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Conserved domains on  [gi|398366541|ref|NP_010665|]
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F1F0 ATP synthase subunit f [Saccharomyces cerevisiae S288C]

Protein Classification

F0F1 ATP synthase subunit f( domain architecture ID 10566719)

F0F1 ATP synthase subunit f is part of the membrane proton channel (F0) of the F-type ATPase that produces ATP from ADP in the presence of a proton gradient across the membrane

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
F1F0-ATPsyn_F pfam10791
Mitochondrial F1-F0 ATP synthase subunit F of fungi; The membrane bound F1-FO-type H+ ATP ...
 7-93 3.20e-53

Mitochondrial F1-F0 ATP synthase subunit F of fungi; The membrane bound F1-FO-type H+ ATP synthase of mitochondria catalyzes the terminal step in oxidative respiration converting the generation of the electrochemical gradient into ATP for cellular biosynthesis. The general structure and the core subunits of the enzyme are highly conserved in both prokaryotic and eukaryotic organizms.


:

Pssm-ID: 431498  Cd Length: 87  Bit Score: 160.85  E-value: 3.20e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366541    7 VSTLIPPKVVSSKNIGSAPNAKRIANVVHFYKSLPQGPAPAIKANTRLARYKAKYFDGDNASGKPLWHFALGIIAFGYSM 86
Cdd:pfam10791   1 LSTLIPPKIASPKALGSAPNAARMARVVSFYSKLPKGPAPAPKPKGLLGRYKAKYFDGKNASGKPLLHLIGGLFLLGYSI 80


                  ....*..
gi 398366541   87 EYYFHLR 93
Cdd:pfam10791  81 EYYFHLR 87
 
Name Accession Description Interval E-value
F1F0-ATPsyn_F pfam10791
Mitochondrial F1-F0 ATP synthase subunit F of fungi; The membrane bound F1-FO-type H+ ATP ...
 7-93 3.20e-53

Mitochondrial F1-F0 ATP synthase subunit F of fungi; The membrane bound F1-FO-type H+ ATP synthase of mitochondria catalyzes the terminal step in oxidative respiration converting the generation of the electrochemical gradient into ATP for cellular biosynthesis. The general structure and the core subunits of the enzyme are highly conserved in both prokaryotic and eukaryotic organizms.


Pssm-ID: 431498  Cd Length: 87  Bit Score: 160.85  E-value: 3.20e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366541    7 VSTLIPPKVVSSKNIGSAPNAKRIANVVHFYKSLPQGPAPAIKANTRLARYKAKYFDGDNASGKPLWHFALGIIAFGYSM 86
Cdd:pfam10791   1 LSTLIPPKIASPKALGSAPNAARMARVVSFYSKLPKGPAPAPKPKGLLGRYKAKYFDGKNASGKPLLHLIGGLFLLGYSI 80


                  ....*..
gi 398366541   87 EYYFHLR 93
Cdd:pfam10791  81 EYYFHLR 87
 
Name Accession Description Interval E-value
F1F0-ATPsyn_F pfam10791
Mitochondrial F1-F0 ATP synthase subunit F of fungi; The membrane bound F1-FO-type H+ ATP ...
 7-93 3.20e-53

Mitochondrial F1-F0 ATP synthase subunit F of fungi; The membrane bound F1-FO-type H+ ATP synthase of mitochondria catalyzes the terminal step in oxidative respiration converting the generation of the electrochemical gradient into ATP for cellular biosynthesis. The general structure and the core subunits of the enzyme are highly conserved in both prokaryotic and eukaryotic organizms.


Pssm-ID: 431498  Cd Length: 87  Bit Score: 160.85  E-value: 3.20e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366541    7 VSTLIPPKVVSSKNIGSAPNAKRIANVVHFYKSLPQGPAPAIKANTRLARYKAKYFDGDNASGKPLWHFALGIIAFGYSM 86
Cdd:pfam10791   1 LSTLIPPKIASPKALGSAPNAARMARVVSFYSKLPKGPAPAPKPKGLLGRYKAKYFDGKNASGKPLLHLIGGLFLLGYSI 80


                  ....*..
gi 398366541   87 EYYFHLR 93
Cdd:pfam10791  81 EYYFHLR 87
 
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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