|
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 ... |
76-660 |
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: 772.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 76 VFVDGYAVKVPKGFTVLQACEVAGVDIPRFCYHSRLSIAGNCRMCLVEVEKSPKPVASCAMPALPGMKIKTDTPIAKKAR 155
Cdd:TIGR01973 1 IFIDGKELEVPKGTTVLQACLSAGIEIPRFCYHEKLSIAGNCRMCLVEVEKFPKPVASCATPVTDGMKISTNSEKVKKAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 156 EGVMEFLLMNHPLDCPICDQGGECDLQDQSMAFGSDRGRFTEMKRSVVDKNLGPLVKTVMTRCIQCTRCVRFASEVAGVQ 235
Cdd:TIGR01973 81 EGVMEFLLINHPLDCPICDQGGECDLQDQAVMYGSDRSRFREKKRTVENKYLGPLIKTEMTRCIHCTRCVRFANEVAGVE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 236 DLGILGRGSGEEIGTYVEKLMTSELSGNVIDICPVGALTSKPFAFKARNWELKATETIDVSDAVGSNIRVDSRGPEVMRI 315
Cdd:TIGR01973 161 DLGVIGRGNNVEIGTYEGKTLESELSGNLIDICPVGALTSKPYAFKARPWELKSTPSICVHDSVGCNIRVDERNGEIMRI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 316 IPRLNEDINEEWISDKTRFCYDGLKRQ-RLSDPMIRDSDGRFKAVSWRDALAVVGDIIhqVKPDEIVGVAGQLSDAESMM 394
Cdd:TIGR01973 241 LPRENDEINEEWLCDKGRFGYDGLNRQdRLTKPLLRNQEGNLLEVSWAEALAIAAEKL--KASSRIGGIAGPRSSLEELF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 395 VLKDFVNRMGSDNV--WCEGTAAGVdADLRYSYLMNTSISGLENADLFLLIGTQPRVEAAMVNARICKTVRASNAKVGYV 472
Cdd:TIGR01973 319 ALKKLVRKLGSENFdlRIRNYEFES-ADLRANYLFNTTLADIEEADLVLLVGADLRQEAPLLNLRLRKAVKKGGAKVALI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 473 GPP-AEFNYDC-----KHLGTGPDTLKEIAEGRHP-FCTALKNAKNPAIIVGAGLFNRTDKNAILSSVESIAQANNVVRP 545
Cdd:TIGR01973 398 GIEkWNLTYPAntnlvFHPGLSPKKLDDIASGAHSdIAAALKAAKKPLIIVGDSAISHLDGAALISAAANIAKVIKVRRK 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 546 DWNGLNFLLQYAAQ---AAALDLGLIQQSAKALESAKFVYLMGAD-DVNVDKIPKDA------FVVYQGHHGDKAVYRAN 615
Cdd:TIGR01973 478 EWNGLNILSSGANSvglLDLGGESTGLDAALNLGAADALFLLGADlERALDKTARDAlskadaFIIYQGHHGTETAEKAD 557
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 30693102 616 VILPASAFTEKEGTYENTEGFTQQTVPAVPTVGDARDDWKIVRAL 660
Cdd:TIGR01973 558 VILPGAAFTEKSGTYVNLEGRAQRFEQAVKPPGEAREDWRILRAL 602
|
|
| MopB_Res-Cmplx1_Nad11 |
cd02773 |
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone ... |
291-664 |
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: 625.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 291 ETIDVSDAVGSNIRVDSRGPEVMRIIPRLNEDINEEWISDKTRFCYDGLKRQRLSDPMIRDSdGRFKAVSWRDALAVVGD 370
Cdd:cd02773 1 ESIDVLDAVGSNIRVDTRGGEVMRILPRLNEDINEEWISDKTRFAYDGLKRQRLDKPYIRKN-GKLKPATWEEALAAIAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 371 IIHQVKPDEIVGVAGQLSDAESMMVLKDFVNRMGSDNVWCEGTAAGVDADLRYSYLMNTSISGLENADLFLLIGTQPRVE 450
Cdd:cd02773 80 ALKGVKPDEIAAIAGDLADVESMVALKDLLNKLGSENLACEQDGPDLPADLRSNYLFNTTIAGIEEADAVLLVGTNPRFE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 451 AAMVNARICKTVRASNAKVGYVGPPAEFNYDCKHLGTGPDTLKEIAEGRHPFCTALKNAKNPAIIVGAGLFNRTDKNAIL 530
Cdd:cd02773 160 APVLNARIRKAWLHGGLKVGVIGPPVDLTYDYDHLGTDAKTLQDIASGKHPFSKALKDAKKPMIIVGSGALARKDGAAIL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 531 SSVESIAQANNVVRPDWNGLNFLLQYAAQAAALDLGLIQQSAKALESA--KFVYLMGADDVNVDKIPKDAFVVYQGHHGD 608
Cdd:cd02773 240 AAVAKLAKKNGVVREGWNGFNVLHRAASRVGALDLGFVPGAGAIRKSGppKVLYLLGADEIDITPIPKDAFVVYQGHHGD 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 30693102 609 KAVYRANVILPASAFTEKEGTYENTEGFTQQTVPAVPTVGDARDDWKIVRALSEVS 664
Cdd:cd02773 320 RGAQIADVILPGAAYTEKSGTYVNTEGRVQQTRKAVSPPGDAREDWKILRALSEVL 375
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
74-692 |
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: 595.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 74 IEVFVDGYAVKVPKGFTVLQACEVAGVDIPRFCYHSRLSIAGNCRMCLVEVEKSPKPVASCAMPALPGMKIKTDTPIAKK 153
Cdd:COG1034 2 VTITIDGKEVEVPKGTTVLQAAEKAGIEIPRFCYHPKLSIAGACRMCLVEVEGAPKPVASCATPVTDGMVVKTDSPKVKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 154 AREGVMEFLLMNHPLDCPICDQGGECDLQDQSMAFGSDRGRFTEMKRSVVDKNLGPLVKTVMTRCIQCTRCVRFASEVAG 233
Cdd:COG1034 82 ARKGVMEFLLINHPLDCPICDQGGECDLQDQAMEYGVDESRYEEEKRTVPKKDLGPLILLDMNRCILCTRCVRFCDEIAG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 234 VQDLGILGRGSGEEIGTYVEKLMTSELSGNVIDICPVGALTSKPFAFKARNWELKATETIDVSDAVGSNIRVDSRGPEVM 313
Cdd:COG1034 162 DPELGVIGRGEHSEIGTYLGKPLDSEFSGNCIDVCPVGALTSKPFRFKARPWELKKTPSICPHCSVGCNIRVDVRGGKVY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 314 RIIPRLNEDINEEWISDKTRFCYDGLKR-QRLSDPMIRdSDGRFKAVSWRDALAVVGDIIhqvkpdeivgvaGQLSDAEs 392
Cdd:COG1034 242 RVLPRENEAVNEEWLCDKGRFGYDGLNSpDRLTRPLVR-KDGELVEASWEEALAAAAEGL------------KALKKAE- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 393 mmvlkdfvNRMGsdnvwcegtaagvdadlrysylmntsisglenadlFLLIGTQPRVEAAmvnaricktvrasnakvgyv 472
