|
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 ... |
34-626 |
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: 912.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 34 VFVDGQSVMVEPGTTVLQACEKVGMQIPRFCYHERLSVAGNCRMCLVEIEKAPKVVAACAMPVMKGWNILTNSEKSKKAR 113
Cdd:TIGR01973 1 IFIDGKELEVPKGTTVLQACLSAGIEIPRFCYHEKLSIAGNCRMCLVEVEKFPKPVASCATPVTDGMKISTNSEKVKKAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 114 EGVMEFLLANHPLDCPICDQGGECDLQDQSMMFGNDRSRFLEGKRAVEDKNIGPLVKTIMTRCIQCTRCIRFASEIAGVD 193
Cdd:TIGR01973 81 EGVMEFLLINHPLDCPICDQGGECDLQDQAVMYGSDRSRFREKKRTVENKYLGPLIKTEMTRCIHCTRCVRFANEVAGVE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 194 DLGTTGRGNDMQVGTYIEKMFMSELSGNIIDICPVGALTSKPYAFTARPWETRKTESIDVMDAVGSNIVVSTRTGEVMRI 273
Cdd:TIGR01973 161 DLGVIGRGNNVEIGTYEGKTLESELSGNLIDICPVGALTSKPYAFKARPWELKSTPSICVHDSVGCNIRVDERNGEIMRI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 274 LPRMHEDINEEWISDKTRFAYDGLKRQ-RLTEPMVRNEKGLLTYTSWEDALSRVAGMLQSfqGKDVAAIAGGLVDAEALV 352
Cdd:TIGR01973 241 LPRENDEINEEWLCDKGRFGYDGLNRQdRLTKPLLRNQEGNLLEVSWAEALAIAAEKLKA--SSRIGGIAGPRSSLEELF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 353 ALKDLLNRVDSDTLCTEEVFPTAGAgTDLRSNYLLNTTIAGVEEADVVLLVGTNPRFEAPLFNARIRKSWLHNDLKVALI 432
Cdd:TIGR01973 319 ALKKLVRKLGSENFDLRIRNYEFES-ADLRANYLFNTTLADIEEADLVLLVGADLRQEAPLLNLRLRKAVKKGGAKVALI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 433 G-SPVDLTY-----TYDHLGDSPKILQDIASGSHP-FSQVLKEAKKPMVVLGSSALQRNDGAAILAAVSSIAQKIRMtsg 505
Cdd:TIGR01973 398 GiEKWNLTYpantnLVFHPGLSPKKLDDIASGAHSdIAAALKAAKKPLIIVGDSAISHLDGAALISAAANIAKVIKV--- 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 506 VTGDWKVMNILHRIASQVAALDLGYKP--GVEAIRKNPPKVLFLLGADGG----CITRQDLPK-DCFIIYQGHHGDVGAP 578
Cdd:TIGR01973 475 RRKEWNGLNILSSGANSVGLLDLGGEStgLDAALNLGAADALFLLGADLEraldKTARDALSKaDAFIIYQGHHGTETAE 554
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 311348856 579 IADVILPGAAYTEKSATYVNTEGRAQQTKVAVTPPGLAREDWKIIRAL 626
Cdd:TIGR01973 555 KADVILPGAAFTEKSGTYVNLEGRAQRFEQAVKPPGEAREDWRILRAL 602
|
|
| MopB_Res-Cmplx1_Nad11 |
cd02773 |
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone ... |
249-630 |
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: 704.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 249 ESIDVMDAVGSNIVVSTRTGEVMRILPRMHEDINEEWISDKTRFAYDGLKRQRLTEPMVRNEkGLLTYTSWEDALSRVAG 328
Cdd:cd02773 1 ESIDVLDAVGSNIRVDTRGGEVMRILPRLNEDINEEWISDKTRFAYDGLKRQRLDKPYIRKN-GKLKPATWEEALAAIAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 329 MLQSFQGKDVAAIAGGLVDAEALVALKDLLNRVDSDTLCTEEVFPTAGAgtDLRSNYLLNTTIAGVEEADVVLLVGTNPR 408
Cdd:cd02773 80 ALKGVKPDEIAAIAGDLADVESMVALKDLLNKLGSENLACEQDGPDLPA--DLRSNYLFNTTIAGIEEADAVLLVGTNPR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 409 FEAPLFNARIRKSWLHNDLKVALIGSPVDLTYTYDHLGDSPKILQDIASGSHPFSQVLKEAKKPMVVLGSSALQRNDGAA 488
Cdd:cd02773 158 FEAPVLNARIRKAWLHGGLKVGVIGPPVDLTYDYDHLGTDAKTLQDIASGKHPFSKALKDAKKPMIIVGSGALARKDGAA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 489 ILAAVSSIAQKIRMtsgVTGDWKVMNILHRIASQVAALDLGYKPGVEAIRK-NPPKVLFLLGADGGCITRQdlPKDCFII 567
Cdd:cd02773 238 ILAAVAKLAKKNGV---VREGWNGFNVLHRAASRVGALDLGFVPGAGAIRKsGPPKVLYLLGADEIDITPI--PKDAFVV 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 311348856 568 YQGHHGDVGAPIADVILPGAAYTEKSATYVNTEGRAQQTKVAVTPPGLAREDWKIIRALSEIA 630
Cdd:cd02773 313 YQGHHGDRGAQIADVILPGAAYTEKSGTYVNTEGRVQQTRKAVSPPGDAREDWKILRALSEVL 375
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
31-658 |
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: 609.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 31 LIEVFVDGQSVMVEPGTTVLQACEKVGMQIPRFCYHERLSVAGNCRMCLVEIEKAPKVVAACAMPVMKGWNILTNSEKSK 110
Cdd:COG1034 1 MVTITIDGKEVEVPKGTTVLQAAEKAGIEIPRFCYHPKLSIAGACRMCLVEVEGAPKPVASCATPVTDGMVVKTDSPKVK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 111 KAREGVMEFLLANHPLDCPICDQGGECDLQDQSMMFGNDRSRFLEGKRAVEDKNIGPLVKTIMTRCIQCTRCIRFASEIA 190
Cdd:COG1034 81 KARKGVMEFLLINHPLDCPICDQGGECDLQDQAMEYGVDESRYEEEKRTVPKKDLGPLILLDMNRCILCTRCVRFCDEIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 191 GVDDLGTTGRGNDMQVGTYIEKMFMSELSGNIIDICPVGALTSKPYAFTARPWETRKTESIDVMDAVGSNIVVSTRTGEV 270
Cdd:COG1034 161 GDPELGVIGRGEHSEIGTYLGKPLDSEFSGNCIDVCPVGALTSKPFRFKARPWELKKTPSICPHCSVGCNIRVDVRGGKV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 271 MRILPRMHEDINEEWISDKTRFAYDGLKR-QRLTEPMVRNEkGLLTYTSWEDALSRVAGMLQSfqgkdvaaiaggLVDAE 349
Cdd:COG1034 241 YRVLPRENEAVNEEWLCDKGRFGYDGLNSpDRLTRPLVRKD-GELVEASWEEALAAAAEGLKA------------LKKAE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 350 alvalkdllNRVdsdtlcteevfptagagtdlrsnyllnttiagveeadvvllvgtnprfeaplfnarirkswlhndlkv 429
Cdd:COG1034 308 ---------NSV-------------------------------------------------------------------- 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 430 aligspvdltytydhlgdspkilqdiasgshpfsqvlkeakkpmvvlgssalqrndGAAILAAVSSIAQkirmtsgvtgd 509
Cdd:COG1034 311 --------------------------------------------------------GAALLGALPDAAA----------- 323
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 510 wkvmnILhriasqvaaldlgykpgvEAIRKNPPKVLFLLGAD----GGCITRQDLPKDCFIIYQGHHGDVGAPIADVILP 585
