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Conserved domains on  [gi|1357711166|ref|XP_024141888|]
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NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial isoform X2 [Oryzias melastigma]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MopB_Res-Cmplx1_Nad11 cd02773
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone ...
151-532 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: 648.94  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 151 ESIDVLDAVGSNIVLSTRGGEVMRVLPRLNEDINEEWISDKTRFAYDGLKRQRLTQPLVKDdSGQLVPTSWEDALAQVAG 230
Cdd:cd02773     1 ESIDVLDAVGSNIRVDTRGGEVMRILPRLNEDINEEWISDKTRFAYDGLKRQRLDKPYIRK-NGKLKPATWEEALAAIAK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 231 ALQGAKGGDIAAVVGGLVEAEALVCLKDLLNCLNSDSLCTEEVFPTAGAgsDLRSNYLLNTGIAGIEEADLLLLVGTNPR 310
Cdd:cd02773    80 ALKGVKPDEIAAIAGDLADVESMVALKDLLNKLGSENLACEQDGPDLPA--DLRSNYLFNTTIAGIEEADAVLLVGTNPR 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 311 FEAPLFNARIRKSWLHNDLHVALLGKPVDLSYTYDHLGESPKVLQEIASGIHPFSQAVTKTKHPVVVVGSSCLQREDGAA 390
Cdd:cd02773   158 FEAPVLNARIRKAWLHGGLKVGVIGPPVDLTYDYDHLGTDAKTLQDIASGKHPFSKALKDAKKPMIIVGSGALARKDGAA 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 391 VMAAVSSIARKAhvsGEVEETWKIVNVLHRVASQVAALDLGYKPGVKTIR-ENPPKVLFLLGADSGSVTRQdlPEDSLVI 469
Cdd:cd02773   238 ILAAVAKLAKKN---GVVREGWNGFNVLHRAASRVGALDLGFVPGAGAIRkSGPPKVLYLLGADEIDITPI--PKDAFVV 312
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1357711166 470 YQGHHGDVGAPMADIILPGAAYTEKRGTYVNTEGRAQQTRVAVTPPGMAREDWRIIRAISELA 532
Cdd:cd02773   313 YQGHHGDRGAQIADVILPGAAYTEKSGTYVNTEGRVQQTRKAVSPPGDAREDWKILRALSEVL 375
PTZ00305 super family cl31423
NADH:ubiquinone oxidoreductase; Provisional
43-154 7.94e-35

NADH:ubiquinone oxidoreductase; Provisional


The actual alignment was detected with superfamily member PTZ00305:

Pssm-ID: 140326 [Multi-domain]  Cd Length: 297  Bit Score: 133.62  E-value: 7.94e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166  43 VFVDGKPVMVEPGT-TVLQACERAGMQIPRFCYHERLSVAGNCRMCLVEIEKVQKPVAACAMPVMKGWNILTNSDKTRKA 121
Cdd:PTZ00305   71 MFVNKRPVEIIPQEeNLLEVLEREGIRVPKFCYHPILSVAGNCRMCLVQVDGTQNLVVSCATVALPGMSIITDSRLVRDA 150
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1357711166 122 REGVMEFLLANHPLDCPICDQGGECDLQTESID 154
Cdd:PTZ00305  151 REGNVELILINHPNDCPICEQATNCDLQNVSMN 183
NADH_dhqG_C pfam09326
NADH-ubiquinone oxidoreductase subunit G, C-terminal; Members of this family of are found at ...
580-612 4.21e-11

NADH-ubiquinone oxidoreductase subunit G, C-terminal; Members of this family of are found at the C-terminus of NADH dehydrogenases subunit G or NADH-ubiquinone oxidoreductase subunit G. EC:1.6.99.5.


:

Pssm-ID: 462757  Cd Length: 41  Bit Score: 58.00  E-value: 4.21e-11
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1357711166 580 ALLTEPLVPPqltVRDFYMTDPVSRASQTMAKC 612
Cdd:pfam09326  12 KLSGAPLKSP---IEDFYMTDPISRASATMAKC 41
 
Name Accession Description Interval E-value
MopB_Res-Cmplx1_Nad11 cd02773
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone ...
151-532 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: 648.94  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 151 ESIDVLDAVGSNIVLSTRGGEVMRVLPRLNEDINEEWISDKTRFAYDGLKRQRLTQPLVKDdSGQLVPTSWEDALAQVAG 230
Cdd:cd02773     1 ESIDVLDAVGSNIRVDTRGGEVMRILPRLNEDINEEWISDKTRFAYDGLKRQRLDKPYIRK-NGKLKPATWEEALAAIAK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 231 ALQGAKGGDIAAVVGGLVEAEALVCLKDLLNCLNSDSLCTEEVFPTAGAgsDLRSNYLLNTGIAGIEEADLLLLVGTNPR 310
Cdd:cd02773    80 ALKGVKPDEIAAIAGDLADVESMVALKDLLNKLGSENLACEQDGPDLPA--DLRSNYLFNTTIAGIEEADAVLLVGTNPR 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 311 FEAPLFNARIRKSWLHNDLHVALLGKPVDLSYTYDHLGESPKVLQEIASGIHPFSQAVTKTKHPVVVVGSSCLQREDGAA 390
Cdd:cd02773   158 FEAPVLNARIRKAWLHGGLKVGVIGPPVDLTYDYDHLGTDAKTLQDIASGKHPFSKALKDAKKPMIIVGSGALARKDGAA 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 391 VMAAVSSIARKAhvsGEVEETWKIVNVLHRVASQVAALDLGYKPGVKTIR-ENPPKVLFLLGADSGSVTRQdlPEDSLVI 469
Cdd:cd02773   238 ILAAVAKLAKKN---GVVREGWNGFNVLHRAASRVGALDLGFVPGAGAIRkSGPPKVLYLLGADEIDITPI--PKDAFVV 312
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1357711166 470 YQGHHGDVGAPMADIILPGAAYTEKRGTYVNTEGRAQQTRVAVTPPGMAREDWRIIRAISELA 532
Cdd:cd02773   313 YQGHHGDRGAQIADVILPGAAYTEKSGTYVNTEGRVQQTRKAVSPPGDAREDWKILRALSEVL 375
NuoG TIGR01973
NADH-quinone oxidoreductase, chain G; This model represents the G subunit (one of 14: A->N) of ...
43-528 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: 584.71  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166  43 VFVDGKPVMVEPGTTVLQACERAGMQIPRFCYHERLSVAGNCRMCLVEIEKVQKPVAACAMPVMKGWNILTNSDKTRKAR 122
Cdd:TIGR01973   1 IFIDGKELEVPKGTTVLQACLSAGIEIPRFCYHEKLSIAGNCRMCLVEVEKFPKPVASCATPVTDGMKISTNSEKVKKAR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 123 EGVMEFLLANHPLDCPICDQGGECDLQ----------------------------------------------------- 149
Cdd:TIGR01973  81 EGVMEFLLINHPLDCPICDQGGECDLQdqavmygsdrsrfrekkrtvenkylgpliktemtrcihctrcvrfanevagve 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 150 ------------------------------------------------------TESIDVLDAVGSNIVLSTRGGEVMRV 175
Cdd:TIGR01973 161 dlgvigrgnnveigtyegktleselsgnlidicpvgaltskpyafkarpwelksTPSICVHDSVGCNIRVDERNGEIMRI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 176 LPRLNEDINEEWISDKTRFAYDGLKRQ-RLTQPLVKDDSGQLVPTSWEDALAQVAGALQGakGGDIAAVVGGLVEAEALV 254
Cdd:TIGR01973 241 LPRENDEINEEWLCDKGRFGYDGLNRQdRLTKPLLRNQEGNLLEVSWAEALAIAAEKLKA--SSRIGGIAGPRSSLEELF 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 255 CLKDLLNCLNSDSLCTEEVFPTAGAgSDLRSNYLLNTGIAGIEEADLLLLVGTNPRFEAPLFNARIRKSWLHNDLHVALL 334
Cdd:TIGR01973 319 ALKKLVRKLGSENFDLRIRNYEFES-ADLRANYLFNTTLADIEEADLVLLVGADLRQEAPLLNLRLRKAVKKGGAKVALI 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 335 GKP-VDLSY-----TYDHLGESPKVLQEIASGIHP-FSQAVTKTKHPVVVVGSSCLQREDGAAVMAAVSSIARkahVSGE 407
Cdd:TIGR01973 398 GIEkWNLTYpantnLVFHPGLSPKKLDDIASGAHSdIAAALKAAKKPLIIVGDSAISHLDGAALISAAANIAK---VIKV 474
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 408 VEETWKIVNVLHRVASQVAALDLGYKP--GVKTIRENPPKVLFLLGADSGS----VTRQDLP-EDSLVIYQGHHGDVGAP 480
Cdd:TIGR01973 475 RRKEWNGLNILSSGANSVGLLDLGGEStgLDAALNLGAADALFLLGADLERaldkTARDALSkADAFIIYQGHHGTETAE 554
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*...
gi 1357711166 481 MADIILPGAAYTEKRGTYVNTEGRAQQTRVAVTPPGMAREDWRIIRAI 528
Cdd:TIGR01973 555 KADVILPGAAFTEKSGTYVNLEGRAQRFEQAVKPPGEAREDWRILRAL 602
NuoG COG1034
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ...
42-560 1.71e-124

