The domain within your query sequence starts at position 31 and ends at position 90; the E-value for the ATP-synt_F domain shown below is 6.7e-22.
AYRRQFLNRDDIGIILINQYIAEMVRHALDAHQRSIPAVLEIPSKEHPYDAAKDSILRRA
ATP-synt_F |
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PFAM accession number: | PF01990 |
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Interpro abstract (IPR008218): | V-ATPases (also known as V1V0-ATPase or vacuolar ATPase) are found in the eukaryotic endomembrane system, and in the plasma membrane of prokaryotes and certain specialised eukaryotic cells. V-ATPases hydrolyse ATP to drive a proton pump, and are involved in a variety of vital intra- and inter-cellular processes such as receptor mediated endocytosis, protein trafficking, active transport of metabolites, homeostasis and neurotransmitter release [ (PUBMED:15629643) ]. V-ATPases are composed of two linked complexes: the V1 complex (subunits A-H) contains the catalytic core that hydrolyses ATP, while the V0 complex (subunits a, c, c', c'', d) forms the membrane-spanning pore. V-ATPases may have an additional role in membrane fusion through binding to t-SNARE proteins [ (PUBMED:15907459) ]. Transmembrane ATPases are membrane-bound enzyme complexes/ion transporters that use ATP hydrolysis to drive the transport of protons across a membrane. Some transmembrane ATPases also work in reverse, harnessing the energy from a proton gradient, using the flux of ions across the membrane via the ATPase proton channel to drive the synthesis of ATP. There are several different types of transmembrane ATPases, which can differ in function (ATP hydrolysis and/or synthesis), structure (e.g., F-, V- and A-ATPases, which contain rotary motors) and in the type of ions they transport [ (PUBMED:15473999) (PUBMED:15078220) ]. The different types include:
This entry represents subunit F in the V1 complex of V-ATPases and Na(+)-translocating ATPase in Enterococcus hirae. Subunit F is a 16kDa protein that is required for the assembly and activity of V-ATPase, and has a potential role in the differential targeting and regulation of the enzyme for specific organelles. This subunit is not necessary for the rotation of the ATPase V1 rotor, but it does promote catalysis [ (PUBMED:14963028) ]. In Enterococcus hirae, Na(+)-translocating ATPase extrudes sodium ions from the cytoplasm and generates the Na+ electrochemical gradient by using the energy of ATP [ (PUBMED:11248190) ]. |
GO process: | ion transmembrane transport (GO:0034220) |
This is a PFAM domain. For full annotation and more information, please see the PFAM entry ATP-synt_F