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Conserved domains on  [gi|67090508|gb|AAY67632|]
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ATP synthase F0 subunit 6, partial (mitochondrion) [Pachyornis elephantopus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ATP-synt_Fo_a_6 super family cl00413
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 1-18 2.14e-06

ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms are designated as ATP synthase, Fo complex, subunit a; eukaryotic (chloroplast and mitochondrial) forms are designated as ATP synthase, Fo complex, subunit 6. The F-ATP synthases (also called FoF1-ATPases) consist of two structural domains: F1 (factor one) complex containing the soluble catalytic core, and Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. F-ATP synthase has also been found in the archaea Methanosarcina acetivorans. F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis.


The actual alignment was detected with superfamily member MTH00120:

Pssm-ID: 469762  Cd Length: 227  Bit Score: 39.81  E-value: 2.14e-06
                         10
                 ....*....|....*...
gi 67090508    1 IQAYVFVLLLSLYLQENI 18
Cdd:MTH00120 210 IQAYVFVLLLSLYLQENT 227
 
Name Accession Description Interval E-value
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
 1-18 2.14e-06

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 39.81  E-value: 2.14e-06
                         10
                 ....*....|....*...
gi 67090508    1 IQAYVFVLLLSLYLQENI 18
Cdd:MTH00120 210 IQAYVFVLLLSLYLQENT 227
 
Name Accession Description Interval E-value
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
 1-18 2.14e-06

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 39.81  E-value: 2.14e-06
                         10
                 ....*....|....*...
gi 67090508    1 IQAYVFVLLLSLYLQENI 18
Cdd:MTH00120 210 IQAYVFVLLLSLYLQENT 227
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 1-18 6.21e-06

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 38.70  E-value: 6.21e-06
                         10
                 ....*....|....*...
gi 67090508    1 IQAYVFVLLLSLYLQENI 18
Cdd:MTH00132 210 IQAYVFVLLLSLYLQENV 227
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
 1-18 2.37e-05

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 36.87  E-value: 2.37e-05
                         10
                 ....*....|....*...
gi 67090508    1 IQAYVFVLLLSLYLQENI 18
Cdd:MTH00073 210 IQAYVFVLLLSLYLQENV 227
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 1-17 2.45e-03

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 31.46  E-value: 2.45e-03
                         10
                 ....*....|....*..
gi 67090508    1 IQAYVFVLLLSLYLQEN 17
Cdd:MTH00101 209 IQAYVFTLLVSLYLHDN 225
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
 1-17 4.52e-03

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 30.69  E-value: 4.52e-03
                         10
                 ....*....|....*..
gi 67090508    1 IQAYVFVLLLSLYLQEN 17
Cdd:MTH00179 210 IQAYVFVLLLSLYLQEN 226
 
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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