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: 375.72  E-value: 1.71e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166  42 EVFVDGKPVMVEPGTTVLQACERAGMQIPRFCYHERLSVAGNCRMCLVEIEKVQKPVAACAMPVMKGWNILTNSDKTRKA 121
Cdd:COG1034     3 TITIDGKEVEVPKGTTVLQAAEKAGIEIPRFCYHPKLSIAGACRMCLVEVEGAPKPVASCATPVTDGMVVKTDSPKVKKA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 122 REGVMEFLLANHPLDCPICDQGGECDLQ---------------------------------------------------- 149
Cdd:COG1034    83 RKGVMEFLLINHPLDCPICDQGGECDLQdqameygvdesryeeekrtvpkkdlgplilldmnrcilctrcvrfcdeiagd 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 150 -------------------------------------------------------TESIDVLDAVGSNIVLSTRGGEVMR 174
Cdd:COG1034   163 pelgvigrgehseigtylgkpldsefsgncidvcpvgaltskpfrfkarpwelkkTPSICPHCSVGCNIRVDVRGGKVYR 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 175 VLPRLNEDINEEWISDKTRFAYDGLKR-QRLTQPLVKDDsGQLVPTSWEDALAQVAGALQgakggdiaavvgGLVEAEal 253
Cdd:COG1034   243 VLPRENEAVNEEWLCDKGRFGYDGLNSpDRLTRPLVRKD-GELVEASWEEALAAAAEGLK------------ALKKAE-- 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 254 vclkdllnclnsdslcteevfptagagsdlrsnyllntgiagieeadllllvgtnprfeaplfNARirkswlhndlhval 333
Cdd:COG1034   308 ---------------------------------------------------------------NSV-------------- 310
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 334 lgkpvdlsytydhlgespkvlqeiasgihpfsqavtktkhpvvvvgssclqredGAAVMAAVSSIArkahvsgeveetwk 413
Cdd:COG1034   311 ------------------------------------------------------GAALLGALPDAA-------------- 322
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 414 ivnvlhrvasqvAALDlgykpgvkTIRENPPKVLFLLGAD----SGSVTRQDLPEDSLVIYQGHHGDVGAPMADIILPGA 489
Cdd:COG1034   323 ------------AILE--------AAEAGKLKALVLLGADpydlDPAAALAALAKADFVVVLDHFGSATAERADVVLPAA 382
                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1357711166 490 AYTEKRGTYVNTEGRAQQTRVAVTPPGMAREDWRIIRAISELAGVKLPYETLDEVRNRLAEVSPNLVRYDE 560
Cdd:COG1034   383 AFAEKSGTFVNLEGRVQRFNAAVPPPGEARPDWRVLRALANALGAGLPYDSLEEVRAELAAEAPATVSAEG 453
Molybdopterin pfam00384
Molybdopterin oxidoreductase;
203-530 3.62e-110

Molybdopterin oxidoreductase;


Pssm-ID: 395308 [Multi-domain]  Cd Length: 359  Bit Score: 335.52  E-value: 3.62e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 203 RLTQPLVKDDSGQLVPTSWEDALAQVAGALQG--AKGGD----IAAVVGGLVEAEALVCLKDLLNCLNSDSLCTEEVF-- 274
Cdd:pfam00384   1 RLKYPMVRRGDGKFVRVSWDEALDLIAKKLKRiiKKYGPdaiaINGGSGGLTDVESLYALKKLLNRLGSKNGNTEDHNgd 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 275 ----PTAGAGSDLRSNYLLNTGIAGIEEADLLLLVGTNPRFEAPLFNARIRKSWLHNDLHVALLGKPVDLSYTYDHLGES 350
Cdd:pfam00384  81 lctaAAAAFGSDLRSNYLFNSSIADIENADLILLIGTNPREEAPILNARIRKAALKGKAKVIVIGPRLDLTYADEHLGIK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 351 PKVLQEIASGI-HPFSQAVTKTK----HPVVVVGSSCLQREDGAAVMAAVSSIARKAHVSGEVEETWKIVNVLHRVASQV 425
Cdd:pfam00384 161 PGTDLALALAGaHVFIKELKKDKdfapKPIIIVGAGVLQRQDGEAIFRAIANLADLTGNIGRPGGGWNGLNILQGAASPV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 426 AALDLGYKPGVK------TIRENPPKVLFLLG-------ADSGSVTRQDLPEDSLVIYQGHHGDVGAPMADIILPGAAYT 492
Cdd:pfam00384 241 GALDLGLVPGIKsveminAIKKGGIKVLYLLGnnpfvthADENRVVKALQKLDLFVVYDGHHGDKTAKYADVILPAAAYT 320
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1357711166 493 EKRGTYVNTEGRAQQTRVAVTPPGMAREDWRIIRAISE 530
Cdd:pfam00384 321 EKNGTYVNTEGRVQSTKQAVPPPGEAREDWKILRALSE 358
PRK07860 PRK07860
NADH dehydrogenase subunit G; Validated
45-553 1.12e-60

NADH dehydrogenase subunit G; Validated


Pssm-ID: 236118 [Multi-domain]  Cd Length: 797  Bit Score: 216.35  E-value: 1.12e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166  45 VDGKPVMVEPGTTVLQACERAGMQIPRFCYHERLSVAGNCRMCLVEIEKVQKPVAACAMPVMKGWNILT--NSDKTRKAR 122
Cdd:PRK07860    9 IDGVEVSVPKGTLVIRAAELLGIQIPRFCDHPLLDPVGACRQCLVEVEGQRKPQASCTTTVTDGMVVKTqlTSPVADKAQ 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 123 EGVMEFLLANHPLDCPICDQGGECDLQ--------TES------------------------------------------ 152
Cdd:PRK07860   89 HGVMELLLINHPLDCPVCDKGGECPLQnqamsngrAESrftdvkrtfpkpinistqvlldrercvlcarctrfsdqiagd 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 153 --IDVL--------------------------------------------------------DAVGSNIVLSTRGGEVMR 174
Cdd:PRK07860  169 pfIDLQergalqqvgiyegepfqsyfsgntvqicpvgaltgaayrfrarpfdlvstpsvcehCASGCAQRTDHRRGKVLR 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 175 VLPRLNEDINEEWISDKTRFAYD-GLKRQRLTQPLVKDDSGQLVPTSWEDALAQVAGALQGAKGGdIAAVVGGLVEAE-- 251
Cdd:PRK07860  249 RLAGDDPEVNEEWNCDKGRWAFTyATQPDRITTPLVRDEDGELEPASWSEALAVAARGLAAARGR-VGVLVGGRLTVEda 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 252 ------ALVCLK----DLLNCLNSDSlctEEVFPTAG-AGSDLRSNYllntgiAGIEEADLLLLVGTNPRFEAPLFNARI 320
Cdd:PRK07860  328 yayakfARVALGtndiDFRARPHSAE---EADFLAARvAGRGLGVTY------ADLEKAPAVLLVGFEPEEESPIVFLRL 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 321 RKSWLHNDLHVALLGKPVD--LSYTYDHL-----GESPKVLQEIASGIHPFSQAVtKTKHPVVVVGssclqrEDGAAVMA 393
Cdd:PRK07860  399 RKAARKHGLKVYSIAPFATrgLEKMGGTLlrtapGGEAAALDALATGAPDVAELL-RTPGAVILVG------ERLATVPG 471
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 394 AVSSIARKAHVSGEveetwKIVNVLHRvASQVAALDLGYKP----------------------GVKTIRENPPKVL--FL 449
Cdd:PRK07860  472 ALSAAARLADATGA-----RLAWVPRR-AGERGALEAGALPtllpggrpvadpaaraevaaawGVDELPAAPGRDTagIL 545
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 450 LGADSGS--------VTRQDLPEDS-----------LVIYQGHHGDVgAPMADIILPGAAYTEKRGTYVNTEGRAQQTRV 510
Cdd:PRK07860  546 AAAAAGElgallvggVEPADLPDPAaalaaldaagfVVSLELRHSAV-TERADVVLPVAPVAEKAGTFLNWEGRLRPFEA 624
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|...
gi 1357711166 511 AVTPPGmAREDWRIIRAISELAGVKLPYETLDEVRNRLAEVSP 553
Cdd:PRK07860  625 ALRTTG-ALSDLRVLDALADEMGVDLGLPTVAAARAELARLGA 666
PTZ00305 PTZ00305
NADH:ubiquinone oxidoreductase; Provisional
43-154 7.94e-35

