NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2438308197|gb|WCI18541|]
View 

ATPase subunit 8, partial (mitochondrion) [Vernicia fordii]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
YMF19_C pfam06449
ATP synthase YMF19, C-terminal; This domain represents the C-terminal region of YMF19 of the ...
67-117 2.34e-20

ATP synthase YMF19, C-terminal; This domain represents the C-terminal region of YMF19 of the F0 complex of mitochondrial F-ATPases from plants. This family is found in conjunction with pfam02326.


:

Pssm-ID: 368914  Cd Length: 51  Bit Score: 78.19  E-value: 2.34e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2438308197  67 DLLGKRRKITLISCFGEISGSRGMERNIFYLISKSSYSISSNPGWGITCRN 117
Cdd:pfam06449   1 DLFGKRRIITFIECFGEISGSRGMERNIFYLISKSSYNTSSNPGWGITCRN 51
ATP-synt_Fo_b super family cl21478
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
6-56 1.19e-07

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The 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. The 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. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


The actual alignment was detected with superfamily member pfam02326:

Pssm-ID: 473877  Cd Length: 84  Bit Score: 46.24  E-value: 1.19e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2438308197   6 DGVLGISRILKLRNQLVSHRG----NNIRSNDPNSLEDILRKG-FSTGVSYMYSSL 56
Cdd:pfam02326  29 FILPKISRILKLRKKLLSSLIssklGKEQSLLGVSKDSLLANSsLSTSNSYLYSSL 84
 
Name Accession Description Interval E-value
YMF19_C pfam06449
ATP synthase YMF19, C-terminal; This domain represents the C-terminal region of YMF19 of the ...
67-117 2.34e-20

ATP synthase YMF19, C-terminal; This domain represents the C-terminal region of YMF19 of the F0 complex of mitochondrial F-ATPases from plants. This family is found in conjunction with pfam02326.


Pssm-ID: 368914  Cd Length: 51  Bit Score: 78.19  E-value: 2.34e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2438308197  67 DLLGKRRKITLISCFGEISGSRGMERNIFYLISKSSYSISSNPGWGITCRN 117
Cdd:pfam06449   1 DLFGKRRIITFIECFGEISGSRGMERNIFYLISKSSYNTSSNPGWGITCRN 51
YMF19 pfam02326
Plant ATP synthase F0; This family corresponds to subunit 8 (YMF19) of the F0 complex of plant ...
6-56 1.19e-07

Plant ATP synthase F0; This family corresponds to subunit 8 (YMF19) of the F0 complex of plant and algae mitochondrial F-ATPases (EC:3.6.1.34).


Pssm-ID: 396760  Cd Length: 84  Bit Score: 46.24  E-value: 1.19e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2438308197   6 DGVLGISRILKLRNQLVSHRG----NNIRSNDPNSLEDILRKG-FSTGVSYMYSSL 56
Cdd:pfam02326  29 FILPKISRILKLRKKLLSSLIssklGKEQSLLGVSKDSLLANSsLSTSNSYLYSSL 84
 
Name Accession Description Interval E-value
YMF19_C pfam06449
ATP synthase YMF19, C-terminal; This domain represents the C-terminal region of YMF19 of the ...
67-117 2.34e-20

ATP synthase YMF19, C-terminal; This domain represents the C-terminal region of YMF19 of the F0 complex of mitochondrial F-ATPases from plants. This family is found in conjunction with pfam02326.


Pssm-ID: 368914  Cd Length: 51  Bit Score: 78.19  E-value: 2.34e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2438308197  67 DLLGKRRKITLISCFGEISGSRGMERNIFYLISKSSYSISSNPGWGITCRN 117
Cdd:pfam06449   1 DLFGKRRIITFIECFGEISGSRGMERNIFYLISKSSYNTSSNPGWGITCRN 51
YMF19 pfam02326
Plant ATP synthase F0; This family corresponds to subunit 8 (YMF19) of the F0 complex of plant ...
6-56 1.19e-07

Plant ATP synthase F0; This family corresponds to subunit 8 (YMF19) of the F0 complex of plant and algae mitochondrial F-ATPases (EC:3.6.1.34).


Pssm-ID: 396760  Cd Length: 84  Bit Score: 46.24  E-value: 1.19e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2438308197   6 DGVLGISRILKLRNQLVSHRG----NNIRSNDPNSLEDILRKG-FSTGVSYMYSSL 56
Cdd:pfam02326  29 FILPKISRILKLRKKLLSSLIssklGKEQSLLGVSKDSLLANSsLSTSNSYLYSSL 84
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH