|
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 ... |
34-590 |
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: 811.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 34 VFVDGQSVMVEPGTTVLQV------------------------------------VAACAMPVMKGWNILTNSEKSKKAR 77
Cdd:TIGR01973 1 IFIDGKELEVPKGTTVLQAclsagieiprfcyheklsiagncrmclvevekfpkpVASCATPVTDGMKISTNSEKVKKAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 78 EGVMEFLLANHPLDCPICDQGGECDLQDQSMMFGNDRSRFLEGKRAVEDKNIGPLVKTIMTRCIQCTRCIRFASEIAGVD 157
Cdd:TIGR01973 81 EGVMEFLLINHPLDCPICDQGGECDLQDQAVMYGSDRSRFREKKRTVENKYLGPLIKTEMTRCIHCTRCVRFANEVAGVE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 158 DLGTTGRGNDMQVGTYIEKMFMSELSGNIIDICPVGALTSKPYAFTARPWETRKTESIDVMDAVGSNIVVSTRTGEVMRI 237
Cdd:TIGR01973 161 DLGVIGRGNNVEIGTYEGKTLESELSGNLIDICPVGALTSKPYAFKARPWELKSTPSICVHDSVGCNIRVDERNGEIMRI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 238 LPRMHEDINEEWISDKTRFAYDGLKRQ-RLTEPMVRNEKGLLTYTSWEDALSRVAGMLQSfqGKDVAAIAGGLVDAEALV 316
Cdd:TIGR01973 241 LPRENDEINEEWLCDKGRFGYDGLNRQdRLTKPLLRNQEGNLLEVSWAEALAIAAEKLKA--SSRIGGIAGPRSSLEELF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 317 ALKDLLNRVDSDTLCTEEVFPTAGAgTDLRSNYLLNTTIAGVEEADVVLLVGTNPRFEAPLFNARIRKSWLHNDLKVALI 396
Cdd:TIGR01973 319 ALKKLVRKLGSENFDLRIRNYEFES-ADLRANYLFNTTLADIEEADLVLLVGADLRQEAPLLNLRLRKAVKKGGAKVALI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 397 G-SPVDLTY-----TYDHLGDSPKILQDIASGSHP-FSQVLKEAKKPMVVLGSSALQRNDGAAILAAVSSIAQKIRMtsg 469
Cdd:TIGR01973 398 GiEKWNLTYpantnLVFHPGLSPKKLDDIASGAHSdIAAALKAAKKPLIIVGDSAISHLDGAALISAAANIAKVIKV--- 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 470 VTGDWKVMNILHRIASQVAALDLGYKP--GVEAIRKNPPKVLFLLGADGG----CITRQDLPK-DCFIIYQGHHGDVGAP 542
Cdd:TIGR01973 475 RRKEWNGLNILSSGANSVGLLDLGGEStgLDAALNLGAADALFLLGADLEraldKTARDALSKaDAFIIYQGHHGTETAE 554
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 316983154 543 IADVILPGAAYTEKSATYVNTEGRAQQTKVAVTPPGLAREDWKIIRAL 590
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 ... |
213-594 |
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: 701.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 213 ESIDVMDAVGSNIVVSTRTGEVMRILPRMHEDINEEWISDKTRFAYDGLKRQRLTEPMVRNEkGLLTYTSWEDALSRVAG 292
Cdd:cd02773 1 ESIDVLDAVGSNIRVDTRGGEVMRILPRLNEDINEEWISDKTRFAYDGLKRQRLDKPYIRKN-GKLKPATWEEALAAIAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 293 MLQSFQGKDVAAIAGGLVDAEALVALKDLLNRVDSDTLCTEEVFPTAGAgtDLRSNYLLNTTIAGVEEADVVLLVGTNPR 372
Cdd:cd02773 80 ALKGVKPDEIAAIAGDLADVESMVALKDLLNKLGSENLACEQDGPDLPA--DLRSNYLFNTTIAGIEEADAVLLVGTNPR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 373 FEAPLFNARIRKSWLHNDLKVALIGSPVDLTYTYDHLGDSPKILQDIASGSHPFSQVLKEAKKPMVVLGSSALQRNDGAA 452
Cdd:cd02773 158 FEAPVLNARIRKAWLHGGLKVGVIGPPVDLTYDYDHLGTDAKTLQDIASGKHPFSKALKDAKKPMIIVGSGALARKDGAA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 453 ILAAVSSIAQKIRMtsgVTGDWKVMNILHRIASQVAALDLGYKPGVEAIRK-NPPKVLFLLGADGGCITRQdlPKDCFII 531
Cdd:cd02773 238 ILAAVAKLAKKNGV---VREGWNGFNVLHRAASRVGALDLGFVPGAGAIRKsGPPKVLYLLGADEIDITPI--PKDAFVV 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 316983154 532 YQGHHGDVGAPIADVILPGAAYTEKSATYVNTEGRAQQTKVAVTPPGLAREDWKIIRALSEIA 594
Cdd:cd02773 313 YQGHHGDRGAQIADVILPGAAYTEKSGTYVNTEGRVQQTRKAVSPPGDAREDWKILRALSEVL 375
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
31-622 |
6.80e-177 |
|
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: 511.69 E-value: 6.80e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 31 LIEVFVDGQSVMVEPGTTVLQV------------------------------------VAACAMPVMKGWNILTNSEKSK 74
Cdd:COG1034 1 MVTITIDGKEVEVPKGTTVLQAaekagieiprfcyhpklsiagacrmclvevegapkpVASCATPVTDGMVVKTDSPKVK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 75 KAREGVMEFLLANHPLDCPICDQGGECDLQDQSMMFGNDRSRFLEGKRAVEDKNIGPLVKTIMTRCIQCTRCIRFASEIA 154
Cdd:COG1034 81 KARKGVMEFLLINHPLDCPICDQGGECDLQDQAMEYGVDESRYEEEKRTVPKKDLGPLILLDMNRCILCTRCVRFCDEIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 155 GVDDLGTTGRGNDMQVGTYIEKMFMSELSGNIIDICPVGALTSKPYAFTARPWETRKTESIDVMDAVGSNIVVSTRTGEV 234
Cdd:COG1034 161 GDPELGVIGRGEHSEIGTYLGKPLDSEFSGNCIDVCPVGALTSKPFRFKARPWELKKTPSICPHCSVGCNIRVDVRGGKV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 235 MRILPRMHEDINEEWISDKTRFAYDGLKR-QRLTEPMVRNEkGLLTYTSWEDALSRVAGMLQSfqgkdvaaiaggLVDAE 313
Cdd:COG1034 241 YRVLPRENEAVNEEWLCDKGRFGYDGLNSpDRLTRPLVRKD-GELVEASWEEALAAAAEGLKA------------LKKAE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 314 alvalkdllNRVdsdtlcteevfptagagtdlrsnyllnttiagveeadvvllvgtnprfeaplfnarirkswlhndlkv 393
Cdd:COG1034 308 ---------NSV-------------------------------------------------------------------- 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 394 aligspvdltytydhlgdspkilqdiasgshpfsqvlkeakkpmvvlgssalqrndGAAILAAVSSIAQkirmtsgvtgd 473
