|
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 ... |
44-632 |
0e+00 |
|
NADH-quinone oxidoreductase, chain G; This model represents the G subunit (one of 14: A->N) of the NADH-quinone oxidoreductase complex I which generally couples NADH and ubiquinone oxidation/reduction in bacteria and mammalian mitochondria while translocating protons, but may act on NADPH and/or plastoquinone in cyanobacteria and plant chloroplasts. This model excludes related subunits from formate dehydrogenase complexes. [Energy metabolism, Electron transport]
Pssm-ID: 273904 [Multi-domain] Cd Length: 602 Bit Score: 778.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 44 VFVDDIPVQVVPGTTVLQAAAQIGVEIPRFCYHERLAVAGNCRMCLVEVEKSPKPVAACAMPVMKGWRIKTNSDLTRKAR 123
Cdd:TIGR01973 1 IFIDGKELEVPKGTTVLQACLSAGIEIPRFCYHEKLSIAGNCRMCLVEVEKFPKPVASCATPVTDGMKISTNSEKVKKAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 124 EGVMEFLLMNHPLDCPICDQGGECDLQDQAMAFGSDRSRFtdinYTGKRAVEDKDIGPLVKTIMTRCIHCTRCVRFASEI 203
Cdd:TIGR01973 81 EGVMEFLLINHPLDCPICDQGGECDLQDQAVMYGSDRSRF----REKKRTVENKYLGPLIKTEMTRCIHCTRCVRFANEV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 204 AGVDDLGTTGRGNDMQIGTYVEKLFLTELSGNVIDLCPVGALTNKPYSFVARPWEIRKVSSIDVLDAVGSNIVVSTRTNE 283
Cdd:TIGR01973 157 AGVEDLGVIGRGNNVEIGTYEGKTLESELSGNLIDICPVGALTSKPYAFKARPWELKSTPSICVHDSVGCNIRVDERNGE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 284 VLRILPRENEDVNEEWLADKSRFACDGLKRQ-RLVAPMVRMPNGELQAVEWEGALiAVAKAIKAAGGQIAGISGQLADLE 362
Cdd:TIGR01973 237 IMRILPRENDEINEEWLCDKGRFGYDGLNRQdRLTKPLLRNQEGNLLEVSWAEAL-AIAAEKLKASSRIGGIAGPRSSLE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 363 AQVALKDLLNRLGSEVVATEQ-GFIAGGTDNRANYLLNSTIAGLEEADAVLLVGTNPRYEAPLVNTRLRKAYVHNELQIA 441
Cdd:TIGR01973 316 ELFALKKLVRKLGSENFDLRIrNYEFESADLRANYLFNTTLADIEEADLVLLVGADLRQEAPLLNLRLRKAVKKGGAKVA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 442 SIGP-KIDLSYDH-----ENLGADAALVKDVCSGAHA-FSKVLEGAKKPAIIIGADLLERADGAAIHATVAEYCKKLKK- 513
Cdd:TIGR01973 396 LIGIeKWNLTYPAntnlvFHPGLSPKKLDDIASGAHSdIAAALKAAKKPLIIVGDSAISHLDGAALISAAANIAKVIKVr 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 514 -PNWNPFNVLQTNAAQVGALDVGYK-AGAQTAVK-AQPKVLFLLNADAGKVTREQ-----LPKDCFVVYIGSHGDNGASI 585
Cdd:TIGR01973 476 rKEWNGLNILSSGANSVGLLDLGGEsTGLDAALNlGAADALFLLGADLERALDKTardalSKADAFIIYQGHHGTETAEK 555
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
8ESZ_S1 586 ADAVLPGAAYTEKQGIYVNTEGRPQQTLPGVSPPGMAREDWKILRAL 632
Cdd:TIGR01973 556 ADVILPGAAFTEKSGTYVNLEGRAQRFEQAVKPPGEAREDWRILRAL 602
|
|
| MopB_Res-Cmplx1_Nad11 |
cd02773 |
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone ... |
263-636 |
0e+00 |
|
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone oxidoreductase/respiratory complex I/NADH dehydrogenase-1(NDH-1) of eukaryotes and the Nqo3/G subunit of alphaproteobacteria NDH-1. The NADH-quinone oxidoreductase is the first energy-transducting complex in the respiratory chains of many prokaryotes and eukaryotes. Mitochondrial complex I and its bacterial counterpart, NDH-1, function as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. The nad11 gene codes for the largest (75 kDa) subunit of the mitochondrial NADH:ubiquinone oxidoreductase, it constitutes the electron input part of the enzyme, or the so-called NADH dehydrogenase fragment. In Paracoccus denitrificans, this subunit is encoded by the nqo3 gene, and is part of the 14 distinct subunits constituting the 'minimal' functional enzyme. The Nad11/Nqo3 subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain belongs to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239174 [Multi-domain] Cd Length: 375 Bit Score: 615.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 263 SSIDVLDAVGSNIVVSTRTNEVLRILPRENEDVNEEWLADKSRFACDGLKRQRLVAPMVRMpNGELQAVEWEGALIAVAK 342
Cdd:cd02773 1 ESIDVLDAVGSNIRVDTRGGEVMRILPRLNEDINEEWISDKTRFAYDGLKRQRLDKPYIRK-NGKLKPATWEEALAAIAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 343 A-IKAAGGQIAGISGQLADLEAQVALKDLLNRLGSEVVATEQGFIAGGTDNRANYLLNSTIAGLEEADAVLLVGTNPRYE 421
Cdd:cd02773 80 AlKGVKPDEIAAIAGDLADVESMVALKDLLNKLGSENLACEQDGPDLPADLRSNYLFNTTIAGIEEADAVLLVGTNPRFE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 422 APLVNTRLRKAYVHNELQIASIGPKIDLSYDHENLGADAALVKDVCSGAHAFSKVLEGAKKPAIIIGADLLERADGAAIH 501
Cdd:cd02773 160 APVLNARIRKAWLHGGLKVGVIGPPVDLTYDYDHLGTDAKTLQDIASGKHPFSKALKDAKKPMIIVGSGALARKDGAAIL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 502 ATVAEYCKKLK--KPNWNPFNVLQTNAAQVGALDVGYKAGAQTAVKA-QPKVLFLLNADAGKVTReqLPKDCFVVYIGSH 578
Cdd:cd02773 240 AAVAKLAKKNGvvREGWNGFNVLHRAASRVGALDLGFVPGAGAIRKSgPPKVLYLLGADEIDITP--IPKDAFVVYQGHH 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
8ESZ_S1 579 GDNGASIADAVLPGAAYTEKQGIYVNTEGRPQQTLPGVSPPGMAREDWKILRALSEVV 636
Cdd:cd02773 318 GDRGAQIADVILPGAAYTEKSGTYVNTEGRVQQTRKAVSPPGDAREDWKILRALSEVL 375
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
41-658 |
0e+00 |
|
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production and conversion]; NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) is part of the Pathway/BioSystem: NADH dehydrogenase
Pssm-ID: 440657 [Multi-domain] Cd Length: 453 Bit Score: 582.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 41 KIEVFVDDIPVQVVPGTTVLQAAAQIGVEIPRFCYHERLAVAGNCRMCLVEVEKSPKPVAACAMPVMKGWRIKTNSDLTR 120
Cdd:COG1034 1 MVTITIDGKEVEVPKGTTVLQAAEKAGIEIPRFCYHPKLSIAGACRMCLVEVEGAPKPVASCATPVTDGMVVKTDSPKVK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 121 KAREGVMEFLLMNHPLDCPICDQGGECDLQDQAMAFGSDRSRFTDinytGKRAVEDKDIGPLVKTIMTRCIHCTRCVRFA 200
Cdd:COG1034 81 KARKGVMEFLLINHPLDCPICDQGGECDLQDQAMEYGVDESRYEE----EKRTVPKKDLGPLILLDMNRCILCTRCVRFC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 201 SEIAGVDDLGTTGRGNDMQIGTYVEKLFLTELSGNVIDLCPVGALTNKPYSFVARPWEIRKVSSIDVLDAVGSNIVVSTR 280