Cdd:COG1034 324 -----IL------------------EAAEAGKLKALVLLGADpydlDPAAALAALAKADFVVVLDHFGSATAERADVVLP 380
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 311348856 586 GAAYTEKSATYVNTEGRAQQTKVAVTPPGLAREDWKIIRALSEIAGMTLPYDTLDQVRNRLEEVSPNLVRYDD 658
Cdd:COG1034 381 AAAFAEKSGTFVNLEGRVQRFNAAVPPPGEARPDWRVLRALANALGAGLPYDSLEEVRAELAAEAPATVSAEG 453
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
301-628 |
7.10e-130 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 389.07 E-value: 7.10e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 301 RLTEPMVRNEKGLLTYTSWEDALSRVAGMLQSFQGK------DVAAIAGGLVDAEALVALKDLLNRVDSDTLCTEEVF-- 372
Cdd:pfam00384 1 RLKYPMVRRGDGKFVRVSWDEALDLIAKKLKRIIKKygpdaiAINGGSGGLTDVESLYALKKLLNRLGSKNGNTEDHNgd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 373 ----PTAGAGTDLRSNYLLNTTIAGVEEADVVLLVGTNPRFEAPLFNARIRKSWLHNDLKVALIGSPVDLTYTYDHLGDS 448
Cdd:pfam00384 81 lctaAAAAFGSDLRSNYLFNSSIADIENADLILLIGTNPREEAPILNARIRKAALKGKAKVIVIGPRLDLTYADEHLGIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 449 PKILQDI-ASGSHPFSQVLKEAK----KPMVVLGSSALQRNDGAAILAAVSSIAQKIRMTSGVTGDWKVMNILHRIASQV 523
Cdd:pfam00384 161 PGTDLALaLAGAHVFIKELKKDKdfapKPIIIVGAGVLQRQDGEAIFRAIANLADLTGNIGRPGGGWNGLNILQGAASPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 524 AALDLGYKPGV------EAIRKNPPKVLFLLG-------ADGGCITRQDLPKDCFIIYQGHHGDVGAPIADVILPGAAYT 590
Cdd:pfam00384 241 GALDLGLVPGIksvemiNAIKKGGIKVLYLLGnnpfvthADENRVVKALQKLDLFVVYDGHHGDKTAKYADVILPAAAYT 320
|
330 340 350
....*....|....*....|....*....|....*...
gi 311348856 591 EKSATYVNTEGRAQQTKVAVTPPGLAREDWKIIRALSE 628
Cdd:pfam00384 321 EKNGTYVNTEGRVQSTKQAVPPPGEAREDWKILRALSE 358
|
|
| PRK07860 |
PRK07860 |
NADH dehydrogenase subunit G; Validated |
28-651 |
1.96e-108 |
|
NADH dehydrogenase subunit G; Validated
Pssm-ID: 236118 [Multi-domain] Cd Length: 797 Bit Score: 347.70 E-value: 1.96e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 28 ASNLIEVFVDGQSVMVEPGTTVLQACEKVGMQIPRFCYHERLSVAGNCRMCLVEIEKAPKVVAACAMPVMKGWNILT--N 105
Cdd:PRK07860 1 PPDLVTLTIDGVEVSVPKGTLVIRAAELLGIQIPRFCDHPLLDPVGACRQCLVEVEGQRKPQASCTTTVTDGMVVKTqlT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 106 SEKSKKAREGVMEFLLANHPLDCPICDQGGECDLQDQSMMFGNDRSRFLEGKRAVEdKNIgPLVKTIM---TRCIQCTRC 182
Cdd:PRK07860 81 SPVADKAQHGVMELLLINHPLDCPVCDKGGECPLQNQAMSNGRAESRFTDVKRTFP-KPI-NISTQVLldrERCVLCARC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 183 IRFASEIAGVDDLGTTGRGNDMQVGTYIEKMFMSELSGNIIDICPVGALTSKPYAFTARPWETRKTESIDVMDAVGSNIV 262
Cdd:PRK07860 159 TRFSDQIAGDPFIDLQERGALQQVGIYEGEPFQSYFSGNTVQICPVGALTGAAYRFRARPFDLVSTPSVCEHCASGCAQR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 263 VSTRTGEVMRILPRMHEDINEEWISDKTRFAYD-GLKRQRLTEPMVRNEKGLLTYTSWEDALSRVAGMLQSFQGkDVAAI 341
Cdd:PRK07860 239 TDHRRGKVLRRLAGDDPEVNEEWNCDKGRWAFTyATQPDRITTPLVRDEDGELEPASWSEALAVAARGLAAARG-RVGVL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 342 AGGLVDAE--------ALVALK----DLLNRVDSDtlcTEEVFPTAG-AGTDlrsnylLNTTIAGVEEADVVLLVGTNPR 408
Cdd:PRK07860 318 VGGRLTVEdayayakfARVALGtndiDFRARPHSA---EEADFLAARvAGRG------LGVTYADLEKAPAVLLVGFEPE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 409 FEAPLFNARIRKSWLHNDLKVALIGSPVD--LTYTYDHL-----GDSPKILQDIASGSHPFSQVLKEAKKpmVVLGSSAL 481
Cdd:PRK07860 389 EESPIVFLRLRKAARKHGLKVYSIAPFATrgLEKMGGTLlrtapGGEAAALDALATGAPDVAELLRTPGA--VILVGERL 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 482 QRNDGAaiLAAVSSIAQkirmTSGVTGDWkvmniLHRIASQVAALDLGYKP----------------------GVEAIRK 539
Cdd:PRK07860 467 ATVPGA--LSAAARLAD----ATGARLAW-----VPRRAGERGALEAGALPtllpggrpvadpaaraevaaawGVDELPA 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 540 NPpkvlfllGADGGCITR-----------------QDLPK-----------DCFIIYQGHHGDVgAPIADVILPGAAYTE 591
Cdd:PRK07860 536 AP-------GRDTAGILAaaaagelgallvggvepADLPDpaaalaaldaaGFVVSLELRHSAV-TERADVVLPVAPVAE 607
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 592 KSATYVNTEGRAQQTKVAVTPPGlAREDWKIIRALSEIAGMTLPYDTLDQVRNRLEEVSP 651
Cdd:PRK07860 608 KAGTFLNWEGRLRPFEAALRTTG-ALSDLRVLDALADEMGVDLGLPTVAAARAELARLGA 666
|
|
| NADH-G_4Fe-4S_3 |
smart00929 |
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region; |
113-153 |
1.18e-17 |
|
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region;
Pssm-ID: 214918 [Multi-domain] Cd Length: 41 Bit Score: 76.85 E-value: 1.18e-17
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 311348856 113 REGVMEFLLANHPLDCPICDQGGECDLQDQSMMFGNDRSRF 153
Cdd:smart00929 1 RKTILELLLANHPLDCPVCDKNGECELQDLAYELGVDEQRY 41
|
|
| NADH_dhqG_C |
pfam09326 |
NADH-ubiquinone oxidoreductase subunit G, C-terminal; Members of this family of are found at ... |
668-710 |
2.65e-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: 58.77 E-value: 2.65e-11
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 311348856 668 ANELSKLVNQ-QLLADPLVPPqltIKDFYMTDSISRASQTMAKC 710
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 ... |
34-626 |
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: 912.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 34 VFVDGQSVMVEPGTTVLQACEKVGMQIPRFCYHERLSVAGNCRMCLVEIEKAPKVVAACAMPVMKGWNILTNSEKSKKAR 113
