The domain within your query sequence starts at position 17 and ends at position 230; the E-value for the PAC2 domain shown below is 3.8e-38.

LLMPAVSVGNVGQLAIDLIISTLNMCKIGYFYTDCLVPMVGNNPYATEEENSNELSINTE
VYSLPSKKLVVLQLRSIFIKYKSKSFCEKLLAWVESSGCARIIVLSSSHSYHRNDAQLRS
TPFRYLLTPCLQKSVQNKIKSLNWLEMEKSRCIPEMSDSEFCIRIPGGGITKTLYDESCS
KEIQMAVLLKFVSEGDNIPDAVSLVEYLNEWLQI

PAC2

PAC2
PFAM accession number:PF09754
Interpro abstract (IPR019151):

This PAC2 (Proteasome assembly chaperone) family of proteins is found in bacteria, archaea and eukaryotes. Proteins in this family are typically between 247 and 307 amino acids in length. These proteins function as a chaperone for the 26S proteasome, which is about 2000 kilodaltons (kDa) in molecular mass and contains one 20S core particle structure and two 19S regulatory caps. The 26S proteasome mediates ubiquitin-dependent proteolysis in eukaryotic cells. A number of studies including very recent ones have revealed that assembly of its 20S catalytic core particle is an ordered process that involves several conserved proteasome assembly chaperones (PACs). Two heterodimeric chaperones, PAC1-PAC2 and PAC3-PAC4, promote the assembly of rings composed of seven alpha subunits [(PUBMED:18786393), (PUBMED:17431397), (PUBMED:17707236), (PUBMED:16251969)].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry PAC2