Cdd:COG1034 308 --------NSVG-----------------------------------AALLGALPDAAAI-------------------- 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 473 gppaefnydckhlgtgpdtLKEIAEGrhpfctalknaknpaiivgaglfnrtdknailssvesiaqannvvrpdwnglnf 552
Cdd:COG1034 325 -------------------LEAAEAG------------------------------------------------------ 331
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 553 llqyaaqaaaldlgliqqsakaleSAKFVYLMGADDVNVDK------IPKDAFVVYQGHHGDKAVYRANVILPASAFTEK 626
Cdd:COG1034 332 ------------------------KLKALVLLGADPYDLDPaaalaaLAKADFVVVLDHFGSATAERADVVLPAAAFAEK 387
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30693102 627 EGTYENTEGFTQQTVPAVPTVGDARDDWKIVRALSEVSGVKLPYNSIEGVRSRIKSVAPNLVHTDE 692
Cdd:COG1034 388 SGTFVNLEGRVQRFNAAVPPPGEARPDWRVLRALANALGAGLPYDSLEEVRAELAAEAPATVSAEG 453
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
343-663 |
6.33e-112 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 343.23 E-value: 6.33e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 343 RLSDPMIRDSDGRFKAVSWRDALAVVGDIIHQVKPD------EIVGVAGQLSDAESMMVLKDFVNRMGSDNVWCEGT--- 413
Cdd:pfam00384 1 RLKYPMVRRGDGKFVRVSWDEALDLIAKKLKRIIKKygpdaiAINGGSGGLTDVESLYALKKLLNRLGSKNGNTEDHngd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 414 -----AAGVDADLRYSYLMNTSISGLENADLFLLIGTQPRVEAAMVNARICKTVRASNAKVGYVGPPAEFNYDCKHLGTG 488
Cdd:pfam00384 81 lctaaAAAFGSDLRSNYLFNSSIADIENADLILLIGTNPREEAPILNARIRKAALKGKAKVIVIGPRLDLTYADEHLGIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 489 PDTLKEI-AEGRHPFCTALKNAK----NPAIIVGAGLFNRTDKNAILSSVESIAQANNVVRP---DWNGLNF------LL 554
Cdd:pfam00384 161 PGTDLALaLAGAHVFIKELKKDKdfapKPIIIVGAGVLQRQDGEAIFRAIANLADLTGNIGRpggGWNGLNIlqgaasPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 555 QYAAQAAALDLGLIQQSAKALESA-KFVYLMG-------ADDVNVDK--IPKDAFVVYQGHHGDKAVYRANVILPASAFT 624
Cdd:pfam00384 241 GALDLGLVPGIKSVEMINAIKKGGiKVLYLLGnnpfvthADENRVVKalQKLDLFVVYDGHHGDKTAKYADVILPAAAYT 320
|
330 340 350
....*....|....*....|....*....|....*....
gi 30693102 625 EKEGTYENTEGFTQQTVPAVPTVGDARDDWKIVRALSEV 663
Cdd:pfam00384 321 EKNGTYVNTEGRVQSTKQAVPPPGEAREDWKILRALSEV 359
|
|
| PRK07860 |
PRK07860 |
NADH dehydrogenase subunit G; Validated |
70-476 |
1.94e-104 |
|
NADH dehydrogenase subunit G; Validated
Pssm-ID: 236118 [Multi-domain] Cd Length: 797 Bit Score: 337.69 E-value: 1.94e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 70 PEDAIEVFVDGYAVKVPKGFTVLQACEVAGVDIPRFCYHSRLSIAGNCRMCLVEVEKSPKPVASCAMPALPGMKIKTD-- 147
Cdd:PRK07860 1 PPDLVTLTIDGVEVSVPKGTLVIRAAELLGIQIPRFCDHPLLDPVGACRQCLVEVEGQRKPQASCTTTVTDGMVVKTQlt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 148 TPIAKKAREGVMEFLLMNHPLDCPICDQGGECDLQDQSMAFGSDRGRFTEMKRsVVDKNLgPLVKTVM---TRCIQCTRC 224
Cdd:PRK07860 81 SPVADKAQHGVMELLLINHPLDCPVCDKGGECPLQNQAMSNGRAESRFTDVKR-TFPKPI-NISTQVLldrERCVLCARC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 225 VRFASEVAGVQDLGILGRGSGEEIGTYVEKLMTSELSGNVIDICPVGALTSKPFAFKARNWELKATETIDVSDAVGSNIR 304
Cdd:PRK07860 159 TRFSDQIAGDPFIDLQERGALQQVGIYEGEPFQSYFSGNTVQICPVGALTGAAYRFRARPFDLVSTPSVCEHCASGCAQR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 305 VDSRGPEVMRiipRLNED---INEEWISDKTRFCYD-GLKRQRLSDPMIRDSDGRFKAVSWRDALAVVGDIIHQVKPDEI 380
Cdd:PRK07860 239 TDHRRGKVLR---RLAGDdpeVNEEWNCDKGRWAFTyATQPDRITTPLVRDEDGELEPASWSEALAVAARGLAAARGRVG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 381 VGVAGQLS--DAESM-----MVLK----DFVNRMGSDN--VWCEGTAAGVDADLRYsylmntsiSGLENADLFLLIGTQP 447
Cdd:PRK07860 316 VLVGGRLTveDAYAYakfarVALGtndiDFRARPHSAEeaDFLAARVAGRGLGVTY--------ADLEKAPAVLLVGFEP 387
|
410 420
....*....|....*....|....*....
gi 30693102 448 RVEAAMVNARICKTVRASNAKVGYVGPPA 476
Cdd:PRK07860 388 EEESPIVFLRLRKAARKHGLKVYSIAPFA 416
|
|
| NADH-G_4Fe-4S_3 |
smart00929 |
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region; |
155-195 |
4.71e-16 |
|
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region;
Pssm-ID: 214918 [Multi-domain] Cd Length: 41 Bit Score: 72.23 E-value: 4.71e-16
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 30693102 155 REGVMEFLLMNHPLDCPICDQGGECDLQDQSMAFGSDRGRF 195
Cdd:smart00929 1 RKTILELLLANHPLDCPVCDKNGECELQDLAYELGVDEQRY 41
|
|
| NADH_dhqG_C |
pfam09326 |
NADH-ubiquinone oxidoreductase subunit G, C-terminal; Members of this family of are found at ... |
703-738 |
5.49e-11 |
|
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: 58.00 E-value: 5.49e-11
10 20 30
....*....|....*....|....*....|....*.
