The domain within your query sequence starts at position 12 and ends at position 112; the E-value for the AAA_22 domain shown below is 6.7e-8.

VHSHPLLLALHGPSGVGKSHVGRLLARHFRAVLEDGALVLQYHARYHCPEPRPVQDCRKE
LAQRVADVVAQAEAEEKTPLLVLDEAELLPPALLDELHDL

AAA_22

AAA_22
PFAM accession number:PF13401
Interpro abstract (IPR003593):

The AAA+ superfamily of ATPases is found in all kingdoms of living organisms where they participate in diverse cellular processes including membrane fusion, proteolysis and DNA replication. Although the terms AAA+ and AAA are often used loosely and interchangeably, the classical AAA family members are distinguished by their possession of the SRH region in the AAA module. Many AAA+ proteins are involved in similar processes to those of AAA proteins (facilitation of protein folding and unfolding, assembly or disassembly of proteins complexes, protein transport and degradation), but others function in replication, recombination, repair and transcription. For a review see [(PUBMED:11473577)].

The proteins in this superfamily are characterised by the structural conservation of a central ATPase domain of about 250 amino acids called the AAA+ module. Typically, the AAA+ domain can be divided into two structural subdomains, an N-terminal P-loop NTPase alpha-beta-alpha subdomain that is connected to a smaller C-terminal all-alpha subdomain. The alpha-beta-alpha subdomain adopts a Rossman fold and contains several motifs involved in ATP binding and hydrolysis, including classical motifs Walker A and Walker B [(PUBMED:11473577), (PUBMED:18466635)]. The all-alpha subdomain [(PUBMED:9927482)], is much less conserved across AAA+ proteins.

This is a PFAM domain. For full annotation and more information, please see the PFAM entry AAA_22