NADH:ubiquinone oxidoreductase; Provisional


Pssm-ID: 140326 [Multi-domain]  Cd Length: 297  Bit Score: 133.62  E-value: 7.94e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166  43 VFVDGKPVMVEPGT-TVLQACERAGMQIPRFCYHERLSVAGNCRMCLVEIEKVQKPVAACAMPVMKGWNILTNSDKTRKA 121
Cdd:PTZ00305   71 MFVNKRPVEIIPQEeNLLEVLEREGIRVPKFCYHPILSVAGNCRMCLVQVDGTQNLVVSCATVALPGMSIITDSRLVRDA 150
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1357711166 122 REGVMEFLLANHPLDCPICDQGGECDLQTESID 154
Cdd:PTZ00305  151 REGNVELILINHPNDCPICEQATNCDLQNVSMN 183
Fer2_4 pfam13510
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ...
41-115 5.29e-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: 70.26  E-value: 5.29e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1357711166  41 LEVFVDGKPVMVEPGTTVLQACERAGMQIPRFCYHER----LSVAGNCRMCLVEIEKVQKpVAACAMPVMKGWNILTNS 115
Cdd:pfam13510   4 VTFTFDGRPVTAPEGDTIAAALLANGVRVPRSCKYGRprgiFCAMGECRNCLVEVDGVPN-VRACTTPVREGMVVRTQN 81
NADH-G_4Fe-4S_3 smart00929
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region;
122-150 4.30e-13

NADH-ubiquinone oxidoreductase-G iron-sulfur binding region;


Pssm-ID: 214918 [Multi-domain]  Cd Length: 41  Bit Score: 63.76  E-value: 4.30e-13
                           10        20
                   ....*....|....*....|....*....
gi 1357711166  122 REGVMEFLLANHPLDCPICDQGGECDLQT 150
Cdd:smart00929   1 RKTILELLLANHPLDCPVCDKNGECELQD 29
NADH_dhqG_C pfam09326
NADH-ubiquinone oxidoreductase subunit G, C-terminal; Members of this family of are found at ...
580-612 4.21e-11

NADH-ubiquinone oxidoreductase subunit G, C-terminal; Members of this family of are found at the C-terminus of NADH dehydrogenases subunit G or NADH-ubiquinone oxidoreductase subunit G. EC:1.6.99.5.


Pssm-ID: 462757  Cd Length: 41  Bit Score: 58.00  E-value: 4.21e-11
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1357711166 580 ALLTEPLVPPqltVRDFYMTDPVSRASQTMAKC 612
Cdd:pfam09326  12 KLSGAPLKSP---IEDFYMTDPISRASATMAKC 41
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
41-111 1.13e-10

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: 58.18  E-value: 1.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166  41 LEVFVDGKPVMVEPGTTVLQACERAGMQIPRFCYHerlsvaGNCRMCLVEIEK----------------VQKPVAACAMP 104
Cdd:cd00207     3 INVPGSGVEVEVPEGETLLDAAREAGIDIPYSCRA------GACGTCKVEVVEgevdqsdpslldeeeaEGGYVLACQTR 76

                  ....*..
gi 1357711166 105 VMKGWNI 111
Cdd:cd00207    77 VTDGLVI 83
Fdx COG0633
Ferredoxin [Energy production and conversion];
46-92 3.24e-03

Ferredoxin [Energy production and conversion];


Pssm-ID: 440398 [Multi-domain]  Cd Length: 87  Bit Score: 37.14  E-value: 3.24e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1357711166  46 DGKPVMVEPGTTVLQACERAGMQIPRFCyheRlsvAGNCRMCLVEIE 92
Cdd:COG0633     9 EGHTVEVPAGESLLEAALRAGIDLPYSC---R---SGACGTCHVRVL 49
 
Name Accession Description Interval E-value
MopB_Res-Cmplx1_Nad11 cd02773
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone ...
151-532 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: 648.94  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 151 ESIDVLDAVGSNIVLSTRGGEVMRVLPRLNEDINEEWISDKTRFAYDGLKRQRLTQPLVKDdSGQLVPTSWEDALAQVAG 230
Cdd:cd02773     1 ESIDVLDAVGSNIRVDTRGGEVMRILPRLNEDINEEWISDKTRFAYDGLKRQRLDKPYIRK-NGKLKPATWEEALAAIAK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 231 ALQGAKGGDIAAVVGGLVEAEALVCLKDLLNCLNSDSLCTEEVFPTAGAgsDLRSNYLLNTGIAGIEEADLLLLVGTNPR 310
Cdd:cd02773    80 ALKGVKPDEIAAIAGDLADVESMVALKDLLNKLGSENLACEQDGPDLPA--DLRSNYLFNTTIAGIEEADAVLLVGTNPR 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 311 FEAPLFNARIRKSWLHNDLHVALLGKPVDLSYTYDHLGESPKVLQEIASGIHPFSQAVTKTKHPVVVVGSSCLQREDGAA 390
Cdd:cd02773   158 FEAPVLNARIRKAWLHGGLKVGVIGPPVDLTYDYDHLGTDAKTLQDIASGKHPFSKALKDAKKPMIIVGSGALARKDGAA 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 391 VMAAVSSIARKAhvsGEVEETWKIVNVLHRVASQVAALDLGYKPGVKTIR-ENPPKVLFLLGADSGSVTRQdlPEDSLVI 469
Cdd:cd02773   238 ILAAVAKLAKKN---GVVREGWNGFNVLHRAASRVGALDLGFVPGAGAIRkSGPPKVLYLLGADEIDITPI--PKDAFVV 312
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1357711166 470 YQGHHGDVGAPMADIILPGAAYTEKRGTYVNTEGRAQQTRVAVTPPGMAREDWRIIRAISELA 532
Cdd:cd02773   313 YQGHHGDRGAQIADVILPGAAYTEKSGTYVNTEGRVQQTRKAVSPPGDAREDWKILRALSEVL 375
NuoG TIGR01973
NADH-quinone oxidoreductase, chain G; This model represents the G subunit (one of 14: A->N) of ...
43-528 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: 584.71  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166  43 VFVDGKPVMVEPGTTVLQACERAGMQIPRFCYHERLSVAGNCRMCLVEIEKVQKPVAACAMPVMKGWNILTNSDKTRKAR 122
Cdd:TIGR01973   1 IFIDGKELEVPKGTTVLQACLSAGIEIPRFCYHEKLSIAGNCRMCLVEVEKFPKPVASCATPVTDGMKISTNSEKVKKAR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 123 EGVMEFLLANHPLDCPICDQGGECDLQ----------------------------------------------------- 149
Cdd:TIGR01973  81 EGVMEFLLINHPLDCPICDQGGECDLQdqavmygsdrsrfrekkrtvenkylgpliktemtrcihctrcvrfanevagve 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 150 ------------------------------------------------------TESIDVLDAVGSNIVLSTRGGEVMRV 175
Cdd:TIGR01973 161 dlgvigrgnnveigtyegktleselsgnlidicpvgaltskpyafkarpwelksTPSICVHDSVGCNIRVDERNGEIMRI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 176 LPRLNEDINEEWISDKTRFAYDGLKRQ-RLTQPLVKDDSGQLVPTSWEDALAQVAGALQGakGGDIAAVVGGLVEAEALV 254
Cdd:TIGR01973 241 LPRENDEINEEWLCDKGRFGYDGLNRQdRLTKPLLRNQEGNLLEVSWAEALAIAAEKLKA--SSRIGGIAGPRSSLEELF 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 255 CLKDLLNCLNSDSLCTEEVFPTAGAgSDLRSNYLLNTGIAGIEEADLLLLVGTNPRFEAPLFNARIRKSWLHNDLHVALL 334
Cdd:TIGR01973 319 ALKKLVRKLGSENFDLRIRNYEFES-ADLRANYLFNTTLADIEEADLVLLVGADLRQEAPLLNLRLRKAVKKGGAKVALI 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 335 GKP-VDLSY-----TYDHLGESPKVLQEIASGIHP-FSQAVTKTKHPVVVVGSSCLQREDGAAVMAAVSSIARkahVSGE 407
Cdd:TIGR01973 398 GIEkWNLTYpantnLVFHPGLSPKKLDDIASGAHSdIAAALKAAKKPLIIVGDSAISHLDGAALISAAANIAK---VIKV 474
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 408 VEETWKIVNVLHRVASQVAALDLGYKP--GVKTIRENPPKVLFLLGADSGS----VTRQDLP-EDSLVIYQGHHGDVGAP 480
Cdd:TIGR01973 475 RRKEWNGLNILSSGANSVGLLDLGGEStgLDAALNLGAADALFLLGADLERaldkTARDALSkADAFIIYQGHHGTETAE 554
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*...
gi 1357711166 481 MADIILPGAAYTEKRGTYVNTEGRAQQTRVAVTPPGMAREDWRIIRAI 528
Cdd:TIGR01973 555 KADVILPGAAFTEKSGTYVNLEGRAQRFEQAVKPPGEAREDWRILRAL 602
MopB_NADH-Q-OR-NuoG2 cd02768
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone ...
151-531 2.12e-158