Cdd:COG1034 157 DEIAGDPELGVIGRGEHSEIGTYLGKPLDSEFSGNCIDVCPVGALTSKPFRFKARPWELKKTPSICPHCSVGCNIRVDVR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 281 TNEVLRILPRENEDVNEEWLADKSRFACDGLKR-QRLVAPMVRmPNGELQAVEWEGALIavakaikaaggqiagisgqla 359
Cdd:COG1034 237 GGKVYRVLPRENEAVNEEWLCDKGRFGYDGLNSpDRLTRPLVR-KDGELVEASWEEALA--------------------- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 360 dleaqvALKDLLNRLGSEvvateqgfiaggtDNRanyllnstiagleeadavllVGtnpryeaplvntrlrkayvhnelq 439
Cdd:COG1034 295 ------AAAEGLKALKKA-------------ENS--------------------VG------------------------ 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 440 iasigpkidlsydhenlgadAALVKDVCSGAHAFSKVLEGAKKPAIIIGADlLERADGAAIhatvaeyckklkkpnwnpf 519
Cdd:COG1034 312 --------------------AALLGALPDAAAILEAAEAGKLKALVLLGAD-PYDLDPAAA------------------- 351
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 520 nvlqtnaaqvgaldvgykagaqtavkaqpkvlfllnadagkvtREQLPKDCFVVYIGSHGDNGASIADAVLPGAAYTEKQ 599
Cdd:COG1034 352 -------------------------------------------LAALAKADFVVVLDHFGSATAERADVVLPAAAFAEKS 388
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
8ESZ_S1 600 GIYVNTEGRPQQTLPGVSPPGMAREDWKILRALSEVVGKPLPYDNLDELRNRLEDVAPH 658
Cdd:COG1034 389 GTFVNLEGRVQRFNAAVPPPGEARPDWRVLRALANALGAGLPYDSLEEVRAELAAEAPA 447
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
315-635 |
1.86e-114 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 349.39 E-value: 1.86e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 315 RLVAPMVRMPNGELQAVEWEGAL-------IAVAKAIKAAGGQIAGISGQLADLEAQVALKDLLNRLGSEVVATEQGF-- 385
Cdd:pfam00384 1 RLKYPMVRRGDGKFVRVSWDEALdliakklKRIIKKYGPDAIAINGGSGGLTDVESLYALKKLLNRLGSKNGNTEDHNgd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 386 ------IAGGTDNRANYLLNSTIAGLEEADAVLLVGTNPRYEAPLVNTRLRKAYVHNELQIASIGPKIDLSYDHENLGAD 459
Cdd:pfam00384 81 lctaaaAAFGSDLRSNYLFNSSIADIENADLILLIGTNPREEAPILNARIRKAALKGKAKVIVIGPRLDLTYADEHLGIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 460 AA-LVKDVCSGAHAFSKVLEGAK----KPAIIIGADLLERADGAAIHATVAEYCKKLKKP-----NWNPFNVLQTNAAQV 529
Cdd:pfam00384 161 PGtDLALALAGAHVFIKELKKDKdfapKPIIIVGAGVLQRQDGEAIFRAIANLADLTGNIgrpggGWNGLNILQGAASPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 530 GALDVGYKAG------AQTAVKAQPKVLFLLN-------ADAGKVTREQLPKDCFVVYIGSHGDNGASIADAVLPGAAYT 596
Cdd:pfam00384 241 GALDLGLVPGiksvemINAIKKGGIKVLYLLGnnpfvthADENRVVKALQKLDLFVVYDGHHGDKTAKYADVILPAAAYT 320
|
330 340 350
....*....|....*....|....*....|....*....
8ESZ_S1 597 EKQGIYVNTEGRPQQTLPGVSPPGMAREDWKILRALSEV 635
Cdd:pfam00384 321 EKNGTYVNTEGRVQSTKQAVPPPGEAREDWKILRALSEV 359
|
|
| PRK07860 |
PRK07860 |
NADH dehydrogenase subunit G; Validated |
38-657 |
3.91e-104 |
|
NADH dehydrogenase subunit G; Validated
Pssm-ID: 236118 [Multi-domain] Cd Length: 797 Bit Score: 336.53 E-value: 3.91e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 38 APEKIEVFVDDIPVQVVPGTTVLQAAAQIGVEIPRFCYHERLAVAGNCRMCLVEVEKSPKPVAACAMPVMKGWRIKT--N 115
Cdd:PRK07860 1 PPDLVTLTIDGVEVSVPKGTLVIRAAELLGIQIPRFCDHPLLDPVGACRQCLVEVEGQRKPQASCTTTVTDGMVVKTqlT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 116 SDLTRKAREGVMEFLLMNHPLDCPICDQGGECDLQDQAMAFGSDRSRFTDInytgKRAVEdKDIgPLVKTIM---TRCIH 192
Cdd:PRK07860 81 SPVADKAQHGVMELLLINHPLDCPVCDKGGECPLQNQAMSNGRAESRFTDV----KRTFP-KPI-NISTQVLldrERCVL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 193 CTRCVRFASEIAGVDDLGTTGRGNDMQIGTYVEKLFLTELSGNVIDLCPVGALTNKPYSFVARPWEIrkVSSIDVL--DA 270
Cdd:PRK07860 155 CARCTRFSDQIAGDPFIDLQERGALQQVGIYEGEPFQSYFSGNTVQICPVGALTGAAYRFRARPFDL--VSTPSVCehCA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 271 VGSNIVVSTRTNEVLRILPRENEDVNEEWLADKSRFACD-GLKRQRLVAPMVRMPNGELQAVEWEGALIAVAKAIKAAGG 349
Cdd:PRK07860 233 SGCAQRTDHRRGKVLRRLAGDDPEVNEEWNCDKGRWAFTyATQPDRITTPLVRDEDGELEPASWSEALAVAARGLAAARG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 350 QIAGISGQLADLE--------AQVALK----DLLNRLGSevvATEQGFIAGGTDNRAnylLNSTIAGLEEADAVLLVGTN 417
Cdd:PRK07860 313 RVGVLVGGRLTVEdayayakfARVALGtndiDFRARPHS---AEEADFLAARVAGRG---LGVTYADLEKAPAVLLVGFE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 418 PRYEAPLVNTRLRKAYVHNELQIASIGPKID--LSYDHENL-----GADAALVKDVcsgAHAFSKVLEGAKKP-AIIIGA 489
Cdd:PRK07860 387 PEEESPIVFLRLRKAARKHGLKVYSIAPFATrgLEKMGGTLlrtapGGEAAALDAL---ATGAPDVAELLRTPgAVILVG 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 490 DLLERADGA--AIHATVAEYCKKLKkpnWNPfnvlqTNAAQVGALDVGY--------------KAGAQTA----VKAQPK 549
Cdd:PRK07860 464 ERLATVPGAlsAAARLADATGARLA---WVP-----RRAGERGALEAGAlptllpggrpvadpAARAEVAaawgVDELPA 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 550 VL------FLLNADAGKV------------------TREQLPKDCFVVYIGSHGDNGASIADAVLPGAAYTEKQGIYVNT 605
Cdd:PRK07860 536 APgrdtagILAAAAAGELgallvggvepadlpdpaaALAALDAAGFVVSLELRHSAVTERADVVLPVAPVAEKAGTFLNW 615
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
8ESZ_S1 606 EGRP---QQTLPGVSPPgmarEDWKILRALSEVVGKPLPYDNLDELRNRLEDVAP 657
Cdd:PRK07860 616 EGRLrpfEAALRTTGAL----SDLRVLDALADEMGVDLGLPTVAAARAELARLGA 666
|
|
| NADH-G_4Fe-4S_3 |
smart00929 |
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region; |
123-163 |
1.83e-17 |
|
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region;
Pssm-ID: 214918 [Multi-domain] Cd Length: 41 Bit Score: 76.08 E-value: 1.83e-17
10 20 30 40
....*....|....*....|....*....|....*....|.
8ESZ_S1 123 REGVMEFLLMNHPLDCPICDQGGECDLQDQAMAFGSDRSRF 163
Cdd:smart00929 1 RKTILELLLANHPLDCPVCDKNGECELQDLAYELGVDEQRY 41
|
|
| NADH_dhqG_C |
pfam09326 |
NADH-ubiquinone oxidoreductase subunit G, C-terminal; Members of this family of are found at ... |
671-712 |
1.22e-09 |
|
NADH-ubiquinone oxidoreductase subunit G, C-terminal; Members of this family of are found at the C-terminus of NADH dehydrogenases subunit G or NADH-ubiquinone oxidoreductase subunit G. EC:1.6.99.5.
