|
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 ... |
48-640 |
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: 912.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 48 VFVDGQSVMVEPGTTVLQACEKVGMQIPRFCYHERLSVAGNCRMCLVEIEKAPKVVAACAMPVMKGWNILTNSEKSKKAR 127
Cdd:TIGR01973 1 IFIDGKELEVPKGTTVLQACLSAGIEIPRFCYHEKLSIAGNCRMCLVEVEKFPKPVASCATPVTDGMKISTNSEKVKKAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 128 EGVMEFLLANHPLDCPICDQGGECDLQDQSMMFGNDRSRFLEGKRAVEDKNIGPLVKTIMTRCIQCTRCIRFASEIAGVD 207
Cdd:TIGR01973 81 EGVMEFLLINHPLDCPICDQGGECDLQDQAVMYGSDRSRFREKKRTVENKYLGPLIKTEMTRCIHCTRCVRFANEVAGVE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 208 DLGTTGRGNDMQVGTYIEKMFMSELSGNIIDICPVGALTSKPYAFTARPWETRKTESIDVMDAVGSNIVVSTRTGEVMRI 287
Cdd:TIGR01973 161 DLGVIGRGNNVEIGTYEGKTLESELSGNLIDICPVGALTSKPYAFKARPWELKSTPSICVHDSVGCNIRVDERNGEIMRI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 288 LPRMHEDINEEWISDKTRFAYDGLKRQ-RLTEPMVRNEKGLLTYTSWEDALSRVAGMLQSfqGKDVAAIAGGLVDAEALV 366
Cdd:TIGR01973 241 LPRENDEINEEWLCDKGRFGYDGLNRQdRLTKPLLRNQEGNLLEVSWAEALAIAAEKLKA--SSRIGGIAGPRSSLEELF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 367 ALKDLLNRVDSDTLCTEEVFPTAGAgTDLRSNYLLNTTIAGVEEADVVLLVGTNPRFEAPLFNARIRKSWLHNDLKVALI 446
Cdd:TIGR01973 319 ALKKLVRKLGSENFDLRIRNYEFES-ADLRANYLFNTTLADIEEADLVLLVGADLRQEAPLLNLRLRKAVKKGGAKVALI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 447 G-SPVDLTY-----TYDHLGDSPKILQDIASGSHP-FSQVLKEAKKPMVVLGSSALQRNDGAAILAAVSSIAQKIRMtsg 519
Cdd:TIGR01973 398 GiEKWNLTYpantnLVFHPGLSPKKLDDIASGAHSdIAAALKAAKKPLIIVGDSAISHLDGAALISAAANIAKVIKV--- 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 520 VTGDWKVMNILHRIASQVAALDLGYKP--GVEAIRKNPPKVLFLLGADGG----CITRQDLPK-DCFIIYQGHHGDVGAP 592
Cdd:TIGR01973 475 RRKEWNGLNILSSGANSVGLLDLGGEStgLDAALNLGAADALFLLGADLEraldKTARDALSKaDAFIIYQGHHGTETAE 554
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 316983160 593 IADVILPGAAYTEKSATYVNTEGRAQQTKVAVTPPGLAREDWKIIRAL 640
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 ... |
263-644 |
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: 704.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 263 ESIDVMDAVGSNIVVSTRTGEVMRILPRMHEDINEEWISDKTRFAYDGLKRQRLTEPMVRNEkGLLTYTSWEDALSRVAG 342
Cdd:cd02773 1 ESIDVLDAVGSNIRVDTRGGEVMRILPRLNEDINEEWISDKTRFAYDGLKRQRLDKPYIRKN-GKLKPATWEEALAAIAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 343 MLQSFQGKDVAAIAGGLVDAEALVALKDLLNRVDSDTLCTEEVFPTAGAgtDLRSNYLLNTTIAGVEEADVVLLVGTNPR 422
Cdd:cd02773 80 ALKGVKPDEIAAIAGDLADVESMVALKDLLNKLGSENLACEQDGPDLPA--DLRSNYLFNTTIAGIEEADAVLLVGTNPR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 423 FEAPLFNARIRKSWLHNDLKVALIGSPVDLTYTYDHLGDSPKILQDIASGSHPFSQVLKEAKKPMVVLGSSALQRNDGAA 502
Cdd:cd02773 158 FEAPVLNARIRKAWLHGGLKVGVIGPPVDLTYDYDHLGTDAKTLQDIASGKHPFSKALKDAKKPMIIVGSGALARKDGAA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 503 ILAAVSSIAQKIRMtsgVTGDWKVMNILHRIASQVAALDLGYKPGVEAIRK-NPPKVLFLLGADGGCITRQdlPKDCFII 581
Cdd:cd02773 238 ILAAVAKLAKKNGV---VREGWNGFNVLHRAASRVGALDLGFVPGAGAIRKsGPPKVLYLLGADEIDITPI--PKDAFVV 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 316983160 582 YQGHHGDVGAPIADVILPGAAYTEKSATYVNTEGRAQQTKVAVTPPGLAREDWKIIRALSEIA 644
Cdd:cd02773 313 YQGHHGDRGAQIADVILPGAAYTEKSGTYVNTEGRVQQTRKAVSPPGDAREDWKILRALSEVL 375
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
45-672 |
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: 610.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 45 LIEVFVDGQSVMVEPGTTVLQACEKVGMQIPRFCYHERLSVAGNCRMCLVEIEKAPKVVAACAMPVMKGWNILTNSEKSK 124
Cdd:COG1034 1 MVTITIDGKEVEVPKGTTVLQAAEKAGIEIPRFCYHPKLSIAGACRMCLVEVEGAPKPVASCATPVTDGMVVKTDSPKVK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 125 KAREGVMEFLLANHPLDCPICDQGGECDLQDQSMMFGNDRSRFLEGKRAVEDKNIGPLVKTIMTRCIQCTRCIRFASEIA 204
Cdd:COG1034 81 KARKGVMEFLLINHPLDCPICDQGGECDLQDQAMEYGVDESRYEEEKRTVPKKDLGPLILLDMNRCILCTRCVRFCDEIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 205 GVDDLGTTGRGNDMQVGTYIEKMFMSELSGNIIDICPVGALTSKPYAFTARPWETRKTESIDVMDAVGSNIVVSTRTGEV 284
Cdd:COG1034 161 GDPELGVIGRGEHSEIGTYLGKPLDSEFSGNCIDVCPVGALTSKPFRFKARPWELKKTPSICPHCSVGCNIRVDVRGGKV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 285 MRILPRMHEDINEEWISDKTRFAYDGLKR-QRLTEPMVRNEkGLLTYTSWEDALSRVAGMLQSfqgkdvaaiaggLVDAE 363
Cdd:COG1034 241 YRVLPRENEAVNEEWLCDKGRFGYDGLNSpDRLTRPLVRKD-GELVEASWEEALAAAAEGLKA------------LKKAE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 364 alvalkdllNRVdsdtlcteevfptagagtdlrsnyllnttiagveeadvvllvgtnprfeaplfnarirkswlhndlkv 443
Cdd:COG1034 308 ---------NSV-------------------------------------------------------------------- 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 444 aligspvdltytydhlgdspkilqdiasgshpfsqvlkeakkpmvvlgssalqrndGAAILAAVSSIAQkirmtsgvtgd 523
Cdd:COG1034 311 --------------------------------------------------------GAALLGALPDAAA----------- 323
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 524 wkvmnILhriasqvaaldlgykpgvEAIRKNPPKVLFLLGAD----GGCITRQDLPKDCFIIYQGHHGDVGAPIADVILP 599
