The domain within your query sequence starts at position 38 and ends at position 224; the E-value for the ATP-synt_S1 domain shown below is 1.2e-60.
QVPLVLWSSDRNLWAPVADTHEGHITSDMQLSTYLDPALELGPRNVLLFLQDKLSIEDFT AYGGVFGNKQDSAFSNLENALDLAPSSLVLPAVDWYAISTLTTYLQEKLGASPLHVDLAT LKELKLNASLPALLLIRLPYTASSGLMAPREVLTDEVIGQVLSTLKSEDVPYTAALTAVR PSRVARD
ATP-synt_S1 |
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PFAM accession number: | PF05827 |
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Interpro abstract (IPR008388): | 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 the S1 subunit (or subunit AC45) found in the V1 complex of V-ATPases. This subunit is synthesized as an N-glycosylated 60kDa precursor that is intracellularly cleaved to a protein of about 45kDa. This subunit may assist the V-ATPase in the acidification of neuroendocrine granules [ (PUBMED:10336633) ]. |
GO process: | proton transmembrane transport (GO:1902600) |
GO component: | proton-transporting V-type ATPase, V1 domain (GO:0033180) |
This is a PFAM domain. For full annotation and more information, please see the PFAM entry ATP-synt_S1