gi 30693102 703 KPECKEAMSTTPFQTVVENFYMTNSITRASKIMAQC 738
Cdd:pfam09326 6 LAGAKGKLSGAPLKSPIEDFYMTDPISRASATMAKC 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 ... |
76-660 |
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: 772.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 76 VFVDGYAVKVPKGFTVLQACEVAGVDIPRFCYHSRLSIAGNCRMCLVEVEKSPKPVASCAMPALPGMKIKTDTPIAKKAR 155
Cdd:TIGR01973 1 IFIDGKELEVPKGTTVLQACLSAGIEIPRFCYHEKLSIAGNCRMCLVEVEKFPKPVASCATPVTDGMKISTNSEKVKKAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 156 EGVMEFLLMNHPLDCPICDQGGECDLQDQSMAFGSDRGRFTEMKRSVVDKNLGPLVKTVMTRCIQCTRCVRFASEVAGVQ 235
Cdd:TIGR01973 81 EGVMEFLLINHPLDCPICDQGGECDLQDQAVMYGSDRSRFREKKRTVENKYLGPLIKTEMTRCIHCTRCVRFANEVAGVE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 236 DLGILGRGSGEEIGTYVEKLMTSELSGNVIDICPVGALTSKPFAFKARNWELKATETIDVSDAVGSNIRVDSRGPEVMRI 315
Cdd:TIGR01973 161 DLGVIGRGNNVEIGTYEGKTLESELSGNLIDICPVGALTSKPYAFKARPWELKSTPSICVHDSVGCNIRVDERNGEIMRI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 316 IPRLNEDINEEWISDKTRFCYDGLKRQ-RLSDPMIRDSDGRFKAVSWRDALAVVGDIIhqVKPDEIVGVAGQLSDAESMM 394
Cdd:TIGR01973 241 LPRENDEINEEWLCDKGRFGYDGLNRQdRLTKPLLRNQEGNLLEVSWAEALAIAAEKL--KASSRIGGIAGPRSSLEELF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 395 VLKDFVNRMGSDNV--WCEGTAAGVdADLRYSYLMNTSISGLENADLFLLIGTQPRVEAAMVNARICKTVRASNAKVGYV 472
Cdd:TIGR01973 319 ALKKLVRKLGSENFdlRIRNYEFES-ADLRANYLFNTTLADIEEADLVLLVGADLRQEAPLLNLRLRKAVKKGGAKVALI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 473 GPP-AEFNYDC-----KHLGTGPDTLKEIAEGRHP-FCTALKNAKNPAIIVGAGLFNRTDKNAILSSVESIAQANNVVRP 545
Cdd:TIGR01973 398 GIEkWNLTYPAntnlvFHPGLSPKKLDDIASGAHSdIAAALKAAKKPLIIVGDSAISHLDGAALISAAANIAKVIKVRRK 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 546 DWNGLNFLLQYAAQ---AAALDLGLIQQSAKALESAKFVYLMGAD-DVNVDKIPKDA------FVVYQGHHGDKAVYRAN 615
Cdd:TIGR01973 478 EWNGLNILSSGANSvglLDLGGESTGLDAALNLGAADALFLLGADlERALDKTARDAlskadaFIIYQGHHGTETAEKAD 557
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 30693102 616 VILPASAFTEKEGTYENTEGFTQQTVPAVPTVGDARDDWKIVRAL 660
Cdd:TIGR01973 558 VILPGAAFTEKSGTYVNLEGRAQRFEQAVKPPGEAREDWRILRAL 602
|
|
| MopB_Res-Cmplx1_Nad11 |
cd02773 |
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone ... |
291-664 |
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: 625.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 291 ETIDVSDAVGSNIRVDSRGPEVMRIIPRLNEDINEEWISDKTRFCYDGLKRQRLSDPMIRDSdGRFKAVSWRDALAVVGD 370
Cdd:cd02773 1 ESIDVLDAVGSNIRVDTRGGEVMRILPRLNEDINEEWISDKTRFAYDGLKRQRLDKPYIRKN-GKLKPATWEEALAAIAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 371 IIHQVKPDEIVGVAGQLSDAESMMVLKDFVNRMGSDNVWCEGTAAGVDADLRYSYLMNTSISGLENADLFLLIGTQPRVE 450
Cdd:cd02773 80 ALKGVKPDEIAAIAGDLADVESMVALKDLLNKLGSENLACEQDGPDLPADLRSNYLFNTTIAGIEEADAVLLVGTNPRFE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 451 AAMVNARICKTVRASNAKVGYVGPPAEFNYDCKHLGTGPDTLKEIAEGRHPFCTALKNAKNPAIIVGAGLFNRTDKNAIL 530
Cdd:cd02773 160 APVLNARIRKAWLHGGLKVGVIGPPVDLTYDYDHLGTDAKTLQDIASGKHPFSKALKDAKKPMIIVGSGALARKDGAAIL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 531 SSVESIAQANNVVRPDWNGLNFLLQYAAQAAALDLGLIQQSAKALESA--KFVYLMGADDVNVDKIPKDAFVVYQGHHGD 608
Cdd:cd02773 240 AAVAKLAKKNGVVREGWNGFNVLHRAASRVGALDLGFVPGAGAIRKSGppKVLYLLGADEIDITPIPKDAFVVYQGHHGD 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 30693102 609 KAVYRANVILPASAFTEKEGTYENTEGFTQQTVPAVPTVGDARDDWKIVRALSEVS 664
Cdd:cd02773 320 RGAQIADVILPGAAYTEKSGTYVNTEGRVQQTRKAVSPPGDAREDWKILRALSEVL 375
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
74-692 |
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: 595.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 74 IEVFVDGYAVKVPKGFTVLQACEVAGVDIPRFCYHSRLSIAGNCRMCLVEVEKSPKPVASCAMPALPGMKIKTDTPIAKK 153
Cdd:COG1034 2 VTITIDGKEVEVPKGTTVLQAAEKAGIEIPRFCYHPKLSIAGACRMCLVEVEGAPKPVASCATPVTDGMVVKTDSPKVKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 154 AREGVMEFLLMNHPLDCPICDQGGECDLQDQSMAFGSDRGRFTEMKRSVVDKNLGPLVKTVMTRCIQCTRCVRFASEVAG 233
Cdd:COG1034 82 ARKGVMEFLLINHPLDCPICDQGGECDLQDQAMEYGVDESRYEEEKRTVPKKDLGPLILLDMNRCILCTRCVRFCDEIAG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 234 VQDLGILGRGSGEEIGTYVEKLMTSELSGNVIDICPVGALTSKPFAFKARNWELKATETIDVSDAVGSNIRVDSRGPEVM 313
Cdd:COG1034 162 DPELGVIGRGEHSEIGTYLGKPLDSEFSGNCIDVCPVGALTSKPFRFKARPWELKKTPSICPHCSVGCNIRVDVRGGKVY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 314 RIIPRLNEDINEEWISDKTRFCYDGLKR-QRLSDPMIRdSDGRFKAVSWRDALAVVGDIIhqvkpdeivgvaGQLSDAEs 392
Cdd:COG1034 242 RVLPRENEAVNEEWLCDKGRFGYDGLNSpDRLTRPLVR-KDGELVEASWEEALAAAAEGL------------KALKKAE- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 393 mmvlkdfvNRMGsdnvwcegtaagvdadlrysylmntsisglenadlFLLIGTQPRVEAAmvnaricktvrasnakvgyv 472
Cdd:COG1034 308 --------NSVG-----------------------------------AALLGALPDAAAI-------------------- 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 473 gppaefnydckhlgtgpdtLKEIAEGrhpfctalknaknpaiivgaglfnrtdknailssvesiaqannvvrpdwnglnf 552
