-NISTQVLldrERCVL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 188 CTRCIRFASEIAGVDDLGTTGRGNDMQIGTYVEKLFLSELSGNVIDLCPVGALTNKPYSFVARPWEIRKVESIDVLDAVG 267
Cdd:PRK07860 155 CARCTRFSDQIAGDPFIDLQERGALQQVGIYEGEPFQSYFSGNTVQICPVGALTGAAYRFRARPFDLVSTPSVCEHCASG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 268 SNIIVSTRTGEVLRILPRENEEINEEWLSDKSRFACD-GLKRQRLIAPMLRNPNGELEAVEWESALITIAQALRSApKGK 346
Cdd:PRK07860 235 CAQRTDHRRGKVLRRLAGDDPEVNEEWNCDKGRWAFTyATQPDRITTPLVRDEDGELEPASWSEALAVAARGLAAA-RGR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 347 VAAVAGGladaealvalkdllnRLGSETLCTEQKFPTDGSGT---DFRS-------SYLLNSSIA---------ACEEAD 407
Cdd:PRK07860 314 VGVLVGG---------------RLTVEDAYAYAKFARVALGTndiDFRArphsaeeADFLAARVAgrglgvtyaDLEKAP 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 408 LVLLVGTNPRYEAPLLNTRLRKGYVHNEQNIALIGPKVNLSYEYEH-------LGSDASLVRDIASGNhPFAKKLKAAKK 480
Cdd:PRK07860 379 AVLLVGFEPEEESPIVFLRLRKAARKHGLKVYSIAPFATRGLEKMGgtllrtaPGGEAAALDALATGA-PDVAELLRTPG 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 481 PLIIVG------------ANQLARKDGAAFV---------TALHVFA-NSLQP-----ADPNWK-----VWNV------- 521
Cdd:PRK07860 458 AVILVGerlatvpgalsaAARLADATGARLAwvprragerGALEAGAlPTLLPggrpvADPAARaevaaAWGVdelpaap 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 522 -------LQTNAA-QTAALDVGytagadaaiAAEPKVLfllgADSNAIkKDQLPKDCFIVYQGHHGDAGAQLAHAILPGA 593
Cdd:PRK07860 538 grdtagiLAAAAAgELGALLVG---------GVEPADL----PDPAAA-LAALDAAGFVVSLELRHSAVTERADVVLPVA 603
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1949577332 594 AYTEKQATYVNTEGRAQQTLVAVTPPGlAREDWKILRALSEIAGAPLPYDTLDELRSRLEDIAP 657
Cdd:PRK07860 604 PVAEKAGTFLNWEGRLRPFEAALRTTG-ALSDLRVLDALADEMGVDLGLPTVAAARAELARLGA 666
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
310-634 |
2.19e-102 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 318.19 E-value: 2.19e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 310 RLIAPMLRNPNGELEAVEWESALITIAQALRSAPK--GK----VAAVAGGLADAEALVALKDLLNRLGSETLCTEQKF-- 381
Cdd:pfam00384 1 RLKYPMVRRGDGKFVRVSWDEALDLIAKKLKRIIKkyGPdaiaINGGSGGLTDVESLYALKKLLNRLGSKNGNTEDHNgd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 382 ----PTDGSGTDFRSSYLLNSSIAACEEADLVLLVGTNPRYEAPLLNTRLRKGYVHNEQNIALIGPKVNLSYEYEHLG-- 455
Cdd:pfam00384 81 lctaAAAAFGSDLRSNYLFNSSIADIENADLILLIGTNPREEAPILNARIRKAALKGKAKVIVIGPRLDLTYADEHLGik 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 456 --SDASLVrdiASGNHPFAKKL----KAAKKPLIIVGANQLARKDGAAFVTALHVFA---NSLQPADPNWKVWNVLQTNA 526
Cdd:pfam00384 161 pgTDLALA---LAGAHVFIKELkkdkDFAPKPIIIVGAGVLQRQDGEAIFRAIANLAdltGNIGRPGGGWNGLNILQGAA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 527 AQTAALDVGYT------AGADAAIAAEPKVLFLLG-------ADSNAIKKDQLPKDCFIVYQGHHGDAGAQLAHAILPGA 593
Cdd:pfam00384 238 SPVGALDLGLVpgiksvEMINAIKKGGIKVLYLLGnnpfvthADENRVVKALQKLDLFVVYDGHHGDKTAKYADVILPAA 317
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1949577332 594 AYTEKQATYVNTEGRAQQTLVAVTPPGLAREDWKILRALSE 634