Cdd:COG1034 324 -----IL------------------EAAEAGKLKALVLLGADpydlDPAAALAALAKADFVVVLDHFGSATAERADVVLP 380
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 316983160 600 GAAYTEKSATYVNTEGRAQQTKVAVTPPGLAREDWKIIRALSEIAGMTLPYDTLDQVRNRLEEVSPNLVRYDD 672
Cdd:COG1034 381 AAAFAEKSGTFVNLEGRVQRFNAAVPPPGEARPDWRVLRALANALGAGLPYDSLEEVRAELAAEAPATVSAEG 453
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
315-642 |
1.05e-129 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 389.07 E-value: 1.05e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 315 RLTEPMVRNEKGLLTYTSWEDALSRVAGMLQSFQGK------DVAAIAGGLVDAEALVALKDLLNRVDSDTLCTEEVF-- 386
Cdd:pfam00384 1 RLKYPMVRRGDGKFVRVSWDEALDLIAKKLKRIIKKygpdaiAINGGSGGLTDVESLYALKKLLNRLGSKNGNTEDHNgd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 387 ----PTAGAGTDLRSNYLLNTTIAGVEEADVVLLVGTNPRFEAPLFNARIRKSWLHNDLKVALIGSPVDLTYTYDHLGDS 462
Cdd:pfam00384 81 lctaAAAAFGSDLRSNYLFNSSIADIENADLILLIGTNPREEAPILNARIRKAALKGKAKVIVIGPRLDLTYADEHLGIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 463 PKILQDI-ASGSHPFSQVLKEAK----KPMVVLGSSALQRNDGAAILAAVSSIAQKIRMTSGVTGDWKVMNILHRIASQV 537
Cdd:pfam00384 161 PGTDLALaLAGAHVFIKELKKDKdfapKPIIIVGAGVLQRQDGEAIFRAIANLADLTGNIGRPGGGWNGLNILQGAASPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 538 AALDLGYKPGV------EAIRKNPPKVLFLLG-------ADGGCITRQDLPKDCFIIYQGHHGDVGAPIADVILPGAAYT 604
Cdd:pfam00384 241 GALDLGLVPGIksvemiNAIKKGGIKVLYLLGnnpfvthADENRVVKALQKLDLFVVYDGHHGDKTAKYADVILPAAAYT 320
|
330 340 350
....*....|....*....|....*....|....*...
gi 316983160 605 EKSATYVNTEGRAQQTKVAVTPPGLAREDWKIIRALSE 642
Cdd:pfam00384 321 EKNGTYVNTEGRVQSTKQAVPPPGEAREDWKILRALSE 358
|
|
| PRK07860 |
PRK07860 |
NADH dehydrogenase subunit G; Validated |
42-665 |
2.27e-108 |
|
NADH dehydrogenase subunit G; Validated
Pssm-ID: 236118 [Multi-domain] Cd Length: 797 Bit Score: 348.09 E-value: 2.27e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 42 ASNLIEVFVDGQSVMVEPGTTVLQACEKVGMQIPRFCYHERLSVAGNCRMCLVEIEKAPKVVAACAMPVMKGWNILT--N 119
Cdd:PRK07860 1 PPDLVTLTIDGVEVSVPKGTLVIRAAELLGIQIPRFCDHPLLDPVGACRQCLVEVEGQRKPQASCTTTVTDGMVVKTqlT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 120 SEKSKKAREGVMEFLLANHPLDCPICDQGGECDLQDQSMMFGNDRSRFLEGKRAVEdKNIgPLVKTIM---TRCIQCTRC 196
Cdd:PRK07860 81 SPVADKAQHGVMELLLINHPLDCPVCDKGGECPLQNQAMSNGRAESRFTDVKRTFP-KPI-NISTQVLldrERCVLCARC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 197 IRFASEIAGVDDLGTTGRGNDMQVGTYIEKMFMSELSGNIIDICPVGALTSKPYAFTARPWETRKTESIDVMDAVGSNIV 276
Cdd:PRK07860 159 TRFSDQIAGDPFIDLQERGALQQVGIYEGEPFQSYFSGNTVQICPVGALTGAAYRFRARPFDLVSTPSVCEHCASGCAQR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 277 VSTRTGEVMRILPRMHEDINEEWISDKTRFAYD-GLKRQRLTEPMVRNEKGLLTYTSWEDALSRVAGMLQSFQGkDVAAI 355
Cdd:PRK07860 239 TDHRRGKVLRRLAGDDPEVNEEWNCDKGRWAFTyATQPDRITTPLVRDEDGELEPASWSEALAVAARGLAAARG-RVGVL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 356 AGGLVDAE--------ALVALK----DLLNRVDSDtlcTEEVFPTAG-AGTDlrsnylLNTTIAGVEEADVVLLVGTNPR 422
Cdd:PRK07860 318 VGGRLTVEdayayakfARVALGtndiDFRARPHSA---EEADFLAARvAGRG------LGVTYADLEKAPAVLLVGFEPE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 423 FEAPLFNARIRKSWLHNDLKVALIGSPVD--LTYTYDHL-----GDSPKILQDIASGSHPFSQVLKEAKKpmVVLGSSAL 495
Cdd:PRK07860 389 EESPIVFLRLRKAARKHGLKVYSIAPFATrgLEKMGGTLlrtapGGEAAALDALATGAPDVAELLRTPGA--VILVGERL 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 496 QRNDGAaiLAAVSSIAQkirmTSGVTGDWkvmniLHRIASQVAALDLGYKP----------------------GVEAIRK 553
Cdd:PRK07860 467 ATVPGA--LSAAARLAD----ATGARLAW-----VPRRAGERGALEAGALPtllpggrpvadpaaraevaaawGVDELPA 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 554 NPpkvlfllGADGGCITR-----------------QDLPK-----------DCFIIYQGHHGDVgAPIADVILPGAAYTE 605
Cdd:PRK07860 536 AP-------GRDTAGILAaaaagelgallvggvepADLPDpaaalaaldaaGFVVSLELRHSAV-TERADVVLPVAPVAE 607
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 606 KSATYVNTEGRAQQTKVAVTPPGlAREDWKIIRALSEIAGMTLPYDTLDQVRNRLEEVSP 665
Cdd:PRK07860 608 KAGTFLNWEGRLRPFEAALRTTG-ALSDLRVLDALADEMGVDLGLPTVAAARAELARLGA 666
|
|
| NADH-G_4Fe-4S_3 |
smart00929 |
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region; |
127-167 |
1.12e-17 |
|
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region;
Pssm-ID: 214918 [Multi-domain] Cd Length: 41 Bit Score: 76.85 E-value: 1.12e-17
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 316983160 127 REGVMEFLLANHPLDCPICDQGGECDLQDQSMMFGNDRSRF 167
Cdd:smart00929 1 RKTILELLLANHPLDCPVCDKNGECELQDLAYELGVDEQRY 41
|
|
| NADH_dhqG_C |
pfam09326 |
NADH-ubiquinone oxidoreductase subunit G, C-terminal; Members of this family of are found at ... |
682-724 |
2.73e-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: 2.73e-11
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 316983160 682 ANELSKLVNQ-QLLADPLVPPqltIKDFYMTDSISRASQTMAKC 724
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 ... |
48-640 |
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: 912.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 48 VFVDGQSVMVEPGTTVLQACEKVGMQIPRFCYHERLSVAGNCRMCLVEIEKAPKVVAACAMPVMKGWNILTNSEKSKKAR 127