Cdd:TIGR01973 1 IFIDGKELEVPKGTTVLQACLSAGIEIPRFCYHEKLSIAGNCRMCLVEVEKFPKPVASCATPVTDGMKISTNSEKVKKAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 114 EGVMEFLLANHPLDCPICDQGGECDLQDQSMMFGNDRSRFLEGKRAVEDKNIGPLVKTIMTRCIQCTRCIRFASEIAGVD 193
Cdd:TIGR01973 81 EGVMEFLLINHPLDCPICDQGGECDLQDQAVMYGSDRSRFREKKRTVENKYLGPLIKTEMTRCIHCTRCVRFANEVAGVE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 194 DLGTTGRGNDMQVGTYIEKMFMSELSGNIIDICPVGALTSKPYAFTARPWETRKTESIDVMDAVGSNIVVSTRTGEVMRI 273
Cdd:TIGR01973 161 DLGVIGRGNNVEIGTYEGKTLESELSGNLIDICPVGALTSKPYAFKARPWELKSTPSICVHDSVGCNIRVDERNGEIMRI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 274 LPRMHEDINEEWISDKTRFAYDGLKRQ-RLTEPMVRNEKGLLTYTSWEDALSRVAGMLQSfqGKDVAAIAGGLVDAEALV 352
Cdd:TIGR01973 241 LPRENDEINEEWLCDKGRFGYDGLNRQdRLTKPLLRNQEGNLLEVSWAEALAIAAEKLKA--SSRIGGIAGPRSSLEELF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 353 ALKDLLNRVDSDTLCTEEVFPTAGAgTDLRSNYLLNTTIAGVEEADVVLLVGTNPRFEAPLFNARIRKSWLHNDLKVALI 432
Cdd:TIGR01973 319 ALKKLVRKLGSENFDLRIRNYEFES-ADLRANYLFNTTLADIEEADLVLLVGADLRQEAPLLNLRLRKAVKKGGAKVALI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 433 G-SPVDLTY-----TYDHLGDSPKILQDIASGSHP-FSQVLKEAKKPMVVLGSSALQRNDGAAILAAVSSIAQKIRMtsg 505
Cdd:TIGR01973 398 GiEKWNLTYpantnLVFHPGLSPKKLDDIASGAHSdIAAALKAAKKPLIIVGDSAISHLDGAALISAAANIAKVIKV--- 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 506 VTGDWKVMNILHRIASQVAALDLGYKP--GVEAIRKNPPKVLFLLGADGG----CITRQDLPK-DCFIIYQGHHGDVGAP 578
Cdd:TIGR01973 475 RRKEWNGLNILSSGANSVGLLDLGGEStgLDAALNLGAADALFLLGADLEraldKTARDALSKaDAFIIYQGHHGTETAE 554
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 311348856 579 IADVILPGAAYTEKSATYVNTEGRAQQTKVAVTPPGLAREDWKIIRAL 626
Cdd:TIGR01973 555 KADVILPGAAFTEKSGTYVNLEGRAQRFEQAVKPPGEAREDWRILRAL 602
|
|
| MopB_Res-Cmplx1_Nad11 |
cd02773 |
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone ... |
249-630 |
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: 704.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 249 ESIDVMDAVGSNIVVSTRTGEVMRILPRMHEDINEEWISDKTRFAYDGLKRQRLTEPMVRNEkGLLTYTSWEDALSRVAG 328
Cdd:cd02773 1 ESIDVLDAVGSNIRVDTRGGEVMRILPRLNEDINEEWISDKTRFAYDGLKRQRLDKPYIRKN-GKLKPATWEEALAAIAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 329 MLQSFQGKDVAAIAGGLVDAEALVALKDLLNRVDSDTLCTEEVFPTAGAgtDLRSNYLLNTTIAGVEEADVVLLVGTNPR 408
Cdd:cd02773 80 ALKGVKPDEIAAIAGDLADVESMVALKDLLNKLGSENLACEQDGPDLPA--DLRSNYLFNTTIAGIEEADAVLLVGTNPR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 409 FEAPLFNARIRKSWLHNDLKVALIGSPVDLTYTYDHLGDSPKILQDIASGSHPFSQVLKEAKKPMVVLGSSALQRNDGAA 488
Cdd:cd02773 158 FEAPVLNARIRKAWLHGGLKVGVIGPPVDLTYDYDHLGTDAKTLQDIASGKHPFSKALKDAKKPMIIVGSGALARKDGAA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 489 ILAAVSSIAQKIRMtsgVTGDWKVMNILHRIASQVAALDLGYKPGVEAIRK-NPPKVLFLLGADGGCITRQdlPKDCFII 567
Cdd:cd02773 238 ILAAVAKLAKKNGV---VREGWNGFNVLHRAASRVGALDLGFVPGAGAIRKsGPPKVLYLLGADEIDITPI--PKDAFVV 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 311348856 568 YQGHHGDVGAPIADVILPGAAYTEKSATYVNTEGRAQQTKVAVTPPGLAREDWKIIRALSEIA 630
Cdd:cd02773 313 YQGHHGDRGAQIADVILPGAAYTEKSGTYVNTEGRVQQTRKAVSPPGDAREDWKILRALSEVL 375
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
31-658 |
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: 609.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 31 LIEVFVDGQSVMVEPGTTVLQACEKVGMQIPRFCYHERLSVAGNCRMCLVEIEKAPKVVAACAMPVMKGWNILTNSEKSK 110
Cdd:COG1034 1 MVTITIDGKEVEVPKGTTVLQAAEKAGIEIPRFCYHPKLSIAGACRMCLVEVEGAPKPVASCATPVTDGMVVKTDSPKVK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 111 KAREGVMEFLLANHPLDCPICDQGGECDLQDQSMMFGNDRSRFLEGKRAVEDKNIGPLVKTIMTRCIQCTRCIRFASEIA 190
Cdd:COG1034 81 KARKGVMEFLLINHPLDCPICDQGGECDLQDQAMEYGVDESRYEEEKRTVPKKDLGPLILLDMNRCILCTRCVRFCDEIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 191 GVDDLGTTGRGNDMQVGTYIEKMFMSELSGNIIDICPVGALTSKPYAFTARPWETRKTESIDVMDAVGSNIVVSTRTGEV 270
Cdd:COG1034 161 GDPELGVIGRGEHSEIGTYLGKPLDSEFSGNCIDVCPVGALTSKPFRFKARPWELKKTPSICPHCSVGCNIRVDVRGGKV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 271 MRILPRMHEDINEEWISDKTRFAYDGLKR-QRLTEPMVRNEkGLLTYTSWEDALSRVAGMLQSfqgkdvaaiaggLVDAE 349
Cdd:COG1034 241 YRVLPRENEAVNEEWLCDKGRFGYDGLNSpDRLTRPLVRKD-GELVEASWEEALAAAAEGLKA------------LKKAE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 350 alvalkdllNRVdsdtlcteevfptagagtdlrsnyllnttiagveeadvvllvgtnprfeaplfnarirkswlhndlkv 429
Cdd:COG1034 308 ---------NSV-------------------------------------------------------------------- 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 430 aligspvdltytydhlgdspkilqdiasgshpfsqvlkeakkpmvvlgssalqrndGAAILAAVSSIAQkirmtsgvtgd 509
Cdd:COG1034 311 --------------------------------------------------------GAALLGALPDAAA----------- 323
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 510 wkvmnILhriasqvaaldlgykpgvEAIRKNPPKVLFLLGAD----GGCITRQDLPKDCFIIYQGHHGDVGAPIADVILP 585
Cdd:COG1034 324 -----IL------------------EAAEAGKLKALVLLGADpydlDPAAALAALAKADFVVVLDHFGSATAERADVVLP 380
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 311348856 586 GAAYTEKSATYVNTEGRAQQTKVAVTPPGLAREDWKIIRALSEIAGMTLPYDTLDQVRNRLEEVSPNLVRYDD 658