Cdd:COG1034 325 -------------------LEAAEAG------------------------------------------------------ 331
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 553 llqyaaqaaaldlgliqqsakaleSAKFVYLMGADDVNVDK------IPKDAFVVYQGHHGDKAVYRANVILPASAFTEK 626
Cdd:COG1034 332 ------------------------KLKALVLLGADPYDLDPaaalaaLAKADFVVVLDHFGSATAERADVVLPAAAFAEK 387
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30693102 627 EGTYENTEGFTQQTVPAVPTVGDARDDWKIVRALSEVSGVKLPYNSIEGVRSRIKSVAPNLVHTDE 692
Cdd:COG1034 388 SGTFVNLEGRVQRFNAAVPPPGEARPDWRVLRALANALGAGLPYDSLEEVRAELAAEAPATVSAEG 453
|
|
| MopB_NADH-Q-OR-NuoG2 |
cd02768 |
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone ... |
291-663 |
8.16e-151 |
|
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: 444.42 E-value: 8.16e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 291 ETIDVSDAVGSNIRVDSRGPEVMRIIPRLNEDINEEWISDKTRFCYDGLK-RQRLSDPMIRDsDGRFKAVSWRDALAVVG 369
Cdd:cd02768 1 ESIDVHDALGSNIRVDVRGGEVMRILPRENEAINEEWISDKGRFGYDGLNsRQRLTQPLIKK-GGKLVPVSWEEALKTVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 370 DIIHQVKPDEIVGVAGQLSDAESMMVLKDFVNRMGSDNVWCE--GTAAGVDADLRYSYLMNTSISGLENADLFLLIGTQP 447
Cdd:cd02768 80 EGLKAVKGDKIGGIAGPRADLESLFLLKKLLNKLGSNNIDHRlrQSDLPADNRLRGNYLFNTSIAEIEEADAVLLIGSNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 448 RVEAAMVNARICKTVRASNAKVGYVGP-----PAEFNYDCKHLGTGPDTLKEIAEGRH--PFCTALKNAKNPAIIVGAGL 520
Cdd:cd02768 160 RKEAPLLNARLRKAVKKKGAKIAVIGPkdtdlIADLTYPVSPLGASLATLLDIAEGKHlkPFAKSLKKAKKPLIILGSSA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 521 FnRTDKNAILSSVESIAQANNVVRPDWNGLNFLLQYAAQAAALDLGLIQQSAKALESAkfVYLMGADDVNVDKIP----- 595
Cdd:cd02768 240 L-RKDGAAILKALANLAAKLGTGAGLWNGLNVLNSVGARLGGAGLDAGLALLEPGKAK--LLLLGEDELDRSNPPaaval 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 596 --KDAFVVYQGHHGDKAVYrANVILPASAFTEKEGTYENTEGFTQQTVPAVPTVGDARDDWKIVRALSEV 663
Cdd:cd02768 317 aaADAFVVYQGHHGDTGAQ-ADVILPAAAFTEKSGTYVNTEGRVQRFKKAVSPPGDAREDWKILRALSNL 385
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
343-663 |
6.33e-112 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 343.23 E-value: 6.33e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 343 RLSDPMIRDSDGRFKAVSWRDALAVVGDIIHQVKPD------EIVGVAGQLSDAESMMVLKDFVNRMGSDNVWCEGT--- 413
Cdd:pfam00384 1 RLKYPMVRRGDGKFVRVSWDEALDLIAKKLKRIIKKygpdaiAINGGSGGLTDVESLYALKKLLNRLGSKNGNTEDHngd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 414 -----AAGVDADLRYSYLMNTSISGLENADLFLLIGTQPRVEAAMVNARICKTVRASNAKVGYVGPPAEFNYDCKHLGTG 488
Cdd:pfam00384 81 lctaaAAAFGSDLRSNYLFNSSIADIENADLILLIGTNPREEAPILNARIRKAALKGKAKVIVIGPRLDLTYADEHLGIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 489 PDTLKEI-AEGRHPFCTALKNAK----NPAIIVGAGLFNRTDKNAILSSVESIAQANNVVRP---DWNGLNF------LL 554
Cdd:pfam00384 161 PGTDLALaLAGAHVFIKELKKDKdfapKPIIIVGAGVLQRQDGEAIFRAIANLADLTGNIGRpggGWNGLNIlqgaasPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 555 QYAAQAAALDLGLIQQSAKALESA-KFVYLMG-------ADDVNVDK--IPKDAFVVYQGHHGDKAVYRANVILPASAFT 624
Cdd:pfam00384 241 GALDLGLVPGIKSVEMINAIKKGGiKVLYLLGnnpfvthADENRVVKalQKLDLFVVYDGHHGDKTAKYADVILPAAAYT 320
|
330 340 350
....*....|....*....|....*....|....*....
gi 30693102 625 EKEGTYENTEGFTQQTVPAVPTVGDARDDWKIVRALSEV 663
Cdd:pfam00384 321 EKNGTYVNTEGRVQSTKQAVPPPGEAREDWKILRALSEV 359
|
|
| PRK07860 |
PRK07860 |
NADH dehydrogenase subunit G; Validated |
70-476 |
1.94e-104 |
|
NADH dehydrogenase subunit G; Validated
Pssm-ID: 236118 [Multi-domain] Cd Length: 797 Bit Score: 337.69 E-value: 1.94e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 70 PEDAIEVFVDGYAVKVPKGFTVLQACEVAGVDIPRFCYHSRLSIAGNCRMCLVEVEKSPKPVASCAMPALPGMKIKTD-- 147
Cdd:PRK07860 1 PPDLVTLTIDGVEVSVPKGTLVIRAAELLGIQIPRFCDHPLLDPVGACRQCLVEVEGQRKPQASCTTTVTDGMVVKTQlt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 148 TPIAKKAREGVMEFLLMNHPLDCPICDQGGECDLQDQSMAFGSDRGRFTEMKRsVVDKNLgPLVKTVM---TRCIQCTRC 224
Cdd:PRK07860 81 SPVADKAQHGVMELLLINHPLDCPVCDKGGECPLQNQAMSNGRAESRFTDVKR-TFPKPI-NISTQVLldrERCVLCARC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 225 VRFASEVAGVQDLGILGRGSGEEIGTYVEKLMTSELSGNVIDICPVGALTSKPFAFKARNWELKATETIDVSDAVGSNIR 304
Cdd:PRK07860 159 TRFSDQIAGDPFIDLQERGALQQVGIYEGEPFQSYFSGNTVQICPVGALTGAAYRFRARPFDLVSTPSVCEHCASGCAQR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 305 VDSRGPEVMRiipRLNED---INEEWISDKTRFCYD-GLKRQRLSDPMIRDSDGRFKAVSWRDALAVVGDIIHQVKPDEI 380
Cdd:PRK07860 239 TDHRRGKVLR---RLAGDdpeVNEEWNCDKGRWAFTyATQPDRITTPLVRDEDGELEPASWSEALAVAARGLAAARGRVG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 381 VGVAGQLS--DAESM-----MVLK----DFVNRMGSDN--VWCEGTAAGVDADLRYsylmntsiSGLENADLFLLIGTQP 447
Cdd:PRK07860 316 VLVGGRLTveDAYAYakfarVALGtndiDFRARPHSAEeaDFLAARVAGRGLGVTY--------ADLEKAPAVLLVGFEP 387
|
410 420
....*....|....*....|....*....