Cdd:TIGR01973 1 IFIDGKELEVPKGTTVLQACLSAGIEIPRFCYHEKLSIAGNCRMCLVEVEKFPKPVASCATPVTDGMKISTNSEKVKKAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 128 EGVMEFLLANHPLDCPICDQGGECDLQDQSMMFGNDRSRFLEGKRAVEDKNIGPLVKTIMTRCIQCTRCIRFASEIAGVD 207
Cdd:TIGR01973 81 EGVMEFLLINHPLDCPICDQGGECDLQDQAVMYGSDRSRFREKKRTVENKYLGPLIKTEMTRCIHCTRCVRFANEVAGVE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 208 DLGTTGRGNDMQVGTYIEKMFMSELSGNIIDICPVGALTSKPYAFTARPWETRKTESIDVMDAVGSNIVVSTRTGEVMRI 287
Cdd:TIGR01973 161 DLGVIGRGNNVEIGTYEGKTLESELSGNLIDICPVGALTSKPYAFKARPWELKSTPSICVHDSVGCNIRVDERNGEIMRI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 288 LPRMHEDINEEWISDKTRFAYDGLKRQ-RLTEPMVRNEKGLLTYTSWEDALSRVAGMLQSfqGKDVAAIAGGLVDAEALV 366
Cdd:TIGR01973 241 LPRENDEINEEWLCDKGRFGYDGLNRQdRLTKPLLRNQEGNLLEVSWAEALAIAAEKLKA--SSRIGGIAGPRSSLEELF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 367 ALKDLLNRVDSDTLCTEEVFPTAGAgTDLRSNYLLNTTIAGVEEADVVLLVGTNPRFEAPLFNARIRKSWLHNDLKVALI 446
Cdd:TIGR01973 319 ALKKLVRKLGSENFDLRIRNYEFES-ADLRANYLFNTTLADIEEADLVLLVGADLRQEAPLLNLRLRKAVKKGGAKVALI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 447 G-SPVDLTY-----TYDHLGDSPKILQDIASGSHP-FSQVLKEAKKPMVVLGSSALQRNDGAAILAAVSSIAQKIRMtsg 519
Cdd:TIGR01973 398 GiEKWNLTYpantnLVFHPGLSPKKLDDIASGAHSdIAAALKAAKKPLIIVGDSAISHLDGAALISAAANIAKVIKV--- 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 520 VTGDWKVMNILHRIASQVAALDLGYKP--GVEAIRKNPPKVLFLLGADGG----CITRQDLPK-DCFIIYQGHHGDVGAP 592
Cdd:TIGR01973 475 RRKEWNGLNILSSGANSVGLLDLGGEStgLDAALNLGAADALFLLGADLEraldKTARDALSKaDAFIIYQGHHGTETAE 554
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 316983160 593 IADVILPGAAYTEKSATYVNTEGRAQQTKVAVTPPGLAREDWKIIRAL 640
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 ... |
263-644 |
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: 704.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 263 ESIDVMDAVGSNIVVSTRTGEVMRILPRMHEDINEEWISDKTRFAYDGLKRQRLTEPMVRNEkGLLTYTSWEDALSRVAG 342
Cdd:cd02773 1 ESIDVLDAVGSNIRVDTRGGEVMRILPRLNEDINEEWISDKTRFAYDGLKRQRLDKPYIRKN-GKLKPATWEEALAAIAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 343 MLQSFQGKDVAAIAGGLVDAEALVALKDLLNRVDSDTLCTEEVFPTAGAgtDLRSNYLLNTTIAGVEEADVVLLVGTNPR 422
Cdd:cd02773 80 ALKGVKPDEIAAIAGDLADVESMVALKDLLNKLGSENLACEQDGPDLPA--DLRSNYLFNTTIAGIEEADAVLLVGTNPR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 423 FEAPLFNARIRKSWLHNDLKVALIGSPVDLTYTYDHLGDSPKILQDIASGSHPFSQVLKEAKKPMVVLGSSALQRNDGAA 502
Cdd:cd02773 158 FEAPVLNARIRKAWLHGGLKVGVIGPPVDLTYDYDHLGTDAKTLQDIASGKHPFSKALKDAKKPMIIVGSGALARKDGAA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 503 ILAAVSSIAQKIRMtsgVTGDWKVMNILHRIASQVAALDLGYKPGVEAIRK-NPPKVLFLLGADGGCITRQdlPKDCFII 581
Cdd:cd02773 238 ILAAVAKLAKKNGV---VREGWNGFNVLHRAASRVGALDLGFVPGAGAIRKsGPPKVLYLLGADEIDITPI--PKDAFVV 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 316983160 582 YQGHHGDVGAPIADVILPGAAYTEKSATYVNTEGRAQQTKVAVTPPGLAREDWKIIRALSEIA 644
Cdd:cd02773 313 YQGHHGDRGAQIADVILPGAAYTEKSGTYVNTEGRVQQTRKAVSPPGDAREDWKILRALSEVL 375
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
45-672 |
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: 610.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 45 LIEVFVDGQSVMVEPGTTVLQACEKVGMQIPRFCYHERLSVAGNCRMCLVEIEKAPKVVAACAMPVMKGWNILTNSEKSK 124
Cdd:COG1034 1 MVTITIDGKEVEVPKGTTVLQAAEKAGIEIPRFCYHPKLSIAGACRMCLVEVEGAPKPVASCATPVTDGMVVKTDSPKVK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 125 KAREGVMEFLLANHPLDCPICDQGGECDLQDQSMMFGNDRSRFLEGKRAVEDKNIGPLVKTIMTRCIQCTRCIRFASEIA 204
Cdd:COG1034 81 KARKGVMEFLLINHPLDCPICDQGGECDLQDQAMEYGVDESRYEEEKRTVPKKDLGPLILLDMNRCILCTRCVRFCDEIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 205 GVDDLGTTGRGNDMQVGTYIEKMFMSELSGNIIDICPVGALTSKPYAFTARPWETRKTESIDVMDAVGSNIVVSTRTGEV 284
Cdd:COG1034 161 GDPELGVIGRGEHSEIGTYLGKPLDSEFSGNCIDVCPVGALTSKPFRFKARPWELKKTPSICPHCSVGCNIRVDVRGGKV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 285 MRILPRMHEDINEEWISDKTRFAYDGLKR-QRLTEPMVRNEkGLLTYTSWEDALSRVAGMLQSfqgkdvaaiaggLVDAE 363
Cdd:COG1034 241 YRVLPRENEAVNEEWLCDKGRFGYDGLNSpDRLTRPLVRKD-GELVEASWEEALAAAAEGLKA------------LKKAE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 364 alvalkdllNRVdsdtlcteevfptagagtdlrsnyllnttiagveeadvvllvgtnprfeaplfnarirkswlhndlkv 443
Cdd:COG1034 308 ---------NSV-------------------------------------------------------------------- 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 444 aligspvdltytydhlgdspkilqdiasgshpfsqvlkeakkpmvvlgssalqrndGAAILAAVSSIAQkirmtsgvtgd 523
Cdd:COG1034 311 --------------------------------------------------------GAALLGALPDAAA----------- 323
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 524 wkvmnILhriasqvaaldlgykpgvEAIRKNPPKVLFLLGAD----GGCITRQDLPKDCFIIYQGHHGDVGAPIADVILP 599
Cdd:COG1034 324 -----IL------------------EAAEAGKLKALVLLGADpydlDPAAALAALAKADFVVVLDHFGSATAERADVVLP 380
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 316983160 600 GAAYTEKSATYVNTEGRAQQTKVAVTPPGLAREDWKIIRALSEIAGMTLPYDTLDQVRNRLEEVSPNLVRYDD 672
