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Conserved domains on  [gi|33150678|gb|AAP97217|]
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F1Fo-ATP synthase complex Fo membrane domain g subunit [Homo sapiens]

Protein Classification

ATP synthase subunit g( domain architecture ID 10520360)

ATP synthase subunit g is a component of the mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) that produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ATP-synt_G pfam04718
Mitochondrial ATP synthase g subunit; The Fo sector of the ATP synthase is a membrane bound ...
 10-100 3.44e-33

Mitochondrial ATP synthase g subunit; The Fo sector of the ATP synthase is a membrane bound complex which mediates proton transport. It is composed of nine different polypeptide subunits (a, b, c, d, e, f, g F6, A6L). The function of subunit g is currently unknown. The conserved region covers all but the very N-terminus of the member sequences. No prokaryotic members have been identified thus far.


:

Pssm-ID: 461408  Cd Length: 92  Bit Score: 110.27  E-value: 3.44e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33150678    10 EKTPALVNAAVTYLKPRLAAFWYYTTVELVPPTPAEIPRAIQSLKKIVSSAQTGSFKQLTVKEALLNGLVATEVSTWFYV 89
Cdd:pfam04718   1 AKVESLIPHAVYYSKVGLELFKQYAKVELAPPTPAEFQSVYQQLFKTRLASPSGRVKNLTVKEALLAGLVGAEVLGWFSV 80

                          90
                  ....*....|.
gi 33150678    90 REITGKRGIIG 100
Cdd:pfam04718  81 GEIIGRRKLVG 91
 
Name Accession Description Interval E-value
ATP-synt_G pfam04718
Mitochondrial ATP synthase g subunit; The Fo sector of the ATP synthase is a membrane bound ...
 10-100 3.44e-33

Mitochondrial ATP synthase g subunit; The Fo sector of the ATP synthase is a membrane bound complex which mediates proton transport. It is composed of nine different polypeptide subunits (a, b, c, d, e, f, g F6, A6L). The function of subunit g is currently unknown. The conserved region covers all but the very N-terminus of the member sequences. No prokaryotic members have been identified thus far.


Pssm-ID: 461408  Cd Length: 92  Bit Score: 110.27  E-value: 3.44e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33150678    10 EKTPALVNAAVTYLKPRLAAFWYYTTVELVPPTPAEIPRAIQSLKKIVSSAQTGSFKQLTVKEALLNGLVATEVSTWFYV 89
Cdd:pfam04718   1 AKVESLIPHAVYYSKVGLELFKQYAKVELAPPTPAEFQSVYQQLFKTRLASPSGRVKNLTVKEALLAGLVGAEVLGWFSV 80

                          90
                  ....*....|.
gi 33150678    90 REITGKRGIIG 100
Cdd:pfam04718  81 GEIIGRRKLVG 91
 
Name Accession Description Interval E-value
ATP-synt_G pfam04718
Mitochondrial ATP synthase g subunit; The Fo sector of the ATP synthase is a membrane bound ...
 10-100 3.44e-33

Mitochondrial ATP synthase g subunit; The Fo sector of the ATP synthase is a membrane bound complex which mediates proton transport. It is composed of nine different polypeptide subunits (a, b, c, d, e, f, g F6, A6L). The function of subunit g is currently unknown. The conserved region covers all but the very N-terminus of the member sequences. No prokaryotic members have been identified thus far.


Pssm-ID: 461408  Cd Length: 92  Bit Score: 110.27  E-value: 3.44e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33150678    10 EKTPALVNAAVTYLKPRLAAFWYYTTVELVPPTPAEIPRAIQSLKKIVSSAQTGSFKQLTVKEALLNGLVATEVSTWFYV 89
Cdd:pfam04718   1 AKVESLIPHAVYYSKVGLELFKQYAKVELAPPTPAEFQSVYQQLFKTRLASPSGRVKNLTVKEALLAGLVGAEVLGWFSV 80

                          90
                  ....*....|.
gi 33150678    90 REITGKRGIIG 100
Cdd:pfam04718  81 GEIIGRRKLVG 91
 
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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