The domain within your query sequence starts at position 18 and ends at position 216; the E-value for the vATP-synt_E domain shown below is 7.6e-80.

FIEQEANEKAEEIDAKAEEEFNIEKGRLVQTQRLKIMEYYEKKEKQIEQQKKIQMSNLMN
QARLKVLRARDDLITDLLNEAKQRLSKVVKDTTRYQVLLDGLVLQGLYQLLEPRMIVRCR
KQDFPLVKAAVQKAIPMYKIATKKDVDVQIDQEAYLPEEIAGGVEIYNGDRKIKVSNTLE
SRLDLIAQQMMPEVRGALF

vATP-synt_E

vATP-synt_E
PFAM accession number:PF01991
Interpro abstract (IPR002842):

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:

  • F-ATPases (ATP synthases, F1F0-ATPases), which are found in mitochondria, chloroplasts and bacterial plasma membranes where they are the prime producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts).
  • V-ATPases (V1V0-ATPases), which are primarily found in eukaryotes and they function as proton pumps that acidify intracellular compartments and, in some cases, transport protons across the plasma membrane [(PUBMED:20450191)]. They are also found in bacteria [(PUBMED:9741106)].
  • A-ATPases (A1A0-ATPases), which are found in Archaea and function like F-ATPases, though with respect to their structure and some inhibitor responses, A-ATPases are more closely related to the V-ATPases [(PUBMED:18937357), (PUBMED:1385979)].
  • P-ATPases (E1E2-ATPases), which are found in bacteria and in eukaryotic plasma membranes and organelles, and function to transport a variety of different ions across membranes.
  • E-ATPases, which are cell-surface enzymes that hydrolyse a range of NTPs, including extracellular ATP.

The V-ATPases (or V1V0-ATPase) and A-ATPases (or A1A0-ATPase) are each composed of two linked complexes: the V1 or A1 complex contains the catalytic core that hydrolyses/synthesizes ATP, and the V0 or A0 complex that forms the membrane-spanning pore. The V- and A-ATPases both contain rotary motors, one that drives proton translocation across the membrane and one that drives ATP synthesis/hydrolysis [(PUBMED:11309608), (PUBMED:15629643), (PUBMED:15168615)]. The V- and A-ATPases more closely resemble one another in subunit structure than they do the F-ATPases, although the function of A-ATPases is closer to that of F-ATPases.

This entry represents subunit E from V-ATPases and A-ATPase/synthases. Subunit E appears to form a tight interaction with subunit G, which together may act as stators to prevent certain subunits from rotating with the central rotary element, much in the same way as the F0 complex subunit B does in F-ATPases [(PUBMED:15292229)]. In addition to its key role in stator structure, subunit E appears to have a role in mediating interactions with putative regulatory subunits [(PUBMED:15751969)].

GO process:ATP hydrolysis coupled proton transport (GO:0015991)
GO component:proton-transporting two-sector ATPase complex, catalytic domain (GO:0033178)
GO function:proton-transporting ATPase activity, rotational mechanism (GO:0046961)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry vATP-synt_E