Cdd:COG1034 311 --------------------------------------------------------GAALLGALPDAAA----------- 323
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 474 wkvmnILhriasqvaaldlgykpgvEAIRKNPPKVLFLLGAD----GGCITRQDLPKDCFIIYQGHHGDVGAPIADVILP 549
Cdd:COG1034 324 -----IL------------------EAAEAGKLKALVLLGADpydlDPAAALAALAKADFVVVLDHFGSATAERADVVLP 380
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 316983154 550 GAAYTEKSATYVNTEGRAQQTKVAVTPPGLAREDWKIIRALSEIAGMTLPYDTLDQVRNRLEEVSPNLVRYDD 622
Cdd:COG1034 381 AAAFAEKSGTFVNLEGRVQRFNAAVPPPGEARPDWRVLRALANALGAGLPYDSLEEVRAELAAEAPATVSAEG 453
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
265-592 |
4.47e-130 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 388.68 E-value: 4.47e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 265 RLTEPMVRNEKGLLTYTSWEDALSRVAGMLQSFQGK------DVAAIAGGLVDAEALVALKDLLNRVDSDTLCTEEVF-- 336
Cdd:pfam00384 1 RLKYPMVRRGDGKFVRVSWDEALDLIAKKLKRIIKKygpdaiAINGGSGGLTDVESLYALKKLLNRLGSKNGNTEDHNgd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 337 ----PTAGAGTDLRSNYLLNTTIAGVEEADVVLLVGTNPRFEAPLFNARIRKSWLHNDLKVALIGSPVDLTYTYDHLGDS 412
Cdd:pfam00384 81 lctaAAAAFGSDLRSNYLFNSSIADIENADLILLIGTNPREEAPILNARIRKAALKGKAKVIVIGPRLDLTYADEHLGIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 413 PKILQDI-ASGSHPFSQVLKEAK----KPMVVLGSSALQRNDGAAILAAVSSIAQKIRMTSGVTGDWKVMNILHRIASQV 487
Cdd:pfam00384 161 PGTDLALaLAGAHVFIKELKKDKdfapKPIIIVGAGVLQRQDGEAIFRAIANLADLTGNIGRPGGGWNGLNILQGAASPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 488 AALDLGYKPGV------EAIRKNPPKVLFLLG-------ADGGCITRQDLPKDCFIIYQGHHGDVGAPIADVILPGAAYT 554
Cdd:pfam00384 241 GALDLGLVPGIksvemiNAIKKGGIKVLYLLGnnpfvthADENRVVKALQKLDLFVVYDGHHGDKTAKYADVILPAAAYT 320
|
330 340 350
....*....|....*....|....*....|....*...
gi 316983154 555 EKSATYVNTEGRAQQTKVAVTPPGLAREDWKIIRALSE 592
Cdd:pfam00384 321 EKNGTYVNTEGRVQSTKQAVPPPGEAREDWKILRALSE 358
|
|
| PRK07860 |
PRK07860 |
NADH dehydrogenase subunit G; Validated |
53-615 |
1.52e-82 |
|
NADH dehydrogenase subunit G; Validated
Pssm-ID: 236118 [Multi-domain] Cd Length: 797 Bit Score: 277.98 E-value: 1.52e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 53 VAACAMPVMKGWNILT--NSEKSKKAREGVMEFLLANHPLDCPICDQGGECDLQDQSMMFGNDRSRFLEGKRAVEdKNIg 130
Cdd:PRK07860 62 QASCTTTVTDGMVVKTqlTSPVADKAQHGVMELLLINHPLDCPVCDKGGECPLQNQAMSNGRAESRFTDVKRTFP-KPI- 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 131 PLVKTIM---TRCIQCTRCIRFASEIAGVDDLGTTGRGNDMQVGTYIEKMFMSELSGNIIDICPVGALTSKPYAFTARPW 207
Cdd:PRK07860 140 NISTQVLldrERCVLCARCTRFSDQIAGDPFIDLQERGALQQVGIYEGEPFQSYFSGNTVQICPVGALTGAAYRFRARPF 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 208 ETRKTESIDVMDAVGSNIVVSTRTGEVMRILPRMHEDINEEWISDKTRFAYD-GLKRQRLTEPMVRNEKGLLTYTSWEDA 286
Cdd:PRK07860 220 DLVSTPSVCEHCASGCAQRTDHRRGKVLRRLAGDDPEVNEEWNCDKGRWAFTyATQPDRITTPLVRDEDGELEPASWSEA 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 287 LSRVAGMLQSFQGkDVAAIAGGLVDAE--------ALVALK----DLLNRVDSDtlcTEEVFPTAG-AGTDlrsnylLNT 353
Cdd:PRK07860 300 LAVAARGLAAARG-RVGVLVGGRLTVEdayayakfARVALGtndiDFRARPHSA---EEADFLAARvAGRG------LGV 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 354 TIAGVEEADVVLLVGTNPRFEAPLFNARIRKSWLHNDLKVALIGSPVD--LTYTYDHL-----GDSPKILQDIASGSHPF 426
Cdd:PRK07860 370 TYADLEKAPAVLLVGFEPEEESPIVFLRLRKAARKHGLKVYSIAPFATrgLEKMGGTLlrtapGGEAAALDALATGAPDV 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 427 SQVLKEAKKpmVVLGSSALQRNDGAaiLAAVSSIAQkirmTSGVTGDWkvmniLHRIASQVAALDLGYKP---------- 496
Cdd:PRK07860 450 AELLRTPGA--VILVGERLATVPGA--LSAAARLAD----ATGARLAW-----VPRRAGERGALEAGALPtllpggrpva 516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 497 ------------GVEAIRKNPpkvlfllGADGGCITR-----------------QDLPK-----------DCFIIYQGHH 536
Cdd:PRK07860 517 dpaaraevaaawGVDELPAAP-------GRDTAGILAaaaagelgallvggvepADLPDpaaalaaldaaGFVVSLELRH 589
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 316983154 537 GDVgAPIADVILPGAAYTEKSATYVNTEGRAQQTKVAVTPPGlAREDWKIIRALSEIAGMTLPYDTLDQVRNRLEEVSP 615
Cdd:PRK07860 590 SAV-TERADVVLPVAPVAEKAGTFLNWEGRLRPFEAALRTTG-ALSDLRVLDALADEMGVDLGLPTVAAARAELARLGA 666
|
|
| NADH-G_4Fe-4S_3 |
smart00929 |
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region; |
77-117 |
7.14e-18 |
|
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region;
Pssm-ID: 214918 [Multi-domain] Cd Length: 41 Bit Score: 77.24 E-value: 7.14e-18
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 316983154 77 REGVMEFLLANHPLDCPICDQGGECDLQDQSMMFGNDRSRF 117
Cdd:smart00929 1 RKTILELLLANHPLDCPVCDKNGECELQDLAYELGVDEQRY 41
|
|
| NADH_dhqG_C |
pfam09326 |
NADH-ubiquinone oxidoreductase subunit G, C-terminal; Members of this family of are found at ... |
632-674 |
2.67e-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: 2.67e-11
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 316983154 632 ANELSKLVNQ-QLLADPLVPPqltIKDFYMTDSISRASQTMAKC 674