Cdd:COG1034 381 AAAFAEKSGTFVNLEGRVQRFNAAVPPPGEARPDWRVLRALANALGAGLPYDSLEEVRAELAAEAPATVSAEG 453
|
|
| MopB_NADH-Q-OR-NuoG2 |
cd02768 |
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone ... |
249-629 |
1.47e-171 |
|
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: 496.81 E-value: 1.47e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 249 ESIDVMDAVGSNIVVSTRTGEVMRILPRMHEDINEEWISDKTRFAYDGLK-RQRLTEPMVRNEkGLLTYTSWEDALSRVA 327
Cdd:cd02768 1 ESIDVHDALGSNIRVDVRGGEVMRILPRENEAINEEWISDKGRFGYDGLNsRQRLTQPLIKKG-GKLVPVSWEEALKTVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 328 GMLQSFQGKDVAAIAGGLVDAEALVALKDLLNRVDSDTLCTEEVFPTAGAGTDLRSNYLLNTTIAGVEEADVVLLVGTNP 407
Cdd:cd02768 80 EGLKAVKGDKIGGIAGPRADLESLFLLKKLLNKLGSNNIDHRLRQSDLPADNRLRGNYLFNTSIAEIEEADAVLLIGSNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 408 RFEAPLFNARIRKSWLHNDLKVALIGS-----PVDLTYTYDHLGDSPKILQDIASGSH--PFSQVLKEAKKPMVVLGSSA 480
Cdd:cd02768 160 RKEAPLLNARLRKAVKKKGAKIAVIGPkdtdlIADLTYPVSPLGASLATLLDIAEGKHlkPFAKSLKKAKKPLIILGSSA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 481 LqRNDGAAILAAVSSIAQKIRMtsgVTGDWKVMNILHRIASQVAA--LDLGYKPGVEAIRKnppkvLFLLGADGGCITRQ 558
Cdd:cd02768 240 L-RKDGAAILKALANLAAKLGT---GAGLWNGLNVLNSVGARLGGagLDAGLALLEPGKAK-----LLLLGEDELDRSNP 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 311348856 559 DL-----PKDCFIIYQGHHGDVGAPiADVILPGAAYTEKSATYVNTEGRAQQTKVAVTPPGLAREDWKIIRALSEI 629
Cdd:cd02768 311 PAavalaAADAFVVYQGHHGDTGAQ-ADVILPAAAFTEKSGTYVNTEGRVQRFKKAVSPPGDAREDWKILRALSNL 385
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
301-628 |
7.10e-130 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 389.07 E-value: 7.10e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 301 RLTEPMVRNEKGLLTYTSWEDALSRVAGMLQSFQGK------DVAAIAGGLVDAEALVALKDLLNRVDSDTLCTEEVF-- 372
Cdd:pfam00384 1 RLKYPMVRRGDGKFVRVSWDEALDLIAKKLKRIIKKygpdaiAINGGSGGLTDVESLYALKKLLNRLGSKNGNTEDHNgd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 373 ----PTAGAGTDLRSNYLLNTTIAGVEEADVVLLVGTNPRFEAPLFNARIRKSWLHNDLKVALIGSPVDLTYTYDHLGDS 448
Cdd:pfam00384 81 lctaAAAAFGSDLRSNYLFNSSIADIENADLILLIGTNPREEAPILNARIRKAALKGKAKVIVIGPRLDLTYADEHLGIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 449 PKILQDI-ASGSHPFSQVLKEAK----KPMVVLGSSALQRNDGAAILAAVSSIAQKIRMTSGVTGDWKVMNILHRIASQV 523
Cdd:pfam00384 161 PGTDLALaLAGAHVFIKELKKDKdfapKPIIIVGAGVLQRQDGEAIFRAIANLADLTGNIGRPGGGWNGLNILQGAASPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 524 AALDLGYKPGV------EAIRKNPPKVLFLLG-------ADGGCITRQDLPKDCFIIYQGHHGDVGAPIADVILPGAAYT 590
Cdd:pfam00384 241 GALDLGLVPGIksvemiNAIKKGGIKVLYLLGnnpfvthADENRVVKALQKLDLFVVYDGHHGDKTAKYADVILPAAAYT 320
|
330 340 350
....*....|....*....|....*....|....*...
gi 311348856 591 EKSATYVNTEGRAQQTKVAVTPPGLAREDWKIIRALSE 628
Cdd:pfam00384 321 EKNGTYVNTEGRVQSTKQAVPPPGEAREDWKILRALSE 358
|
|
| PRK07860 |
PRK07860 |
NADH dehydrogenase subunit G; Validated |
28-651 |
1.96e-108 |
|
NADH dehydrogenase subunit G; Validated
Pssm-ID: 236118 [Multi-domain] Cd Length: 797 Bit Score: 347.70 E-value: 1.96e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 28 ASNLIEVFVDGQSVMVEPGTTVLQACEKVGMQIPRFCYHERLSVAGNCRMCLVEIEKAPKVVAACAMPVMKGWNILT--N 105
Cdd:PRK07860 1 PPDLVTLTIDGVEVSVPKGTLVIRAAELLGIQIPRFCDHPLLDPVGACRQCLVEVEGQRKPQASCTTTVTDGMVVKTqlT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 106 SEKSKKAREGVMEFLLANHPLDCPICDQGGECDLQDQSMMFGNDRSRFLEGKRAVEdKNIgPLVKTIM---TRCIQCTRC 182
Cdd:PRK07860 81 SPVADKAQHGVMELLLINHPLDCPVCDKGGECPLQNQAMSNGRAESRFTDVKRTFP-KPI-NISTQVLldrERCVLCARC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 183 IRFASEIAGVDDLGTTGRGNDMQVGTYIEKMFMSELSGNIIDICPVGALTSKPYAFTARPWETRKTESIDVMDAVGSNIV 262
Cdd:PRK07860 159 TRFSDQIAGDPFIDLQERGALQQVGIYEGEPFQSYFSGNTVQICPVGALTGAAYRFRARPFDLVSTPSVCEHCASGCAQR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 263 VSTRTGEVMRILPRMHEDINEEWISDKTRFAYD-GLKRQRLTEPMVRNEKGLLTYTSWEDALSRVAGMLQSFQGkDVAAI 341
Cdd:PRK07860 239 TDHRRGKVLRRLAGDDPEVNEEWNCDKGRWAFTyATQPDRITTPLVRDEDGELEPASWSEALAVAARGLAAARG-RVGVL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 342 AGGLVDAE--------ALVALK----DLLNRVDSDtlcTEEVFPTAG-AGTDlrsnylLNTTIAGVEEADVVLLVGTNPR 408
Cdd:PRK07860 318 VGGRLTVEdayayakfARVALGtndiDFRARPHSA---EEADFLAARvAGRG------LGVTYADLEKAPAVLLVGFEPE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 409 FEAPLFNARIRKSWLHNDLKVALIGSPVD--LTYTYDHL-----GDSPKILQDIASGSHPFSQVLKEAKKpmVVLGSSAL 481
Cdd:PRK07860 389 EESPIVFLRLRKAARKHGLKVYSIAPFATrgLEKMGGTLlrtapGGEAAALDALATGAPDVAELLRTPGA--VILVGERL 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 482 QRNDGAaiLAAVSSIAQkirmTSGVTGDWkvmniLHRIASQVAALDLGYKP----------------------GVEAIRK 539
Cdd:PRK07860 467 ATVPGA--LSAAARLAD----ATGARLAW-----VPRRAGERGALEAGALPtllpggrpvadpaaraevaaawGVDELPA 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 540 NPpkvlfllGADGGCITR-----------------QDLPK-----------DCFIIYQGHHGDVgAPIADVILPGAAYTE 591
Cdd:PRK07860 536 AP-------GRDTAGILAaaaagelgallvggvepADLPDpaaalaaldaaGFVVSLELRHSAV-TERADVVLPVAPVAE 607
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 592 KSATYVNTEGRAQQTKVAVTPPGlAREDWKIIRALSEIAGMTLPYDTLDQVRNRLEEVSP 651