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: 459.83  E-value: 2.12e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 151 ESIDVLDAVGSNIVLSTRGGEVMRVLPRLNEDINEEWISDKTRFAYDGLK-RQRLTQPLVKDDsGQLVPTSWEDALAQVA 229
Cdd:cd02768     1 ESIDVHDALGSNIRVDVRGGEVMRILPRENEAINEEWISDKGRFGYDGLNsRQRLTQPLIKKG-GKLVPVSWEEALKTVA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 230 GALQGAKGGDIAAVVGGLVEAEALVCLKDLLNCLNSDSLCTEEVFPTAGAGSDLRSNYLLNTGIAGIEEADLLLLVGTNP 309
Cdd:cd02768    80 EGLKAVKGDKIGGIAGPRADLESLFLLKKLLNKLGSNNIDHRLRQSDLPADNRLRGNYLFNTSIAEIEEADAVLLIGSNL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 310 RFEAPLFNARIRKSWLHNDLHVALLG-----KPVDLSYTYDHLGESPKVLQEIASGIH--PFSQAVTKTKHPVVVVGSSc 382
Cdd:cd02768   160 RKEAPLLNARLRKAVKKKGAKIAVIGpkdtdLIADLTYPVSPLGASLATLLDIAEGKHlkPFAKSLKKAKKPLIILGSS- 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 383 LQREDGAAVMAAVSSIARKAHVSGEVeetWKIVNVLHRVASQVAA--LDLGYKPGVKTIREnppkvLFLLGADSGSVTRQ 460
Cdd:cd02768   239 ALRKDGAAILKALANLAAKLGTGAGL---WNGLNVLNSVGARLGGagLDAGLALLEPGKAK-----LLLLGEDELDRSNP 310
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1357711166 461 DL-----PEDSLVIYQGHHGDVGAPmADIILPGAAYTEKRGTYVNTEGRAQQTRVAVTPPGMAREDWRIIRAISEL 531
Cdd:cd02768   311 PAavalaAADAFVVYQGHHGDTGAQ-ADVILPAAAFTEKSGTYVNTEGRVQRFKKAVSPPGDAREDWKILRALSNL 385
NuoG COG1034
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ...
42-560 1.71e-124

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: 375.72  E-value: 1.71e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166  42 EVFVDGKPVMVEPGTTVLQACERAGMQIPRFCYHERLSVAGNCRMCLVEIEKVQKPVAACAMPVMKGWNILTNSDKTRKA 121
Cdd:COG1034     3 TITIDGKEVEVPKGTTVLQAAEKAGIEIPRFCYHPKLSIAGACRMCLVEVEGAPKPVASCATPVTDGMVVKTDSPKVKKA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 122 REGVMEFLLANHPLDCPICDQGGECDLQ---------------------------------------------------- 149
Cdd:COG1034    83 RKGVMEFLLINHPLDCPICDQGGECDLQdqameygvdesryeeekrtvpkkdlgplilldmnrcilctrcvrfcdeiagd 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 150 -------------------------------------------------------TESIDVLDAVGSNIVLSTRGGEVMR 174
Cdd:COG1034   163 pelgvigrgehseigtylgkpldsefsgncidvcpvgaltskpfrfkarpwelkkTPSICPHCSVGCNIRVDVRGGKVYR 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 175 VLPRLNEDINEEWISDKTRFAYDGLKR-QRLTQPLVKDDsGQLVPTSWEDALAQVAGALQgakggdiaavvgGLVEAEal 253
Cdd:COG1034   243 VLPRENEAVNEEWLCDKGRFGYDGLNSpDRLTRPLVRKD-GELVEASWEEALAAAAEGLK------------ALKKAE-- 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 254 vclkdllnclnsdslcteevfptagagsdlrsnyllntgiagieeadllllvgtnprfeaplfNARirkswlhndlhval 333
Cdd:COG1034   308 ---------------------------------------------------------------NSV-------------- 310
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 334 lgkpvdlsytydhlgespkvlqeiasgihpfsqavtktkhpvvvvgssclqredGAAVMAAVSSIArkahvsgeveetwk 413
Cdd:COG1034   311 ------------------------------------------------------GAALLGALPDAA-------------- 322
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 414 ivnvlhrvasqvAALDlgykpgvkTIRENPPKVLFLLGAD----SGSVTRQDLPEDSLVIYQGHHGDVGAPMADIILPGA 489
Cdd:COG1034   323 ------------AILE--------AAEAGKLKALVLLGADpydlDPAAALAALAKADFVVVLDHFGSATAERADVVLPAA 382
                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1357711166 490 AYTEKRGTYVNTEGRAQQTRVAVTPPGMAREDWRIIRAISELAGVKLPYETLDEVRNRLAEVSPNLVRYDE 560
Cdd:COG1034   383 AFAEKSGTFVNLEGRVQRFNAAVPPPGEARPDWRVLRALANALGAGLPYDSLEEVRAELAAEAPATVSAEG 453
Molybdopterin pfam00384
Molybdopterin oxidoreductase;
203-530 3.62e-110

Molybdopterin oxidoreductase;


Pssm-ID: 395308 [Multi-domain]  Cd Length: 359  Bit Score: 335.52  E-value: 3.62e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 203 RLTQPLVKDDSGQLVPTSWEDALAQVAGALQG--AKGGD----IAAVVGGLVEAEALVCLKDLLNCLNSDSLCTEEVF-- 274
Cdd:pfam00384   1 RLKYPMVRRGDGKFVRVSWDEALDLIAKKLKRiiKKYGPdaiaINGGSGGLTDVESLYALKKLLNRLGSKNGNTEDHNgd 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 275 ----PTAGAGSDLRSNYLLNTGIAGIEEADLLLLVGTNPRFEAPLFNARIRKSWLHNDLHVALLGKPVDLSYTYDHLGES 350
Cdd:pfam00384  81 lctaAAAAFGSDLRSNYLFNSSIADIENADLILLIGTNPREEAPILNARIRKAALKGKAKVIVIGPRLDLTYADEHLGIK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 351 PKVLQEIASGI-HPFSQAVTKTK----HPVVVVGSSCLQREDGAAVMAAVSSIARKAHVSGEVEETWKIVNVLHRVASQV 425
Cdd:pfam00384 161 PGTDLALALAGaHVFIKELKKDKdfapKPIIIVGAGVLQRQDGEAIFRAIANLADLTGNIGRPGGGWNGLNILQGAASPV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 426 AALDLGYKPGVK------TIRENPPKVLFLLG-------ADSGSVTRQDLPEDSLVIYQGHHGDVGAPMADIILPGAAYT 492
Cdd:pfam00384 241 GALDLGLVPGIKsveminAIKKGGIKVLYLLGnnpfvthADENRVVKALQKLDLFVVYDGHHGDKTAKYADVILPAAAYT 320
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1357711166 493 EKRGTYVNTEGRAQQTRVAVTPPGMAREDWRIIRAISE 530
Cdd:pfam00384 321 EKNGTYVNTEGRVQSTKQAVPPPGEAREDWKILRALSE 358
MopB_Res-Cmplx1_Nad11-M cd02774
MopB_Res_Cmplx1_Nad11_M: Mitochondrial-encoded NADH-quinone oxidoreductase/respiratory complex ...
151-528 7.82e-72