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 ... |
34-590 |
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: 811.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 34 VFVDGQSVMVEPGTTVLQV------------------------------------VAACAMPVMKGWNILTNSEKSKKAR 77
Cdd:TIGR01973 1 IFIDGKELEVPKGTTVLQAclsagieiprfcyheklsiagncrmclvevekfpkpVASCATPVTDGMKISTNSEKVKKAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 78 EGVMEFLLANHPLDCPICDQGGECDLQDQSMMFGNDRSRFLEGKRAVEDKNIGPLVKTIMTRCIQCTRCIRFASEIAGVD 157
Cdd:TIGR01973 81 EGVMEFLLINHPLDCPICDQGGECDLQDQAVMYGSDRSRFREKKRTVENKYLGPLIKTEMTRCIHCTRCVRFANEVAGVE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 158 DLGTTGRGNDMQVGTYIEKMFMSELSGNIIDICPVGALTSKPYAFTARPWETRKTESIDVMDAVGSNIVVSTRTGEVMRI 237
Cdd:TIGR01973 161 DLGVIGRGNNVEIGTYEGKTLESELSGNLIDICPVGALTSKPYAFKARPWELKSTPSICVHDSVGCNIRVDERNGEIMRI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 238 LPRMHEDINEEWISDKTRFAYDGLKRQ-RLTEPMVRNEKGLLTYTSWEDALSRVAGMLQSfqGKDVAAIAGGLVDAEALV 316
Cdd:TIGR01973 241 LPRENDEINEEWLCDKGRFGYDGLNRQdRLTKPLLRNQEGNLLEVSWAEALAIAAEKLKA--SSRIGGIAGPRSSLEELF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 317 ALKDLLNRVDSDTLCTEEVFPTAGAgTDLRSNYLLNTTIAGVEEADVVLLVGTNPRFEAPLFNARIRKSWLHNDLKVALI 396
Cdd:TIGR01973 319 ALKKLVRKLGSENFDLRIRNYEFES-ADLRANYLFNTTLADIEEADLVLLVGADLRQEAPLLNLRLRKAVKKGGAKVALI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 397 G-SPVDLTY-----TYDHLGDSPKILQDIASGSHP-FSQVLKEAKKPMVVLGSSALQRNDGAAILAAVSSIAQKIRMtsg 469
Cdd:TIGR01973 398 GiEKWNLTYpantnLVFHPGLSPKKLDDIASGAHSdIAAALKAAKKPLIIVGDSAISHLDGAALISAAANIAKVIKV--- 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 470 VTGDWKVMNILHRIASQVAALDLGYKP--GVEAIRKNPPKVLFLLGADGG----CITRQDLPK-DCFIIYQGHHGDVGAP 542
Cdd:TIGR01973 475 RRKEWNGLNILSSGANSVGLLDLGGEStgLDAALNLGAADALFLLGADLEraldKTARDALSKaDAFIIYQGHHGTETAE 554
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 316983154 543 IADVILPGAAYTEKSATYVNTEGRAQQTKVAVTPPGLAREDWKIIRAL 590
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 ... |
213-594 |
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: 701.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 213 ESIDVMDAVGSNIVVSTRTGEVMRILPRMHEDINEEWISDKTRFAYDGLKRQRLTEPMVRNEkGLLTYTSWEDALSRVAG 292
Cdd:cd02773 1 ESIDVLDAVGSNIRVDTRGGEVMRILPRLNEDINEEWISDKTRFAYDGLKRQRLDKPYIRKN-GKLKPATWEEALAAIAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 293 MLQSFQGKDVAAIAGGLVDAEALVALKDLLNRVDSDTLCTEEVFPTAGAgtDLRSNYLLNTTIAGVEEADVVLLVGTNPR 372
Cdd:cd02773 80 ALKGVKPDEIAAIAGDLADVESMVALKDLLNKLGSENLACEQDGPDLPA--DLRSNYLFNTTIAGIEEADAVLLVGTNPR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 373 FEAPLFNARIRKSWLHNDLKVALIGSPVDLTYTYDHLGDSPKILQDIASGSHPFSQVLKEAKKPMVVLGSSALQRNDGAA 452
Cdd:cd02773 158 FEAPVLNARIRKAWLHGGLKVGVIGPPVDLTYDYDHLGTDAKTLQDIASGKHPFSKALKDAKKPMIIVGSGALARKDGAA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 453 ILAAVSSIAQKIRMtsgVTGDWKVMNILHRIASQVAALDLGYKPGVEAIRK-NPPKVLFLLGADGGCITRQdlPKDCFII 531
Cdd:cd02773 238 ILAAVAKLAKKNGV---VREGWNGFNVLHRAASRVGALDLGFVPGAGAIRKsGPPKVLYLLGADEIDITPI--PKDAFVV 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 316983154 532 YQGHHGDVGAPIADVILPGAAYTEKSATYVNTEGRAQQTKVAVTPPGLAREDWKIIRALSEIA 594
Cdd:cd02773 313 YQGHHGDRGAQIADVILPGAAYTEKSGTYVNTEGRVQQTRKAVSPPGDAREDWKILRALSEVL 375
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
31-622 |
6.80e-177 |
|
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: 511.69 E-value: 6.80e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 31 LIEVFVDGQSVMVEPGTTVLQV------------------------------------VAACAMPVMKGWNILTNSEKSK 74
Cdd:COG1034 1 MVTITIDGKEVEVPKGTTVLQAaekagieiprfcyhpklsiagacrmclvevegapkpVASCATPVTDGMVVKTDSPKVK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 75 KAREGVMEFLLANHPLDCPICDQGGECDLQDQSMMFGNDRSRFLEGKRAVEDKNIGPLVKTIMTRCIQCTRCIRFASEIA 154
Cdd:COG1034 81 KARKGVMEFLLINHPLDCPICDQGGECDLQDQAMEYGVDESRYEEEKRTVPKKDLGPLILLDMNRCILCTRCVRFCDEIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 155 GVDDLGTTGRGNDMQVGTYIEKMFMSELSGNIIDICPVGALTSKPYAFTARPWETRKTESIDVMDAVGSNIVVSTRTGEV 234
Cdd:COG1034 161 GDPELGVIGRGEHSEIGTYLGKPLDSEFSGNCIDVCPVGALTSKPFRFKARPWELKKTPSICPHCSVGCNIRVDVRGGKV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 235 MRILPRMHEDINEEWISDKTRFAYDGLKR-QRLTEPMVRNEkGLLTYTSWEDALSRVAGMLQSfqgkdvaaiaggLVDAE 313
Cdd:COG1034 241 YRVLPRENEAVNEEWLCDKGRFGYDGLNSpDRLTRPLVRKD-GELVEASWEEALAAAAEGLKA------------LKKAE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 314 alvalkdllNRVdsdtlcteevfptagagtdlrsnyllnttiagveeadvvllvgtnprfeaplfnarirkswlhndlkv 393
Cdd:COG1034 308 ---------NSV-------------------------------------------------------------------- 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 394 aligspvdltytydhlgdspkilqdiasgshpfsqvlkeakkpmvvlgssalqrndGAAILAAVSSIAQkirmtsgvtgd 473