gi 30693102 448 RVEAAMVNARICKTVRASNAKVGYVGPPA 476
Cdd:PRK07860 388 EEESPIVFLRLRKAARKHGLKVYSIAPFA 416
|
|
| MopB_Res-Cmplx1_Nad11-M |
cd02774 |
MopB_Res_Cmplx1_Nad11_M: Mitochondrial-encoded NADH-quinone oxidoreductase/respiratory complex ... |
291-660 |
1.16e-81 |
|
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: 264.61 E-value: 1.16e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 291 ETIDVSDAVGSNIRVDSRGPEVMRIIPRLNEDINEEWISDKTRFCYDGLKRQRLSDPMIRDSDGRFKAVSWRDALAVVGD 370
Cdd:cd02774 1 ESIDVLDSLGSNIRVDIKGNEILRILPKINDELNEEWISDKIRFSYDSLKYQRIKTPLLKLSNNSFLEIGWKTAFKFLNK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 371 IIHQVKPDEIVGVAGQLSDAESMMVLKDFVNRMGSDNVWCEG--TAAGVDADLRYSYLMNTSISGLENADLFLLIGTQPR 448
Cdd:cd02774 81 FILLKKFSKLNFIIGSKIDLETLFYYKKLLNKLGSLNTNSNNflENNNYFNLDLENYLFNNSLKNLDKSDLCLLIGSNLR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 449 VEAAMVNARICKTVRASNAKVGYVGPPAEFNYDCKHLGTGPDTLKEIAEGRHPFCTALKNAKNPAIIVGAGLFNRTDKNA 528
Cdd:cd02774 161 VESPILNIRLRNRYNKGNKKIFVIGNKFDTTYPSKHIGLSLNTLLKILEGKHLFCKQLKKSKKPLIIIGSSFSLRKNYSF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 529 ILSSVESIAqanNVVRPDWNGLNFLLQYAAQAAALDLgliqqSAKALESAKFVYLMGADdvNVDKIPKDAFVVYQGHHGD 608
Cdd:cd02774 241 IISKLKNFS---SNNENNFNFLNIISNSLYYLGIKKF-----NSNNKKNLSNLYYIKET--NFQKFNKNNFVIYQGHHFL 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 30693102 609 KAVYRANVILPASAFTEKEGTYENTEGFTQQTVPAVPTVGDARDDWKIVRAL 660
Cdd:cd02774 311 NLANNSNLILPSKTFFEKEALYLNLEGILQKTKKILSFKENIKSDDNIIFSL 362
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
291-662 |
9.01e-64 |
|
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: 217.20 E-value: 9.01e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 291 ETIDVSDAVGSNIRVDSRGPEVMRIIPRLNEDINEEWISDKTRFCYDGLK-RQRLSDPMIRDSD-GRFKAVSWRDALAVV 368
Cdd:cd00368 1 PSVCPFCGVGCGILVYVKDGKVVRIEGDPNHPVNEGRLCDKGRAGLDGLYsPDRLKYPLIRVGGrGKFVPISWDEALDEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 369 GDIIHQVK----PDEIVGVAGQLSDAESMMVLKDFVNRMGSDNVWCEGT----AAGVDADLRYSYLMNTSISGLENADLF 440
Cdd:cd00368 81 AEKLKEIRekygPDAIAFYGGGGASNEEAYLLQKLLRALGSNNVDSHARlchaSAVAALKAFGGGAPTNTLADIENADLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 441 LLIGTQPRVEAAMVNARICKTVRAsNAKVGYVGP-----PAEFNYDCKHL-----------------GTGPDTLKEIAEg 498
Cdd:cd00368 161 LLWGSNPAETHPVLAARLRRAKKR-GAKLIVIDPrrtetAAKADEWLPIRpgtdaalalaewaaeitGVPAETIRALAR- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 499 rhpfctALKNAKNPAIIVGAGLFNRTDKNAILSSVESIAQAN-NVVRPDWNGL---NFLLQYAAQaaaldlgliQQSAKA 574
Cdd:cd00368 239 ------EFAAAKRAVILWGMGLTQHTNGTQNVRAIANLAALTgNIGRPGGGLGpggNPLVSAPDA---------NRVRAA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 575 LESAKFVylmgaddvnvdkipkdafVVYQGHHGDKAVYrANVILPASAFTEKEGTYENTEGFTQQTVPAVPTVGDARDDW 654
Cdd:cd00368 304 LKKLDFV------------------VVIDIFMTETAAY-ADVVLPAATYLEKEGTYTNTEGRVQLFRQAVEPPGEARSDW 364
|
....*...
gi 30693102 655 KIVRALSE 662
Cdd:cd00368 365 EILRELAK 372
|
|
| PTZ00305 |
PTZ00305 |
NADH:ubiquinone oxidoreductase; Provisional |
76-273 |
1.15e-61 |
|
NADH:ubiquinone oxidoreductase; Provisional
Pssm-ID: 140326 [Multi-domain] Cd Length: 297 Bit Score: 209.12 E-value: 1.15e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 76 VFVDGYAVKV-PKGFTVLQACEVAGVDIPRFCYHSRLSIAGNCRMCLVEVEKSPKPVASCAMPALPGMKIKTDTPIAKKA 154
Cdd:PTZ00305 71 MFVNKRPVEIiPQEENLLEVLEREGIRVPKFCYHPILSVAGNCRMCLVQVDGTQNLVVSCATVALPGMSIITDSRLVRDA 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 155 REGVMEFLLMNHPLDCPICDQGGECDLQDQSMAFGSDRGRFTEMKRSVVDKNLGPLVKTVMTRCIQCTRCVRFASEVAGV 234
Cdd:PTZ00305 151 REGNVELILINHPNDCPICEQATNCDLQNVSMNYGTDIPRYKEDKRAVQDFYFDPQTRVVLNRCIHCTRCVRFLNEHAQD 230
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 30693102 235 QDLGILGRGSGEEIGTYVEKL-MTSELSGNVIDICPVGAL 273
Cdd:PTZ00305 231 FNLGMIGRGGLSEISTFLDELeVKTDNNMPVSQLCPVGKL 270
|
|
| MopB_NDH-1_NuoG2 |
cd02772 |
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase ... |
297-660 |
5.17e-45 |
|
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: 166.76 E-value: 5.17e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 297 DAVGSNIRVDSRGPEVMRIIPRLNEDINEEWISDKTRFCYDGLKRQ-RLSDPMIRdSDGRFKAVSWRDALAVVGDIIHQV 375
Cdd:cd02772 7 DALGSNLVVHVKNNKVMRVVPRENEAINECWLSDRDRFSYEGLNSEdRLTKPMIK-KDGQWQEVDWETALEYVAEGLSAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 376 K----PDEIVGVAGQLSDAESMMVLKDFVNRMGSDNV-----WcegTAAGVDADLRYSYLMNTSISGLENADLFLLIGTQ 446
Cdd:cd02772 86 IkkhgADQIGALASPHSTLEELYLLQKLARGLGSDNIdhrlrQ---SDFRDDAKASGAPWLGMPIAEISELDRVLVIGSN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 447 PRVEAAMVNARICKTVRaSNAKVGYVGPPAE---FNYDCKHL----------------------GTGPDTLK--EIAEGR 499
Cdd:cd02772 163 LRKEHPLLAQRLRQAVK-KGAKLSAINPADDdflFPLSGKAIvapsalanalaqvakalaeekgLAVPDEDAkvEASEEA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 500 HPFCTALKNAKNPAIIVGAGLFNRTDKNAILSSVESIAQ------------ANNV------VRPdWNGLNfllqyaaqaa 561
Cdd:cd02772 242 RKIAASLVSAERAAVFLGNLAQNHPQAATLRALAQEIAKltgatlgvlgegANSVgaylagALP-HGGLN---------- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 562 aldlgliqqSAKALESAKFVY-LMGA----DDVN----VDKIPKDAFVVYQGHHGDKAV-YRANVILPASAFTEKEGTYE 631
Cdd:cd02772 311 ---------AAAMLEQPRKAYlLLNVepelDCANpaqaLAALNQAEFVVALSAFASAALlDYADVLLPIAPFTETSGTFV 381
|
410 420
....*....|....*....|....*....