Pssm-ID: 462757 Cd Length: 41 Bit Score: 54.15 E-value: 1.22e-09
10 20 30 40
....*....|....*....|....*....|....*....|..
8ESZ_S1 671 AGAAGTISksigGGAIDiklKELRDYFMTDAISRASPTMAKC 712
Cdd:pfam09326 7 AGAKGKLS----GAPLK---SPIEDFYMTDPISRASATMAKC 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 ... |
44-632 |
0e+00 |
|
NADH-quinone oxidoreductase, chain G; This model represents the G subunit (one of 14: A->N) of the NADH-quinone oxidoreductase complex I which generally couples NADH and ubiquinone oxidation/reduction in bacteria and mammalian mitochondria while translocating protons, but may act on NADPH and/or plastoquinone in cyanobacteria and plant chloroplasts. This model excludes related subunits from formate dehydrogenase complexes. [Energy metabolism, Electron transport]
Pssm-ID: 273904 [Multi-domain] Cd Length: 602 Bit Score: 778.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 44 VFVDDIPVQVVPGTTVLQAAAQIGVEIPRFCYHERLAVAGNCRMCLVEVEKSPKPVAACAMPVMKGWRIKTNSDLTRKAR 123
Cdd:TIGR01973 1 IFIDGKELEVPKGTTVLQACLSAGIEIPRFCYHEKLSIAGNCRMCLVEVEKFPKPVASCATPVTDGMKISTNSEKVKKAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 124 EGVMEFLLMNHPLDCPICDQGGECDLQDQAMAFGSDRSRFtdinYTGKRAVEDKDIGPLVKTIMTRCIHCTRCVRFASEI 203
Cdd:TIGR01973 81 EGVMEFLLINHPLDCPICDQGGECDLQDQAVMYGSDRSRF----REKKRTVENKYLGPLIKTEMTRCIHCTRCVRFANEV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 204 AGVDDLGTTGRGNDMQIGTYVEKLFLTELSGNVIDLCPVGALTNKPYSFVARPWEIRKVSSIDVLDAVGSNIVVSTRTNE 283
Cdd:TIGR01973 157 AGVEDLGVIGRGNNVEIGTYEGKTLESELSGNLIDICPVGALTSKPYAFKARPWELKSTPSICVHDSVGCNIRVDERNGE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 284 VLRILPRENEDVNEEWLADKSRFACDGLKRQ-RLVAPMVRMPNGELQAVEWEGALiAVAKAIKAAGGQIAGISGQLADLE 362
Cdd:TIGR01973 237 IMRILPRENDEINEEWLCDKGRFGYDGLNRQdRLTKPLLRNQEGNLLEVSWAEAL-AIAAEKLKASSRIGGIAGPRSSLE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 363 AQVALKDLLNRLGSEVVATEQ-GFIAGGTDNRANYLLNSTIAGLEEADAVLLVGTNPRYEAPLVNTRLRKAYVHNELQIA 441
Cdd:TIGR01973 316 ELFALKKLVRKLGSENFDLRIrNYEFESADLRANYLFNTTLADIEEADLVLLVGADLRQEAPLLNLRLRKAVKKGGAKVA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 442 SIGP-KIDLSYDH-----ENLGADAALVKDVCSGAHA-FSKVLEGAKKPAIIIGADLLERADGAAIHATVAEYCKKLKK- 513
Cdd:TIGR01973 396 LIGIeKWNLTYPAntnlvFHPGLSPKKLDDIASGAHSdIAAALKAAKKPLIIVGDSAISHLDGAALISAAANIAKVIKVr 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 514 -PNWNPFNVLQTNAAQVGALDVGYK-AGAQTAVK-AQPKVLFLLNADAGKVTREQ-----LPKDCFVVYIGSHGDNGASI 585
Cdd:TIGR01973 476 rKEWNGLNILSSGANSVGLLDLGGEsTGLDAALNlGAADALFLLGADLERALDKTardalSKADAFIIYQGHHGTETAEK 555
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
8ESZ_S1 586 ADAVLPGAAYTEKQGIYVNTEGRPQQTLPGVSPPGMAREDWKILRAL 632
Cdd:TIGR01973 556 ADVILPGAAFTEKSGTYVNLEGRAQRFEQAVKPPGEAREDWRILRAL 602
|
|
| MopB_Res-Cmplx1_Nad11 |
cd02773 |
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone ... |
263-636 |
0e+00 |
|
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone oxidoreductase/respiratory complex I/NADH dehydrogenase-1(NDH-1) of eukaryotes and the Nqo3/G subunit of alphaproteobacteria NDH-1. The NADH-quinone oxidoreductase is the first energy-transducting complex in the respiratory chains of many prokaryotes and eukaryotes. Mitochondrial complex I and its bacterial counterpart, NDH-1, function as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. The nad11 gene codes for the largest (75 kDa) subunit of the mitochondrial NADH:ubiquinone oxidoreductase, it constitutes the electron input part of the enzyme, or the so-called NADH dehydrogenase fragment. In Paracoccus denitrificans, this subunit is encoded by the nqo3 gene, and is part of the 14 distinct subunits constituting the 'minimal' functional enzyme. The Nad11/Nqo3 subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain belongs to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239174 [Multi-domain] Cd Length: 375 Bit Score: 615.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 263 SSIDVLDAVGSNIVVSTRTNEVLRILPRENEDVNEEWLADKSRFACDGLKRQRLVAPMVRMpNGELQAVEWEGALIAVAK 342
Cdd:cd02773 1 ESIDVLDAVGSNIRVDTRGGEVMRILPRLNEDINEEWISDKTRFAYDGLKRQRLDKPYIRK-NGKLKPATWEEALAAIAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 343 A-IKAAGGQIAGISGQLADLEAQVALKDLLNRLGSEVVATEQGFIAGGTDNRANYLLNSTIAGLEEADAVLLVGTNPRYE 421
Cdd:cd02773 80 AlKGVKPDEIAAIAGDLADVESMVALKDLLNKLGSENLACEQDGPDLPADLRSNYLFNTTIAGIEEADAVLLVGTNPRFE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 422 APLVNTRLRKAYVHNELQIASIGPKIDLSYDHENLGADAALVKDVCSGAHAFSKVLEGAKKPAIIIGADLLERADGAAIH 501
Cdd:cd02773 160 APVLNARIRKAWLHGGLKVGVIGPPVDLTYDYDHLGTDAKTLQDIASGKHPFSKALKDAKKPMIIVGSGALARKDGAAIL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 502 ATVAEYCKKLK--KPNWNPFNVLQTNAAQVGALDVGYKAGAQTAVKA-QPKVLFLLNADAGKVTReqLPKDCFVVYIGSH 578
Cdd:cd02773 240 AAVAKLAKKNGvvREGWNGFNVLHRAASRVGALDLGFVPGAGAIRKSgPPKVLYLLGADEIDITP--IPKDAFVVYQGHH 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