Cdd:COG1034 311 --------------------------------------------------------GAALLGALPDAAA----------- 323
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 474 wkvmnILhriasqvaaldlgykpgvEAIRKNPPKVLFLLGAD----GGCITRQDLPKDCFIIYQGHHGDVGAPIADVILP 549
Cdd:COG1034 324 -----IL------------------EAAEAGKLKALVLLGADpydlDPAAALAALAKADFVVVLDHFGSATAERADVVLP 380
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 316983154 550 GAAYTEKSATYVNTEGRAQQTKVAVTPPGLAREDWKIIRALSEIAGMTLPYDTLDQVRNRLEEVSPNLVRYDD 622
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 ... |
213-593 |
8.96e-172 |
|
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: 496.03 E-value: 8.96e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 213 ESIDVMDAVGSNIVVSTRTGEVMRILPRMHEDINEEWISDKTRFAYDGLK-RQRLTEPMVRNEkGLLTYTSWEDALSRVA 291
Cdd:cd02768 1 ESIDVHDALGSNIRVDVRGGEVMRILPRENEAINEEWISDKGRFGYDGLNsRQRLTQPLIKKG-GKLVPVSWEEALKTVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 292 GMLQSFQGKDVAAIAGGLVDAEALVALKDLLNRVDSDTLCTEEVFPTAGAGTDLRSNYLLNTTIAGVEEADVVLLVGTNP 371
Cdd:cd02768 80 EGLKAVKGDKIGGIAGPRADLESLFLLKKLLNKLGSNNIDHRLRQSDLPADNRLRGNYLFNTSIAEIEEADAVLLIGSNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 372 RFEAPLFNARIRKSWLHNDLKVALIGS-----PVDLTYTYDHLGDSPKILQDIASGSH--PFSQVLKEAKKPMVVLGSSA 444
Cdd:cd02768 160 RKEAPLLNARLRKAVKKKGAKIAVIGPkdtdlIADLTYPVSPLGASLATLLDIAEGKHlkPFAKSLKKAKKPLIILGSSA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 445 LqRNDGAAILAAVSSIAQKIRMtsgVTGDWKVMNILHRIASQVAA--LDLGYKPGVEAIRKnppkvLFLLGADGGCITRQ 522
Cdd:cd02768 240 L-RKDGAAILKALANLAAKLGT---GAGLWNGLNVLNSVGARLGGagLDAGLALLEPGKAK-----LLLLGEDELDRSNP 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 316983154 523 DL-----PKDCFIIYQGHHGDVGAPiADVILPGAAYTEKSATYVNTEGRAQQTKVAVTPPGLAREDWKIIRALSEI 593
Cdd:cd02768 311 PAavalaAADAFVVYQGHHGDTGAQ-ADVILPAAAFTEKSGTYVNTEGRVQRFKKAVSPPGDAREDWKILRALSNL 385
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
265-592 |
4.47e-130 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 388.68 E-value: 4.47e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 265 RLTEPMVRNEKGLLTYTSWEDALSRVAGMLQSFQGK------DVAAIAGGLVDAEALVALKDLLNRVDSDTLCTEEVF-- 336
Cdd:pfam00384 1 RLKYPMVRRGDGKFVRVSWDEALDLIAKKLKRIIKKygpdaiAINGGSGGLTDVESLYALKKLLNRLGSKNGNTEDHNgd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 337 ----PTAGAGTDLRSNYLLNTTIAGVEEADVVLLVGTNPRFEAPLFNARIRKSWLHNDLKVALIGSPVDLTYTYDHLGDS 412
Cdd:pfam00384 81 lctaAAAAFGSDLRSNYLFNSSIADIENADLILLIGTNPREEAPILNARIRKAALKGKAKVIVIGPRLDLTYADEHLGIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 413 PKILQDI-ASGSHPFSQVLKEAK----KPMVVLGSSALQRNDGAAILAAVSSIAQKIRMTSGVTGDWKVMNILHRIASQV 487
Cdd:pfam00384 161 PGTDLALaLAGAHVFIKELKKDKdfapKPIIIVGAGVLQRQDGEAIFRAIANLADLTGNIGRPGGGWNGLNILQGAASPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 488 AALDLGYKPGV------EAIRKNPPKVLFLLG-------ADGGCITRQDLPKDCFIIYQGHHGDVGAPIADVILPGAAYT 554
Cdd:pfam00384 241 GALDLGLVPGIksvemiNAIKKGGIKVLYLLGnnpfvthADENRVVKALQKLDLFVVYDGHHGDKTAKYADVILPAAAYT 320
|
330 340 350
....*....|....*....|....*....|....*...
gi 316983154 555 EKSATYVNTEGRAQQTKVAVTPPGLAREDWKIIRALSE 592
Cdd:pfam00384 321 EKNGTYVNTEGRVQSTKQAVPPPGEAREDWKILRALSE 358
|
|
| PRK07860 |
PRK07860 |
NADH dehydrogenase subunit G; Validated |
53-615 |
1.52e-82 |
|
NADH dehydrogenase subunit G; Validated
Pssm-ID: 236118 [Multi-domain] Cd Length: 797 Bit Score: 277.98 E-value: 1.52e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 53 VAACAMPVMKGWNILT--NSEKSKKAREGVMEFLLANHPLDCPICDQGGECDLQDQSMMFGNDRSRFLEGKRAVEdKNIg 130
Cdd:PRK07860 62 QASCTTTVTDGMVVKTqlTSPVADKAQHGVMELLLINHPLDCPVCDKGGECPLQNQAMSNGRAESRFTDVKRTFP-KPI- 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 131 PLVKTIM---TRCIQCTRCIRFASEIAGVDDLGTTGRGNDMQVGTYIEKMFMSELSGNIIDICPVGALTSKPYAFTARPW 207
Cdd:PRK07860 140 NISTQVLldrERCVLCARCTRFSDQIAGDPFIDLQERGALQQVGIYEGEPFQSYFSGNTVQICPVGALTGAAYRFRARPF 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 208 ETRKTESIDVMDAVGSNIVVSTRTGEVMRILPRMHEDINEEWISDKTRFAYD-GLKRQRLTEPMVRNEKGLLTYTSWEDA 286
Cdd:PRK07860 220 DLVSTPSVCEHCASGCAQRTDHRRGKVLRRLAGDDPEVNEEWNCDKGRWAFTyATQPDRITTPLVRDEDGELEPASWSEA 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 287 LSRVAGMLQSFQGkDVAAIAGGLVDAE--------ALVALK----DLLNRVDSDtlcTEEVFPTAG-AGTDlrsnylLNT 353
Cdd:PRK07860 300 LAVAARGLAAARG-RVGVLVGGRLTVEdayayakfARVALGtndiDFRARPHSA---EEADFLAARvAGRG------LGV 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 354 TIAGVEEADVVLLVGTNPRFEAPLFNARIRKSWLHNDLKVALIGSPVD--LTYTYDHL-----GDSPKILQDIASGSHPF 426
Cdd:PRK07860 370 TYADLEKAPAVLLVGFEPEEESPIVFLRLRKAARKHGLKVYSIAPFATrgLEKMGGTLlrtapGGEAAALDALATGAPDV 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 427 SQVLKEAKKpmVVLGSSALQRNDGAaiLAAVSSIAQkirmTSGVTGDWkvmniLHRIASQVAALDLGYKP---------- 496