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 ... |
263-643 |
2.30e-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: 2.30e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 263 ESIDVMDAVGSNIVVSTRTGEVMRILPRMHEDINEEWISDKTRFAYDGLK-RQRLTEPMVRNEkGLLTYTSWEDALSRVA 341
Cdd:cd02768 1 ESIDVHDALGSNIRVDVRGGEVMRILPRENEAINEEWISDKGRFGYDGLNsRQRLTQPLIKKG-GKLVPVSWEEALKTVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 342 GMLQSFQGKDVAAIAGGLVDAEALVALKDLLNRVDSDTLCTEEVFPTAGAGTDLRSNYLLNTTIAGVEEADVVLLVGTNP 421
Cdd:cd02768 80 EGLKAVKGDKIGGIAGPRADLESLFLLKKLLNKLGSNNIDHRLRQSDLPADNRLRGNYLFNTSIAEIEEADAVLLIGSNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 422 RFEAPLFNARIRKSWLHNDLKVALIGS-----PVDLTYTYDHLGDSPKILQDIASGSH--PFSQVLKEAKKPMVVLGSSA 494
Cdd:cd02768 160 RKEAPLLNARLRKAVKKKGAKIAVIGPkdtdlIADLTYPVSPLGASLATLLDIAEGKHlkPFAKSLKKAKKPLIILGSSA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 495 LqRNDGAAILAAVSSIAQKIRMtsgVTGDWKVMNILHRIASQVAA--LDLGYKPGVEAIRKnppkvLFLLGADGGCITRQ 572
Cdd:cd02768 240 L-RKDGAAILKALANLAAKLGT---GAGLWNGLNVLNSVGARLGGagLDAGLALLEPGKAK-----LLLLGEDELDRSNP 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 316983160 573 DL-----PKDCFIIYQGHHGDVGAPiADVILPGAAYTEKSATYVNTEGRAQQTKVAVTPPGLAREDWKIIRALSEI 643
Cdd:cd02768 311 PAavalaAADAFVVYQGHHGDTGAQ-ADVILPAAAFTEKSGTYVNTEGRVQRFKKAVSPPGDAREDWKILRALSNL 385
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
315-642 |
1.05e-129 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 389.07 E-value: 1.05e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 315 RLTEPMVRNEKGLLTYTSWEDALSRVAGMLQSFQGK------DVAAIAGGLVDAEALVALKDLLNRVDSDTLCTEEVF-- 386
Cdd:pfam00384 1 RLKYPMVRRGDGKFVRVSWDEALDLIAKKLKRIIKKygpdaiAINGGSGGLTDVESLYALKKLLNRLGSKNGNTEDHNgd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 387 ----PTAGAGTDLRSNYLLNTTIAGVEEADVVLLVGTNPRFEAPLFNARIRKSWLHNDLKVALIGSPVDLTYTYDHLGDS 462
Cdd:pfam00384 81 lctaAAAAFGSDLRSNYLFNSSIADIENADLILLIGTNPREEAPILNARIRKAALKGKAKVIVIGPRLDLTYADEHLGIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 463 PKILQDI-ASGSHPFSQVLKEAK----KPMVVLGSSALQRNDGAAILAAVSSIAQKIRMTSGVTGDWKVMNILHRIASQV 537
Cdd:pfam00384 161 PGTDLALaLAGAHVFIKELKKDKdfapKPIIIVGAGVLQRQDGEAIFRAIANLADLTGNIGRPGGGWNGLNILQGAASPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 538 AALDLGYKPGV------EAIRKNPPKVLFLLG-------ADGGCITRQDLPKDCFIIYQGHHGDVGAPIADVILPGAAYT 604
Cdd:pfam00384 241 GALDLGLVPGIksvemiNAIKKGGIKVLYLLGnnpfvthADENRVVKALQKLDLFVVYDGHHGDKTAKYADVILPAAAYT 320
|
330 340 350
....*....|....*....|....*....|....*...
gi 316983160 605 EKSATYVNTEGRAQQTKVAVTPPGLAREDWKIIRALSE 642
Cdd:pfam00384 321 EKNGTYVNTEGRVQSTKQAVPPPGEAREDWKILRALSE 358
|
|
| PRK07860 |
PRK07860 |
NADH dehydrogenase subunit G; Validated |
42-665 |
2.27e-108 |
|
NADH dehydrogenase subunit G; Validated
Pssm-ID: 236118 [Multi-domain] Cd Length: 797 Bit Score: 348.09 E-value: 2.27e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 42 ASNLIEVFVDGQSVMVEPGTTVLQACEKVGMQIPRFCYHERLSVAGNCRMCLVEIEKAPKVVAACAMPVMKGWNILT--N 119
Cdd:PRK07860 1 PPDLVTLTIDGVEVSVPKGTLVIRAAELLGIQIPRFCDHPLLDPVGACRQCLVEVEGQRKPQASCTTTVTDGMVVKTqlT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 120 SEKSKKAREGVMEFLLANHPLDCPICDQGGECDLQDQSMMFGNDRSRFLEGKRAVEdKNIgPLVKTIM---TRCIQCTRC 196
Cdd:PRK07860 81 SPVADKAQHGVMELLLINHPLDCPVCDKGGECPLQNQAMSNGRAESRFTDVKRTFP-KPI-NISTQVLldrERCVLCARC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 197 IRFASEIAGVDDLGTTGRGNDMQVGTYIEKMFMSELSGNIIDICPVGALTSKPYAFTARPWETRKTESIDVMDAVGSNIV 276
Cdd:PRK07860 159 TRFSDQIAGDPFIDLQERGALQQVGIYEGEPFQSYFSGNTVQICPVGALTGAAYRFRARPFDLVSTPSVCEHCASGCAQR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 277 VSTRTGEVMRILPRMHEDINEEWISDKTRFAYD-GLKRQRLTEPMVRNEKGLLTYTSWEDALSRVAGMLQSFQGkDVAAI 355
Cdd:PRK07860 239 TDHRRGKVLRRLAGDDPEVNEEWNCDKGRWAFTyATQPDRITTPLVRDEDGELEPASWSEALAVAARGLAAARG-RVGVL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 356 AGGLVDAE--------ALVALK----DLLNRVDSDtlcTEEVFPTAG-AGTDlrsnylLNTTIAGVEEADVVLLVGTNPR 422
Cdd:PRK07860 318 VGGRLTVEdayayakfARVALGtndiDFRARPHSA---EEADFLAARvAGRG------LGVTYADLEKAPAVLLVGFEPE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 423 FEAPLFNARIRKSWLHNDLKVALIGSPVD--LTYTYDHL-----GDSPKILQDIASGSHPFSQVLKEAKKpmVVLGSSAL 495
Cdd:PRK07860 389 EESPIVFLRLRKAARKHGLKVYSIAPFATrgLEKMGGTLlrtapGGEAAALDALATGAPDVAELLRTPGA--VILVGERL 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 496 QRNDGAaiLAAVSSIAQkirmTSGVTGDWkvmniLHRIASQVAALDLGYKP----------------------GVEAIRK 553
Cdd:PRK07860 467 ATVPGA--LSAAARLAD----ATGARLAW-----VPRRAGERGALEAGALPtllpggrpvadpaaraevaaawGVDELPA 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 554 NPpkvlfllGADGGCITR-----------------QDLPK-----------DCFIIYQGHHGDVgAPIADVILPGAAYTE 605
Cdd:PRK07860 536 AP-------GRDTAGILAaaaagelgallvggvepADLPDpaaalaaldaaGFVVSLELRHSAV-TERADVVLPVAPVAE 607
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 606 KSATYVNTEGRAQQTKVAVTPPGlAREDWKIIRALSEIAGMTLPYDTLDQVRNRLEEVSP 665
Cdd:PRK07860 608 KAGTFLNWEGRLRPFEAALRTTG-ALSDLRVLDALADEMGVDLGLPTVAAARAELARLGA 666
