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Conserved domains on  [gi|353251551|pdb|2YBB|7]
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Chain 7, NADH-QUINONE OXIDOREDUCTASE SUBUNIT 15

Protein Classification

NADH-quinone oxidoreductase subunit 15( domain architecture ID 10568788)

NADH-quinone oxidoreductase subunit 15 is part of the NDH-1 complex that shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain

PubMed:  23417064

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NADH_Oxid_Nqo15 pfam11497
NADH-quinone oxidoreductase chain 15; This protein, Nqo15, is a part of respiratory complex 1 ...
 4-126 4.10e-72

NADH-quinone oxidoreductase chain 15; This protein, Nqo15, is a part of respiratory complex 1 which is a complex that plays a central role in cellular energy production in both bacteria and mitochondria. Nqo15 has a similar fold to Frataxin, the mitochondrial iron chaperone. This protein may have a role in iron-sulphur cluster regeneration in the complex. This domain represents more than half the molecular mass of the entire complex.


:

Pssm-ID: 431910  Cd Length: 123  Bit Score: 211.18  E-value: 4.10e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2YBB_7          4 SSERELYEAWVELLSWMREYAQAKGVRFEKEADFPDFIYRMERPYDLPTTIMTASLSDGLGEPFLLADVSPRHAKLKRIG 83
Cdd:pfam11497   1 ASDAALYDAWVELLGWLREYAAARGLRFEKEADFPDYIYRMERPYDLPTTVMSASLSDGNGEPFLLAAVSPRHADLKGVS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
2YBB_7         84 LRLPRAHIHLHAHYEPGKGLVTGKIPLTKERFFALADRAREAL 126
Cdd:pfam11497  81 LRLPGGHKHWHLHEAGKGLLLEGKRPFTKERLFALLDGARRGV 123
 
Name Accession Description Interval E-value
NADH_Oxid_Nqo15 pfam11497
NADH-quinone oxidoreductase chain 15; This protein, Nqo15, is a part of respiratory complex 1 ...
 4-126 4.10e-72

NADH-quinone oxidoreductase chain 15; This protein, Nqo15, is a part of respiratory complex 1 which is a complex that plays a central role in cellular energy production in both bacteria and mitochondria. Nqo15 has a similar fold to Frataxin, the mitochondrial iron chaperone. This protein may have a role in iron-sulphur cluster regeneration in the complex. This domain represents more than half the molecular mass of the entire complex.


Pssm-ID: 431910  Cd Length: 123  Bit Score: 211.18  E-value: 4.10e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2YBB_7          4 SSERELYEAWVELLSWMREYAQAKGVRFEKEADFPDFIYRMERPYDLPTTIMTASLSDGLGEPFLLADVSPRHAKLKRIG 83
Cdd:pfam11497   1 ASDAALYDAWVELLGWLREYAAARGLRFEKEADFPDYIYRMERPYDLPTTVMSASLSDGNGEPFLLAAVSPRHADLKGVS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
2YBB_7         84 LRLPRAHIHLHAHYEPGKGLVTGKIPLTKERFFALADRAREAL 126
Cdd:pfam11497  81 LRLPGGHKHWHLHEAGKGLLLEGKRPFTKERLFALLDGARRGV 123
 
Name Accession Description Interval E-value
NADH_Oxid_Nqo15 pfam11497
NADH-quinone oxidoreductase chain 15; This protein, Nqo15, is a part of respiratory complex 1 ...
 4-126 4.10e-72

NADH-quinone oxidoreductase chain 15; This protein, Nqo15, is a part of respiratory complex 1 which is a complex that plays a central role in cellular energy production in both bacteria and mitochondria. Nqo15 has a similar fold to Frataxin, the mitochondrial iron chaperone. This protein may have a role in iron-sulphur cluster regeneration in the complex. This domain represents more than half the molecular mass of the entire complex.


Pssm-ID: 431910  Cd Length: 123  Bit Score: 211.18  E-value: 4.10e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2YBB_7          4 SSERELYEAWVELLSWMREYAQAKGVRFEKEADFPDFIYRMERPYDLPTTIMTASLSDGLGEPFLLADVSPRHAKLKRIG 83
Cdd:pfam11497   1 ASDAALYDAWVELLGWLREYAAARGLRFEKEADFPDYIYRMERPYDLPTTVMSASLSDGNGEPFLLAAVSPRHADLKGVS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
2YBB_7         84 LRLPRAHIHLHAHYEPGKGLVTGKIPLTKERFFALADRAREAL 126
Cdd:pfam11497  81 LRLPGGHKHWHLHEAGKGLLLEGKRPFTKERLFALLDGARRGV 123
 
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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