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: 236.11  E-value: 7.82e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 151 ESIDVLDAVGSNIVLSTRGGEVMRVLPRLNEDINEEWISDKTRFAYDGLKRQRLTQPLVKDDSGQLVPTSWEDALAQVAG 230
Cdd:cd02774     1 ESIDVLDSLGSNIRVDIKGNEILRILPKINDELNEEWISDKIRFSYDSLKYQRIKTPLLKLSNNSFLEIGWKTAFKFLNK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 231 ALQGAKGGDIAAVVGGLVEAEALVCLKDLLNCLNSDSLCTEEVFPTAGAGSDLRSNYLLNTGIAGIEEADLLLLVGTNPR 310
Cdd:cd02774    81 FILLKKFSKLNFIIGSKIDLETLFYYKKLLNKLGSLNTNSNNFLENNNYFNLDLENYLFNNSLKNLDKSDLCLLIGSNLR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 311 FEAPLFNARIRKSWLHNDLHVALLGKPVDLSYTYDHLGESPKVLQEIASGIHPFSQAVTKTKHPVVVVGSSCLQREDGAa 390
Cdd:cd02774   161 VESPILNIRLRNRYNKGNKKIFVIGNKFDTTYPSKHIGLSLNTLLKILEGKHLFCKQLKKSKKPLIIIGSSFSLRKNYS- 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 391 vmaavSSIARKAHVSGEVEETWKIVNVLHRVasqvaALDLG-YKPGVKTIRenppKVLFLLGADSGSVTRQDlpEDSLVI 469
Cdd:cd02774   240 -----FIISKLKNFSSNNENNFNFLNIISNS-----LYYLGiKKFNSNNKK----NLSNLYYIKETNFQKFN--KNNFVI 303
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1357711166 470 YQGHHGDVGAPMADIILPGAAYTEKRGTYVNTEGRAQQTRVAVTPPGMAREDWRIIRAI 528
Cdd:cd02774   304 YQGHHFLNLANNSNLILPSKTFFEKEALYLNLEGILQKTKKILSFKENIKSDDNIIFSL 362
Molybdopterin-Binding cd00368
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ...
151-530 2.22e-64

Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, heterogeneous superfamily of enzymes that, in general, bind molybdopterin as a cofactor. The MopB domain is found in a wide variety of molybdenum- and tungsten-containing enzymes, including formate dehydrogenase-H (Fdh-H) and -N (Fdh-N), several forms of nitrate reductase (Nap, Nas, NarG), dimethylsulfoxide reductase (DMSOR), thiosulfate reductase, formylmethanofuran dehydrogenase, and arsenite oxidase. Molybdenum is present in most of these enzymes in the form of molybdopterin, a modified pterin ring with a dithiolene side chain, which is responsible for ligating the Mo. In many bacterial and archaeal species, molybdopterin is in the form of a dinucleotide, with two molybdopterin dinucleotide units per molybdenum. These proteins can function as monomers, heterodimers, or heterotrimers, depending on the protein and organism. Also included in the MopB superfamily is the eukaryotic/eubacterial protein domain family of the 75-kDa subunit/Nad11/NuoG (second domain) of respiratory complex 1/NADH-quinone oxidoreductase which is postulated to have lost an ancestral formate dehydrogenase activity and only vestigial sequence evidence remains of a molybdopterin binding site.


Pssm-ID: 238218 [Multi-domain]  Cd Length: 374  Bit Score: 216.43  E-value: 2.22e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 151 ESIDVLDAVGSNIVLSTRGGEVMRVLPRLNEDINEEWISDKTRFAYDGLK-RQRLTQPLVKD-DSGQLVPTSWEDALAQV 228
Cdd:cd00368     1 PSVCPFCGVGCGILVYVKDGKVVRIEGDPNHPVNEGRLCDKGRAGLDGLYsPDRLKYPLIRVgGRGKFVPISWDEALDEI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 229 AGALQGAK---GGD-IAAVVGGLVEAEALVCLKDLLNCLNSDSLCTEEVFPTAGAGSDLR--SNYLLNTGIAGIEEADLL 302
Cdd:cd00368    81 AEKLKEIRekyGPDaIAFYGGGGASNEEAYLLQKLLRALGSNNVDSHARLCHASAVAALKafGGGAPTNTLADIENADLI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 303 LLVGTNPRFEAPLFNARIRKSWL-----------------HNDLHVA---------LLGKPVDlsytyDHLGESPKVLQE 356
Cdd:cd00368   161 LLWGSNPAETHPVLAARLRRAKKrgaklividprrtetaaKADEWLPirpgtdaalALAEWAA-----EITGVPAETIRA 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 357 IAsgihpfsQAVTKTKHPVVVVGSSCLQREDGAAVMAAVSSIArkahvsgeveetwkivnvlhrvasqvAALDLGYKPGV 436
Cdd:cd00368   236 LA-------REFAAAKRAVILWGMGLTQHTNGTQNVRAIANLA--------------------------ALTGNIGRPGG 282
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 437 KTI-RENPpkvlFLLGADSGSVTRQDLPEDSLVIYQGHHGDVGApMADIILPGAAYTEKRGTYVNTEGRAQQTRVAVTPP 515
Cdd:cd00368   283 GLGpGGNP----LVSAPDANRVRAALKKLDFVVVIDIFMTETAA-YADVVLPAATYLEKEGTYTNTEGRVQLFRQAVEPP 357
                         410
                  ....*....|....*
gi 1357711166 516 GMAREDWRIIRAISE 530
Cdd:cd00368   358 GEARSDWEILRELAK 372
PRK07860 PRK07860
NADH dehydrogenase subunit G; Validated
45-553 1.12e-60

NADH dehydrogenase subunit G; Validated


Pssm-ID: 236118 [Multi-domain]  Cd Length: 797  Bit Score: 216.35  E-value: 1.12e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166  45 VDGKPVMVEPGTTVLQACERAGMQIPRFCYHERLSVAGNCRMCLVEIEKVQKPVAACAMPVMKGWNILT--NSDKTRKAR 122
Cdd:PRK07860    9 IDGVEVSVPKGTLVIRAAELLGIQIPRFCDHPLLDPVGACRQCLVEVEGQRKPQASCTTTVTDGMVVKTqlTSPVADKAQ 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 123 EGVMEFLLANHPLDCPICDQGGECDLQ--------TES------------------------------------------ 152
Cdd:PRK07860   89 HGVMELLLINHPLDCPVCDKGGECPLQnqamsngrAESrftdvkrtfpkpinistqvlldrercvlcarctrfsdqiagd 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 153 --IDVL--------------------------------------------------------DAVGSNIVLSTRGGEVMR 174
Cdd:PRK07860  169 pfIDLQergalqqvgiyegepfqsyfsgntvqicpvgaltgaayrfrarpfdlvstpsvcehCASGCAQRTDHRRGKVLR 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 175 VLPRLNEDINEEWISDKTRFAYD-GLKRQRLTQPLVKDDSGQLVPTSWEDALAQVAGALQGAKGGdIAAVVGGLVEAE-- 251
Cdd:PRK07860  249 RLAGDDPEVNEEWNCDKGRWAFTyATQPDRITTPLVRDEDGELEPASWSEALAVAARGLAAARGR-VGVLVGGRLTVEda 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 252 ------ALVCLK----DLLNCLNSDSlctEEVFPTAG-AGSDLRSNYllntgiAGIEEADLLLLVGTNPRFEAPLFNARI 320
Cdd:PRK07860  328 yayakfARVALGtndiDFRARPHSAE---EADFLAARvAGRGLGVTY------ADLEKAPAVLLVGFEPEEESPIVFLRL 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 321 RKSWLHNDLHVALLGKPVD--LSYTYDHL-----GESPKVLQEIASGIHPFSQAVtKTKHPVVVVGssclqrEDGAAVMA 393
Cdd:PRK07860  399 RKAARKHGLKVYSIAPFATrgLEKMGGTLlrtapGGEAAALDALATGAPDVAELL-RTPGAVILVG------ERLATVPG 471
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 394 AVSSIARKAHVSGEveetwKIVNVLHRvASQVAALDLGYKP----------------------GVKTIRENPPKVL--FL 449
Cdd:PRK07860  472 ALSAAARLADATGA-----RLAWVPRR-AGERGALEAGALPtllpggrpvadpaaraevaaawGVDELPAAPGRDTagIL 545
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 450 LGADSGS--------VTRQDLPEDS-----------LVIYQGHHGDVgAPMADIILPGAAYTEKRGTYVNTEGRAQQTRV 510
Cdd:PRK07860  546 AAAAAGElgallvggVEPADLPDPAaalaaldaagfVVSLELRHSAV-TERADVVLPVAPVAEKAGTFLNWEGRLRPFEA 624
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|...
gi 1357711166 511 AVTPPGmAREDWRIIRAISELAGVKLPYETLDEVRNRLAEVSP 553
Cdd:PRK07860  625 ALRTTG-ALSDLRVLDALADEMGVDLGLPTVAAARAELARLGA 666
MopB_NDH-1_NuoG2 cd02772
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase ...
152-531 5.05e-57