|
|
| MopB_Res-Cmplx1_Nad11-M |
cd02774 |
MopB_Res_Cmplx1_Nad11_M: Mitochondrial-encoded NADH-quinone oxidoreductase/respiratory complex ... |
263-640 |
1.45e-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: 1.45e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 263 ESIDVMDAVGSNIVVSTRTGEVMRILPRMHEDINEEWISDKTRFAYDGLKRQRLTEPMVRNEKGLLTYTSWEDALSRVAG 342
Cdd:cd02774 1 ESIDVLDSLGSNIRVDIKGNEILRILPKINDELNEEWISDKIRFSYDSLKYQRIKTPLLKLSNNSFLEIGWKTAFKFLNK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 343 MLQSFQGKDVAAIAGGLVDAEALVALKDLLNRVDSDTLCTEEVFPTAGAGTDLRSNYLLNTTIAGVEEADVVLLVGTNPR 422
Cdd:cd02774 81 FILLKKFSKLNFIIGSKIDLETLFYYKKLLNKLGSLNTNSNNFLENNNYFNLDLENYLFNNSLKNLDKSDLCLLIGSNLR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 423 FEAPLFNARIRKSWLHNDLKVALIGSPVDLTYTYDHLGDSPKILQDIASGSHPFSQVLKEAKKPMVVLGSSALQRNDGaa 502
Cdd:cd02774 161 VESPILNIRLRNRYNKGNKKIFVIGNKFDTTYPSKHIGLSLNTLLKILEGKHLFCKQLKKSKKPLIIIGSSFSLRKNY-- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 503 ilaavSSIAQKIRMTSGVTGDwkVMNILHRIASQVAALDLgYKPGVEAIRKnpPKVLFLLGADggciTRQDLPKDCFIIY 582
Cdd:cd02774 239 -----SFIISKLKNFSSNNEN--NFNFLNIISNSLYYLGI-KKFNSNNKKN--LSNLYYIKET----NFQKFNKNNFVIY 304
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 316983160 583 QGHHGDVGAPIADVILPGAAYTEKSATYVNTEGRAQQTKVAVTPPGLAREDWKIIRAL 640
Cdd:cd02774 305 QGHHFLNLANNSNLILPSKTFFEKEALYLNLEGILQKTKKILSFKENIKSDDNIIFSL 362
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
263-642 |
1.05e-66 |
|
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: 224.90 E-value: 1.05e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 263 ESIDVMDAVGSNIVVSTRTGEVMRILPRMHEDINEEWISDKTRFAYDGLK-RQRLTEPMVR-NEKGLLTYTSWEDALSRV 340
Cdd:cd00368 1 PSVCPFCGVGCGILVYVKDGKVVRIEGDPNHPVNEGRLCDKGRAGLDGLYsPDRLKYPLIRvGGRGKFVPISWDEALDEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 341 AGMLQSFQGKD----VAAIAGGLVDAEALVALKDLLNRVDSDTLCTEEVFPTAGAGTDLR--SNYLLNTTIAGVEEADVV 414
Cdd:cd00368 81 AEKLKEIREKYgpdaIAFYGGGGASNEEAYLLQKLLRALGSNNVDSHARLCHASAVAALKafGGGAPTNTLADIENADLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 415 LLVGTNPRFEAPLFNARIRKSWLhNDLKVALIGSPVDLTYTYDHLGDSPKILQDIAsgshpfsqvLKEAKKPMVVLGSSA 494
Cdd:cd00368 161 LLWGSNPAETHPVLAARLRRAKK-RGAKLIVIDPRRTETAAKADEWLPIRPGTDAA---------LALAEWAAEITGVPA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 495 lqrndgAAILAAVSSIAQK----IRMTSGVT----GDWKVMNILhriasqVAALDLGY--KPGVEAIRKNPPkvlFLLGA 564
Cdd:cd00368 231 ------ETIRALAREFAAAkravILWGMGLTqhtnGTQNVRAIA------NLAALTGNigRPGGGLGPGGNP---LVSAP 295
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 316983160 565 DGGCITRQDLPKDCFIIYQGHHGDVGApIADVILPGAAYTEKSATYVNTEGRAQQTKVAVTPPGLAREDWKIIRALSE 642
Cdd:cd00368 296 DANRVRAALKKLDFVVVIDIFMTETAA-YADVVLPAATYLEKEGTYTNTEGRVQLFRQAVEPPGEARSDWEILRELAK 372
|
|
| PTZ00305 |
PTZ00305 |
NADH:ubiquinone oxidoreductase; Provisional |
48-245 |
1.95e-56 |
|
NADH:ubiquinone oxidoreductase; Provisional
Pssm-ID: 140326 [Multi-domain] Cd Length: 297 Bit Score: 194.87 E-value: 1.95e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 48 VFVDGQSVMVEPGT-TVLQACEKVGMQIPRFCYHERLSVAGNCRMCLVEIEKAPKVVAACAMPVMKGWNILTNSEKSKKA 126
Cdd:PTZ00305 71 MFVNKRPVEIIPQEeNLLEVLEREGIRVPKFCYHPILSVAGNCRMCLVQVDGTQNLVVSCATVALPGMSIITDSRLVRDA 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 127 REGVMEFLLANHPLDCPICDQGGECDLQDQSMMFGNDRSRFLEGKRAVEDKNIGPLVKTIMTRCIQCTRCIRFASEIAGV 206
Cdd:PTZ00305 151 REGNVELILINHPNDCPICEQATNCDLQNVSMNYGTDIPRYKEDKRAVQDFYFDPQTRVVLNRCIHCTRCVRFLNEHAQD 230
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 316983160 207 DDLGTTGRGNDMQVGTYIEKM-FMSELSGNIIDICPVGAL 245
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 ... |
264-640 |
2.86e-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: 2.86e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 264 SIDVMDAVGSNIVVSTRTGEVMRILPRMHEDINEEWISDKTRFAYDGLKRQ-RLTEPMVRnEKGLLTYTSWEDALSRVAG 342
Cdd:cd02772 2 SVSPHDALGSNLVVHVKNNKVMRVVPRENEAINECWLSDRDRFSYEGLNSEdRLTKPMIK-KDGQWQEVDWETALEYVAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 343 MLQSFQGKDVAAIAGGLVDA----EALVALKDLLNRVDSDTLCTEEVFPTAGAGTDLRSNYLLNTTIAGVEEADVVLLVG 418
Cdd:cd02772 81 GLSAIIKKHGADQIGALASPhstlEELYLLQKLARGLGSDNIDHRLRQSDFRDDAKASGAPWLGMPIAEISELDRVLVIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 419 TNPRFEAPLFNARIRKSW---------------LHNDLKVALIGSPVDLTYT--------YDHLGDSPKILQDIASGSHP 475
Cdd:cd02772 161 SNLRKEHPLLAQRLRQAVkkgaklsainpadddFLFPLSGKAIVAPSALANAlaqvakalAEEKGLAVPDEDAKVEASEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 476 FSQV---LKEAKKPMVVLGSSALQRNDGAAILAAVSSIAQkirmTSGVTGdwkvmNILHRIASQVAALDLGYKPGV---- 548
Cdd:cd02772 241 ARKIaasLVSAERAAVFLGNLAQNHPQAATLRALAQEIAK----LTGATL-----GVLGEGANSVGAYLAGALPHGglna 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 549 EAIRKNPPKVLFLLGA------DGGCITRQDLPKDCFIIYQGHHGDVGA-PIADVILPGAAYTEKSATYVNTEGRAQQTK 621
Cdd:cd02772 312 AAMLEQPRKAYLLLNVepeldcANPAQALAALNQAEFVVALSAFASAALlDYADVLLPIAPFTETSGTFVNLEGRVQSFK 391
|
410
....*....|....*....