Cdd:PRK07860 608 KAGTFLNWEGRLRPFEAALRTTG-ALSDLRVLDALADEMGVDLGLPTVAAARAELARLGA 666
|
|
| MopB_Res-Cmplx1_Nad11-M |
cd02774 |
MopB_Res_Cmplx1_Nad11_M: Mitochondrial-encoded NADH-quinone oxidoreductase/respiratory complex ... |
249-626 |
1.10e-79 |
|
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: 258.84 E-value: 1.10e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 249 ESIDVMDAVGSNIVVSTRTGEVMRILPRMHEDINEEWISDKTRFAYDGLKRQRLTEPMVRNEKGLLTYTSWEDALSRVAG 328
Cdd:cd02774 1 ESIDVLDSLGSNIRVDIKGNEILRILPKINDELNEEWISDKIRFSYDSLKYQRIKTPLLKLSNNSFLEIGWKTAFKFLNK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 329 MLQSFQGKDVAAIAGGLVDAEALVALKDLLNRVDSDTLCTEEVFPTAGAGTDLRSNYLLNTTIAGVEEADVVLLVGTNPR 408
Cdd:cd02774 81 FILLKKFSKLNFIIGSKIDLETLFYYKKLLNKLGSLNTNSNNFLENNNYFNLDLENYLFNNSLKNLDKSDLCLLIGSNLR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 409 FEAPLFNARIRKSWLHNDLKVALIGSPVDLTYTYDHLGDSPKILQDIASGSHPFSQVLKEAKKPMVVLGSSALQRNDGaa 488
Cdd:cd02774 161 VESPILNIRLRNRYNKGNKKIFVIGNKFDTTYPSKHIGLSLNTLLKILEGKHLFCKQLKKSKKPLIIIGSSFSLRKNY-- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 489 ilaavSSIAQKIRMTSGVTGDwkVMNILHRIASQVAALDLgYKPGVEAIRKnpPKVLFLLGADggciTRQDLPKDCFIIY 568
Cdd:cd02774 239 -----SFIISKLKNFSSNNEN--NFNFLNIISNSLYYLGI-KKFNSNNKKN--LSNLYYIKET----NFQKFNKNNFVIY 304
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 311348856 569 QGHHGDVGAPIADVILPGAAYTEKSATYVNTEGRAQQTKVAVTPPGLAREDWKIIRAL 626
Cdd:cd02774 305 QGHHFLNLANNSNLILPSKTFFEKEALYLNLEGILQKTKKILSFKENIKSDDNIIFSL 362
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
249-628 |
7.11e-67 |
|
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: 225.28 E-value: 7.11e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 249 ESIDVMDAVGSNIVVSTRTGEVMRILPRMHEDINEEWISDKTRFAYDGLK-RQRLTEPMVR-NEKGLLTYTSWEDALSRV 326
Cdd:cd00368 1 PSVCPFCGVGCGILVYVKDGKVVRIEGDPNHPVNEGRLCDKGRAGLDGLYsPDRLKYPLIRvGGRGKFVPISWDEALDEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 327 AGMLQSFQGKD----VAAIAGGLVDAEALVALKDLLNRVDSDTLCTEEVFPTAGAGTDLR--SNYLLNTTIAGVEEADVV 400
Cdd:cd00368 81 AEKLKEIREKYgpdaIAFYGGGGASNEEAYLLQKLLRALGSNNVDSHARLCHASAVAALKafGGGAPTNTLADIENADLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 401 LLVGTNPRFEAPLFNARIRKSWLhNDLKVALIGSPVDLTYTYDHLGDSPKILQDIAsgshpfsqvLKEAKKPMVVLGSSA 480
Cdd:cd00368 161 LLWGSNPAETHPVLAARLRRAKK-RGAKLIVIDPRRTETAAKADEWLPIRPGTDAA---------LALAEWAAEITGVPA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 481 lqrndgAAILAAVSSIAQK----IRMTSGVT----GDWKVMNILhriasqVAALDLGY--KPGVEAIRKNPPkvlFLLGA 550
Cdd:cd00368 231 ------ETIRALAREFAAAkravILWGMGLTqhtnGTQNVRAIA------NLAALTGNigRPGGGLGPGGNP---LVSAP 295
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 311348856 551 DGGCITRQDLPKDCFIIYQGHHGDVGApIADVILPGAAYTEKSATYVNTEGRAQQTKVAVTPPGLAREDWKIIRALSE 628
Cdd:cd00368 296 DANRVRAALKKLDFVVVIDIFMTETAA-YADVVLPAATYLEKEGTYTNTEGRVQLFRQAVEPPGEARSDWEILRELAK 372
|
|
| PTZ00305 |
PTZ00305 |
NADH:ubiquinone oxidoreductase; Provisional |
34-231 |
1.64e-56 |
|
NADH:ubiquinone oxidoreductase; Provisional
Pssm-ID: 140326 [Multi-domain] Cd Length: 297 Bit Score: 194.87 E-value: 1.64e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 34 VFVDGQSVMVEPGT-TVLQACEKVGMQIPRFCYHERLSVAGNCRMCLVEIEKAPKVVAACAMPVMKGWNILTNSEKSKKA 112
Cdd:PTZ00305 71 MFVNKRPVEIIPQEeNLLEVLEREGIRVPKFCYHPILSVAGNCRMCLVQVDGTQNLVVSCATVALPGMSIITDSRLVRDA 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 113 REGVMEFLLANHPLDCPICDQGGECDLQDQSMMFGNDRSRFLEGKRAVEDKNIGPLVKTIMTRCIQCTRCIRFASEIAGV 192
Cdd:PTZ00305 151 REGNVELILINHPNDCPICEQATNCDLQNVSMNYGTDIPRYKEDKRAVQDFYFDPQTRVVLNRCIHCTRCVRFLNEHAQD 230
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 311348856 193 DDLGTTGRGNDMQVGTYIEKM-FMSELSGNIIDICPVGAL 231
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 ... |
250-626 |
2.71e-55 |
|
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: 195.27 E-value: 2.71e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 250 SIDVMDAVGSNIVVSTRTGEVMRILPRMHEDINEEWISDKTRFAYDGLKRQ-RLTEPMVRnEKGLLTYTSWEDALSRVAG 328
Cdd:cd02772 2 SVSPHDALGSNLVVHVKNNKVMRVVPRENEAINECWLSDRDRFSYEGLNSEdRLTKPMIK-KDGQWQEVDWETALEYVAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 329 MLQSFQGKDVAAIAGGLVDA----EALVALKDLLNRVDSDTLCTEEVFPTAGAGTDLRSNYLLNTTIAGVEEADVVLLVG 404
Cdd:cd02772 81 GLSAIIKKHGADQIGALASPhstlEELYLLQKLARGLGSDNIDHRLRQSDFRDDAKASGAPWLGMPIAEISELDRVLVIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 405 TNPRFEAPLFNARIRKSW---------------LHNDLKVALIGSPVDLTYT--------YDHLGDSPKILQDIASGSHP 461
Cdd:cd02772 161 SNLRKEHPLLAQRLRQAVkkgaklsainpadddFLFPLSGKAIVAPSALANAlaqvakalAEEKGLAVPDEDAKVEASEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 462 FSQV---LKEAKKPMVVLGSSALQRNDGAAILAAVSSIAQkirmTSGVTGdwkvmNILHRIASQVAALDLGYKPGV---- 534
Cdd:cd02772 241 ARKIaasLVSAERAAVFLGNLAQNHPQAATLRALAQEIAK----LTGATL-----GVLGEGANSVGAYLAGALPHGglna 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 535 EAIRKNPPKVLFLLGA------DGGCITRQDLPKDCFIIYQGHHGDVGA-PIADVILPGAAYTEKSATYVNTEGRAQQTK 607
Cdd:cd02772 312 AAMLEQPRKAYLLLNVepeldcANPAQALAALNQAEFVVALSAFASAALlDYADVLLPIAPFTETSGTFVNLEGRVQSFK 391
|
410
....*....|....*....