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: 197.96  E-value: 5.05e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 152 SIDVLDAVGSNIVLSTRGGEVMRVLPRLNEDINEEWISDKTRFAYDGLKRQ-RLTQPLVKDDsGQLVPTSWEDALAQVAG 230
Cdd:cd02772     2 SVSPHDALGSNLVVHVKNNKVMRVVPRENEAINECWLSDRDRFSYEGLNSEdRLTKPMIKKD-GQWQEVDWETALEYVAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 231 ALQGAKGGDIAAVVGGLVEA----EALVCLKDLLNCLNSDSLCTEEVFPTAGAGSDLRSNYLLNTGIAGIEEADLLLLVG 306
Cdd:cd02772    81 GLSAIIKKHGADQIGALASPhstlEELYLLQKLARGLGSDNIDHRLRQSDFRDDAKASGAPWLGMPIAEISELDRVLVIG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 307 TNPRFEAPLFNARIRK--------SWLH---NDLHVALLGK----PVDLSYTydhLGESPKVLQEIASGIHPFSQ----A 367
Cdd:cd02772   161 SNLRKEHPLLAQRLRQavkkgaklSAINpadDDFLFPLSGKaivaPSALANA---LAQVAKALAEEKGLAVPDEDakveA 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 368 VTKTKH----------PVVVVGSSCLQREDGAAVMAAVSSIARkahVSGEVeetwkiVNVLHRVASQVAALDLGYKPGV- 436
Cdd:cd02772   238 SEEARKiaaslvsaerAAVFLGNLAQNHPQAATLRALAQEIAK---LTGAT------LGVLGEGANSVGAYLAGALPHGg 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 437 ---KTIRENPPKVLFLLGA------DSGSVTRQDLPEDSLVIYQGHHgdVGAPM---ADIILPGAAYTEKRGTYVNTEGR 504
Cdd:cd02772   309 lnaAAMLEQPRKAYLLLNVepeldcANPAQALAALNQAEFVVALSAF--ASAALldyADVLLPIAPFTETSGTFVNLEGR 386
                         410       420
                  ....*....|....*....|....*..
gi 1357711166 505 AQQTRVAVTPPGMAREDWRIIRAISEL 531
Cdd:cd02772   387 VQSFKGVVKPLGEARPAWKVLRVLGNL 413
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 ...
158-553 4.21e-41

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: 155.62  E-value: 4.21e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 158 AVGSNIVLSTRGGEVMRVLPRLNEDINEEWISDKTRFAYDGLK-RQRLTQPLVKDDsGQLVPTSWEDALAQVAGALQGAK 236
Cdd:cd02771     8 SVGCNISLGERYGELRRVENRYNGAVNHYFLCDRGRFGYGYVNsRDRLTQPLIRRG-GTLVPVSWNEALDVAAARLKEAK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 237 GGdIAAVVGGLVEAEALVCLKDL----LNCLNSDSLCTEevfptaGAGSDLRSNYLLNTGIAGIEEADLLLLVGTNPRFE 312
Cdd:cd02771    87 DK-VGGIGSPRASNESNYALQKLvgavLGTNNVDHRARR------LIAEILRNGPIYIPSLRDIESADAVLVLGEDLTQT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 313 APLFNARIRKSWLHNDLHVALL-GKPVDLSYTYDHLGESPKV-----------LQEIA---------------------- 358
Cdd:cd02771   160 APRIALALRQAARRKAVELAALsGIPKWQDAAVRNIAQGAKSplfivnalatrLDDIAaesiraspggqarlgaalarav 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 359 -------SGIHPFS------QAVTKTKHPVVVVGSSCLQREdgaavmaAVSSIARKAHVSGEVEETWKIVNVLHRVASQV 425
Cdd:cd02771   240 dasaagvSGLAPKEkaariaARLTGAKKPLIVSGTLSGSLE-------LIKAAANLAKALKRRGENAGLTLAVEEGNSPG 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 426 AAL--DLGYKPG------VKTIRENPPKVLFLLGAD---SGSVTRQD--LPEDSLVIYQGHHGDVGAPMADIILPGAAYT 492
Cdd:cd02771   313 LLLlgGHVTEPGldldgaLAALEDGSADALIVLGNDlyrSAPERRVEaaLDAAEFVVVLDHFLTETAERADVVLPAASFA 392
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1357711166 493 EKRGTYVNTEGRAQQTRVAV-TPPGMAREDWRIIRAISELAGVKL---PYETLDEVRNRLAEVSP 553
Cdd:cd02771   393 EKSGTFVNYEGRAQRFFKAYdDPAGDARSDWRWLHALAAKLGGKLvpsDAAILDEIIALVPGKAP 457
PTZ00305 PTZ00305
NADH:ubiquinone oxidoreductase; Provisional
43-154 7.94e-35

NADH:ubiquinone oxidoreductase; Provisional


Pssm-ID: 140326 [Multi-domain]  Cd Length: 297  Bit Score: 133.62  E-value: 7.94e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166  43 VFVDGKPVMVEPGT-TVLQACERAGMQIPRFCYHERLSVAGNCRMCLVEIEKVQKPVAACAMPVMKGWNILTNSDKTRKA 121
Cdd:PTZ00305   71 MFVNKRPVEIIPQEeNLLEVLEREGIRVPKFCYHPILSVAGNCRMCLVQVDGTQNLVVSCATVALPGMSIITDSRLVRDA 150
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1357711166 122 REGVMEFLLANHPLDCPICDQGGECDLQTESID 154
Cdd:PTZ00305  151 REGNVELILINHPNDCPICEQATNCDLQNVSMN 183
YjgC COG3383
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
158-563 1.37e-34

Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];


Pssm-ID: 442610 [Multi-domain]  Cd Length: 684  Bit Score: 139.63  E-value: 1.37e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 158 AVGSNIVLSTRGGEVMRVLPRLNEDINEEWISDKTRFAYDGL-KRQRLTQPLVKDDsGQLVPTSWEDALAQVAGALQGAK 236
Cdd:COG3383    15 GVGCGIDLEVKDGKIVKVEGDPDHPVNRGRLCVKGRFGFEFVnSPDRLTTPLIRRG-GEFREVSWDEALDLVAERLREIQ 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 237 ---GGD-IAAVVGG--LVEAEALVC--LKDLLNCLNSDS---LCTEevfPTAGA-----GSDLRSNyllntGIAGIEEAD 300
Cdd:COG3383    94 aehGPDaVAFYGSGqlTNEENYLLQklARGVLGTNNIDNnarLCMA---SAVAGlkqsfGSDAPPN-----SYDDIEEAD 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 301 LLLLVGTNPRFEAPLFNARIRKSWLHN-----------------DLH--------VALL---------GKPVDLSYTYDH 346
Cdd:COG3383   166 VILVIGSNPAEAHPVLARRIKKAKKNGaklivvdprrtetarlaDLHlqikpgtdLALLngllhviieEGLVDEDFIAER 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 347 -----------LGESPKVLQEI----ASGIHPFSQAVTKTKHPVVVVGSSCLQREDGAAvmaAVSSIARKAHVSGEVEET 411
Cdd:COG3383   246 tegfeelkasvAKYTPERVAEItgvpAEDIREAARLIAEAKRAMILWGMGVNQHTQGTD---NVNAIINLALATGNIGRP 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 412 WKIVNVLH--------RVASQVAALDLGYKP--------------GVKTIRENP---------------PKVLFLLG--- 451
Cdd:COG3383   323 GTGPFPLTgqnnvqggRDMGALPNVLPGYRDvtdpehrakvadawGVPPLPDKPgltavemfdaiadgeIKALWIIGenp 402
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 452 ----ADSGSVtRQDLPEDSLVIYQghhgDV----GAPMADIILPGAAYTEKRGTYVNTEGRAQQTRVAVTPPGMAREDWR 523
Cdd:COG3383   403 avsdPDANHV-REALEKLEFLVVQ----DIflteTAEYADVVLPAASWAEKDGTFTNTERRVQRVRKAVEPPGEARPDWE 477
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|..
gi 1357711166 524 IIRAISELAGVKLPYETLDEVRNRLAEVSPNL--VRYDEVEE 563
Cdd:COG3383   478 IIAELARRLGYGFDYDSPEEVFDEIARLTPDYsgISYERLEA 519
MopB_Formate-Dh-H cd02753
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ...
158-563 2.11e-24