gi 316983160 622 VAVTPPGLAREDWKIIRAL 640
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 ... |
270-641 |
3.09e-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: 145.61 E-value: 3.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 270 AVGSNIVVSTRTGEVMRILPRMHEDINEEWISDKTRFAYDGLK-RQRLTEPMVRNeKGLLTYTSWEDALSRVAGMLQSFQ 348
Cdd:cd02771 8 SVGCNISLGERYGELRRVENRYNGAVNHYFLCDRGRFGYGYVNsRDRLTQPLIRR-GGTLVPVSWNEALDVAAARLKEAK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 349 GKdVAAIAGGLVDAEALVALKDLL------NRVDSDTLcteevfptAGAGTDLRSNYLLNTTIAGVEEADVVLLVGTNPR 422
Cdd:cd02771 87 DK-VGGIGSPRASNESNYALQKLVgavlgtNNVDHRAR--------RLIAEILRNGPIYIPSLRDIESADAVLVLGEDLT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 423 FEAPLFNARIRKSWLHNDLK-VALIGSPVDLTYTYDHLGDSPKI-----------LQDIA-------------------- 470
Cdd:cd02771 158 QTAPRIALALRQAARRKAVElAALSGIPKWQDAAVRNIAQGAKSplfivnalatrLDDIAaesiraspggqarlgaalar 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 471 ---------SGSHPFS------QVLKEAKKPMVVLGSSALqrndGAAILAAVSSIAQKIRMTSGVTGdwkVMNILHRIAS 535
Cdd:cd02771 238 avdasaagvSGLAPKEkaariaARLTGAKKPLIVSGTLSG----SLELIKAAANLAKALKRRGENAG---LTLAVEEGNS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 536 QVAAL--DLGYKPG------VEAIRKNPPKVLFLLGAD-------GGCitRQDLPKDCFIIYQGHHGDVGAPIADVILPG 600
Cdd:cd02771 311 PGLLLlgGHVTEPGldldgaLAALEDGSADALIVLGNDlyrsapeRRV--EAALDAAEFVVVLDHFLTETAERADVVLPA 388
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 316983160 601 AAYTEKSATYVNTEGRAQQ-TKVAVTPPGLAREDWKIIRALS 641
Cdd:cd02771 389 ASFAEKSGTFVNYEGRAQRfFKAYDDPAGDARSDWRWLHALA 430
|
|
| PRK07569 |
PRK07569 |
bidirectional hydrogenase complex protein HoxU; Validated |
50-248 |
9.20e-37 |
|
bidirectional hydrogenase complex protein HoxU; Validated
Pssm-ID: 181037 [Multi-domain] Cd Length: 234 Bit Score: 137.86 E-value: 9.20e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 50 VDGQSVMVEPGTTVLQACEKVGMQIPRFCYHERLSVAGNCRMCLVEIEKAPKVVAACAMPVMKGWNILTNSEKSKKAREG 129
Cdd:PRK07569 8 IDDQLVSAREGETLLEAAREAGIPIPTLCHLDGLSDVGACRLCLVEIEGSNKLLPACVTPVAEGMVVQTNTPRLQEYRRM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 130 VMEFLLA--NHPldCPICDQGGECDLQDQSMMFGNDRSRF--LEGKRAVE--------DKNigplvktimtRCIQCTRCI 197
Cdd:PRK07569 88 IVELLFAegNHV--CAVCVANGNCELQDLAIEVGMDHVRFpyLFPRRPVDishprfgiDHN----------RCVLCTRCV 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 316983160 198 RFASEIAGVDDLGTTGRGNDMQVGTYIEKMFMSELS----GNIIDICPVGALTSK 248
Cdd:PRK07569 156 RVCDEIEGAHTWDVAGRGAKSRVITDLNQPWGTSETctscGKCVQACPTGAIFRK 210
|
|
| PRK08493 |
PRK08493 |
NADH-quinone oxidoreductase subunit G; |
45-309 |
1.61e-36 |
|
NADH-quinone oxidoreductase subunit G;
Pssm-ID: 236277 [Multi-domain] Cd Length: 819 Bit Score: 147.54 E-value: 1.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 45 LIEVFVDGQSVMVEPGTTVLQACEKVGMQIPRFCYHERLSVAGNCRMCLVEIEKapKVVAACAMPVMKGWNILTNSEKSK 124
Cdd:PRK08493 1 MITITINGKECEAQEGEYILNVARRNGIFIPAICYLSGCSPTLACRLCMVEADG--KRVYSCNTKAKEGMNILTNTPNLM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 125 KAREGVMEFLLANHPLDCPICDQGGECDLQDQSMMFGNDRSRFlegkrAVEDKNiGPLVKTIMTR-----CIQCTRCIRF 199
Cdd:PRK08493 79 DERNAIMQTYDVNHPLECGVCDKSGECELQNFTHEMGVNHQPY-----AIKDTH-KPHKHWGKINydpslCIVCERCVTV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 200 ASEIAGVDDLGTTGRGNDMQVGTYIEKMFMSELS-----------------------GNIIDICPVGALTSKPYAFTARP 256
Cdd:PRK08493 153 CKDKIGESALKTVPRGLDAPDKSFKESMPKDAYAvwskkqksligpvggetldcsfcGECIAVCPVGALSSSDFQYTSNA 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 316983160 257 WETRKTESIDVMDAVGSNIVVSTR----TGEVMRILpRMHEDINEEWISDKTRFAYD 309
Cdd:PRK08493 233 WELKKIPATCPHCSDCCLIYYDVKhssiLNQESKIY-RVSNDFYFNPLCGAGRFAFD 288
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
270-680 |
6.82e-31 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 129.23 E-value: 6.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 270 AVGSNIVVSTRTGEVMRILPRMHEDINEEWISDKTRFAYDGL-KRQRLTEPMVRnEKGLLTYTSWEDALSRVAGMLQSFQ 348
Cdd:COG3383 15 GVGCGIDLEVKDGKIVKVEGDPDHPVNRGRLCVKGRFGFEFVnSPDRLTTPLIR-RGGEFREVSWDEALDLVAERLREIQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 349 ---GKD-VAAIAGGLVDAEALVALKDLL------NRVDSDT-LCTEevfPTAGA-----GTDLRSNyllntTIAGVEEAD 412
Cdd:COG3383 94 aehGPDaVAFYGSGQLTNEENYLLQKLArgvlgtNNIDNNArLCMA---SAVAGlkqsfGSDAPPN-----SYDDIEEAD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 413 VVLLVGTNPRFEAPLFNARIRKSWLHN-----------------DLKVALI-GSPVDLTYTYDH------LGDSPKI--- 465