gi 30693102 632 NTEGFTQQTVPAVPTVGDARDDWKIVRAL 660
Cdd:cd02772 382 NLEGRVQSFKGVVKPLGEARPAWKVLRVL 410
|
|
| PRK08493 |
PRK08493 |
NADH-quinone oxidoreductase subunit G; |
74-337 |
8.17e-35 |
|
NADH-quinone oxidoreductase subunit G;
Pssm-ID: 236277 [Multi-domain] Cd Length: 819 Bit Score: 142.15 E-value: 8.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 74 IEVFVDGYAVKVPKGFTVLQACEVAGVDIPRFCYHSRLSIAGNCRMCLVEVekSPKPVASCAMPALPGMKIKTDTPIAKK 153
Cdd:PRK08493 2 ITITINGKECEAQEGEYILNVARRNGIFIPAICYLSGCSPTLACRLCMVEA--DGKRVYSCNTKAKEGMNILTNTPNLMD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 154 AREGVMEFLLMNHPLDCPICDQGGECDLQDQSMAFGSDrgrftEMKRSVVDKNlGPLVKTVMTR-----CIQCTRCVRFA 228
Cdd:PRK08493 80 ERNAIMQTYDVNHPLECGVCDKSGECELQNFTHEMGVN-----HQPYAIKDTH-KPHKHWGKINydpslCIVCERCVTVC 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 229 SEVAGVQDLGILGRGSGEEIGTYVEKLMTSELS-----------------------GNVIDICPVGALTSKPFAFKARNW 285
Cdd:PRK08493 154 KDKIGESALKTVPRGLDAPDKSFKESMPKDAYAvwskkqksligpvggetldcsfcGECIAVCPVGALSSSDFQYTSNAW 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 30693102 286 ELKATETIDVSDAVGSNIRVDSR-----GPEVMriIPRLNEDINEEWISDKTRFCYD 337
Cdd:PRK08493 234 ELKKIPATCPHCSDCCLIYYDVKhssilNQESK--IYRVSNDFYFNPLCGAGRFAFD 288
|
|
| PRK07569 |
PRK07569 |
bidirectional hydrogenase complex protein HoxU; Validated |
78-276 |
1.37e-34 |
|
bidirectional hydrogenase complex protein HoxU; Validated
Pssm-ID: 181037 [Multi-domain] Cd Length: 234 Bit Score: 131.70 E-value: 1.37e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 78 VDGYAVKVPKGFTVLQACEVAGVDIPRFCYHSRLSIAGNCRMCLVEVEKSPKPVASCAMPALPGMKIKTDTPIAKKAREG 157
Cdd:PRK07569 8 IDDQLVSAREGETLLEAAREAGIPIPTLCHLDGLSDVGACRLCLVEIEGSNKLLPACVTPVAEGMVVQTNTPRLQEYRRM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 158 VMEFLLM--NHPldCPICDQGGECDLQDQSMAFGSDRGRFTEM--KRSV--------VDKNlgplvktvmtRCIQCTRCV 225
Cdd:PRK07569 88 IVELLFAegNHV--CAVCVANGNCELQDLAIEVGMDHVRFPYLfpRRPVdishprfgIDHN----------RCVLCTRCV 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 30693102 226 RFASEVAGVQDLGILGRGSGEEI--------GTyVEKLmTSelSGNVIDICPVGALTSK 276
Cdd:PRK07569 156 RVCDEIEGAHTWDVAGRGAKSRVitdlnqpwGT-SETC-TS--CGKCVQACPTGAIFRK 210
|
|
| 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 ... |
298-668 |
8.11e-30 |
|
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: 123.65 E-value: 8.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 298 AVGSNIRVDSRGPEVMRIIPRLNEDINEEWISDKTRFCYDGLK-RQRLSDPMIRDsDGRFKAVSWRDALAVVGDIIHQVK 376
Cdd:cd02771 8 SVGCNISLGERYGELRRVENRYNGAVNHYFLCDRGRFGYGYVNsRDRLTQPLIRR-GGTLVPVSWNEALDVAAARLKEAK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 377 PDEIVGVAGQLSDaESMMVLKDFV-NRMGSDNVWCEGTAAGVDaDLRYSYLMNTSISGLENADLFLLIGTQPRVEAAMVN 455
Cdd:cd02771 87 DKVGGIGSPRASN-ESNYALQKLVgAVLGTNNVDHRARRLIAE-ILRNGPIYIPSLRDIESADAVLVLGEDLTQTAPRIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 456 ARICKTVR-------ASNAKVGYVGPPA-EFNYDCKH----LGTGPDTLKEIAEG----------RHPFC---------- 503
Cdd:cd02771 165 LALRQAARrkavelaALSGIPKWQDAAVrNIAQGAKSplfiVNALATRLDDIAAEsiraspggqaRLGAAlaravdasaa 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 504 ---------------TALKNAKNPAIIVGAGLFNRTDKNA---ILSSVESIAQANNVVRPDWNGLNFLLQYAAQAAALDL 565
Cdd:cd02771 245 gvsglapkekaariaARLTGAKKPLIVSGTLSGSLELIKAaanLAKALKRRGENAGLTLAVEEGNSPGLLLLGGHVTEPG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 566 GLIQQSAKALE--SAKFVYLMGADDVN------VDKIPKDA-FVVYQGHHGDKAVYRANVILPASAFTEKEGTYENTEGF 636
Cdd:cd02771 325 LDLDGALAALEdgSADALIVLGNDLYRsaperrVEAALDAAeFVVVLDHFLTETAERADVVLPAASFAEKSGTFVNYEGR 404
|
410 420 430
....*....|....*....|....*....|...