Cdd:pfam00384 318 AYTEKNGTYVNTEGRVQSTKQAVPPPGEAREDWKILRALSE 358
|
|
| MopB_Res-Cmplx1_Nad11-M |
cd02774 |
MopB_Res_Cmplx1_Nad11_M: Mitochondrial-encoded NADH-quinone oxidoreductase/respiratory complex ... |
258-632 |
1.68e-71 |
|
MopB_Res_Cmplx1_Nad11_M: Mitochondrial-encoded NADH-quinone oxidoreductase/respiratory complex I, the second domain of the Nad11/75-kDa subunit of some protists. NADH-quinone oxidoreductase 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. The nad11 gene codes for the largest (75-kDa) subunit of the mitochondrial NADH-quinone oxidoreductase, it constitutes the electron input part of the enzyme, or the so-called NADH dehydrogenase fragment. The Nad11 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: 239175 [Multi-domain] Cd Length: 366 Bit Score: 237.26 E-value: 1.68e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 258 ESIDVLDAVGSNIIVSTRTGEVLRILPRENEEINEEWLSDKSRFACDGLKRQRLIAPMLRNPNGELEAVEWESALITIAQ 337
Cdd:cd02774 1 ESIDVLDSLGSNIRVDIKGNEILRILPKINDELNEEWISDKIRFSYDSLKYQRIKTPLLKLSNNSFLEIGWKTAFKFLNK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 338 ALRSAPKGKVAAVAGGLADAEALVALKDLLNRLGSETLCTEQKFPTDGSGTDFRSSYLLNSSIAACEEADLVLLVGTNPR 417
Cdd:cd02774 81 FILLKKFSKLNFIIGSKIDLETLFYYKKLLNKLGSLNTNSNNFLENNNYFNLDLENYLFNNSLKNLDKSDLCLLIGSNLR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 418 YEAPLLNTRLRKGYVHNEQNIALIGPKVNLSYEYEHLGSDASLVRDIASGNHPFAKKLKAAKKPLIIVGANQLARKDGAA 497
Cdd:cd02774 161 VESPILNIRLRNRYNKGNKKIFVIGNKFDTTYPSKHIGLSLNTLLKILEGKHLFCKQLKKSKKPLIIIGSSFSLRKNYSF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 498 FVTALHVFANSlqpadpNWKVWNVLQTNAAQTAALdvgytAGADAAIAAEPKVLFLLGADSNAIKKDQlpKDCFIVYQGH 577
Cdd:cd02774 241 IISKLKNFSSN------NENNFNFLNIISNSLYYL-----GIKKFNSNNKKNLSNLYYIKETNFQKFN--KNNFVIYQGH 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1949577332 578 HGDAGAQLAHAILPGAAYTEKQATYVNTEGRAQQTLVAVTPPGLAREDWKILRAL 632
Cdd:cd02774 308 HFLNLANNSNLILPSKTFFEKEALYLNLEGILQKTKKILSFKENIKSDDNIIFSL 362
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
258-634 |
3.37e-57 |
|
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: 199.09 E-value: 3.37e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 258 ESIDVLDAVGSNIIVSTRTGEVLRILPRENEEINEEWLSDKSRFACDGLK-RQRLIAPMLR-NPNGELEAVEWESALITI 335
Cdd:cd00368 1 PSVCPFCGVGCGILVYVKDGKVVRIEGDPNHPVNEGRLCDKGRAGLDGLYsPDRLKYPLIRvGGRGKFVPISWDEALDEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 336 AQALRSAPK----GKVAAVAGGLADAEALVALKDLLNRLGSETLCTEQKFPT--DGSGTDFRSSYLLNSSIAACEEADLV 409
Cdd:cd00368 81 AEKLKEIREkygpDAIAFYGGGGASNEEAYLLQKLLRALGSNNVDSHARLCHasAVAALKAFGGGAPTNTLADIENADLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 410 LLVGTNPRYEAPLLNTRLRKGyVHNEQNIALIGPKVNLSYEY--EHL----GSDASLvrdiASGNhpfakklkaakKPLI 483
Cdd:cd00368 161 LLWGSNPAETHPVLAARLRRA-KKRGAKLIVIDPRRTETAAKadEWLpirpGTDAAL----ALAE-----------WAAE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 484 IVGAnqlarkdGAAFVTAL-HVFANSlQPADPNWkvWNVLQTNAAQTAALDVGYTAGADAAIAAEPKVLFLLGA------ 556