8ESZ_S1 579 GDNGASIADAVLPGAAYTEKQGIYVNTEGRPQQTLPGVSPPGMAREDWKILRALSEVV 636
Cdd:cd02773 318 GDRGAQIADVILPGAAYTEKSGTYVNTEGRVQQTRKAVSPPGDAREDWKILRALSEVL 375
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
41-658 |
0e+00 |
|
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production and conversion]; NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) is part of the Pathway/BioSystem: NADH dehydrogenase
Pssm-ID: 440657 [Multi-domain] Cd Length: 453 Bit Score: 582.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 41 KIEVFVDDIPVQVVPGTTVLQAAAQIGVEIPRFCYHERLAVAGNCRMCLVEVEKSPKPVAACAMPVMKGWRIKTNSDLTR 120
Cdd:COG1034 1 MVTITIDGKEVEVPKGTTVLQAAEKAGIEIPRFCYHPKLSIAGACRMCLVEVEGAPKPVASCATPVTDGMVVKTDSPKVK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 121 KAREGVMEFLLMNHPLDCPICDQGGECDLQDQAMAFGSDRSRFTDinytGKRAVEDKDIGPLVKTIMTRCIHCTRCVRFA 200
Cdd:COG1034 81 KARKGVMEFLLINHPLDCPICDQGGECDLQDQAMEYGVDESRYEE----EKRTVPKKDLGPLILLDMNRCILCTRCVRFC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 201 SEIAGVDDLGTTGRGNDMQIGTYVEKLFLTELSGNVIDLCPVGALTNKPYSFVARPWEIRKVSSIDVLDAVGSNIVVSTR 280
Cdd:COG1034 157 DEIAGDPELGVIGRGEHSEIGTYLGKPLDSEFSGNCIDVCPVGALTSKPFRFKARPWELKKTPSICPHCSVGCNIRVDVR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 281 TNEVLRILPRENEDVNEEWLADKSRFACDGLKR-QRLVAPMVRmPNGELQAVEWEGALIavakaikaaggqiagisgqla 359
Cdd:COG1034 237 GGKVYRVLPRENEAVNEEWLCDKGRFGYDGLNSpDRLTRPLVR-KDGELVEASWEEALA--------------------- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 360 dleaqvALKDLLNRLGSEvvateqgfiaggtDNRanyllnstiagleeadavllVGtnpryeaplvntrlrkayvhnelq 439
Cdd:COG1034 295 ------AAAEGLKALKKA-------------ENS--------------------VG------------------------ 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 440 iasigpkidlsydhenlgadAALVKDVCSGAHAFSKVLEGAKKPAIIIGADlLERADGAAIhatvaeyckklkkpnwnpf 519
Cdd:COG1034 312 --------------------AALLGALPDAAAILEAAEAGKLKALVLLGAD-PYDLDPAAA------------------- 351
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 520 nvlqtnaaqvgaldvgykagaqtavkaqpkvlfllnadagkvtREQLPKDCFVVYIGSHGDNGASIADAVLPGAAYTEKQ 599
Cdd:COG1034 352 -------------------------------------------LAALAKADFVVVLDHFGSATAERADVVLPAAAFAEKS 388
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
8ESZ_S1 600 GIYVNTEGRPQQTLPGVSPPGMAREDWKILRALSEVVGKPLPYDNLDELRNRLEDVAPH 658
Cdd:COG1034 389 GTFVNLEGRVQRFNAAVPPPGEARPDWRVLRALANALGAGLPYDSLEEVRAELAAEAPA 447
|
|
| MopB_NADH-Q-OR-NuoG2 |
cd02768 |
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone ... |
264-635 |
2.23e-142 |
|
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: 422.46 E-value: 2.23e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 264 SIDVLDAVGSNIVVSTRTNEVLRILPRENEDVNEEWLADKSRFACDGLK-RQRLVAPMVRMpNGELQAVEWEGALIAVAK 342
Cdd:cd02768 2 SIDVHDALGSNIRVDVRGGEVMRILPRENEAINEEWISDKGRFGYDGLNsRQRLTQPLIKK-GGKLVPVSWEEALKTVAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 343 A-IKAAGGQIAGISGQLADLEAQVALKDLLNRLGSEVVATEQGFIAGGTDNRA--NYLLNSTIAGLEEADAVLLVGTNPR 419
Cdd:cd02768 81 GlKAVKGDKIGGIAGPRADLESLFLLKKLLNKLGSNNIDHRLRQSDLPADNRLrgNYLFNTSIAEIEEADAVLLIGSNLR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 420 YEAPLVNTRLRKAYVHNELQIASIGPK-----IDLSYDHENLGADAALVKDVCSGAH--AFSKVLEGAKKPAIIIGADLL 492
Cdd:cd02768 161 KEAPLLNARLRKAVKKKGAKIAVIGPKdtdliADLTYPVSPLGASLATLLDIAEGKHlkPFAKSLKKAKKPLIILGSSAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 493 eRADGAAIHATVAEYCKKLKK--PNWNPFNVLQTNAAQVGA--LDVGYKAGAQTAVKaqpkvLFLLNADAGKVTREQL-- 566
Cdd:cd02768 241 -RKDGAAILKALANLAAKLGTgaGLWNGLNVLNSVGARLGGagLDAGLALLEPGKAK-----LLLLGEDELDRSNPPAav 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
8ESZ_S1 567 ---PKDCFVVYIGSHGDNGASiADAVLPGAAYTEKQGIYVNTEGRPQQTLPGVSPPGMAREDWKILRALSEV 635
Cdd:cd02768 315 alaAADAFVVYQGHHGDTGAQ-ADVILPAAAFTEKSGTYVNTEGRVQRFKKAVSPPGDAREDWKILRALSNL 385
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
315-635 |
1.86e-114 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 349.39 E-value: 1.86e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 315 RLVAPMVRMPNGELQAVEWEGAL-------IAVAKAIKAAGGQIAGISGQLADLEAQVALKDLLNRLGSEVVATEQGF-- 385
Cdd:pfam00384 1 RLKYPMVRRGDGKFVRVSWDEALdliakklKRIIKKYGPDAIAINGGSGGLTDVESLYALKKLLNRLGSKNGNTEDHNgd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 386 ------IAGGTDNRANYLLNSTIAGLEEADAVLLVGTNPRYEAPLVNTRLRKAYVHNELQIASIGPKIDLSYDHENLGAD 459
Cdd:pfam00384 81 lctaaaAAFGSDLRSNYLFNSSIADIENADLILLIGTNPREEAPILNARIRKAALKGKAKVIVIGPRLDLTYADEHLGIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 460 AA-LVKDVCSGAHAFSKVLEGAK----KPAIIIGADLLERADGAAIHATVAEYCKKLKKP-----NWNPFNVLQTNAAQV 529
Cdd:pfam00384 161 PGtDLALALAGAHVFIKELKKDKdfapKPIIIVGAGVLQRQDGEAIFRAIANLADLTGNIgrpggGWNGLNILQGAASPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 530 GALDVGYKAG------AQTAVKAQPKVLFLLN-------ADAGKVTREQLPKDCFVVYIGSHGDNGASIADAVLPGAAYT 596
Cdd:pfam00384 241 GALDLGLVPGiksvemINAIKKGGIKVLYLLGnnpfvthADENRVVKALQKLDLFVVYDGHHGDKTAKYADVILPAAAYT 320
|
330 340 350
....*....|....*....|....*....|....*....