Cdd:PRK07860 450 AELLRTPGA--VILVGERLATVPGA--LSAAARLAD----ATGARLAW-----VPRRAGERGALEAGALPtllpggrpva 516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 497 ------------GVEAIRKNPpkvlfllGADGGCITR-----------------QDLPK-----------DCFIIYQGHH 536
Cdd:PRK07860 517 dpaaraevaaawGVDELPAAP-------GRDTAGILAaaaagelgallvggvepADLPDpaaalaaldaaGFVVSLELRH 589
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 316983154 537 GDVgAPIADVILPGAAYTEKSATYVNTEGRAQQTKVAVTPPGlAREDWKIIRALSEIAGMTLPYDTLDQVRNRLEEVSP 615
Cdd:PRK07860 590 SAV-TERADVVLPVAPVAEKAGTFLNWEGRLRPFEAALRTTG-ALSDLRVLDALADEMGVDLGLPTVAAARAELARLGA 666
|
|
| MopB_Res-Cmplx1_Nad11-M |
cd02774 |
MopB_Res_Cmplx1_Nad11_M: Mitochondrial-encoded NADH-quinone oxidoreductase/respiratory complex ... |
213-590 |
5.19e-80 |
|
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: 5.19e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 213 ESIDVMDAVGSNIVVSTRTGEVMRILPRMHEDINEEWISDKTRFAYDGLKRQRLTEPMVRNEKGLLTYTSWEDALSRVAG 292
Cdd:cd02774 1 ESIDVLDSLGSNIRVDIKGNEILRILPKINDELNEEWISDKIRFSYDSLKYQRIKTPLLKLSNNSFLEIGWKTAFKFLNK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 293 MLQSFQGKDVAAIAGGLVDAEALVALKDLLNRVDSDTLCTEEVFPTAGAGTDLRSNYLLNTTIAGVEEADVVLLVGTNPR 372
Cdd:cd02774 81 FILLKKFSKLNFIIGSKIDLETLFYYKKLLNKLGSLNTNSNNFLENNNYFNLDLENYLFNNSLKNLDKSDLCLLIGSNLR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 373 FEAPLFNARIRKSWLHNDLKVALIGSPVDLTYTYDHLGDSPKILQDIASGSHPFSQVLKEAKKPMVVLGSSALQRNDGaa 452
Cdd:cd02774 161 VESPILNIRLRNRYNKGNKKIFVIGNKFDTTYPSKHIGLSLNTLLKILEGKHLFCKQLKKSKKPLIIIGSSFSLRKNY-- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 453 ilaavSSIAQKIRMTSGVTGDwkVMNILHRIASQVAALDLgYKPGVEAIRKnpPKVLFLLGADggciTRQDLPKDCFIIY 532
Cdd:cd02774 239 -----SFIISKLKNFSSNNEN--NFNFLNIISNSLYYLGI-KKFNSNNKKN--LSNLYYIKET----NFQKFNKNNFVIY 304
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 316983154 533 QGHHGDVGAPIADVILPGAAYTEKSATYVNTEGRAQQTKVAVTPPGLAREDWKIIRAL 590
Cdd:cd02774 305 QGHHFLNLANNSNLILPSKTFFEKEALYLNLEGILQKTKKILSFKENIKSDDNIIFSL 362
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
213-592 |
4.97e-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: 224.90 E-value: 4.97e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 213 ESIDVMDAVGSNIVVSTRTGEVMRILPRMHEDINEEWISDKTRFAYDGLK-RQRLTEPMVR-NEKGLLTYTSWEDALSRV 290
Cdd:cd00368 1 PSVCPFCGVGCGILVYVKDGKVVRIEGDPNHPVNEGRLCDKGRAGLDGLYsPDRLKYPLIRvGGRGKFVPISWDEALDEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 291 AGMLQSFQGKD----VAAIAGGLVDAEALVALKDLLNRVDSDTLCTEEVFPTAGAGTDLR--SNYLLNTTIAGVEEADVV 364
Cdd:cd00368 81 AEKLKEIREKYgpdaIAFYGGGGASNEEAYLLQKLLRALGSNNVDSHARLCHASAVAALKafGGGAPTNTLADIENADLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 365 LLVGTNPRFEAPLFNARIRKSWLhNDLKVALIGSPVDLTYTYDHLGDSPKILQDIAsgshpfsqvLKEAKKPMVVLGSSA 444
Cdd:cd00368 161 LLWGSNPAETHPVLAARLRRAKK-RGAKLIVIDPRRTETAAKADEWLPIRPGTDAA---------LALAEWAAEITGVPA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 445 lqrndgAAILAAVSSIAQK----IRMTSGVT----GDWKVMNILhriasqVAALDLGY--KPGVEAIRKNPPkvlFLLGA 514
Cdd:cd00368 231 ------ETIRALAREFAAAkravILWGMGLTqhtnGTQNVRAIA------NLAALTGNigRPGGGLGPGGNP---LVSAP 295
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 316983154 515 DGGCITRQDLPKDCFIIYQGHHGDVGApIADVILPGAAYTEKSATYVNTEGRAQQTKVAVTPPGLAREDWKIIRALSE 592
Cdd:cd00368 296 DANRVRAALKKLDFVVVIDIFMTETAA-YADVVLPAATYLEKEGTYTNTEGRVQLFRQAVEPPGEARSDWEILRELAK 372
|
|
| MopB_NDH-1_NuoG2 |
cd02772 |
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase ... |
214-590 |
3.38e-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: 194.11 E-value: 3.38e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 214 SIDVMDAVGSNIVVSTRTGEVMRILPRMHEDINEEWISDKTRFAYDGLKRQ-RLTEPMVRnEKGLLTYTSWEDALSRVAG 292
Cdd:cd02772 2 SVSPHDALGSNLVVHVKNNKVMRVVPRENEAINECWLSDRDRFSYEGLNSEdRLTKPMIK-KDGQWQEVDWETALEYVAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 293 MLQSFQGKDVAAIAGGLVDA----EALVALKDLLNRVDSDTLCTEEVFPTAGAGTDLRSNYLLNTTIAGVEEADVVLLVG 368
Cdd:cd02772 81 GLSAIIKKHGADQIGALASPhstlEELYLLQKLARGLGSDNIDHRLRQSDFRDDAKASGAPWLGMPIAEISELDRVLVIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 369 TNPRFEAPLFNARIRKSW---------------LHNDLKVALIGSPVDLTYT--------YDHLGDSPKILQDIASGSHP 425
Cdd:cd02772 161 SNLRKEHPLLAQRLRQAVkkgaklsainpadddFLFPLSGKAIVAPSALANAlaqvakalAEEKGLAVPDEDAKVEASEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 426 FSQV---LKEAKKPMVVLGSSALQRNDGAAILAAVSSIAQkirmTSGVTGdwkvmNILHRIASQVAALDLGYKPGV---- 498
Cdd:cd02772 241 ARKIaasLVSAERAAVFLGNLAQNHPQAATLRALAQEIAK----LTGATL-----GVLGEGANSVGAYLAGALPHGglna 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 499 EAIRKNPPKVLFLLGA------DGGCITRQDLPKDCFIIYQGHHGDVGA-PIADVILPGAAYTEKSATYVNTEGRAQQTK 571
Cdd:cd02772 312 AAMLEQPRKAYLLLNVepeldcANPAQALAALNQAEFVVALSAFASAALlDYADVLLPIAPFTETSGTFVNLEGRVQSFK 391
|
410
....*....|....*....