Cdd:cd00368 225 ITGV-------PAETIRALaREFAAA-KRAVILW--GMGLTQHTNGTQNVRAIANLAALTGNIGRPGGGLGPGGnplvsa 294
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1949577332 557 -DSNAIKKDQLPKDCFIVYQGHHGDAgAQLAHAILPGAAYTEKQATYVNTEGRAQQTLVAVTPPGLAREDWKILRALSE 634
Cdd:cd00368 295 pDANRVRAALKKLDFVVVIDIFMTET-AAYADVVLPAATYLEKEGTYTNTEGRVQLFRQAVEPPGEARSDWEILRELAK 372
|
|
| PTZ00305 |
PTZ00305 |
NADH:ubiquinone oxidoreductase; Provisional |
4-240 |
2.40e-56 |
|
NADH:ubiquinone oxidoreductase; Provisional
Pssm-ID: 140326 [Multi-domain] Cd Length: 297 Bit Score: 194.49 E-value: 2.40e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 4 TPLTRALTLGARGcpSQVVRTAASNTPAKA----------PELIeVFVDDQSVMVAPGT-TVLQAAAQVGVEIPRFCYHE 72
Cdd:PTZ00305 29 TPYNSDMTDILHG--SEYNHRGGVEAAAEGvaagqyaehkPRAI-MFVNKRPVEIIPQEeNLLEVLEREGIRVPKFCYHP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 73 RLAVAGNCRMCLVEVEKSPKPVAACAMPVMKGWRIKTNSEMTRKAREGVMEFLLMNHPLDCPICDQGGECDLQDQAMAFG 152
Cdd:PTZ00305 106 ILSVAGNCRMCLVQVDGTQNLVVSCATVALPGMSIITDSRLVRDAREGNVELILINHPNDCPICEQATNCDLQNVSMNYG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 153 SDRSRFTDidhsGKRAVEDKDIGPLVKTIMTRCIHCTRCIRFASEIAGVDDLGTTGRGNDMQIGTYVEKLFL-SELSGNV 231
Cdd:PTZ00305 186 TDIPRYKE----DKRAVQDFYFDPQTRVVLNRCIHCTRCVRFLNEHAQDFNLGMIGRGGLSEISTFLDELEVkTDNNMPV 261
|
....*....
gi 1949577332 232 IDLCPVGAL 240
Cdd:PTZ00305 262 SQLCPVGKL 270
|
|
| MopB_NDH-1_NuoG2 |
cd02772 |
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase ... |
259-632 |
6.78e-43 |
|
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: 160.60 E-value: 6.78e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 259 SIDVLDAVGSNIIVSTRTGEVLRILPRENEEINEEWLSDKSRFACDGLKRQ-RLIAPMLRNpNGELEAVEWESALITIAQ 337
Cdd:cd02772 2 SVSPHDALGSNLVVHVKNNKVMRVVPRENEAINECWLSDRDRFSYEGLNSEdRLTKPMIKK-DGQWQEVDWETALEYVAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 338 ALRSAPKGKVAAVAGGLADA----EALVALKDLLNRLGSETLCT---EQKFPTDGSgtdFRSSYLLNSSIAACEEADLVL 410
Cdd:cd02772 81 GLSAIIKKHGADQIGALASPhstlEELYLLQKLARGLGSDNIDHrlrQSDFRDDAK---ASGAPWLGMPIAEISELDRVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 411 LVGTNPRYEAPLLNTRLRKGYVHNEQNIALIGPKVNLSYEYEH---------LGSDASLVRDIAS--GNHPFAKKLKAAK 479
Cdd:cd02772 158 VIGSNLRKEHPLLAQRLRQAVKKGAKLSAINPADDDFLFPLSGkaivapsalANALAQVAKALAEekGLAVPDEDAKVEA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 480 KPLIIVGANQLARKDGAAFVT---ALH------VFANSLQPADPNWKVWNVLQTNAAQTAALDVG---YTAGADAAIAAE 547
Cdd:cd02772 238 SEEARKIAASLVSAERAAVFLgnlAQNhpqaatLRALAQEIAKLTGATLGVLGEGANSVGAYLAGalpHGGLNAAAMLEQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 548 P-KVLFLLGA------DSNAIKKDQLPKDCFIVYQGHHGDAgAQLAHA--ILPGAAYTEKQATYVNTEGRAQQTLVAVTP 618
Cdd:cd02772 318 PrKAYLLLNVepeldcANPAQALAALNQAEFVVALSAFASA-ALLDYAdvLLPIAPFTETSGTFVNLEGRVQSFKGVVKP 396
|
410
....*....|....