8ESZ_S1 597 EKQGIYVNTEGRPQQTLPGVSPPGMAREDWKILRALSEV 635
Cdd:pfam00384 321 EKNGTYVNTEGRVQSTKQAVPPPGEAREDWKILRALSEV 359
|
|
| PRK07860 |
PRK07860 |
NADH dehydrogenase subunit G; Validated |
38-657 |
3.91e-104 |
|
NADH dehydrogenase subunit G; Validated
Pssm-ID: 236118 [Multi-domain] Cd Length: 797 Bit Score: 336.53 E-value: 3.91e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 38 APEKIEVFVDDIPVQVVPGTTVLQAAAQIGVEIPRFCYHERLAVAGNCRMCLVEVEKSPKPVAACAMPVMKGWRIKT--N 115
Cdd:PRK07860 1 PPDLVTLTIDGVEVSVPKGTLVIRAAELLGIQIPRFCDHPLLDPVGACRQCLVEVEGQRKPQASCTTTVTDGMVVKTqlT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 116 SDLTRKAREGVMEFLLMNHPLDCPICDQGGECDLQDQAMAFGSDRSRFTDInytgKRAVEdKDIgPLVKTIM---TRCIH 192
Cdd:PRK07860 81 SPVADKAQHGVMELLLINHPLDCPVCDKGGECPLQNQAMSNGRAESRFTDV----KRTFP-KPI-NISTQVLldrERCVL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 193 CTRCVRFASEIAGVDDLGTTGRGNDMQIGTYVEKLFLTELSGNVIDLCPVGALTNKPYSFVARPWEIrkVSSIDVL--DA 270
Cdd:PRK07860 155 CARCTRFSDQIAGDPFIDLQERGALQQVGIYEGEPFQSYFSGNTVQICPVGALTGAAYRFRARPFDL--VSTPSVCehCA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 271 VGSNIVVSTRTNEVLRILPRENEDVNEEWLADKSRFACD-GLKRQRLVAPMVRMPNGELQAVEWEGALIAVAKAIKAAGG 349
Cdd:PRK07860 233 SGCAQRTDHRRGKVLRRLAGDDPEVNEEWNCDKGRWAFTyATQPDRITTPLVRDEDGELEPASWSEALAVAARGLAAARG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 350 QIAGISGQLADLE--------AQVALK----DLLNRLGSevvATEQGFIAGGTDNRAnylLNSTIAGLEEADAVLLVGTN 417
Cdd:PRK07860 313 RVGVLVGGRLTVEdayayakfARVALGtndiDFRARPHS---AEEADFLAARVAGRG---LGVTYADLEKAPAVLLVGFE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 418 PRYEAPLVNTRLRKAYVHNELQIASIGPKID--LSYDHENL-----GADAALVKDVcsgAHAFSKVLEGAKKP-AIIIGA 489
Cdd:PRK07860 387 PEEESPIVFLRLRKAARKHGLKVYSIAPFATrgLEKMGGTLlrtapGGEAAALDAL---ATGAPDVAELLRTPgAVILVG 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 490 DLLERADGA--AIHATVAEYCKKLKkpnWNPfnvlqTNAAQVGALDVGY--------------KAGAQTA----VKAQPK 549
Cdd:PRK07860 464 ERLATVPGAlsAAARLADATGARLA---WVP-----RRAGERGALEAGAlptllpggrpvadpAARAEVAaawgVDELPA 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 550 VL------FLLNADAGKV------------------TREQLPKDCFVVYIGSHGDNGASIADAVLPGAAYTEKQGIYVNT 605
Cdd:PRK07860 536 APgrdtagILAAAAAGELgallvggvepadlpdpaaALAALDAAGFVVSLELRHSAVTERADVVLPVAPVAEKAGTFLNW 615
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
8ESZ_S1 606 EGRP---QQTLPGVSPPgmarEDWKILRALSEVVGKPLPYDNLDELRNRLEDVAP 657
Cdd:PRK07860 616 EGRLrpfEAALRTTGAL----SDLRVLDALADEMGVDLGLPTVAAARAELARLGA 666
|
|
| MopB_Res-Cmplx1_Nad11-M |
cd02774 |
MopB_Res_Cmplx1_Nad11_M: Mitochondrial-encoded NADH-quinone oxidoreductase/respiratory complex ... |
264-632 |
4.04e-66 |
|
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: 223.01 E-value: 4.04e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 264 SIDVLDAVGSNIVVSTRTNEVLRILPRENEDVNEEWLADKSRFACDGLKRQRLVAPMVRMPNGELQAVEWEGALIA-VAK 342
Cdd:cd02774 2 SIDVLDSLGSNIRVDIKGNEILRILPKINDELNEEWISDKIRFSYDSLKYQRIKTPLLKLSNNSFLEIGWKTAFKFlNKF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 343 AIKAAGGQIAGISGQLADLEAQVALKDLLNRLGSEVVATEQGFIAGG--TDNRANYLLNSTIAGLEEADAVLLVGTNPRY 420
Cdd:cd02774 82 ILLKKFSKLNFIIGSKIDLETLFYYKKLLNKLGSLNTNSNNFLENNNyfNLDLENYLFNNSLKNLDKSDLCLLIGSNLRV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 421 EAPLVNTRLRKAYVHNELQIASIGPKIDLSYDHENLGADAALVKDVCSGAHAFSKVLEGAKKPAIIIGADLLERADGAAI 500
Cdd:cd02774 162 ESPILNIRLRNRYNKGNKKIFVIGNKFDTTYPSKHIGLSLNTLLKILEGKHLFCKQLKKSKKPLIIIGSSFSLRKNYSFI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 501 HATVaeycKKLKKPNWNPFNVLQTNAAQVGALDVGYKAGAQtavKAQPKVLFLLNADAGKVTReqlpKDCFVVYIGSHGD 580
Cdd:cd02774 242 ISKL----KNFSSNNENNFNFLNIISNSLYYLGIKKFNSNN---KKNLSNLYYIKETNFQKFN----KNNFVIYQGHHFL 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
8ESZ_S1 581 NGASIADAVLPGAAYTEKQGIYVNTEGRPQQTLPGVSPPGMAREDWKILRAL 632
Cdd:cd02774 311 NLANNSNLILPSKTFFEKEALYLNLEGILQKTKKILSFKENIKSDDNIIFSL 362
|
|
| PTZ00305 |
PTZ00305 |
NADH:ubiquinone oxidoreductase; Provisional |
17-245 |
7.98e-60 |
|
NADH:ubiquinone oxidoreductase; Provisional
Pssm-ID: 140326 [Multi-domain] Cd Length: 297 Bit Score: 203.73 E-value: 7.98e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 17 THQMASRAVRTSAMVAQTPAKAPEKIeVFVDDIPVQVVPGT-TVLQAAAQIGVEIPRFCYHERLAVAGNCRMCLVEVEKS 95
Cdd:PTZ00305 45 NHRGGVEAAAEGVAAGQYAEHKPRAI-MFVNKRPVEIIPQEeNLLEVLEREGIRVPKFCYHPILSVAGNCRMCLVQVDGT 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 96 PKPVAACAMPVMKGWRIKTNSDLTRKAREGVMEFLLMNHPLDCPICDQGGECDLQDQAMAFGSDRSRFTDinytGKRAVE 175
Cdd:PTZ00305 124 QNLVVSCATVALPGMSIITDSRLVRDAREGNVELILINHPNDCPICEQATNCDLQNVSMNYGTDIPRYKE----DKRAVQ 199
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
8ESZ_S1 176 DKDIGPLVKTIMTRCIHCTRCVRFASEIAGVDDLGTTGRGNDMQIGTYVEKLFL-TELSGNVIDLCPVGAL 245
Cdd:PTZ00305 200 DFYFDPQTRVVLNRCIHCTRCVRFLNEHAQDFNLGMIGRGGLSEISTFLDELEVkTDNNMPVSQLCPVGKL 270
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
264-636 |
1.55e-58 |
|
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: 202.94 E-value: 1.55e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 264 SIDVLDAVGSNIVVSTRTNEVLRILPRENEDVNEEWLADKSRFACDGLK-RQRLVAPMVRM-PNGELQAVEWEGALIA-- 339
Cdd:cd00368 2 SVCPFCGVGCGILVYVKDGKVVRIEGDPNHPVNEGRLCDKGRAGLDGLYsPDRLKYPLIRVgGRGKFVPISWDEALDEia 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 340 ---VAKAIKAAGGQIAGISGQLADLEAQVALKDLLNRLGSEVVATEQGFIAGGTDNRA----NYLLNSTIAGLEEADAVL 412
Cdd:cd00368 82 eklKEIREKYGPDAIAFYGGGGASNEEAYLLQKLLRALGSNNVDSHARLCHASAVAALkafgGGAPTNTLADIENADLIL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 413 LVGTNPRYEAPLVNTRLRKAyVHNELQIASIGPKIDLSYDHENL------GADAALVKdvcsgahafskvlegAKKPAII 486