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: 107.30  E-value: 2.11e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 158 AVGSNIVLSTRGGEVMRVLPRLNEDINEEWISDKTRFAYDGLK-RQRLTQPLVKDDsGQLVPTSWEDALAQVAGALQGAK 236
Cdd:cd02753     8 GVGCGLELWVKDNKIVGVEPVKGHPVNRGKLCVKGRFGFDFVNsKDRLTKPLIRKN-GKFVEASWDEALSLVASRLKEIK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 237 GGDIAAVVGGLVEA-----EALVCLKDLLNCL---NSDS---LC----TEEVFPTAGAGSDLRSnyllntgIAGIEEADL 301
Cdd:cd02753    87 DKYGPDAIAFFGSAkctneENYLFQKLARAVGgtnNVDHcarLChsptVAGLAETLGSGAMTNS-------IADIEEADV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 302 LLLVGTNPRFEAPLFNARI---------------RKSWLHN--DLH--------VALLG--------------------- 335
Cdd:cd02753   160 ILVIGSNTTEAHPVIARRIkrakrngaklivadpRRTELARfaDLHlqlrpgtdVALLNamahviieeglydeefieert 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 336 ----------KPVDLSYTYDHLGESPKVLQEIASGIHpfsqavtkTKHPVVVV-GSSCLQREDGA-AVMAavssIARKAH 403
Cdd:cd02753   240 egfeelkeivEKYTPEYAERITGVPAEDIREAARMYA--------TAKSAAILwGMGVTQHSHGTdNVMA----LSNLAL 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 404 VSGEVEETWKIVNVLhRVASQV-AALDLG----YKPG-VKTIR---ENPpkvlFLLGADSGSVtRQDLPEDSLVIYQghh 474
Cdd:cd02753   308 LTGNIGRPGTGVNPL-RGQNNVqGACDMGalpnVLPGyVKALYimgENP----ALSDPNTNHV-RKALESLEFLVVQ--- 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 475 gDV----GAPMADIILPGAAYTEKRGTYVNTEGRAQQTRVAVTPPGMAREDWRIIRAISELAGVKLPYETLDEVRNRLAE 550
Cdd:cd02753   379 -DIflteTAELADVVLPAASFAEKDGTFTNTERRVQRVRKAVEPPGEARPDWEIIQELANRLGYPGFYSHPEEIFDEIAR 457
                         490
                  ....*....|....*
gi 1357711166 551 VSPNL--VRYDEVEE 563
Cdd:cd02753   458 LTPQYagISYERLER 472
PRK07569 PRK07569
bidirectional hydrogenase complex protein HoxU; Validated
45-155 1.07e-23

bidirectional hydrogenase complex protein HoxU; Validated


Pssm-ID: 181037 [Multi-domain]  Cd Length: 234  Bit Score: 100.11  E-value: 1.07e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166  45 VDGKPVMVEPGTTVLQACERAGMQIPRFCYHERLSVAGNCRMCLVEIEKVQKPVAACAMPVMKGWNILTNSDKTRKAREG 124
Cdd:PRK07569    8 IDDQLVSAREGETLLEAAREAGIPIPTLCHLDGLSDVGACRLCLVEIEGSNKLLPACVTPVAEGMVVQTNTPRLQEYRRM 87
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1357711166 125 VMEFLLA--NHPldCPICDQGGECDLQTESIDV 155
Cdd:PRK07569   88 IVELLFAegNHV--CAVCVANGNCELQDLAIEV 118
PRK08493 PRK08493
NADH-quinone oxidoreductase subunit G;
45-149 2.13e-22

NADH-quinone oxidoreductase subunit G;


Pssm-ID: 236277 [Multi-domain]  Cd Length: 819  Bit Score: 102.09  E-value: 2.13e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166  45 VDGKPVMVEPGTTVLQACERAGMQIPRFCYHERLSVAGNCRMCLVEIEKvqKPVAACAMPVMKGWNILTNSDKTRKAREG 124
Cdd:PRK08493    6 INGKECEAQEGEYILNVARRNGIFIPAICYLSGCSPTLACRLCMVEADG--KRVYSCNTKAKEGMNILTNTPNLMDERNA 83
                          90       100
                  ....*....|....*....|....*
gi 1357711166 125 VMEFLLANHPLDCPICDQGGECDLQ 149
Cdd:PRK08493   84 IMQTYDVNHPLECGVCDKSGECELQ 108
MopB_Nitrate-R-NapA-like cd02754
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ...
158-553 6.57e-21

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: 96.91  E-value: 6.57e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 158 AVGSNIVLSTRGGEVMRVLPRLNEDINEEWISDK-TRFAYDGLKRQRLTQPLVKDDSGQLVPTSWEDALAQVAG---ALQ 233
Cdd:cd02754     8 GVGCGVEIGVKDGKVVAVRGDPEHPVNRGRLCIKgLNLHKTLNGPERLTRPLLRRNGGELVPVSWDEALDLIAErfkAIQ 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 234 GAKGGDIAAVVGG---LVEAEALV--CLKDLLNCLNSDS---LCTEevfpTAGAGsdlrsnYLLNTGIAG-------IEE 298
Cdd:cd02754    88 AEYGPDSVAFYGSgqlLTEEYYAAnkLAKGGLGTNNIDTnsrLCMA----SAVAG------YKRSFGADGppgsyddIEH 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 299 ADLLLLVGTNPRFEAPLFNARIRKSWLHN-------------------DLH--------VALL----------------- 334
Cdd:cd02754   158 ADCFFLIGSNMAECHPILFRRLLDRKKANpgakiivvdprrtrtadiaDLHlpirpgtdLALLngllhvlieeglidrdf 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 335 ---------------------------GKPV-DLSYTYDHLGESPKVLQEIASGIHPFSQAVTKTKHPVVVV-------- 378
Cdd:cd02754   238 idahtegfeelkafvadytpekvaeitGVPEaDIREAARLFGEARKVMSLWTMGVNQSTQGTAANNAIINLHlatgkigr 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 379 -GSSCLQ----------REDG--AAVMAAVSSIARKAHVSgEVEETWKivnvlhrvasqVAALDLGYKPGVKT------I 439
Cdd:cd02754   318 pGSGPFSltgqpnamggREVGglANLLPGHRSVNNPEHRA-EVAKFWG-----------VPEGTIPPKPGLHAvemfeaI 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 440 RENPPKVLFLLG-------ADSGSVTRQDLPEDSLVIYQGHHGDVGAPMADIILPGAAYTEKRGTYVNTEGRAQQTRVAV 512
Cdd:cd02754   386 EDGEIKALWVMCtnpavslPNANRVREALERLEFVVVQDAFADTETAEYADLVLPAASWGEKEGTMTNSERRVSLLRAAV 465
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|...
gi 1357711166 513 TPPGMAREDWRIIRAISELAGVK--LPYETLDEVRNRLAEVSP 553
Cdd:cd02754   466 EPPGEARPDWWILADVARRLGFGelFPYTSPEEVFEEYRRLSR 508
PRK12814 PRK12814
putative NADPH-dependent glutamate synthase small subunit; Provisional
45-148 5.94e-17