gi 1949577332 619 PGLAREDWKILRAL 632
Cdd:cd02772 397 LGEARPAWKVLRVL 410
|
|
| PRK07569 |
PRK07569 |
bidirectional hydrogenase complex protein HoxU; Validated |
41-243 |
1.44e-38 |
|
bidirectional hydrogenase complex protein HoxU; Validated
Pssm-ID: 181037 [Multi-domain] Cd Length: 234 Bit Score: 142.87 E-value: 1.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 41 VDDQSVMVAPGTTVLQAAAQVGVEIPRFCYHERLAVAGNCRMCLVEVEKSPKPVAACAMPVMKGWRIKTNSEMTRKAREG 120
Cdd:PRK07569 8 IDDQLVSAREGETLLEAAREAGIPIPTLCHLDGLSDVGACRLCLVEIEGSNKLLPACVTPVAEGMVVQTNTPRLQEYRRM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 121 VMEFLLM--NHPldCPICDQGGECDLQDQAMAFGSDRSRFT------DIDHSGKRAVEDKDigplvktimtRCIHCTRCI 192
Cdd:PRK07569 88 IVELLFAegNHV--CAVCVANGNCELQDLAIEVGMDHVRFPylfprrPVDISHPRFGIDHN----------RCVLCTRCV 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1949577332 193 RFASEIAGVDDLGTTGRGNDMQIGTYVEKLFLSELS----GNVIDLCPVGALTNK 243
Cdd:PRK07569 156 RVCDEIEGAHTWDVAGRGAKSRVITDLNQPWGTSETctscGKCVQACPTGAIFRK 210
|
|
| PRK08493 |
PRK08493 |
NADH-quinone oxidoreductase subunit G; |
36-434 |
3.02e-31 |
|
NADH-quinone oxidoreductase subunit G;
Pssm-ID: 236277 [Multi-domain] Cd Length: 819 Bit Score: 130.98 E-value: 3.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 36 LIEVFVDDQSVMVAPGTTVLQAAAQVGVEIPRFCYHERLAVAGNCRMCLVEVekSPKPVAACAMPVMKGWRIKTNSEMTR 115
Cdd:PRK08493 1 MITITINGKECEAQEGEYILNVARRNGIFIPAICYLSGCSPTLACRLCMVEA--DGKRVYSCNTKAKEGMNILTNTPNLM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 116 KAREGVMEFLLMNHPLDCPICDQGGECDLQDQAMAFGSD------RSRFTDIDHSGKrAVEDKDIgplvktimtrCIHCT 189
Cdd:PRK08493 79 DERNAIMQTYDVNHPLECGVCDKSGECELQNFTHEMGVNhqpyaiKDTHKPHKHWGK-INYDPSL----------CIVCE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 190 RCIRFASEIAGVDDLGTTGRGNDMQIGTYVEKLFLSELS-----------------------GNVIDLCPVGALTNKPYS 246
Cdd:PRK08493 148 RCVTVCKDKIGESALKTVPRGLDAPDKSFKESMPKDAYAvwskkqksligpvggetldcsfcGECIAVCPVGALSSSDFQ 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 247 FVARPWEIRKVESIDVLDAVGSNIIVSTR----TGEVLRILpRENEEINEEWLSDKSRFACDglkrqrliapmLRNpnge 322
Cdd:PRK08493 228 YTSNAWELKKIPATCPHCSDCCLIYYDVKhssiLNQESKIY-RVSNDFYFNPLCGAGRFAFD-----------FQN---- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 323 lEAVEWESALITIAQALRSApkgKVAAVAGGLADAEALV--ALKDLLN-RLGSETLCTEQKFpTDGSGTDFRSSYllNSS 399
Cdd:PRK08493 292 -EADKDEKAFKEAVEAFKEA---KAIKFNSFITNEEALIlqRLKKKFGlKLINEEALKFQQF-LKVFSEVSGKSY--SAN 364
|
410 420 430
....*....|....*....|....*....|....*
gi 1949577332 400 IAACEEADLVLLVGTNPRYEAPLLNTRLRKGYVHN 434
Cdd:PRK08493 365 LEDIKTSDFVVVAGSALKTDNPLLRYAINNALKMN 399
|
|
| 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 ... |
265-633 |
2.98e-28 |
|
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: 119.03 E-value: 2.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 265 AVGSNIIVSTRTGEVLRILPRENEEINEEWLSDKSRFACDGLK-RQRLIAPMLRNpNGELEAVEWESALITIAQALRSAp 343