Cdd:cd00368 162 LWGSNPAETHPVLAARLRRA-KKRGAKLIVIDPRRTETAAKADEwlpirpGTDAALAL---------------AEWAAEI 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 487 IGADlleradgAAIHATVAEYCKKLKKPNWNPFNVLQ--TNAAQVG------ALDVGY--KAGAQTAVKAQPkvlFLLNA 556
Cdd:cd00368 226 TGVP-------AETIRALAREFAAAKRAVILWGMGLTqhTNGTQNVraianlAALTGNigRPGGGLGPGGNP---LVSAP 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 557 DAGKVTREQLPKDCFVVYIGSHGDNGAsIADAVLPGAAYTEKQGIYVNTEGRPQQTLPGVSPPGMAREDWKILRALSEVV 636
Cdd:cd00368 296 DANRVRAALKKLDFVVVIDIFMTETAA-YADVVLPAATYLEKEGTYTNTEGRVQLFRQAVEPPGEARSDWEILRELAKRL 374
|
|
| MopB_NDH-1_NuoG2 |
cd02772 |
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase ... |
264-632 |
3.85e-56 |
|
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: 197.58 E-value: 3.85e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 264 SIDVLDAVGSNIVVSTRTNEVLRILPRENEDVNEEWLADKSRFACDGLKRQ-RLVAPMVRMpNGELQAVEWEGALIAVAK 342
Cdd:cd02772 2 SVSPHDALGSNLVVHVKNNKVMRVVPRENEAINECWLSDRDRFSYEGLNSEdRLTKPMIKK-DGQWQEVDWETALEYVAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 343 -----AIKAAGGQIAGISGQLADLEAQVALKDLLNRLGSEVVAT---EQGFIAGGTDNRANYlLNSTIAGLEEADAVLLV 414
Cdd:cd02772 81 glsaiIKKHGADQIGALASPHSTLEELYLLQKLARGLGSDNIDHrlrQSDFRDDAKASGAPW-LGMPIAEISELDRVLVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 415 GTNPRYEAPLVNTRLRKAyVHNELQIASIGPKID---LSYDHENLGADAALV------------------------KDVC 467
Cdd:cd02772 160 GSNLRKEHPLLAQRLRQA-VKKGAKLSAINPADDdflFPLSGKAIVAPSALAnalaqvakalaeekglavpdedakVEAS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 468 SGAHAFSKVLEGAKKPAIIIGADLLERADGAAIHATVAEyckkLKKPNWNPFNVLQTNAAQVGAldvgYKAGAQ------ 541
Cdd:cd02772 239 EEARKIAASLVSAERAAVFLGNLAQNHPQAATLRALAQE----IAKLTGATLGVLGEGANSVGA----YLAGALphggln 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 542 -TAVKAQP-KVLFLLNADAG------KVTREQLPKDCFVVYIGSHGDNGA-SIADAVLPGAAYTEKQGIYVNTEGRPQQT 612
Cdd:cd02772 311 aAAMLEQPrKAYLLLNVEPEldcanpAQALAALNQAEFVVALSAFASAALlDYADVLLPIAPFTETSGTFVNLEGRVQSF 390
|
410 420
....*....|....*....|
8ESZ_S1 613 LPGVSPPGMAREDWKILRAL 632
Cdd:cd02772 391 KGVVKPLGEARPAWKVLRVL 410
|
|
| PRK07569 |
PRK07569 |
bidirectional hydrogenase complex protein HoxU; Validated |
46-248 |
3.61e-36 |
|
bidirectional hydrogenase complex protein HoxU; Validated
Pssm-ID: 181037 [Multi-domain] Cd Length: 234 Bit Score: 136.32 E-value: 3.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 46 VDDIPVQVVPGTTVLQAAAQIGVEIPRFCYHERLAVAGNCRMCLVEVEKSPKPVAACAMPVMKGWRIKTNSDLTRKAREG 125
Cdd:PRK07569 8 IDDQLVSAREGETLLEAAREAGIPIPTLCHLDGLSDVGACRLCLVEIEGSNKLLPACVTPVAEGMVVQTNTPRLQEYRRM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 126 VMEFLLM--NHPldCPICDQGGECDLQDQAMAFGSDRSRFT------DINYTGKRAVEDKDigplvktimtRCIHCTRCV 197
Cdd:PRK07569 88 IVELLFAegNHV--CAVCVANGNCELQDLAIEVGMDHVRFPylfprrPVDISHPRFGIDHN----------RCVLCTRCV 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
8ESZ_S1 198 RFASEIAGVDDLGTTGRGNDMQIGTYVEKLFLTELS----GNVIDLCPVGALTNK 248
Cdd:PRK07569 156 RVCDEIEGAHTWDVAGRGAKSRVITDLNQPWGTSETctscGKCVQACPTGAIFRK 210
|
|
| PRK08493 |
PRK08493 |
NADH-quinone oxidoreductase subunit G; |
41-264 |
1.10e-29 |
|
NADH-quinone oxidoreductase subunit G;
Pssm-ID: 236277 [Multi-domain] Cd Length: 819 Bit Score: 125.97 E-value: 1.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 41 KIEVFVDDIPVQVVPGTTVLQAAAQIGVEIPRFCYHERLAVAGNCRMCLVEVekSPKPVAACAMPVMKGWRIKTNSDLTR 120
Cdd:PRK08493 1 MITITINGKECEAQEGEYILNVARRNGIFIPAICYLSGCSPTLACRLCMVEA--DGKRVYSCNTKAKEGMNILTNTPNLM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 121 KAREGVMEFLLMNHPLDCPICDQGGECDLQDQAMAFGSDRSRFtdinytgkrAVEDkDIGPLVKTIMTR-----CIHCTR 195
Cdd:PRK08493 79 DERNAIMQTYDVNHPLECGVCDKSGECELQNFTHEMGVNHQPY---------AIKD-THKPHKHWGKINydpslCIVCER 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 196 CVRFASEIAGVDDLGTTGRGNDMQIGTYVEKLFLTELS-----------------------GNVIDLCPVGALTNKPYSF 252
Cdd:PRK08493 149 CVTVCKDKIGESALKTVPRGLDAPDKSFKESMPKDAYAvwskkqksligpvggetldcsfcGECIAVCPVGALSSSDFQY 228
|
250
....*....|..
8ESZ_S1 253 VARPWEIRKVSS 264
Cdd:PRK08493 229 TSNAWELKKIPA 240
|
|
| 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 ... |
270-673 |
2.59e-28 |
|
MopB_NDH-1_NuoG2-N7: The second domain of the NuoG subunit (with a [4Fe-4S] cluster, N7) of the NADH-quinone oxidoreductase/NADH dehydrogenase-1 (NDH-1) found in various bacteria. The NDH-1 is the first energy-transducting complex in the respiratory chain and functions as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. In Escherichia coli NDH-1, the largest subunit is encoded by the nuoG gene, and is part of the 14 distinct subunits constituting the functional enzyme. The NuoG subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Unique to this group, compared to the other prokaryotic and eukaryotic groups in this domain protein family (NADH-Q-OR-NuoG2), is an N-terminal [4Fe-4S] cluster (N7/N1c) present in the second domain. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain belongs to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239172 [Multi-domain] Cd Length: 472 Bit Score: 119.03 E-value: 2.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 270 AVGSNIVVSTRTNEVLRILPRENEDVNEEWLADKSRFACDGLK-RQRLVAPMVRMpNGELQAVEWEGALIAVAKAIKAAG 348
Cdd:cd02771 8 SVGCNISLGERYGELRRVENRYNGAVNHYFLCDRGRFGYGYVNsRDRLTQPLIRR-GGTLVPVSWNEALDVAAARLKEAK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 349 GQIAGISGQLADLEAQVALKDLL-NRLGSEVVatEQGFIAGGTDN-RANYLLNSTIAGLEEADAVLLVGTNPRYEAPLVN 426
Cdd:cd02771 87 DKVGGIGSPRASNESNYALQKLVgAVLGTNNV--DHRARRLIAEIlRNGPIYIPSLRDIESADAVLVLGEDLTQTAPRIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 427 TRLRKA------------------------YVH---NELQIASIGPKIDLSYDHENLGAD-----------AALVKDVCS 468
