NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1980524067|ref|YP_009988342|]
View 

Atp4 (mitochondrion) [Gelidiella flabella]

Protein Classification

ATP synthase subunit B family protein( domain architecture ID 229537)

ATP synthase subunit B family protein such as subunits b and b' from the F(o) complex in F-type ATP synthase (FoF1-ATPase) found in chloroplasts and in bacterial plasma membranes; the b subunits are part of the peripheral stalk that links the F(1) and F(o) complexes together, and which acts as a stator to prevent certain subunits from rotating with the central rotary element

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
ATP-synt_Fo_b super family cl21478
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
19-68 2.16e-03

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 pfam05405:

Pssm-ID: 473877 [Multi-domain]  Cd Length: 163  Bit Score: 36.87  E-value: 2.16e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1980524067  19 IILLNEETLILICFITFIWLLSSKIGLSVKQDLDNQASNVHNYLENSFNQ 68
Cdd:pfam05405  10 IYVVNEETIVALCFIGFLIFVYKSLGPSIKEWLDKRIEKIQDELNQSRNL 59
 
Name Accession Description Interval E-value
Mt_ATP-synt_B pfam05405
Mitochondrial ATP synthase B chain precursor (ATP-synt_B); The Fo sector of the ATP synthase ...
19-68 2.16e-03

Mitochondrial ATP synthase B chain precursor (ATP-synt_B); 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).


Pssm-ID: 368426 [Multi-domain]  Cd Length: 163  Bit Score: 36.87  E-value: 2.16e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1980524067  19 IILLNEETLILICFITFIWLLSSKIGLSVKQDLDNQASNVHNYLENSFNQ 68
Cdd:pfam05405  10 IYVVNEETIVALCFIGFLIFVYKSLGPSIKEWLDKRIEKIQDELNQSRNL 59
 
Name Accession Description Interval E-value
Mt_ATP-synt_B pfam05405
Mitochondrial ATP synthase B chain precursor (ATP-synt_B); The Fo sector of the ATP synthase ...
19-68 2.16e-03

Mitochondrial ATP synthase B chain precursor (ATP-synt_B); 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).


Pssm-ID: 368426 [Multi-domain]  Cd Length: 163  Bit Score: 36.87  E-value: 2.16e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1980524067  19 IILLNEETLILICFITFIWLLSSKIGLSVKQDLDNQASNVHNYLENSFNQ 68
Cdd:pfam05405  10 IYVVNEETIVALCFIGFLIFVYKSLGPSIKEWLDKRIEKIQDELNQSRNL 59
 
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