Cdd:cd02771 8 SVGCNISLGERYGELRRVENRYNGAVNHYFLCDRGRFGYGYVNsRDRLTQPLIRR-GGTLVPVSWNEALDVAAARLKEA- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 344 KGKVAAVAGGLADAEALVALKdllnRLGSETLCTEQK-FPTDGSGTDF-RSSYLLNSSIAACEEADLVLLVGTNPRYEAP 421
Cdd:cd02771 86 KDKVGGIGSPRASNESNYALQ----KLVGAVLGTNNVdHRARRLIAEIlRNGPIYIPSLRDIESADAVLVLGEDLTQTAP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 422 LLNTRLRK------------------------GYVHNEQN-IALIGP-KVNLSyeyEHLGSD---------------ASL 460
Cdd:cd02771 162 RIALALRQaarrkavelaalsgipkwqdaavrNIAQGAKSpLFIVNAlATRLD---DIAAESiraspggqarlgaalARA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 461 VRDIASGNHPFAKKLKAAKK---------PLIIVG---------------ANQLARKDGAAFVTALHVFANSLQ------ 510
Cdd:cd02771 239 VDASAAGVSGLAPKEKAARIaarltgakkPLIVSGtlsgslelikaaanlAKALKRRGENAGLTLAVEEGNSPGllllgg 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 511 -PADPNWKVWNVLQTNAAQTAaldvgytagadaaiaaepKVLFLLGAD-----SNAIKKDQLPKDCFIVYQGHHGDAGAQ 584
Cdd:cd02771 319 hVTEPGLDLDGALAALEDGSA------------------DALIVLGNDlyrsaPERRVEAALDAAEFVVVLDHFLTETAE 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1949577332 585 LAHAILPGAAYTEKQATYVNTEGRAQQTLVAV-TPPGLAREDWKILRALS 633
Cdd:cd02771 381 RADVVLPAASFAEKSGTFVNYEGRAQRFFKAYdDPAGDARSDWRWLHALA 430
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
265-656 |
7.62e-21 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 97.65 E-value: 7.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 265 AVGSNIIVSTRTGEVLRILPRENEEINEEWLSDKSRFACDGL-KRQRLIAPMLRnPNGELEAVEWESALITIAQALRsap 343
Cdd:COG3383 15 GVGCGIDLEVKDGKIVKVEGDPDHPVNRGRLCVKGRFGFEFVnSPDRLTTPLIR-RGGEFREVSWDEALDLVAERLR--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 344 kgkvAAVAGGLADAealVALkdllnrLGSETLCTE-----QKFPTDGSGT---DFRSSYLLNSSIAA------------- 402
Cdd:COG3383 91 ----EIQAEHGPDA---VAF------YGSGQLTNEenyllQKLARGVLGTnniDNNARLCMASAVAGlkqsfgsdappns 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 403 ---CEEADLVLLVGTNPRYEAPLLNTRLRKGyVHNEQNIALIGPKVNLSYEY--EHL----GSDASL------------- 460
Cdd:COG3383 158 yddIEEADVILVIGSNPAEAHPVLARRIKKA-KKNGAKLIVVDPRRTETARLadLHLqikpGTDLALlngllhviieegl 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 461 ---------------VRDIASGNHPFAKKLKAAKKP-LIIVGANQLARKDGAAFVTAL----------HVFA-------- 506
Cdd:COG3383 237 vdedfiaertegfeeLKASVAKYTPERVAEITGVPAeDIREAARLIAEAKRAMILWGMgvnqhtqgtdNVNAiinlalat 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 507 ----------NSL--QP---------ADPNW-----------------KVWNVLQTNAaqtaalDVGYTAGA--DAAIAA 546
Cdd:COG3383 317 gnigrpgtgpFPLtgQNnvqggrdmgALPNVlpgyrdvtdpehrakvaDAWGVPPLPD------KPGLTAVEmfDAIADG 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 547 EPKVLFLLG-------ADSNAIKKdQLPKDCFIVYQGHHGDAGAQLAHAILPGAAYTEKQATYVNTEGRAQQTLVAVTPP 619
Cdd:COG3383 391 EIKALWIIGenpavsdPDANHVRE-ALEKLEFLVVQDIFLTETAEYADVVLPAASWAEKDGTFTNTERRVQRVRKAVEPP 469