gi 311348856 608 VAVTPPGLAREDWKIIRAL 626
Cdd:cd02772 392 GVVKPLGEARPAWKVLRVL 410
|
|
| 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 ... |
256-627 |
2.66e-37 |
|
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: 145.99 E-value: 2.66e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 256 AVGSNIVVSTRTGEVMRILPRMHEDINEEWISDKTRFAYDGLK-RQRLTEPMVRNeKGLLTYTSWEDALSRVAGMLQSFQ 334
Cdd:cd02771 8 SVGCNISLGERYGELRRVENRYNGAVNHYFLCDRGRFGYGYVNsRDRLTQPLIRR-GGTLVPVSWNEALDVAAARLKEAK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 335 GKdVAAIAGGLVDAEALVALKDLL------NRVDSDTLcteevfptAGAGTDLRSNYLLNTTIAGVEEADVVLLVGTNPR 408
Cdd:cd02771 87 DK-VGGIGSPRASNESNYALQKLVgavlgtNNVDHRAR--------RLIAEILRNGPIYIPSLRDIESADAVLVLGEDLT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 409 FEAPLFNARIRKSWLHNDLK-VALIGSPVDLTYTYDHLGDSPKI-----------LQDIA-------------------- 456
Cdd:cd02771 158 QTAPRIALALRQAARRKAVElAALSGIPKWQDAAVRNIAQGAKSplfivnalatrLDDIAaesiraspggqarlgaalar 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 457 ---------SGSHPFS------QVLKEAKKPMVVLGSSALqrndGAAILAAVSSIAQKIRMTSGVTGdwkVMNILHRIAS 521
Cdd:cd02771 238 avdasaagvSGLAPKEkaariaARLTGAKKPLIVSGTLSG----SLELIKAAANLAKALKRRGENAG---LTLAVEEGNS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 522 QVAAL--DLGYKPG------VEAIRKNPPKVLFLLGAD-------GGCitRQDLPKDCFIIYQGHHGDVGAPIADVILPG 586
Cdd:cd02771 311 PGLLLlgGHVTEPGldldgaLAALEDGSADALIVLGNDlyrsapeRRV--EAALDAAEFVVVLDHFLTETAERADVVLPA 388
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 311348856 587 AAYTEKSATYVNTEGRAQQ-TKVAVTPPGLAREDWKIIRALS 627
Cdd:cd02771 389 ASFAEKSGTFVNYEGRAQRfFKAYDDPAGDARSDWRWLHALA 430
|
|
| PRK07569 |
PRK07569 |
bidirectional hydrogenase complex protein HoxU; Validated |
36-234 |
8.54e-37 |
|
bidirectional hydrogenase complex protein HoxU; Validated
Pssm-ID: 181037 [Multi-domain] Cd Length: 234 Bit Score: 137.86 E-value: 8.54e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 36 VDGQSVMVEPGTTVLQACEKVGMQIPRFCYHERLSVAGNCRMCLVEIEKAPKVVAACAMPVMKGWNILTNSEKSKKAREG 115
Cdd:PRK07569 8 IDDQLVSAREGETLLEAAREAGIPIPTLCHLDGLSDVGACRLCLVEIEGSNKLLPACVTPVAEGMVVQTNTPRLQEYRRM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 116 VMEFLLA--NHPldCPICDQGGECDLQDQSMMFGNDRSRF--LEGKRAVE--------DKNigplvktimtRCIQCTRCI 183
Cdd:PRK07569 88 IVELLFAegNHV--CAVCVANGNCELQDLAIEVGMDHVRFpyLFPRRPVDishprfgiDHN----------RCVLCTRCV 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 311348856 184 RFASEIAGVDDLGTTGRGNDMQVGTYIEKMFMSELS----GNIIDICPVGALTSK 234
Cdd:PRK07569 156 RVCDEIEGAHTWDVAGRGAKSRVITDLNQPWGTSETctscGKCVQACPTGAIFRK 210
|
|
| PRK08493 |
PRK08493 |
NADH-quinone oxidoreductase subunit G; |
31-295 |
1.47e-36 |
|
NADH-quinone oxidoreductase subunit G;
Pssm-ID: 236277 [Multi-domain] Cd Length: 819 Bit Score: 147.54 E-value: 1.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 31 LIEVFVDGQSVMVEPGTTVLQACEKVGMQIPRFCYHERLSVAGNCRMCLVEIEKapKVVAACAMPVMKGWNILTNSEKSK 110
Cdd:PRK08493 1 MITITINGKECEAQEGEYILNVARRNGIFIPAICYLSGCSPTLACRLCMVEADG--KRVYSCNTKAKEGMNILTNTPNLM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 111 KAREGVMEFLLANHPLDCPICDQGGECDLQDQSMMFGNDRSRFlegkrAVEDKNiGPLVKTIMTR-----CIQCTRCIRF 185
Cdd:PRK08493 79 DERNAIMQTYDVNHPLECGVCDKSGECELQNFTHEMGVNHQPY-----AIKDTH-KPHKHWGKINydpslCIVCERCVTV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 186 ASEIAGVDDLGTTGRGNDMQVGTYIEKMFMSELS-----------------------GNIIDICPVGALTSKPYAFTARP 242
Cdd:PRK08493 153 CKDKIGESALKTVPRGLDAPDKSFKESMPKDAYAvwskkqksligpvggetldcsfcGECIAVCPVGALSSSDFQYTSNA 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 311348856 243 WETRKTESIDVMDAVGSNIVVSTR----TGEVMRILpRMHEDINEEWISDKTRFAYD 295
Cdd:PRK08493 233 WELKKIPATCPHCSDCCLIYYDVKhssiLNQESKIY-RVSNDFYFNPLCGAGRFAFD 288
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
256-666 |
6.47e-31 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 129.23 E-value: 6.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 256 AVGSNIVVSTRTGEVMRILPRMHEDINEEWISDKTRFAYDGL-KRQRLTEPMVRnEKGLLTYTSWEDALSRVAGMLQSFQ 334
Cdd:COG3383 15 GVGCGIDLEVKDGKIVKVEGDPDHPVNRGRLCVKGRFGFEFVnSPDRLTTPLIR-RGGEFREVSWDEALDLVAERLREIQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 335 ---GKD-VAAIAGGLVDAEALVALKDLL------NRVDSDT-LCTEevfPTAGA-----GTDLRSNyllntTIAGVEEAD 398
Cdd:COG3383 94 aehGPDaVAFYGSGQLTNEENYLLQKLArgvlgtNNIDNNArLCMA---SAVAGlkqsfGSDAPPN-----SYDDIEEAD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 399 VVLLVGTNPRFEAPLFNARIRKSWLHN-----------------DLKVALI-GSPVDLTYTYDH------LGDSPKI--- 451