putative NADPH-dependent glutamate synthase small subunit; Provisional


Pssm-ID: 139246 [Multi-domain]  Cd Length: 652  Bit Score: 84.78  E-value: 5.94e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166  45 VDGKPVMVEPGTTVLQACERAGMQIPRFCYHERLSVAGNCRMCLVEIEKVQKPVAACAMPVMKGWNILTNSDKTRKAREG 124
Cdd:PRK12814    8 INGRSVTAAPGTSILEAAASAGITIPTLCFHQELEATGSCWMCIVEIKGKNRFVPACSTAVSEGMVIETENAELHAMRRQ 87
                          90       100
                  ....*....|....*....|....
gi 1357711166 125 VMEFLLANHPLDCPicdqgGECDL 148
Cdd:PRK12814   88 SLERLIEQHCGDCL-----GPCEL 106
Fer2_4 pfam13510
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ...
41-115 5.29e-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: 70.26  E-value: 5.29e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1357711166  41 LEVFVDGKPVMVEPGTTVLQACERAGMQIPRFCYHER----LSVAGNCRMCLVEIEKVQKpVAACAMPVMKGWNILTNS 115
Cdd:pfam13510   4 VTFTFDGRPVTAPEGDTIAAALLANGVRVPRSCKYGRprgiFCAMGECRNCLVEVDGVPN-VRACTTPVREGMVVRTQN 81
NADH-G_4Fe-4S_3 pfam10588
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region;
122-149 1.60e-13

NADH-ubiquinone oxidoreductase-G iron-sulfur binding region;


Pssm-ID: 463159 [Multi-domain]  Cd Length: 40  Bit Score: 64.78  E-value: 1.60e-13
                          10        20
                  ....*....|....*....|....*...
gi 1357711166 122 REGVMEFLLANHPLDCPICDQGGECDLQ 149
Cdd:pfam10588   1 RKTILELLLSNHPLDCPTCDKNGNCELQ 28
NADH-G_4Fe-4S_3 smart00929
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region;
122-150 4.30e-13

NADH-ubiquinone oxidoreductase-G iron-sulfur binding region;


Pssm-ID: 214918 [Multi-domain]  Cd Length: 41  Bit Score: 63.76  E-value: 4.30e-13
                           10        20
                   ....*....|....*....|....*....
gi 1357711166  122 REGVMEFLLANHPLDCPICDQGGECDLQT 150
Cdd:smart00929   1 RKTILELLLANHPLDCPVCDKNGECELQD 29
BisC COG0243
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
203-566 9.50e-12

Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];


Pssm-ID: 440013 [Multi-domain]  Cd Length: 674  Bit Score: 67.95  E-value: 9.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 203 RLTQPLVKDD---SGQLVPTSWEDALAQVAGALQGAK---GGD-IAAVVGG----LVEAEALVCLKDLLNCL------NS 265
Cdd:COG0243    78 RLTYPMKRVGprgSGKFERISWDEALDLIAEKLKAIIdeyGPEaVAFYTSGgsagRLSNEAAYLAQRFARALgtnnldDN 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 266 DSLCTE--EVFPTAGAGSDLRSNyllntGIAGIEEADLLLLVGTNP---------RFEA-------------PLFNARIR 321
Cdd:COG0243   158 SRLCHEsaVAGLPRTFGSDKGTV-----SYEDLEHADLIVLWGSNPaenhprllrRLREaakkrgakivvidPRRTETAA 232
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 322 KSwlhnDLHVALlgKP-------------------VDL----SYT--YDHLGE-----SPKVLQEIaSGIhP------FS 365
Cdd:COG0243   233 IA----DEWLPI--RPgtdaalllalahvlieeglYDRdflaRHTvgFDELAAyvaayTPEWAAEI-TGV-PaedireLA 304
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 366 QAVTKTKhPVVVVGSSCLQR-EDG-------AAVMAAVSSIARK----AHVSGEveetwkivnvlhrvasqvaALDLGYK 433
Cdd:COG0243   305 REFATAK-PAVILWGMGLQQhSNGtqtvraiANLALLTGNIGKPgggpFSLTGE-------------------AILDGKP 364
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 434 PGVKtirenppkVLFLLG-------ADSGsVTRQDLPEDSLVIYQGHHGDVGAPMADIILPGAAYTEKRGTYVNTE-GRA 505
Cdd:COG0243   365 YPIK--------ALWVYGgnpavsaPDTN-RVREALRKLDFVVVIDTFLTETARYADIVLPATTWLERDDIVTNSEdRRV 435
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1357711166 506 QQTRVAVTPPGMAREDWRIIRAISELAGVKLPY---ETLDE-VRNRLAEVSPNLVRYDEVEEANY 566
Cdd:COG0243   436 HLSRPAVEPPGEARSDWEIFAELAKRLGFEEAFpwgRTEEDyLRELLEATRGRGITFEELREKGP 500
NADH_dhqG_C pfam09326
NADH-ubiquinone oxidoreductase subunit G, C-terminal; Members of this family of are found at ...
580-612 4.21e-11

NADH-ubiquinone oxidoreductase subunit G, C-terminal; Members of this family of are found at the C-terminus of NADH dehydrogenases subunit G or NADH-ubiquinone oxidoreductase subunit G. EC:1.6.99.5.


Pssm-ID: 462757  Cd Length: 41  Bit Score: 58.00  E-value: 4.21e-11
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1357711166 580 ALLTEPLVPPqltVRDFYMTDPVSRASQTMAKC 612
Cdd:pfam09326  12 KLSGAPLKSP---IEDFYMTDPISRASATMAKC 41
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
41-111 1.13e-10

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: 58.18  E-value: 1.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166  41 LEVFVDGKPVMVEPGTTVLQACERAGMQIPRFCYHerlsvaGNCRMCLVEIEK----------------VQKPVAACAMP 104
Cdd:cd00207     3 INVPGSGVEVEVPEGETLLDAAREAGIDIPYSCRA------GACGTCKVEVVEgevdqsdpslldeeeaEGGYVLACQTR 76

                  ....*..
gi 1357711166 105 VMKGWNI 111
Cdd:cd00207    77 VTDGLVI 83
Fer2 pfam00111
2Fe-2S iron-sulfur cluster binding domain;
43-91 2.14e-06

2Fe-2S iron-sulfur cluster binding domain;


Pssm-ID: 395061 [Multi-domain]  Cd Length: 77  Bit Score: 45.59  E-value: 2.14e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1357711166  43 VFVDGKPVMVE---PGTTVLQACERAGMQIPRFCYHerlsvaGNCRMCLVEI 91
Cdd:pfam00111   1 VTINGKGVTIEvpdGETTLLDAAEEAGIDIPYSCRG------GGCGTCAVKV 46
PRK13532 PRK13532
nitrate reductase catalytic subunit NapA;
477-525 5.97e-06

nitrate reductase catalytic subunit NapA;


Pssm-ID: 237416 [Multi-domain]  Cd Length: 830  Bit Score: 49.51  E-value: 5.97e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1357711166 477 VGAPMADIILPGAAYTEKRGTYVNTEGRAQQTRVAVTPPGMARED-WRII 525
Cdd:PRK13532  516 VSALAADLILPTAMWVEKEGAYGNAERRTQFWRQQVKAPGEAKSDlWQLV 565
MopB_Nitrate-R-NarG-like cd02750
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ...
476-541 1.65e-05

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: 47.70  E-value: 1.65e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1357711166 476 DVGAPMADIILPGAAYTEKRG-------TYVNTEGRAqqtrvaVTPPGMAREDWRIIRAISElagvKLPYETL 541
Cdd:cd02750   374 DSTALYSDIVLPAATWYEKHDlsttdmhPFIHPFSPA------VDPLWEAKSDWEIFKALAK----KVPWRTL 436
Fdx COG0633
Ferredoxin [Energy production and conversion];
46-92 3.24e-03

Ferredoxin [Energy production and conversion];


Pssm-ID: 440398 [Multi-domain]  Cd Length: 87  Bit Score: 37.14  E-value: 3.24e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1357711166  46 DGKPVMVEPGTTVLQACERAGMQIPRFCyheRlsvAGNCRMCLVEIE 92
Cdd:COG0633     9 EGHTVEVPAGESLLEAALRAGIDLPYSC---R---SGACGTCHVRVL 49
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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