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1949577332 620 GLAREDWKILRALSEIAGAPLPYDT----LDELRSRLEDIA 656
Cdd:COG3383 470 GEARPDWEIIAELARRLGYGFDYDSpeevFDEIARLTPDYS 510
|
|
| NADH-G_4Fe-4S_3 |
smart00929 |
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region; |
118-158 |
3.91e-17 |
|
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region;
Pssm-ID: 214918 [Multi-domain] Cd Length: 41 Bit Score: 75.31 E-value: 3.91e-17
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1949577332 118 REGVMEFLLMNHPLDCPICDQGGECDLQDQAMAFGSDRSRF 158
Cdd:smart00929 1 RKTILELLLANHPLDCPVCDKNGECELQDLAYELGVDEQRY 41
|
|
| NADH-G_4Fe-4S_3 |
pfam10588 |
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region; |
118-157 |
4.41e-17 |
|
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region;
Pssm-ID: 463159 [Multi-domain] Cd Length: 40 Bit Score: 75.18 E-value: 4.41e-17
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1949577332 118 REGVMEFLLMNHPLDCPICDQGGECDLQDQAMAFGSDRSR 157
Cdd:pfam10588 1 RKTILELLLSNHPLDCPTCDKNGNCELQDLAYELGVDEVR 40
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
265-650 |
4.39e-16 |
|
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: 81.88 E-value: 4.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 265 AVGSNIIVSTRTGEVLRILPRENEEINEEWLSDKSRFACDGLK-RQRLIAPMLRNpNGELEAVEWESALITIAQALRSAp 343
Cdd:cd02753 8 GVGCGLELWVKDNKIVGVEPVKGHPVNRGKLCVKGRFGFDFVNsKDRLTKPLIRK-NGKFVEASWDEALSLVASRLKEI- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 344 KGKVAAVA-GGLADA-----EALVALKdlLNRLGSET--------LC----TEQKFPTDGSGTDfrssyllNSSIAACEE 405
Cdd:cd02753 86 KDKYGPDAiAFFGSAkctneENYLFQK--LARAVGGTnnvdhcarLChsptVAGLAETLGSGAM-------TNSIADIEE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 406 ADLVLLVGTNPRYEAPLLNTRLRKGyVHNEQNIALIGP-KVNLS-YEYEHL----GSDASLV------------------ 461
Cdd:cd02753 157 ADVILVIGSNTTEAHPVIARRIKRA-KRNGAKLIVADPrRTELArFADLHLqlrpGTDVALLnamahviieeglydeefi 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 462 ----------RDIASGNHPFAKKLKAAKKP-LIIVGANQLARKDGAAFVTAL----HVFA--NSLQPAD----------P 514
Cdd:cd02753 236 eertegfeelKEIVEKYTPEYAERITGVPAeDIREAARMYATAKSAAILWGMgvtqHSHGtdNVMALSNlalltgnigrP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 515 NWKVwNVL--QTN---AAQTAALDV---GYTagadaaiaaepKVLFLLG-------ADSNAIKK--DQLpkDCFIVyQGH 577
Cdd:cd02753 316 GTGV-NPLrgQNNvqgACDMGALPNvlpGYV-----------KALYIMGenpalsdPNTNHVRKalESL--EFLVV-QDI 380
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1949577332 578 HGDAGAQLAHAILPGAAYTEKQATYVNTEGRAQQTLVAVTPPGLAREDWKILRALSEIAGAPLPYDT----LDELRS 650
Cdd:cd02753 381 FLTETAELADVVLPAASFAEKDGTFTNTERRVQRVRKAVEPPGEARPDWEIIQELANRLGYPGFYSHpeeiFDEIAR 457
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
37-155 |
8.47e-16 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 81.31 E-value: 8.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 37 IEVFVDDQSVMVAPGTTVLQAAAQVGVEIPRFCYHERLAVAGNCRMCLVEVEKSPKPVAACAMPVMKGWRIKTNSEMTRK 116