Cdd:COG3383 166 VILVIGSNPAEAHPVLARRIKKAKKNGaklivvdprrtetarlaDLHLQIKpGTDLALLNGLLHviieegLVDEDFIaer 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 452 ------LQDIASGSHP----------------FSQVLKEAKKPMVVLGSSALQRNDGAAILAAVSSIAQkirMT------ 503
Cdd:COG3383 246 tegfeeLKASVAKYTPervaeitgvpaedireAARLIAEAKRAMILWGMGVNQHTQGTDNVNAIINLAL---ATgnigrp 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 504 -SGV---TG--------DW-----------KVMNILHRiaSQVAAL----DLGYKPG------VEAIRKNPPKVLFLLG- 549
Cdd:COG3383 323 gTGPfplTGqnnvqggrDMgalpnvlpgyrDVTDPEHR--AKVADAwgvpPLPDKPGltavemFDAIADGEIKALWIIGe 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 550 ------ADGGCItRQDLPKDCFIIYQghhgDV----GAPIADVILPGAAYTEKSATYVNTEGRAQQTKVAVTPPGLARED 619
Cdd:COG3383 401 npavsdPDANHV-REALEKLEFLVVQ----DIflteTAEYADVVLPAASWAEKDGTFTNTERRVQRVRKAVEPPGEARPD 475
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 311348856 620 WKIIRALSEIAGMTLPYDTLDQVRNRLEEVSPNL--VRYDDIEGANYFQ 666
Cdd:COG3383 476 WEIIAELARRLGYGFDYDSPEEVFDEIARLTPDYsgISYERLEALGGVQ 524
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
256-666 |
4.15e-21 |
|
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: 97.67 E-value: 4.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 256 AVGSNIVVSTRTGEVMRILPRMHEDINEEWISDKTRFAYDGLK-RQRLTEPMVRnEKGLLTYTSWEDALSRVAGMLQSFQ 334
Cdd:cd02753 8 GVGCGLELWVKDNKIVGVEPVKGHPVNRGKLCVKGRFGFDFVNsKDRLTKPLIR-KNGKFVEASWDEALSLVASRLKEIK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 335 ---GKD-VAAIAGGLVDAEALVALKDLL------NRVDSDT-LC----TEEVFPTAGAGTDlrSNyllntTIAGVEEADV 399
Cdd:cd02753 87 dkyGPDaIAFFGSAKCTNEENYLFQKLAravggtNNVDHCArLChsptVAGLAETLGSGAM--TN-----SIADIEEADV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 400 VLLVGTNPRFEAPLFNARI---------------------RKSWLHNDLK----VALIGS-------------------- 434
Cdd:cd02753 160 ILVIGSNTTEAHPVIARRIkrakrngaklivadprrtelaRFADLHLQLRpgtdVALLNAmahviieeglydeefieert 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 435 -----------PVDLTYTYDHLGDSPKILQDIAsgshpfsQVLKEAKKPMVVLGSSALQRNDGAAILAAVSSIAQkirmt 503
Cdd:cd02753 240 egfeelkeiveKYTPEYAERITGVPAEDIREAA-------RMYATAKSAAILWGMGVTQHSHGTDNVMALSNLAL----- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 504 sgVTGdwkvmNI------LHRIASQ--V-AALDLGYKPGVEairknpP---KVLFLLGADGGCI------TRQDLPKDCF 565
Cdd:cd02753 308 --LTG-----NIgrpgtgVNPLRGQnnVqGACDMGALPNVL------PgyvKALYIMGENPALSdpntnhVRKALESLEF 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 566 IIYQghhgDV----GAPIADVILPGAAYTEKSATYVNTEGRAQQTKVAVTPPGLAREDWKIIRALSEIAGMTLPYDTLDQ 641
Cdd:cd02753 375 LVVQ----DIflteTAELADVVLPAASFAEKDGTFTNTERRVQRVRKAVEPPGEARPDWEIIQELANRLGYPGFYSHPEE 450
|
490 500
....*....|....*....|....*..
gi 311348856 642 VRNRLEEVSPNL--VRYDDIEGANYFQ 666
Cdd:cd02753 451 IFDEIARLTPQYagISYERLERPGGLQ 477
|
|
| NADH-G_4Fe-4S_3 |
smart00929 |
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region; |
113-153 |
1.18e-17 |
|
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region;
Pssm-ID: 214918 [Multi-domain] Cd Length: 41 Bit Score: 76.85 E-value: 1.18e-17
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 311348856 113 REGVMEFLLANHPLDCPICDQGGECDLQDQSMMFGNDRSRF 153
Cdd:smart00929 1 RKTILELLLANHPLDCPVCDKNGECELQDLAYELGVDEQRY 41
|
|
| NADH-G_4Fe-4S_3 |
pfam10588 |
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region; |
113-152 |
2.02e-17 |
|
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region;
Pssm-ID: 463159 [Multi-domain] Cd Length: 40 Bit Score: 75.95 E-value: 2.02e-17
10 20 30 40
....*....|....*....|....*....|....*....|
gi 311348856 113 REGVMEFLLANHPLDCPICDQGGECDLQDQSMMFGNDRSR 152
Cdd:pfam10588 1 RKTILELLLSNHPLDCPTCDKNGNCELQDLAYELGVDEVR 40
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
30-139 |
4.61e-17 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 85.55 E-value: 4.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 30 NLIEVFVDGQSVMVEPGTTVLQACEKVGMQIPRFCYHERLSVAGNCRMCLVEIEKAPKVVAACAMPVMKGWNILTNSEKS 109
Cdd:PRK12814 2 NTISLTINGRSVTAAPGTSILEAAASAGITIPTLCFHQELEATGSCWMCIVEIKGKNRFVPACSTAVSEGMVIETENAEL 81
|
90 100 110
....*....|....*....|....*....|
gi 311348856 110 KKAREGVMEFLLANHPLDCPicdqgGECDL 139
Cdd:PRK12814 82 HAMRRQSLERLIEQHCGDCL-----GPCEL 106
|
|
| Fer2_4 |
pfam13510 |
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ... |
29-107 |
2.90e-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: 71.42 E-value: 2.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 29 SNLIEVFVDGQSVMVEPGTTVLQACEKVGMQIPRFCYHER----LSVAGNCRMCLVEIEKAPKvVAACAMPVMKGWNILT 104
Cdd:pfam13510 1 SRPVTFTFDGRPVTAPEGDTIAAALLANGVRVPRSCKYGRprgiFCAMGECRNCLVEVDGVPN-VRACTTPVREGMVVRT 79
|
...