Cdd:COG3383 166 VILVIGSNPAEAHPVLARRIKKAKKNGaklivvdprrtetarlaDLHLQIKpGTDLALLNGLLHviieegLVDEDFIaer 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 466 ------LQDIASGSHP----------------FSQVLKEAKKPMVVLGSSALQRNDGAAILAAVSSIAQkirMT------ 517
Cdd:COG3383 246 tegfeeLKASVAKYTPervaeitgvpaedireAARLIAEAKRAMILWGMGVNQHTQGTDNVNAIINLAL---ATgnigrp 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 518 -SGV---TG--------DW-----------KVMNILHRiaSQVAAL----DLGYKPG------VEAIRKNPPKVLFLLG- 563
Cdd:COG3383 323 gTGPfplTGqnnvqggrDMgalpnvlpgyrDVTDPEHR--AKVADAwgvpPLPDKPGltavemFDAIADGEIKALWIIGe 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 564 ------ADGGCItRQDLPKDCFIIYQghhgDV----GAPIADVILPGAAYTEKSATYVNTEGRAQQTKVAVTPPGLARED 633
Cdd:COG3383 401 npavsdPDANHV-REALEKLEFLVVQ----DIflteTAEYADVVLPAASWAEKDGTFTNTERRVQRVRKAVEPPGEARPD 475
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 316983160 634 WKIIRALSEIAGMTLPYDTLDQVRNRLEEVSPNL--VRYDDIEGANYFQ 680
Cdd:COG3383 476 WEIIAELARRLGYGFDYDSPEEVFDEIARLTPDYsgISYERLEALGGVQ 524
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
270-680 |
4.26e-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: 4.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 270 AVGSNIVVSTRTGEVMRILPRMHEDINEEWISDKTRFAYDGLK-RQRLTEPMVRnEKGLLTYTSWEDALSRVAGMLQSFQ 348
Cdd:cd02753 8 GVGCGLELWVKDNKIVGVEPVKGHPVNRGKLCVKGRFGFDFVNsKDRLTKPLIR-KNGKFVEASWDEALSLVASRLKEIK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 349 ---GKD-VAAIAGGLVDAEALVALKDLL------NRVDSDT-LC----TEEVFPTAGAGTDlrSNyllntTIAGVEEADV 413
Cdd:cd02753 87 dkyGPDaIAFFGSAKCTNEENYLFQKLAravggtNNVDHCArLChsptVAGLAETLGSGAM--TN-----SIADIEEADV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 414 VLLVGTNPRFEAPLFNARI---------------------RKSWLHNDLK----VALIGS-------------------- 448
Cdd:cd02753 160 ILVIGSNTTEAHPVIARRIkrakrngaklivadprrtelaRFADLHLQLRpgtdVALLNAmahviieeglydeefieert 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 449 -----------PVDLTYTYDHLGDSPKILQDIAsgshpfsQVLKEAKKPMVVLGSSALQRNDGAAILAAVSSIAQkirmt 517
Cdd:cd02753 240 egfeelkeiveKYTPEYAERITGVPAEDIREAA-------RMYATAKSAAILWGMGVTQHSHGTDNVMALSNLAL----- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 518 sgVTGdwkvmNI------LHRIASQ--V-AALDLGYKPGVEairknpP---KVLFLLGADGGCI------TRQDLPKDCF 579
Cdd:cd02753 308 --LTG-----NIgrpgtgVNPLRGQnnVqGACDMGALPNVL------PgyvKALYIMGENPALSdpntnhVRKALESLEF 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 580 IIYQghhgDV----GAPIADVILPGAAYTEKSATYVNTEGRAQQTKVAVTPPGLAREDWKIIRALSEIAGMTLPYDTLDQ 655
Cdd:cd02753 375 LVVQ----DIflteTAELADVVLPAASFAEKDGTFTNTERRVQRVRKAVEPPGEARPDWEIIQELANRLGYPGFYSHPEE 450
|
490 500
....*....|....*....|....*..
gi 316983160 656 VRNRLEEVSPNL--VRYDDIEGANYFQ 680
Cdd:cd02753 451 IFDEIARLTPQYagISYERLERPGGLQ 477
|
|
| NADH-G_4Fe-4S_3 |
smart00929 |
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region; |
127-167 |
1.12e-17 |
|
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region;
Pssm-ID: 214918 [Multi-domain] Cd Length: 41 Bit Score: 76.85 E-value: 1.12e-17
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 316983160 127 REGVMEFLLANHPLDCPICDQGGECDLQDQSMMFGNDRSRF 167
Cdd:smart00929 1 RKTILELLLANHPLDCPVCDKNGECELQDLAYELGVDEQRY 41
|
|
| NADH-G_4Fe-4S_3 |
pfam10588 |
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region; |
127-166 |
2.06e-17 |
|
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region;
Pssm-ID: 463159 [Multi-domain] Cd Length: 40 Bit Score: 75.95 E-value: 2.06e-17
10 20 30 40
....*....|....*....|....*....|....*....|
gi 316983160 127 REGVMEFLLANHPLDCPICDQGGECDLQDQSMMFGNDRSR 166
Cdd:pfam10588 1 RKTILELLLSNHPLDCPTCDKNGNCELQDLAYELGVDEVR 40
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
44-153 |
4.95e-17 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 85.17 E-value: 4.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 44 NLIEVFVDGQSVMVEPGTTVLQACEKVGMQIPRFCYHERLSVAGNCRMCLVEIEKAPKVVAACAMPVMKGWNILTNSEKS 123
Cdd:PRK12814 2 NTISLTINGRSVTAAPGTSILEAAASAGITIPTLCFHQELEATGSCWMCIVEIKGKNRFVPACSTAVSEGMVIETENAEL 81
|
90 100 110
....*....|....*....|....*....|
gi 316983160 124 KKAREGVMEFLLANHPLDCPicdqgGECDL 153
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 ... |
43-121 |
3.30e-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: 71.03 E-value: 3.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 43 SNLIEVFVDGQSVMVEPGTTVLQACEKVGMQIPRFCYHER----LSVAGNCRMCLVEIEKAPKvVAACAMPVMKGWNILT 118
Cdd:pfam13510 1 SRPVTFTFDGRPVTAPEGDTIAAALLANGVRVPRSCKYGRprgiFCAMGECRNCLVEVDGVPN-VRACTTPVREGMVVRT 79
|
...