Cdd:PRK12814 4 ISLTINGRSVTAAPGTSILEAAASAGITIPTLCFHQELEATGSCWMCIVEIKGKNRFVPACSTAVSEGMVIETENAELHA 83
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1949577332 117 AREGVMEFLLMNHPLDC--PI---CDQGgeCDLQD--QAMAFGSDR 155
Cdd:PRK12814 84 MRRQSLERLIEQHCGDClgPCelaCPAG--CNIPGfiAAIARGDDR 127
|
|
| Fer2_4 |
pfam13510 |
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ... |
35-112 |
1.46e-15 |
|
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core structure consisting of beta(2)-alpha-beta(2) which a beta-grasp type fold. The domain is around one hundred amino acids with four conserved cysteine residues to which the 2Fe-2S cluster is ligated. This cluster appears within sarcosine oxidase proteins.
Pssm-ID: 433268 [Multi-domain] Cd Length: 82 Bit Score: 72.19 E-value: 1.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 35 ELIEVFVDDQSVMVAPGTTVLQAAAQVGVEIPRFCYHER----LAVAGNCRMCLVEVEKSPKpVAACAMPVMKGWRIKTN 110
Cdd:pfam13510 2 RPVTFTFDGRPVTAPEGDTIAAALLANGVRVPRSCKYGRprgiFCAMGECRNCLVEVDGVPN-VRACTTPVREGMVVRTQ 80
|
..
gi 1949577332 111 SE 112
Cdd:pfam13510 81 NG 82
|
|
| fer2 |
cd00207 |
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ... |
37-108 |
1.03e-11 |
|
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in electron transfer processes and in various enzymatic reactions. The family includes plant and algal ferredoxins, which act as electron carriers in photosynthesis and ferredoxins, which participate in redox chains (from bacteria to mammals). Fold is ismilar to thioredoxin.
Pssm-ID: 238126 [Multi-domain] Cd Length: 84 Bit Score: 61.26 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 37 IEVFVDDQSVMVAPGTTVLQAAAQVGVEIPRFCYHerlavaGNCRMCLVEVEK----------------SPKPVAACAMP 100
Cdd:cd00207 3 INVPGSGVEVEVPEGETLLDAAREAGIDIPYSCRA------GACGTCKVEVVEgevdqsdpslldeeeaEGGYVLACQTR 76
|
....*...
gi 1949577332 101 VMKGWRIK 108
Cdd:cd00207 77 VTDGLVIE 84
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
547-657 |
8.80e-11 |
|
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: 64.94 E-value: 8.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 547 EPKVLFLLG-------ADSNAIKKDQLPKDCFIVYQGHHGDAGAQLAHAILPGAAYTEKQATYVNTEGRAQQTLVAVTPP 619
Cdd:cd02754 389 EIKALWVMCtnpavslPNANRVREALERLEFVVVQDAFADTETAEYADLVLPAASWGEKEGTMTNSERRVSLLRAAVEPP 468
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1949577332 620 GLAREDWKILRALSEIAGAP--LPYDT----LDEL----RSRLEDIAP 657
Cdd:cd02754 469 GEARPDWWILADVARRLGFGelFPYTSpeevFEEYrrlsRGRGADLSG 516
|
|
| NADH_dhqG_C |
pfam09326 |
NADH-ubiquinone oxidoreductase subunit G, C-terminal; Members of this family of are found at ... |
673-716 |
2.23e-09 |
|
NADH-ubiquinone oxidoreductase subunit G, C-terminal; Members of this family of are found at the C-terminus of NADH dehydrogenases subunit G or NADH-ubiquinone oxidoreductase subunit G. EC:1.6.99.5.