Cdd:cd02771 165 LALRQAarrkavelaalsgipkwqdaavrnIAQgakSPLFIVNALATRLDDIAAESIRASpggqarlgaalARAVDASAA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 469 GA---HAFSKV------LEGAKKPAIIIG-ADLLERADGAAIHATVAeyckkLKKPNWN-------PFNVLQTNAAQVGA 531
Cdd:cd02771 245 GVsglAPKEKAariaarLTGAKKPLIVSGtLSGSLELIKAAANLAKA-----LKRRGENagltlavEEGNSPGLLLLGGH 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 532 LDVGYK---AGAQTAVKAQPKVLFLL------NADAGKVTREQLPKDCFVVYIGSHGDNgASIADAVLPGAAYTEKQGIY 602
Cdd:cd02771 320 VTEPGLdldGALAALEDGSADALIVLgndlyrSAPERRVEAALDAAEFVVVLDHFLTET-AERADVVLPAASFAEKSGTF 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
8ESZ_S1 603 VNTEGRPQQTLPGV-SPPGMAREDWKILRALSEVVGKPL---PYDNLDELRNRLEDVAPhltrLGQLEPAGDAGA 673
Cdd:cd02771 399 VNYEGRAQRFFKAYdDPAGDARSDWRWLHALAAKLGGKLvpsDAAILDEIIALVPGKAP----VGGHLYGGDPGV 469
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
270-649 |
4.51e-26 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 114.21 E-value: 4.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 270 AVGSNIVVSTRTNEVLRILPRENEDVNEEWLADKSRFACDGL-KRQRLVAPMVRmPNGELQAVEWEGALiavakaikaag 348
Cdd:COG3383 15 GVGCGIDLEVKDGKIVKVEGDPDHPVNRGRLCVKGRFGFEFVnSPDRLTTPLIR-RGGEFREVSWDEAL----------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 349 gqiagisgqlaDLEAQvALKDLLNRLGSEVVAteqGFIAGGTDNRANYLLN---------------------STIAGL-- 405
Cdd:COG3383 83 -----------DLVAE-RLREIQAEHGPDAVA---FYGSGQLTNEENYLLQklargvlgtnnidnnarlcmaSAVAGLkq 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 406 --------------EEADAVLLVGTNPRYEAPLVNTRLRKAyVHNELQIASIGP-KIDLS-YDHENL----GADAAL--- 462
Cdd:COG3383 148 sfgsdappnsyddiEEADVILVIGSNPAEAHPVLARRIKKA-KKNGAKLIVVDPrRTETArLADLHLqikpGTDLALlng 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 463 ---------------VKDVCSGAHAFSKVLE-----------GAKKPAIIIGADLLERADGAAI----------HAT--- 503
Cdd:COG3383 227 llhviieeglvdedfIAERTEGFEELKASVAkytpervaeitGVPAEDIREAARLIAEAKRAMIlwgmgvnqhtQGTdnv 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 504 -----VAEYCKKLKKPNWNPFNVLQTNAAQvGALDVGYKAGA-------------------------------------Q 541
Cdd:COG3383 307 naiinLALATGNIGRPGTGPFPLTGQNNVQ-GGRDMGALPNVlpgyrdvtdpehrakvadawgvpplpdkpgltavemfD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 542 TAVKAQPKVLFLL-------NADAGKVtREQLPKDCFVVYIGSHGDNGASIADAVLPGAAYTEKQGIYVNTEGRPQQTLP 614
Cdd:COG3383 386 AIADGEIKALWIIgenpavsDPDANHV-REALEKLEFLVVQDIFLTETAEYADVVLPAASWAEKDGTFTNTERRVQRVRK 464
|
490 500 510
....*....|....*....|....*....|....*....
8ESZ_S1 615 GVSPPGMAREDWKILRALSEVVGKPLPYDN----LDELR 649
Cdd:COG3383 465 AVEPPGEARPDWEIIAELARRLGYGFDYDSpeevFDEIA 503
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
270-649 |
3.25e-20 |
|
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: 94.59 E-value: 3.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 270 AVGSNIVVSTRTNEVLRILPRENEDVNEEWLADKSRFACDGLK-RQRLVAPMVRMpNGELQAVEWEGALIAVAKA----I 344
Cdd:cd02753 8 GVGCGLELWVKDNKIVGVEPVKGHPVNRGKLCVKGRFGFDFVNsKDRLTKPLIRK-NGKFVEASWDEALSLVASRlkeiK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 345 KAAGGQ-IAGISGQLADLE--------AQVALK----DLLNRL--GSEVVATEQGFIAGGTDNranyllnsTIAGLEEAD 409
Cdd:cd02753 87 DKYGPDaIAFFGSAKCTNEenylfqklARAVGGtnnvDHCARLchSPTVAGLAETLGSGAMTN--------SIADIEEAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 410 AVLLVGTNPRYEAPLVNTRLRKAyVHNELQIASIGP-KIDLSyDHENL------GADAAL------------------VK 464
Cdd:cd02753 159 VILVIGSNTTEAHPVIARRIKRA-KRNGAKLIVADPrRTELA-RFADLhlqlrpGTDVALlnamahviieeglydeefIE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 465 DVCSGAHAFSKVLE-----------GAKKPAIIIGADLLERADGAAI--------H----------ATVAEYCKKLKKPN 515
Cdd:cd02753 237 ERTEGFEELKEIVEkytpeyaeritGVPAEDIREAARMYATAKSAAIlwgmgvtqHshgtdnvmalSNLALLTGNIGRPG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 516 W--NPF----NVlQtNAAQVGALDV---GYkagaqtaVKAqpkvLFLLN-------ADAGKVtREQLPK-DCFVVYigsh 578
Cdd:cd02753 317 TgvNPLrgqnNV-Q-GACDMGALPNvlpGY-------VKA----LYIMGenpalsdPNTNHV-RKALESlEFLVVQ---- 378
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
8ESZ_S1 579 gD----NGASIADAVLPGAAYTEKQGIYVNTEGRPQQTLPGVSPPGMAREDWKILRALSEVVGKPLPYDN----LDELR 649
Cdd:cd02753 379 -DifltETAELADVVLPAASFAEKDGTFTNTERRVQRVRKAVEPPGEARPDWEIIQELANRLGYPGFYSHpeeiFDEIA 456
|
|
| NADH-G_4Fe-4S_3 |
smart00929 |
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region; |
123-163 |
1.83e-17 |
|
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region;
Pssm-ID: 214918 [Multi-domain] Cd Length: 41 Bit Score: 76.08 E-value: 1.83e-17
10 20 30 40
....*....|....*....|....*....|....*....|.
8ESZ_S1 123 REGVMEFLLMNHPLDCPICDQGGECDLQDQAMAFGSDRSRF 163
Cdd:smart00929 1 RKTILELLLANHPLDCPVCDKNGECELQDLAYELGVDEQRY 41
|
|
| NADH-G_4Fe-4S_3 |
pfam10588 |
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region; |
123-162 |
2.07e-17 |
|
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region;
Pssm-ID: 463159 [Multi-domain] Cd Length: 40 Bit Score: 75.95 E-value: 2.07e-17
10 20 30 40
....*....|....*....|....*....|....*....|
8ESZ_S1 123 REGVMEFLLMNHPLDCPICDQGGECDLQDQAMAFGSDRSR 162
Cdd:pfam10588 1 RKTILELLLSNHPLDCPTCDKNGNCELQDLAYELGVDEVR 40
|
|
| Fer2_4 |
pfam13510 |
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ... |
40-116 |
2.33e-15 |
|
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core structure consisting of beta(2)-alpha-beta(2) which a beta-grasp type fold. The domain is around one hundred amino acids with four conserved cysteine residues to which the 2Fe-2S cluster is ligated. This cluster appears within sarcosine oxidase proteins.
Pssm-ID: 433268 [Multi-domain] Cd Length: 82 Bit Score: 71.42 E-value: 2.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 40 EKIEVFVDDIPVQVVPGTTVLQAAAQIGVEIPRFCYHER----LAVAGNCRMCLVEVEKSPKpVAACAMPVMKGWRIKTN 115
Cdd:pfam13510 2 RPVTFTFDGRPVTAPEGDTIAAALLANGVRVPRSCKYGRprgiFCAMGECRNCLVEVDGVPN-VRACTTPVREGMVVRTQ 80
|
.