gi 316983160 119 NSE 121
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 ... |
270-678 |
4.79e-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: 78.81 E-value: 4.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 270 AVGSNIVVSTRTGEVMRILPRMHEDINEEWISDK-TRFAYDGLKRQRLTEPMVRNEKGLLTYTSWEDALSRVAGMLQSFQ 348
Cdd:cd02754 8 GVGCGVEIGVKDGKVVAVRGDPEHPVNRGRLCIKgLNLHKTLNGPERLTRPLLRRNGGELVPVSWDEALDLIAERFKAIQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 349 ---GKD-VAAIAGGLVDAEALVALKDLL------NRVDSDT-LCTEevfpTAGA------GTDLRSNyllntTIAGVEEA 411
Cdd:cd02754 88 aeyGPDsVAFYGSGQLLTEEYYAANKLAkgglgtNNIDTNSrLCMA----SAVAgykrsfGADGPPG-----SYDDIEHA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 412 DVVLLVGTNPRFEAPLFNARIRKSwLHNDLKVALI---------------------GSPVDLTYTYDH-LGDSPKILQD- 468
Cdd:cd02754 159 DCFFLIGSNMAECHPILFRRLLDR-KKANPGAKIIvvdprrtrtadiadlhlpirpGTDLALLNGLLHvLIEEGLIDRDf 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 469 IAS---GSHPFSQVLK--------------------------EAKKPMVVLGSSALQRNDGAAilaAVSSI--------- 510
Cdd:cd02754 238 IDAhteGFEELKAFVAdytpekvaeitgvpeadireaarlfgEARKVMSLWTMGVNQSTQGTA---ANNAIinlhlatgk 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 511 ----------------AQKIRMTSGVT----GDWKVMNILHR--IAS--QVAALDLGYKPGV------EAIRKNPPKVLF 560
Cdd:cd02754 315 igrpgsgpfsltgqpnAMGGREVGGLAnllpGHRSVNNPEHRaeVAKfwGVPEGTIPPKPGLhavemfEAIEDGEIKALW 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 561 LLG-------ADGGCItRQDLPKDCFIIYQ-GHHGDVGAPIADVILPGAAYTEKSATYVNTEGRAQQTKVAVTPPGLARE 632
Cdd:cd02754 395 VMCtnpavslPNANRV-REALERLEFVVVQdAFADTETAEYADLVLPAASWGEKEGTMTNSERRVSLLRAAVEPPGEARP 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 316983160 633 DWKIIRALSEIAGMT--LPYDTLDQVRNRLEEVSPnlVRYDDIEGANY 678
Cdd:cd02754 474 DWWILADVARRLGFGelFPYTSPEEVFEEYRRLSR--GRGADLSGLSY 519
|
|
| NADH_dhqG_C |
pfam09326 |
NADH-ubiquinone oxidoreductase subunit G, C-terminal; Members of this family of are found at ... |
682-724 |
2.73e-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: 2.73e-11
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 316983160 682 ANELSKLVNQ-QLLADPLVPPqltIKDFYMTDSISRASQTMAKC 724
Cdd:pfam09326 1 ALVLALAGAKgKLSGAPLKSP---IEDFYMTDPISRASATMAKC 41
|
|
| fer2 |
cd00207 |
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ... |
46-116 |
4.55e-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: 4.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 46 IEVFVDGQSVMVEPGTTVLQACEKVGMQIPRFCYHerlsvaGNCRMCLVEIEK----------------APKVVAACAMP 109
Cdd:cd00207 3 INVPGSGVEVEVPEGETLLDAAREAGIDIPYSCRA------GACGTCKVEVVEgevdqsdpslldeeeaEGGYVLACQTR 76
|
....*..
gi 316983160 110 VMKGWNI 116
Cdd:cd00207 77 VTDGLVI 83
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
315-680 |
9.82e-09 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 58.70 E-value: 9.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 315 RLTEPMVR-NEKGLLTY--TSWEDALSRVAGMLQSFQGKD----VAAIAGGLVD----------AEALVALKDLLNRVDS 377
Cdd:COG0243 78 RLTYPMKRvGPRGSGKFerISWDEALDLIAEKLKAIIDEYgpeaVAFYTSGGSAgrlsneaaylAQRFARALGTNNLDDN 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 378 DTLCTE--EVFPTAGAGTDLRSNyllntTIAGVEEADVVLLVGTNPRFEAPLFNARIRKSWLHNDLKVALIgSPV----- 450
Cdd:COG0243 158 SRLCHEsaVAGLPRTFGSDKGTV-----SYEDLEHADLIVLWGSNPAENHPRLLRRLREAAKKRGAKIVVI-DPRrteta 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 451 -------------DL----------------------TYT--YDHL----------------GDSPKILQDIAsgshpfs 477
Cdd:COG0243 232 aiadewlpirpgtDAalllalahvlieeglydrdflaRHTvgFDELaayvaaytpewaaeitGVPAEDIRELA------- 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 478 QVLKEAKKPMVVLGSSALQRNDGAAILAAVSSIAqkirmtsGVTGdwkvmNILHRIASqvaaldLGYKPGVEAIRKNPPK 557
Cdd:COG0243 305 REFATAKPAVILWGMGLQQHSNGTQTVRAIANLA-------LLTG-----NIGKPGGG------PFSLTGEAILDGKPYP 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 558 VLFLLGADGGCI--------TRQDLPKDCFIIYQGHHGDVGAPIADVILPGAAYTEKSATYVNTE-GRAQQTKVAVTPPG 628
Cdd:COG0243 367 IKALWVYGGNPAvsapdtnrVREALRKLDFVVVIDTFLTETARYADIVLPATTWLERDDIVTNSEdRRVHLSRPAVEPPG 446
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 316983160 629 LAREDWKIIRALSEIAGMTLPYDTL----DQVRNRLEEVSPNLVRYDDIEGANYFQ 680
Cdd:COG0243 447 EARSDWEIFAELAKRLGFEEAFPWGrteeDYLRELLEATRGRGITFEELREKGPVQ 502
|
|
| Fer2 |
pfam00111 |
2Fe-2S iron-sulfur cluster binding domain; |
48-110 |
7.82e-06 |
|
2Fe-2S iron-sulfur cluster binding domain;
Pssm-ID: 395061 [Multi-domain] Cd Length: 77 Bit Score: 44.44 E-value: 7.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 48 VFVDGQSVMVE---PGTTVLQACEKVGMQIPRFCYHerlsvaGNCRMCLVEIEK----------------APKVVAACAM 108
Cdd:pfam00111 1 VTINGKGVTIEvpdGETTLLDAAEEAGIDIPYSCRG------GGCGTCAVKVLEgedqsdqsfleddelaAGYVVLACQT 74
|
..
gi 316983160 109 PV 110
Cdd:pfam00111 75 YP 76
|
|
| MopB_Nitrate-R-NarG-like |
cd02750 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
588-653 |
1.86e-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: 1.86e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 316983160 588 DVGAPIADVILPGAAYTEK---SATYVNTEGRAQQTkvAVTPPGLAREDWKIIRALSEiagmTLPYDTL 653
Cdd:cd02750 374 DSTALYSDIVLPAATWYEKhdlSTTDMHPFIHPFSP--AVDPLWEAKSDWEIFKALAK----KVPWRTL 436
|
|
| PRK13532 |
PRK13532 |
nitrate reductase catalytic subunit NapA; |
589-637 |
3.84e-04 |
|
nitrate reductase catalytic subunit NapA;
Pssm-ID: 237416 [Multi-domain] Cd Length: 830 Bit Score: 44.12 E-value: 3.84e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 316983160 589 VGAPIADVILPGAAYTEKSATYVNTEGRAQQTKVAVTPPGLARED-WKII 637
Cdd:PRK13532 516 VSALAADLILPTAMWVEKEGAYGNAERRTQFWRQQVKAPGEAKSDlWQLV 565
|
|
| Nar1 |
COG4624 |
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion]; |
104-250 |
1.71e-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: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983160 104 AACAMPVMKGWNILTNSEKSKKAREGVMEFLLANHPLDCPICDQGGECDLQDQSMMFGNDRSRFLEGKRAVEDKNIGPLV 183
Cdd:COG4624 7 ACCCCCIEEGDELLLLEEAERVLRIIILEALLPEHVDDDSACSCCPRCCLCCCCCCRCCVAISCIQVRGIIIIDKRGPSI 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 316983160 184 KTIMTRCIQCTRCIR--------FASEIAGVDDLGTTGRGNDMQVgtyiekmfmselsgniidiCPVGALTSKPY 250
Cdd:COG4624 87 IRDKEKCKNCYPCVRacpvkaikVDDGKAEIDEEKCISCGQCVAV-------------------CPFGAITEKSD 142
|
|
| |