Pssm-ID: 462757 Cd Length: 41 Bit Score: 53.38 E-value: 2.23e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1949577332 673 QAEEMLRNAAVHFDGAKVEVPqksLQDFFMTDPITRASPTMAKC 716
Cdd:pfam09326 1 ALVLALAGAKGKLSGAPLKSP---IEDFYMTDPISRASATMAKC 41
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
310-662 |
3.32e-07 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 53.69 E-value: 3.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 310 RLIAPMLRNP---NGELEAVEWESALITIAQALRSAPK----GKVAAVAGG-----LADAEALVALKdLLNRLGS----- 372
Cdd:COG0243 78 RLTYPMKRVGprgSGKFERISWDEALDLIAEKLKAIIDeygpEAVAFYTSGgsagrLSNEAAYLAQR-FARALGTnnldd 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 373 -ETLCTEQKF----PTDGSGTdfrssylLNSSIAACEEADLVLLVGTNPRYEAPLLNTRLRKGYVHNEQNIALIGPKVNL 447
Cdd:COG0243 157 nSRLCHESAVaglpRTFGSDK-------GTVSYEDLEHADLIVLWGSNPAENHPRLLRRLREAAKKRGAKIVVIDPRRTE 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 448 SYEY--EHL----GSDASLVRDIAsgnHpfakklkaakkpLIIvgANQLARKDG-AAFVTALHVFANSLQPADPNW---- 516
Cdd:COG0243 230 TAAIadEWLpirpGTDAALLLALA---H------------VLI--EEGLYDRDFlARHTVGFDELAAYVAAYTPEWaaei 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 517 ----------------KVWNVL---------QTNAAQTA--------------------------ALDVGYTAgadaaia 545
Cdd:COG0243 293 tgvpaedirelarefaTAKPAVilwgmglqqHSNGTQTVraianlalltgnigkpgggpfsltgeAILDGKPY------- 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 546 aEPKVLFLLG-------ADSNAIKKdQLPKDCFIVYQGHHGDAGAQLAHAILPGAAYTEKQATYVNTEGRA----QQtlv 614
Cdd:COG0243 366 -PIKALWVYGgnpavsaPDTNRVRE-ALRKLDFVVVIDTFLTETARYADIVLPATTWLERDDIVTNSEDRRvhlsRP--- 440
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1949577332 615 AVTPPGLAREDWKILRALSEIAGAPLPYD---TLDE-LRSRLEDIAPHLVRY 662
Cdd:COG0243 441 AVEPPGEARSDWEIFAELAKRLGFEEAFPwgrTEEDyLRELLEATRGRGITF 492
|
|
| Fer2 |
pfam00111 |
2Fe-2S iron-sulfur cluster binding domain; |
39-87 |
8.57e-05 |
|
2Fe-2S iron-sulfur cluster binding domain;
Pssm-ID: 395061 [Multi-domain] Cd Length: 77 Bit Score: 41.36 E-value: 8.57e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1949577332 39 VFVDDQSVMV---APGTTVLQAAAQVGVEIPRFCYHerlavaGNCRMCLVEV 87
Cdd:pfam00111 1 VTINGKGVTIevpDGETTLLDAAEEAGIDIPYSCRG------GGCGTCAVKV 46
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
308-416 |
6.08e-03 |
|
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: 39.69 E-value: 6.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949577332 308 RQRLIAPMLRNPnGELEAVEWESALITIAQ---ALRSAPKGKVAAVAGGLADAEA------LVALKDLLNRLGSETLCTE 378
Cdd:cd02762 52 PDRLRTPMRRRG-GSFEEIDWDEAFDEIAErlrAIRARHGGDAVGVYGGNPQAHThaggaySPALLKALGTSNYFSAATA 130
|
90 100 110
....*....|....*....|....*....|....*...
gi 1949577332 379 QKFPTDGSGTDFRSSYLLnSSIAACEEADLVLLVGTNP 416
Cdd:cd02762 131 DQKPGHFWSGLMFGHPGL-HPVPDIDRTDYLLILGANP 167
|
|
| |