8ESZ_S1 116 S 116
Cdd:pfam13510 81 N 81
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
42-160 |
5.48e-15 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 78.62 E-value: 5.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 42 IEVFVDDIPVQVVPGTTVLQAAAQIGVEIPRFCYHERLAVAGNCRMCLVEVEKSPKPVAACAMPVMKGWRIKT-NSDLTR 120
Cdd:PRK12814 4 ISLTINGRSVTAAPGTSILEAAASAGITIPTLCFHQELEATGSCWMCIVEIKGKNRFVPACSTAVSEGMVIETeNAELHA 83
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
8ESZ_S1 121 KAREGvMEFLLMNHPLDC--PI---CDQGgeCDLQD--QAMAFGSDR 160
Cdd:PRK12814 84 MRRQS-LERLIEQHCGDClgPCelaCPAG--CNIPGfiAAIARGDDR 127
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
270-644 |
2.09e-14 |
|
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: 76.50 E-value: 2.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 270 AVGSNIVVSTRTNEVLRILPRENEDVNEEWLADKSRFACDGLKRQ-RLVAPMVRMPNGELQAVEWEGALiavakaikaag 348
Cdd:cd02754 8 GVGCGVEIGVKDGKVVAVRGDPEHPVNRGRLCIKGLNLHKTLNGPeRLTRPLLRRNGGELVPVSWDEAL----------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 349 gqiagisgqlaDLEAQVaLKDLLNRLGSEVVA--------TEQGFIAG-------GTDN-RANYLL--NSTIAG------ 404
Cdd:cd02754 77 -----------DLIAER-FKAIQAEYGPDSVAfygsgqllTEEYYAANklakgglGTNNiDTNSRLcmASAVAGykrsfg 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 405 ----------LEEADAVLLVGTNPRYEAPLVNTRLRKA--------------YVHNELQIASIG----PKIDLS------ 450
Cdd:cd02754 145 adgppgsyddIEHADCFFLIGSNMAECHPILFRRLLDRkkanpgakiivvdpRRTRTADIADLHlpirPGTDLAllngll 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 451 -YDHENLGADAALVKDVCSGAHAFSKVLE--GAKKPAIIIG---ADLLERAD--GAAIhATVAEYCK------------- 509
Cdd:cd02754 225 hVLIEEGLIDRDFIDAHTEGFEELKAFVAdyTPEKVAEITGvpeADIREAARlfGEAR-KVMSLWTMgvnqstqgtaann 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 510 ----------KLKKPNWNPFNVL-QTNAaqVGALDVGYKA-----------------------------GAQTAVKA--- 546
Cdd:cd02754 304 aiinlhlatgKIGRPGSGPFSLTgQPNA--MGGREVGGLAnllpghrsvnnpehraevakfwgvpegtiPPKPGLHAvem 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 547 -------QPKVLFLL--N-----ADAGKVTREQLPKDCFVVYIGSHGDNGASIADAVLPGAAYTEKQGIYVNTEGRPQQT 612
Cdd:cd02754 382 feaiedgEIKALWVMctNpavslPNANRVREALERLEFVVVQDAFADTETAEYADLVLPAASWGEKEGTMTNSERRVSLL 461
|
490 500 510
....*....|....*....|....*....|....
8ESZ_S1 613 LPGVSPPGMAREDWKILRALSEVVGKP--LPYDN 644
Cdd:cd02754 462 RAAVEPPGEARPDWWILADVARRLGFGelFPYTS 495
|
|
| fer2 |
cd00207 |
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ... |
41-113 |
6.07e-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: 58.95 E-value: 6.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 41 KIEVFVDDIPVQVVPGTTVLQAAAQIGVEIPRFCYHerlavaGNCRMCLVEVEK----------------SPKPVAACAM 104
Cdd:cd00207 2 TINVPGSGVEVEVPEGETLLDAAREAGIDIPYSCRA------GACGTCKVEVVEgevdqsdpslldeeeaEGGYVLACQT 75
|
....*....
8ESZ_S1 105 PVMKGWRIK 113
Cdd:cd00207 76 RVTDGLVIE 84
|
|
| NADH_dhqG_C |
pfam09326 |
NADH-ubiquinone oxidoreductase subunit G, C-terminal; Members of this family of are found at ... |
671-712 |
1.22e-09 |
|
NADH-ubiquinone oxidoreductase subunit G, C-terminal; Members of this family of are found at the C-terminus of NADH dehydrogenases subunit G or NADH-ubiquinone oxidoreductase subunit G. EC:1.6.99.5.
Pssm-ID: 462757 Cd Length: 41 Bit Score: 54.15 E-value: 1.22e-09
10 20 30 40
....*....|....*....|....*....|....*....|..
8ESZ_S1 671 AGAAGTISksigGGAIDiklKELRDYFMTDAISRASPTMAKC 712
Cdd:pfam09326 7 AGAKGKLS----GAPLK---SPIEDFYMTDPISRASATMAKC 41
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
315-643 |
6.94e-08 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 56.00 E-value: 6.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 315 RLVAPMVRMP---NGELQAVEWEGALIAvakaikaaggqIA---------------------GISGQLADLEAQVALKdL 370
Cdd:COG0243 78 RLTYPMKRVGprgSGKFERISWDEALDL-----------IAeklkaiideygpeavafytsgGSAGRLSNEAAYLAQR-F 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 371 LNRLG-------------SEVVATEQGFiagGTDNRANyllnsTIAGLEEADAVLLVGTNPRYEAPLVNTRLRKAYVHNE 437
Cdd:COG0243 146 ARALGtnnlddnsrlcheSAVAGLPRTF---GSDKGTV-----SYEDLEHADLIVLWGSNPAENHPRLLRRLREAAKKRG 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 438 LQIASIGPKIDLSYDHENL------GADAAL------------------VKDVCSGAHAFSKVLEgAKKPAII-----IG 488
Cdd:COG0243 218 AKIVVIDPRRTETAAIADEwlpirpGTDAALllalahvlieeglydrdfLARHTVGFDELAAYVA-AYTPEWAaeitgVP 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 489 ADLLER-------ADGAAIHATVAeyckklkkPNWNPFNVLQTNAAQV-----GALD-----VGYKAG--AQTAVKAQPK 549
Cdd:COG0243 297 AEDIRElarefatAKPAVILWGMG--------LQQHSNGTQTVRAIANlalltGNIGkpgggPFSLTGeaILDGKPYPIK 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 550 VLFLLN-------ADAGKvTREQLPKDCFVVYIGSHGDNGASIADAVLPGAAYTEKQGIYVNTEGR---PQQtlPGVSPP 619
Cdd:COG0243 369 ALWVYGgnpavsaPDTNR-VREALRKLDFVVVIDTFLTETARYADIVLPATTWLERDDIVTNSEDRrvhLSR--PAVEPP 445
|
410 420
....*....|....*....|....
8ESZ_S1 620 GMAREDWKILRALSEVVGKPLPYD 643
Cdd:COG0243 446 GEARSDWEIFAELAKRLGFEEAFP 469
|
|
| MopB_Nitrate-R-NarG-like |
cd02750 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
546-642 |
8.71e-06 |
|
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: 48.85 E-value: 8.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
8ESZ_S1 546 AQPKVLFLL-------NADAGKVTREQLPKDC-FVVYIGSHGDNGASIADAVLPGAAYTEKQGI-------YVNtegrPQ 610
Cdd:cd02750 332 GQPRVLFVWrgnlfgsSGKGHEYFEDAPEGKLdLIVDLDFRMDSTALYSDIVLPAATWYEKHDLsttdmhpFIH----PF 407
|
90 100 110
....*....|....*....|....*....|..
8ESZ_S1 611 QtlPGVSPPGMAREDWKILRALSevvgKPLPY 642
Cdd:cd02750 408 S--PAVDPLWEAKSDWEIFKALA----KKVPW 433
|
|
| Fer2 |
pfam00111 |
2Fe-2S iron-sulfur cluster binding domain; |
44-92 |
1.23e-04 |
|
2Fe-2S iron-sulfur cluster binding domain;
Pssm-ID: 395061 [Multi-domain] Cd Length: 77 Bit Score: 40.97 E-value: 1.23e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
8ESZ_S1 44 VFVDDIPVQVV---PGTTVLQAAAQIGVEIPRFCYHerlavaGNCRMCLVEV 92
Cdd:pfam00111 1 VTINGKGVTIEvpdGETTLLDAAEEAGIDIPYSCRG------GGCGTCAVKV 46
|
|
| PRK13532 |
PRK13532 |
nitrate reductase catalytic subunit NapA; |
583-629 |
2.73e-03 |
|
nitrate reductase catalytic subunit NapA;
Pssm-ID: 237416 [Multi-domain] Cd Length: 830 Bit Score: 41.04 E-value: 2.73e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
8ESZ_S1 583 ASIADAVLPGAAYTEKQGIYVNTEGRPQQTLPGVSPPGMARED-WKIL 629
Cdd:PRK13532 518 ALAADLILPTAMWVEKEGAYGNAERRTQFWRQQVKAPGEAKSDlWQLV 565
|
|
| |