gi 311348856 105 NSE 107
Cdd:pfam13510 80 QNG 82
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
256-664 |
5.14e-15 |
|
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: 78.42 E-value: 5.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 256 AVGSNIVVSTRTGEVMRILPRMHEDINEEWISDK-TRFAYDGLKRQRLTEPMVRNEKGLLTYTSWEDALSRVAGMLQSFQ 334
Cdd:cd02754 8 GVGCGVEIGVKDGKVVAVRGDPEHPVNRGRLCIKgLNLHKTLNGPERLTRPLLRRNGGELVPVSWDEALDLIAERFKAIQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 335 ---GKD-VAAIAGGLVDAEALVALKDLL------NRVDSDT-LCTEevfpTAGA------GTDLRSNyllntTIAGVEEA 397
Cdd:cd02754 88 aeyGPDsVAFYGSGQLLTEEYYAANKLAkgglgtNNIDTNSrLCMA----SAVAgykrsfGADGPPG-----SYDDIEHA 158
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170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 398 DVVLLVGTNPRFEAPLFNARIRKSwLHNDLKVALI---------------------GSPVDLTYTYDH-LGDSPKILQD- 454
Cdd:cd02754 159 DCFFLIGSNMAECHPILFRRLLDR-KKANPGAKIIvvdprrtrtadiadlhlpirpGTDLALLNGLLHvLIEEGLIDRDf 237
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250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 455 IAS---GSHPFSQVLK--------------------------EAKKPMVVLGSSALQRNDGAAilaAVSSI--------- 496
Cdd:cd02754 238 IDAhteGFEELKAFVAdytpekvaeitgvpeadireaarlfgEARKVMSLWTMGVNQSTQGTA---ANNAIinlhlatgk 314
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330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 497 ----------------AQKIRMTSGVT----GDWKVMNILHR--IAS--QVAALDLGYKPGV------EAIRKNPPKVLF 546
Cdd:cd02754 315 igrpgsgpfsltgqpnAMGGREVGGLAnllpGHRSVNNPEHRaeVAKfwGVPEGTIPPKPGLhavemfEAIEDGEIKALW 394
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410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 547 LLG-------ADGGCItRQDLPKDCFIIYQ-GHHGDVGAPIADVILPGAAYTEKSATYVNTEGRAQQTKVAVTPPGLARE 618
Cdd:cd02754 395 VMCtnpavslPNANRV-REALERLEFVVVQdAFADTETAEYADLVLPAASWGEKEGTMTNSERRVSLLRAAVEPPGEARP 473
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490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 311348856 619 DWKIIRALSEIAGMT--LPYDTLDQVRNRLEEVSPnlVRYDDIEGANY 664
Cdd:cd02754 474 DWWILADVARRLGFGelFPYTSPEEVFEEYRRLSR--GRGADLSGLSY 519
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| NADH_dhqG_C |
pfam09326 |
NADH-ubiquinone oxidoreductase subunit G, C-terminal; Members of this family of are found at ... |
668-710 |
2.65e-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: 58.77 E-value: 2.65e-11
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 311348856 668 ANELSKLVNQ-QLLADPLVPPqltIKDFYMTDSISRASQTMAKC 710
Cdd:pfam09326 1 ALVLALAGAKgKLSGAPLKSP---IEDFYMTDPISRASATMAKC 41
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|
| fer2 |
cd00207 |
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ... |
32-102 |
4.87e-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: 59.33 E-value: 4.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 32 IEVFVDGQSVMVEPGTTVLQACEKVGMQIPRFCYHerlsvaGNCRMCLVEIEK----------------APKVVAACAMP 95
Cdd:cd00207 3 INVPGSGVEVEVPEGETLLDAAREAGIDIPYSCRA------GACGTCKVEVVEgevdqsdpslldeeeaEGGYVLACQTR 76
|
....*..
gi 311348856 96 VMKGWNI 102
Cdd:cd00207 77 VTDGLVI 83
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| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
301-666 |
1.02e-08 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 58.70 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 301 RLTEPMVR-NEKGLLTY--TSWEDALSRVAGMLQSFQGKD----VAAIAGGLVD----------AEALVALKDLLNRVDS 363
Cdd:COG0243 78 RLTYPMKRvGPRGSGKFerISWDEALDLIAEKLKAIIDEYgpeaVAFYTSGGSAgrlsneaaylAQRFARALGTNNLDDN 157
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 364 DTLCTE--EVFPTAGAGTDLRSNyllntTIAGVEEADVVLLVGTNPRFEAPLFNARIRKSWLHNDLKVALIgSPV----- 436
Cdd:COG0243 158 SRLCHEsaVAGLPRTFGSDKGTV-----SYEDLEHADLIVLWGSNPAENHPRLLRRLREAAKKRGAKIVVI-DPRrteta 231
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170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 437 -------------DL----------------------TYT--YDHL----------------GDSPKILQDIAsgshpfs 463
Cdd:COG0243 232 aiadewlpirpgtDAalllalahvlieeglydrdflaRHTvgFDELaayvaaytpewaaeitGVPAEDIRELA------- 304
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250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 464 QVLKEAKKPMVVLGSSALQRNDGAAILAAVSSIAqkirmtsGVTGdwkvmNILHRIASqvaaldLGYKPGVEAIRKNPPK 543
Cdd:COG0243 305 REFATAKPAVILWGMGLQQHSNGTQTVRAIANLA-------LLTG-----NIGKPGGG------PFSLTGEAILDGKPYP 366
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330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 544 VLFLLGADGGCI--------TRQDLPKDCFIIYQGHHGDVGAPIADVILPGAAYTEKSATYVNTE-GRAQQTKVAVTPPG 614
Cdd:COG0243 367 IKALWVYGGNPAvsapdtnrVREALRKLDFVVVIDTFLTETARYADIVLPATTWLERDDIVTNSEdRRVHLSRPAVEPPG 446
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410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 311348856 615 LAREDWKIIRALSEIAGMTLPYDTL----DQVRNRLEEVSPNLVRYDDIEGANYFQ 666
Cdd:COG0243 447 EARSDWEIFAELAKRLGFEEAFPWGrteeDYLRELLEATRGRGITFEELREKGPVQ 502
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|
| Fer2 |
pfam00111 |
2Fe-2S iron-sulfur cluster binding domain; |
34-96 |
8.62e-06 |
|
2Fe-2S iron-sulfur cluster binding domain;
Pssm-ID: 395061 [Multi-domain] Cd Length: 77 Bit Score: 44.44 E-value: 8.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 34 VFVDGQSVMVE---PGTTVLQACEKVGMQIPRFCYHerlsvaGNCRMCLVEIEK----------------APKVVAACAM 94
Cdd:pfam00111 1 VTINGKGVTIEvpdGETTLLDAAEEAGIDIPYSCRG------GGCGTCAVKVLEgedqsdqsfleddelaAGYVVLACQT 74
|
..
gi 311348856 95 PV 96
Cdd:pfam00111 75 YP 76
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| MopB_Nitrate-R-NarG-like |
cd02750 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
574-639 |
1.82e-04 |
|
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under anaerobic conditions in the presence of nitrate, E. coli synthesizes the cytoplasmic membrane-bound quinol-nitrate oxidoreductase (NarGHI), which reduces nitrate to nitrite and forms part of a redox loop generating a proton-motive force. Found in prokaryotes and some archaea, NarGHI usually functions as a heterotrimer. The alpha chain contains the molybdenum cofactor-containing Mo-bisMGD catalytic subunit. Members of the MopB_Nitrate-R-NarG-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239151 [Multi-domain] Cd Length: 461 Bit Score: 44.62 E-value: 1.82e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 311348856 574 DVGAPIADVILPGAAYTEK---SATYVNTEGRAQQTkvAVTPPGLAREDWKIIRALSEiagmTLPYDTL 639
Cdd:cd02750 374 DSTALYSDIVLPAATWYEKhdlSTTDMHPFIHPFSP--AVDPLWEAKSDWEIFKALAK----KVPWRTL 436
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|
| PRK13532 |
PRK13532 |
nitrate reductase catalytic subunit NapA; |
575-623 |
3.75e-04 |
|
nitrate reductase catalytic subunit NapA;
Pssm-ID: 237416 [Multi-domain] Cd Length: 830 Bit Score: 44.12 E-value: 3.75e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 311348856 575 VGAPIADVILPGAAYTEKSATYVNTEGRAQQTKVAVTPPGLARED-WKII 623
Cdd:PRK13532 516 VSALAADLILPTAMWVEKEGAYGNAERRTQFWRQQVKAPGEAKSDlWQLV 565
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|
| Nar1 |
COG4624 |
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion]; |
90-236 |
1.75e-03 |
|
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
Pssm-ID: 443663 [Multi-domain] Cd Length: 450 Bit Score: 41.55 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311348856 90 AACAMPVMKGWNILTNSEKSKKAREGVMEFLLANHPLDCPICDQGGECDLQDQSMMFGNDRSRFLEGKRAVEDKNIGPLV 169
Cdd:COG4624 7 ACCCCCIEEGDELLLLEEAERVLRIIILEALLPEHVDDDSACSCCPRCCLCCCCCCRCCVAISCIQVRGIIIIDKRGPSI 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 311348856 170 KTIMTRCIQCTRCIR--------FASEIAGVDDLGTTGRGNDMQVgtyiekmfmselsgniidiCPVGALTSKPY 236
Cdd:COG4624 87 IRDKEKCKNCYPCVRacpvkaikVDDGKAEIDEEKCISCGQCVAV-------------------CPFGAITEKSD 142
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