gi 316983154 572 VAVTPPGLAREDWKIIRAL 590
Cdd:cd02772 392 GVVKPLGEARPAWKVLRVL 410
|
|
| PTZ00305 |
PTZ00305 |
NADH:ubiquinone oxidoreductase; Provisional |
17-195 |
1.67e-37 |
|
NADH:ubiquinone oxidoreductase; Provisional
Pssm-ID: 140326 [Multi-domain] Cd Length: 297 Bit Score: 141.71 E-value: 1.67e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 17 PKGCVRTTATAASN--LIEVFVDGQSvmvepgttvlQVVAACAMPVMKGWNILTNSEKSKKAREGVMEFLLANHPLDCPI 94
Cdd:PTZ00305 99 PKFCYHPILSVAGNcrMCLVQVDGTQ----------NLVVSCATVALPGMSIITDSRLVRDAREGNVELILINHPNDCPI 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 95 CDQGGECDLQDQSMMFGNDRSRFLEGKRAVEDKNIGPLVKTIMTRCIQCTRCIRFASEIAGVDDLGTTGRGNDMQVGTYI 174
Cdd:PTZ00305 169 CEQATNCDLQNVSMNYGTDIPRYKEDKRAVQDFYFDPQTRVVLNRCIHCTRCVRFLNEHAQDFNLGMIGRGGLSEISTFL 248
|
170 180
....*....|....*....|..
gi 316983154 175 EKM-FMSELSGNIIDICPVGAL 195
Cdd:PTZ00305 249 DELeVKTDNNMPVSQLCPVGKL 270
|
|
| 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 ... |
220-591 |
3.57e-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: 145.22 E-value: 3.57e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 220 AVGSNIVVSTRTGEVMRILPRMHEDINEEWISDKTRFAYDGLK-RQRLTEPMVRNeKGLLTYTSWEDALSRVAGMLQSFQ 298
Cdd:cd02771 8 SVGCNISLGERYGELRRVENRYNGAVNHYFLCDRGRFGYGYVNsRDRLTQPLIRR-GGTLVPVSWNEALDVAAARLKEAK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 299 GKdVAAIAGGLVDAEALVALKDLL------NRVDSDTLcteevfptAGAGTDLRSNYLLNTTIAGVEEADVVLLVGTNPR 372
Cdd:cd02771 87 DK-VGGIGSPRASNESNYALQKLVgavlgtNNVDHRAR--------RLIAEILRNGPIYIPSLRDIESADAVLVLGEDLT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 373 FEAPLFNARIRKSWLHNDLK-VALIGSPVDLTYTYDHLGDSPKI-----------LQDIA-------------------- 420
Cdd:cd02771 158 QTAPRIALALRQAARRKAVElAALSGIPKWQDAAVRNIAQGAKSplfivnalatrLDDIAaesiraspggqarlgaalar 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 421 ---------SGSHPFS------QVLKEAKKPMVVLGSSALqrndGAAILAAVSSIAQKIRMTSGVTGdwkVMNILHRIAS 485
Cdd:cd02771 238 avdasaagvSGLAPKEkaariaARLTGAKKPLIVSGTLSG----SLELIKAAANLAKALKRRGENAG---LTLAVEEGNS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 486 QVAAL--DLGYKPG------VEAIRKNPPKVLFLLGAD-------GGCitRQDLPKDCFIIYQGHHGDVGAPIADVILPG 550
Cdd:cd02771 311 PGLLLlgGHVTEPGldldgaLAALEDGSADALIVLGNDlyrsapeRRV--EAALDAAEFVVVLDHFLTETAERADVVLPA 388
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 316983154 551 AAYTEKSATYVNTEGRAQQ-TKVAVTPPGLAREDWKIIRALS 591
Cdd:cd02771 389 ASFAEKSGTFVNYEGRAQRfFKAYDDPAGDARSDWRWLHALA 430
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
220-630 |
5.70e-31 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 129.23 E-value: 5.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 220 AVGSNIVVSTRTGEVMRILPRMHEDINEEWISDKTRFAYDGL-KRQRLTEPMVRnEKGLLTYTSWEDALSRVAGMLQSFQ 298
Cdd:COG3383 15 GVGCGIDLEVKDGKIVKVEGDPDHPVNRGRLCVKGRFGFEFVnSPDRLTTPLIR-RGGEFREVSWDEALDLVAERLREIQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 299 ---GKD-VAAIAGGLVDAEALVALKDLL------NRVDSDT-LCTEevfPTAGA-----GTDLRSNyllntTIAGVEEAD 362
Cdd:COG3383 94 aehGPDaVAFYGSGQLTNEENYLLQKLArgvlgtNNIDNNArLCMA---SAVAGlkqsfGSDAPPN-----SYDDIEEAD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 363 VVLLVGTNPRFEAPLFNARIRKSWLHN-----------------DLKVALI-GSPVDLTYTYDH------LGDSPKI--- 415
Cdd:COG3383 166 VILVIGSNPAEAHPVLARRIKKAKKNGaklivvdprrtetarlaDLHLQIKpGTDLALLNGLLHviieegLVDEDFIaer 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 416 ------LQDIASGSHP----------------FSQVLKEAKKPMVVLGSSALQRNDGAAILAAVSSIAQkirMT------ 467
Cdd:COG3383 246 tegfeeLKASVAKYTPervaeitgvpaedireAARLIAEAKRAMILWGMGVNQHTQGTDNVNAIINLAL---ATgnigrp 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 468 -SGV---TG--------DW-----------KVMNILHRiaSQVAAL----DLGYKPG------VEAIRKNPPKVLFLLG- 513
Cdd:COG3383 323 gTGPfplTGqnnvqggrDMgalpnvlpgyrDVTDPEHR--AKVADAwgvpPLPDKPGltavemFDAIADGEIKALWIIGe 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 514 ------ADGGCItRQDLPKDCFIIYQghhgDV----GAPIADVILPGAAYTEKSATYVNTEGRAQQTKVAVTPPGLARED 583