gi 30693102 637 TQQTVPAVPT-VGDARDDWKIVRALSEVSGVKL 668
Cdd:cd02771 405 AQRFFKAYDDpAGDARSDWRWLHALAAKLGGKL 437
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
298-685 |
1.04e-22 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 103.43 E-value: 1.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 298 AVGSNIRVDSRGPEVMRIIPRLNEDINEEWISDKTRFCYDGL-KRQRLSDPMIRDsDGRFKAVSWRDALAVVGD----II 372
Cdd:COG3383 15 GVGCGIDLEVKDGKIVKVEGDPDHPVNRGRLCVKGRFGFEFVnSPDRLTTPLIRR-GGEFREVSWDEALDLVAErlreIQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 373 HQVKPDEIVGVA-GQLSDaESMMVLKDFV-NRMGSDNV-----WCEGTAA-------GVDAdlrysylMNTSISGLENAD 438
Cdd:COG3383 94 AEHGPDAVAFYGsGQLTN-EENYLLQKLArGVLGTNNIdnnarLCMASAVaglkqsfGSDA-------PPNSYDDIEEAD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 439 LFLLIGTQPRVEAAMVNARICKTVRAsNAKVGYVGP--------------------PAEFNYDCKHLG------------ 486
Cdd:COG3383 166 VILVIGSNPAEAHPVLARRIKKAKKN-GAKLIVVDPrrtetarladlhlqikpgtdLALLNGLLHVIIeeglvdedfiae 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 487 --TGPDTLKEIAEGRHP----------------FCTALKNAKNPAIIVGAGLfNR----TDK-NAIL------------- 530
Cdd:COG3383 245 rtEGFEELKASVAKYTPervaeitgvpaedireAARLIAEAKRAMILWGMGV-NQhtqgTDNvNAIInlalatgnigrpg 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 531 SSVESIAQANNV-----------------------VR------------PDWNGLNfllqyaaqaaaldlglIQQSAKAL 575
Cdd:COG3383 324 TGPFPLTGQNNVqggrdmgalpnvlpgyrdvtdpeHRakvadawgvpplPDKPGLT----------------AVEMFDAI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 576 ESA--KFVYLMGADDVNVDKIPKDA--------FVVYQG-HHGDKAVYrANVILPASAFTEKEGTYENTEGFTQQTVPAV 644
Cdd:COG3383 388 ADGeiKALWIIGENPAVSDPDANHVrealekleFLVVQDiFLTETAEY-ADVVLPAASWAEKDGTFTNTERRVQRVRKAV 466
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 30693102 645 PTVGDARDDWKIVRALSEVSGVKLPYNSIEGVRSRIKSVAP 685
Cdd:COG3383 467 EPPGEARPDWEIIAELARRLGYGFDYDSPEEVFDEIARLTP 507
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
298-686 |
1.95e-19 |
|
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: 92.28 E-value: 1.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 298 AVGSNIRVDSRGPEVMRIIPRLNEDINEEWISDKTRFCYDGLK-RQRLSDPMIRDsDGRFKAVSWRDALAVV----GDII 372
Cdd:cd02753 8 GVGCGLELWVKDNKIVGVEPVKGHPVNRGKLCVKGRFGFDFVNsKDRLTKPLIRK-NGKFVEASWDEALSLVasrlKEIK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 373 HQVKPDEIVGVAGQLSDAESMMVLKDFVnRM--GSDNV-----WCEG-TAAGVDADLRYSyLMNTSISGLENADLFLLIG 444
Cdd:cd02753 87 DKYGPDAIAFFGSAKCTNEENYLFQKLA-RAvgGTNNVdhcarLCHSpTVAGLAETLGSG-AMTNSIADIEEADVILVIG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 445 TQPRVEAAMVNARICKTVRASnAKVGYVGPP----AEF---------------------------NYDCKHL-------- 485
Cdd:cd02753 165 SNTTEAHPVIARRIKRAKRNG-AKLIVADPRrtelARFadlhlqlrpgtdvallnamahviieegLYDEEFIeertegfe 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 486 ------------------GTGPDTLKEIAEgrhpfctALKNAKNPAIIVGAGL---FNRTDKNAILSSVESIAqaNNVVR 544
Cdd:cd02753 244 elkeivekytpeyaeritGVPAEDIREAAR-------MYATAKSAAILWGMGVtqhSHGTDNVMALSNLALLT--GNIGR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 545 PDwNGLNfllqyaaqaAALDLGLIQQSAK--ALESA-----KFVYLMGADDV-------NVDKIPKDA-FVVYQGHHGDK 609
Cdd:cd02753 315 PG-TGVN---------PLRGQNNVQGACDmgALPNVlpgyvKALYIMGENPAlsdpntnHVRKALESLeFLVVQDIFLTE 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30693102 610 AVYRANVILPASAFTEKEGTYENTEGFTQQTVPAVPTVGDARDDWKIVRALSEVSGVKLPYNSIEGVRSRIKSVAPN 686
Cdd:cd02753 385 TAELADVVLPAASFAEKDGTFTNTERRVQRVRKAVEPPGEARPDWEIIQELANRLGYPGFYSHPEEIFDEIARLTPQ 461
|
|
| Fer2_4 |
pfam13510 |
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ... |
71-149 |
6.46e-19 |
|
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: 81.82 E-value: 6.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 71 EDAIEVFVDGYAVKVPKGFTVLQACEVAGVDIPRFCYHSR----LSIAGNCRMCLVEVEKSPKpVASCAMPALPGMKIKT 146
Cdd:pfam13510 1 SRPVTFTFDGRPVTAPEGDTIAAALLANGVRVPRSCKYGRprgiFCAMGECRNCLVEVDGVPN-VRACTTPVREGMVVRT 79
|
...