Cdd:COG3383 401 npavsdPDANHV-REALEKLEFLVVQ----DIflteTAEYADVVLPAASWAEKDGTFTNTERRVQRVRKAVEPPGEARPD 475
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 316983154 584 WKIIRALSEIAGMTLPYDTLDQVRNRLEEVSPNL--VRYDDIEGANYFQ 630
Cdd:COG3383 476 WEIIAELARRLGYGFDYDSPEEVFDEIARLTPDYsgISYERLEALGGVQ 524
|
|
| PRK08493 |
PRK08493 |
NADH-quinone oxidoreductase subunit G; |
22-259 |
2.21e-23 |
|
NADH-quinone oxidoreductase subunit G;
Pssm-ID: 236277 [Multi-domain] Cd Length: 819 Bit Score: 105.56 E-value: 2.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 22 RTTATAASNLIEVFVDGQSVMvepgttvlqvvaACAMPVMKGWNILTNSEKSKKAREGVMEFLLANHPLDCPICDQGGEC 101
Cdd:PRK08493 38 GCSPTLACRLCMVEADGKRVY------------SCNTKAKEGMNILTNTPNLMDERNAIMQTYDVNHPLECGVCDKSGEC 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 102 DLQDQSMMFGNDRSRFlegkrAVEDKNiGPLVKTIMTR-----CIQCTRCIRFASEIAGVDDLGTTGRGNDMQVGTYIEK 176
Cdd:PRK08493 106 ELQNFTHEMGVNHQPY-----AIKDTH-KPHKHWGKINydpslCIVCERCVTVCKDKIGESALKTVPRGLDAPDKSFKES 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 177 MFMSELS-----------------------GNIIDICPVGALTSKPYAFTARPWETRKTESIDVMDAVGSNIVVSTR--- 230
Cdd:PRK08493 180 MPKDAYAvwskkqksligpvggetldcsfcGECIAVCPVGALSSSDFQYTSNAWELKKIPATCPHCSDCCLIYYDVKhss 259
|
250 260 270
....*....|....*....|....*....|
gi 316983154 231 -TGEVMRILpRMHEDINEEWISDKTRFAYD 259
Cdd:PRK08493 260 iLNQESKIY-RVSNDFYFNPLCGAGRFAFD 288
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
220-630 |
3.40e-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: 3.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 220 AVGSNIVVSTRTGEVMRILPRMHEDINEEWISDKTRFAYDGLK-RQRLTEPMVRnEKGLLTYTSWEDALSRVAGMLQSFQ 298
Cdd:cd02753 8 GVGCGLELWVKDNKIVGVEPVKGHPVNRGKLCVKGRFGFDFVNsKDRLTKPLIR-KNGKFVEASWDEALSLVASRLKEIK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 299 ---GKD-VAAIAGGLVDAEALVALKDLL------NRVDSDT-LC----TEEVFPTAGAGTDlrSNyllntTIAGVEEADV 363
Cdd:cd02753 87 dkyGPDaIAFFGSAKCTNEENYLFQKLAravggtNNVDHCArLChsptVAGLAETLGSGAM--TN-----SIADIEEADV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 364 VLLVGTNPRFEAPLFNARI---------------------RKSWLHNDLK----VALIGS-------------------- 398
Cdd:cd02753 160 ILVIGSNTTEAHPVIARRIkrakrngaklivadprrtelaRFADLHLQLRpgtdVALLNAmahviieeglydeefieert 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 399 -----------PVDLTYTYDHLGDSPKILQDIAsgshpfsQVLKEAKKPMVVLGSSALQRNDGAAILAAVSSIAQkirmt 467
Cdd:cd02753 240 egfeelkeiveKYTPEYAERITGVPAEDIREAA-------RMYATAKSAAILWGMGVTQHSHGTDNVMALSNLAL----- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 468 sgVTGdwkvmNI------LHRIASQ--V-AALDLGYKPGVEairknpP---KVLFLLGADGGCI------TRQDLPKDCF 529
Cdd:cd02753 308 --LTG-----NIgrpgtgVNPLRGQnnVqGACDMGALPNVL------PgyvKALYIMGENPALSdpntnhVRKALESLEF 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 530 IIYQghhgDV----GAPIADVILPGAAYTEKSATYVNTEGRAQQTKVAVTPPGLAREDWKIIRALSEIAGMTLPYDTLDQ 605
Cdd:cd02753 375 LVVQ----DIflteTAELADVVLPAASFAEKDGTFTNTERRVQRVRKAVEPPGEARPDWEIIQELANRLGYPGFYSHPEE 450
|
490 500
....*....|....*....|....*..
gi 316983154 606 VRNRLEEVSPNL--VRYDDIEGANYFQ 630
Cdd:cd02753 451 IFDEIARLTPQYagISYERLERPGGLQ 477
|
|
| PRK07569 |
PRK07569 |
bidirectional hydrogenase complex protein HoxU; Validated |
42-198 |
4.70e-18 |
|
bidirectional hydrogenase complex protein HoxU; Validated
Pssm-ID: 181037 [Multi-domain] Cd Length: 234 Bit Score: 83.93 E-value: 4.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 42 MVE-PGTTVLQvvAACAMPVMKGWNILTNSEKSKKAREGVMEFLLA--NHPldCPICDQGGECDLQDQSMMFGNDRSRF- 117
Cdd:PRK07569 51 LVEiEGSNKLL--PACVTPVAEGMVVQTNTPRLQEYRRMIVELLFAegNHV--CAVCVANGNCELQDLAIEVGMDHVRFp 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 118 -LEGKRAVE--------DKNigplvktimtRCIQCTRCIRFASEIAGVDDLGTTGRGNDMQVGTYIEKMFMSELS----G 184
Cdd:PRK07569 127 yLFPRRPVDishprfgiDHN----------RCVLCTRCVRVCDEIEGAHTWDVAGRGAKSRVITDLNQPWGTSETctscG 196
|
170
....*....|....
gi 316983154 185 NIIDICPVGALTSK 198
Cdd:PRK07569 197 KCVQACPTGAIFRK 210
|
|
| NADH-G_4Fe-4S_3 |
smart00929 |
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region; |
77-117 |
7.14e-18 |
|
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region;
Pssm-ID: 214918 [Multi-domain] Cd Length: 41 Bit Score: 77.24 E-value: 7.14e-18
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 316983154 77 REGVMEFLLANHPLDCPICDQGGECDLQDQSMMFGNDRSRF 117
Cdd:smart00929 1 RKTILELLLANHPLDCPVCDKNGECELQDLAYELGVDEQRY 41
|
|
| NADH-G_4Fe-4S_3 |
pfam10588 |
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region; |
77-116 |
1.36e-17 |
|
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region;
Pssm-ID: 463159 [Multi-domain] Cd Length: 40 Bit Score: 76.33 E-value: 1.36e-17
10 20 30 40
....*....|....*....|....*....|....*....|
gi 316983154 77 REGVMEFLLANHPLDCPICDQGGECDLQDQSMMFGNDRSR 116
Cdd:pfam10588 1 RKTILELLLSNHPLDCPTCDKNGNCELQDLAYELGVDEVR 40
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
220-628 |
5.22e-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: 5.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 220 AVGSNIVVSTRTGEVMRILPRMHEDINEEWISDK-TRFAYDGLKRQRLTEPMVRNEKGLLTYTSWEDALSRVAGMLQSFQ 298
Cdd:cd02754 8 GVGCGVEIGVKDGKVVAVRGDPEHPVNRGRLCIKgLNLHKTLNGPERLTRPLLRRNGGELVPVSWDEALDLIAERFKAIQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 299 ---GKD-VAAIAGGLVDAEALVALKDLL------NRVDSDT-LCTEevfpTAGA------GTDLRSNyllntTIAGVEEA 361
Cdd:cd02754 88 aeyGPDsVAFYGSGQLLTEEYYAANKLAkgglgtNNIDTNSrLCMA----SAVAgykrsfGADGPPG-----SYDDIEHA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 362 DVVLLVGTNPRFEAPLFNARIRKSwLHNDLKVALI---------------------GSPVDLTYTYDH-LGDSPKILQD- 418
Cdd:cd02754 159 DCFFLIGSNMAECHPILFRRLLDR-KKANPGAKIIvvdprrtrtadiadlhlpirpGTDLALLNGLLHvLIEEGLIDRDf 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 419 IAS---GSHPFSQVLK--------------------------EAKKPMVVLGSSALQRNDGAAilaAVSSI--------- 460
Cdd:cd02754 238 IDAhteGFEELKAFVAdytpekvaeitgvpeadireaarlfgEARKVMSLWTMGVNQSTQGTA---ANNAIinlhlatgk 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 461 ----------------AQKIRMTSGVT----GDWKVMNILHR--IAS--QVAALDLGYKPGV------EAIRKNPPKVLF 510
Cdd:cd02754 315 igrpgsgpfsltgqpnAMGGREVGGLAnllpGHRSVNNPEHRaeVAKfwGVPEGTIPPKPGLhavemfEAIEDGEIKALW 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 511 LLG-------ADGGCItRQDLPKDCFIIYQ-GHHGDVGAPIADVILPGAAYTEKSATYVNTEGRAQQTKVAVTPPGLARE 582
Cdd:cd02754 395 VMCtnpavslPNANRV-REALERLEFVVVQdAFADTETAEYADLVLPAASWGEKEGTMTNSERRVSLLRAAVEPPGEARP 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 316983154 583 DWKIIRALSEIAGMT--LPYDTLDQVRNRLEEVSPnlVRYDDIEGANY 628
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 ... |
632-674 |
2.67e-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: 2.67e-11
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 316983154 632 ANELSKLVNQ-QLLADPLVPPqltIKDFYMTDSISRASQTMAKC 674
Cdd:pfam09326 1 ALVLALAGAKgKLSGAPLKSP---IEDFYMTDPISRASATMAKC 41
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
265-630 |
9.32e-09 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 58.70 E-value: 9.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 265 RLTEPMVR-NEKGLLTY--TSWEDALSRVAGMLQSFQGKD----VAAIAGGLVD----------AEALVALKDLLNRVDS 327
Cdd:COG0243 78 RLTYPMKRvGPRGSGKFerISWDEALDLIAEKLKAIIDEYgpeaVAFYTSGGSAgrlsneaaylAQRFARALGTNNLDDN 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 328 DTLCTE--EVFPTAGAGTDLRSNyllntTIAGVEEADVVLLVGTNPRFEAPLFNARIRKSWLHNDLKVALIgSPV----- 400
Cdd:COG0243 158 SRLCHEsaVAGLPRTFGSDKGTV-----SYEDLEHADLIVLWGSNPAENHPRLLRRLREAAKKRGAKIVVI-DPRrteta 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 401 -------------DL----------------------TYT--YDHL----------------GDSPKILQDIAsgshpfs 427
Cdd:COG0243 232 aiadewlpirpgtDAalllalahvlieeglydrdflaRHTvgFDELaayvaaytpewaaeitGVPAEDIRELA------- 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 428 QVLKEAKKPMVVLGSSALQRNDGAAILAAVSSIAqkirmtsGVTGdwkvmNILHRIASqvaaldLGYKPGVEAIRKNPPK 507
Cdd:COG0243 305 REFATAKPAVILWGMGLQQHSNGTQTVRAIANLA-------LLTG-----NIGKPGGG------PFSLTGEAILDGKPYP 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 508 VLFLLGADGGCI--------TRQDLPKDCFIIYQGHHGDVGAPIADVILPGAAYTEKSATYVNTE-GRAQQTKVAVTPPG 578
Cdd:COG0243 367 IKALWVYGGNPAvsapdtnrVREALRKLDFVVVIDTFLTETARYADIVLPATTWLERDDIVTNSEdRRVHLSRPAVEPPG 446
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 316983154 579 LAREDWKIIRALSEIAGMTLPYDTL----DQVRNRLEEVSPNLVRYDDIEGANYFQ 630
Cdd:COG0243 447 EARSDWEIFAELAKRLGFEEAFPWGrteeDYLRELLEATRGRGITFEELREKGPVQ 502
|
|
| MopB_Nitrate-R-NarG-like |
cd02750 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
538-603 |
1.70e-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: 1.70e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 316983154 538 DVGAPIADVILPGAAYTEK---SATYVNTEGRAQQTkvAVTPPGLAREDWKIIRALSEiagmTLPYDTL 603
Cdd:cd02750 374 DSTALYSDIVLPAATWYEKhdlSTTDMHPFIHPFSP--AVDPLWEAKSDWEIFKALAK----KVPWRTL 436
|
|
| PRK13532 |
PRK13532 |
nitrate reductase catalytic subunit NapA; |
539-587 |
3.51e-04 |
|
nitrate reductase catalytic subunit NapA;
Pssm-ID: 237416 [Multi-domain] Cd Length: 830 Bit Score: 44.12 E-value: 3.51e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 316983154 539 VGAPIADVILPGAAYTEKSATYVNTEGRAQQTKVAVTPPGLARED-WKII 587
Cdd:PRK13532 516 VSALAADLILPTAMWVEKEGAYGNAERRTQFWRQQVKAPGEAKSDlWQLV 565
|
|
| Nar1 |
COG4624 |
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion]; |
54-200 |
1.01e-03 |
|
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
Pssm-ID: 443663 [Multi-domain] Cd Length: 450 Bit Score: 42.32 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316983154 54 AACAMPVMKGWNILTNSEKSKKAREGVMEFLLANHPLDCPICDQGGECDLQDQSMMFGNDRSRFLEGKRAVEDKNIGPLV 133
Cdd:COG4624 7 ACCCCCIEEGDELLLLEEAERVLRIIILEALLPEHVDDDSACSCCPRCCLCCCCCCRCCVAISCIQVRGIIIIDKRGPSI 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 316983154 134 KTIMTRCIQCTRCIR--------FASEIAGVDDLGTTGRGNDMQVgtyiekmfmselsgniidiCPVGALTSKPY 200
Cdd:COG4624 87 IRDKEKCKNCYPCVRacpvkaikVDDGKAEIDEEKCISCGQCVAV-------------------CPFGAITEKSD 142
|
|
| |