gi 30693102 147 DTP 149
Cdd:pfam13510 80 QNG 82
|
|
| NADH-G_4Fe-4S_3 |
pfam10588 |
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region; |
155-194 |
3.42e-16 |
|
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region;
Pssm-ID: 463159 [Multi-domain] Cd Length: 40 Bit Score: 72.48 E-value: 3.42e-16
10 20 30 40
....*....|....*....|....*....|....*....|
gi 30693102 155 REGVMEFLLMNHPLDCPICDQGGECDLQDQSMAFGSDRGR 194
Cdd:pfam10588 1 RKTILELLLSNHPLDCPTCDKNGNCELQDLAYELGVDEVR 40
|
|
| NADH-G_4Fe-4S_3 |
smart00929 |
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region; |
155-195 |
4.71e-16 |
|
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region;
Pssm-ID: 214918 [Multi-domain] Cd Length: 41 Bit Score: 72.23 E-value: 4.71e-16
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 30693102 155 REGVMEFLLMNHPLDCPICDQGGECDLQDQSMAFGSDRGRF 195
Cdd:smart00929 1 RKTILELLLANHPLDCPVCDKNGECELQDLAYELGVDEQRY 41
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
73-202 |
9.86e-16 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 81.31 E-value: 9.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 73 AIEVFVDGYAVKVPKGFTVLQACEVAGVDIPRFCYHSRLSIAGNCRMCLVEVEKSPKPVASCAMPALPGMKIKTDTPIAK 152
Cdd:PRK12814 3 TISLTINGRSVTAAPGTSILEAAASAGITIPTLCFHQELEATGSCWMCIVEIKGKNRFVPACSTAVSEGMVIETENAELH 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 30693102 153 KAREGVMEFLLMNHPLDC--PI---CDQGgeCDLQD--QSMAFGSDRGRFTEMKRSV 202
Cdd:PRK12814 83 AMRRQSLERLIEQHCGDClgPCelaCPAG--CNIPGfiAAIARGDDREAIRIIKETI 137
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
343-671 |
3.50e-13 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 72.95 E-value: 3.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 343 RLSDPMIRDS---DGRFKAVSWRDALAVVGDIIHQVK----PDEIV-----GVAGQLSDAESMMVLKdFVNRMGSDNVWC 410
Cdd:COG0243 78 RLTYPMKRVGprgSGKFERISWDEALDLIAEKLKAIIdeygPEAVAfytsgGSAGRLSNEAAYLAQR-FARALGTNNLDD 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 411 EGT---AAGVDAdLRYSY---LMNTSISGLENADLFLLIG-----TQPRVEAAMVNARicktvRASNAKVGYVGP----P 475
Cdd:COG0243 157 NSRlchESAVAG-LPRTFgsdKGTVSYEDLEHADLIVLWGsnpaeNHPRLLRRLREAA-----KKRGAKIVVIDPrrteT 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 476 AEFnYDcKHL----GTgpDT------LKE-IAEGRH-------------PFCTALKnAKNPAIIVG------------AG 519
Cdd:COG0243 231 AAI-AD-EWLpirpGT--DAalllalAHVlIEEGLYdrdflarhtvgfdELAAYVA-AYTPEWAAEitgvpaedirelAR 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 520 LFNRTDKNAILSSVeSIAQANNVVRPDW----------------NGLNFLlqyaaqaaaldlgliqqSAKALES-----A 578
Cdd:COG0243 306 EFATAKPAVILWGM-GLQQHSNGTQTVRaianlalltgnigkpgGGPFSL-----------------TGEAILDgkpypI 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 579 KFVYLMGAD------DVN-VDKI-PKDAFVVYQGHHGDKAVYRANVILPASAFTEKEGTYENTE-GFTQQTVPAVPTVGD 649
Cdd:COG0243 368 KALWVYGGNpavsapDTNrVREAlRKLDFVVVIDTFLTETARYADIVLPATTWLERDDIVTNSEdRRVHLSRPAVEPPGE 447
|
410 420
....*....|....*....|..
gi 30693102 650 ARDDWKIVRALSEVSGVKLPYN 671
Cdd:COG0243 448 ARSDWEIFAELAKRLGFEEAFP 469
|
|
| fer2 |
cd00207 |
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ... |
74-145 |
8.71e-12 |
|
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: 61.64 E-value: 8.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 74 IEVFVDGYAVKVPKGFTVLQACEVAGVDIPRFCYHsrlsiaGNCRMCLVEVEK----------------SPKPVASCAMP 137
Cdd:cd00207 3 INVPGSGVEVEVPEGETLLDAAREAGIDIPYSCRA------GACGTCKVEVVEgevdqsdpslldeeeaEGGYVLACQTR 76
|
....*...
gi 30693102 138 ALPGMKIK 145
Cdd:cd00207 77 VTDGLVIE 84
|
|
| NADH_dhqG_C |
pfam09326 |
NADH-ubiquinone oxidoreductase subunit G, C-terminal; Members of this family of are found at ... |
703-738 |
5.49e-11 |
|
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: 58.00 E-value: 5.49e-11
10 20 30
....*....|....*....|....*....|....*.
gi 30693102 703 KPECKEAMSTTPFQTVVENFYMTNSITRASKIMAQC 738
Cdd:pfam09326 6 LAGAKGKLSGAPLKSPIEDFYMTDPISRASATMAKC 41
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
596-676 |
7.66e-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: 65.32 E-value: 7.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 596 KDAFVVYQG--HHGDKAVYrANVILPASAFTEKEGTYENTEGFTQQTVPAVPTVGDARDDWKIVRALSEVSGVK--LPYN 671
Cdd:cd02754 416 RLEFVVVQDafADTETAEY-ADLVLPAASWGEKEGTMTNSERRVSLLRAAVEPPGEARPDWWILADVARRLGFGelFPYT 494
|
....*
gi 30693102 672 SIEGV 676
Cdd:cd02754 495 SPEEV 499
|
|
| MopB_ydeP |
cd02767 |
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
343-457 |
5.14e-05 |
|
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: 46.53 E-value: 5.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 343 RLSDPMIRDS-DGRFKAVSWRDALAVVGDIIHQVKPDEIVGVAGQLSDAESMMVLKDFVNRMGSDNV-----WC-EGTAA 415
Cdd:cd02767 64 RLTYPMRYDAgSDHYRPISWDEAFAEIAARLRALDPDRAAFYTSGRASNEAAYLYQLFARAYGTNNLpdcsnMChEPSSV 143
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 30693102 416 GVDADLRYSYLMnTSISGLENADLFLLIG-----TQPRVEAAMVNAR 457
Cdd:cd02767 144 GLKKSIGVGKGT-VSLEDFEHTDLIFFIGqnpgtNHPRMLHYLREAK 189
|
|
| Fer2 |
pfam00111 |
2Fe-2S iron-sulfur cluster binding domain; |
76-124 |
1.40e-04 |
|
2Fe-2S iron-sulfur cluster binding domain;
Pssm-ID: 395061 [Multi-domain] Cd Length: 77 Bit Score: 40.97 E-value: 1.40e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 30693102 76 VFVDGYAVKVPK---GFTVLQACEVAGVDIPRFCYHsrlsiaGNCRMCLVEV 124
Cdd:pfam00111 1 VTINGKGVTIEVpdgETTLLDAAEEAGIDIPYSCRG------GGCGTCAVKV 46
|
|
| PRK13532 |
PRK13532 |
nitrate reductase catalytic subunit NapA; |
614-657 |
8.78e-04 |
|
nitrate reductase catalytic subunit NapA;
Pssm-ID: 237416 [Multi-domain] Cd Length: 830 Bit Score: 42.96 E-value: 8.78e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 30693102 614 ANVILPASAFTEKEGTYENTEGFTQ---QTVPAvptVGDARDD-WKIV 657
Cdd:PRK13532 521 ADLILPTAMWVEKEGAYGNAERRTQfwrQQVKA---PGEAKSDlWQLV 565
|
|
| Nar1 |
COG4624 |
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion]; |
132-276 |
2.96e-03 |
|
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
Pssm-ID: 443663 [Multi-domain] Cd Length: 450 Bit Score: 40.78 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693102 132 ASCAMPALPGMKIKTDTPIAKKAREGVMEFLLMNHPLDCPICDQGGECDLQDQSMAFGSDRGRFTEMKRSVVDKNLGPLV 211
Cdd:COG4624 7 ACCCCCIEEGDELLLLEEAERVLRIIILEALLPEHVDDDSACSCCPRCCLCCCCCCRCCVAISCIQVRGIIIIDKRGPSI 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30693102 212 KTVMTRCIQCTRCVRFASEVAgvqdlgILGRGSGEEIgtyVEKLMTSelSGNVIDICPVGALTSK 276
Cdd:COG4624 87 IRDKEKCKNCYPCVRACPVKA------IKVDDGKAEI---DEEKCIS--CGQCVAVCPFGAITEK 140
|
|
| |
