The domain within your query sequence starts at position 228 and ends at position 473; the E-value for the Peptidase_M48 domain shown below is 5.5e-75.

PLPEGKLKQEIEVMAKSIDFPLTKVYVVEGSKRSSHSNAYFYGFFKNKRIVLFDTLLEEY
SVPNKDNQEESGMEARNEGEGDSEEVKAKVKNKKQGCKNEEVLAVLGHELGHWKLGHTVK
NIIISQMNSFLCFFLFAVLIGRRELFAAFGFYDSQPTLIGLLIIFQFIFSPYNEVLSFCL
TVLSRRFEFQADAFAKKLGKAKDLYSALIKLNKDNLGFPVSDWLFSTWHYSHPPLLERLQ
ALKNAK

Peptidase_M48

Peptidase_M48
PFAM accession number:PF01435
Interpro abstract (IPR001915):

This entry represents the largely extracellular catalytic region of CAAX prenyl protease homologues such as Human FACE-1 protease. These are metallopeptidases, with the characteristic HExxH motif giving the two histidine-zinc-ligands and an adjacent glutamate on the next helix being the third. The whole molecule folds to form a deep groove/cleft into which the substrate can fit [(PUBMED:23539602), (PUBMED:23539603)].

This group of metallopeptidases belong to MEROPS peptidase family M48. Proteins with this domain are mostly described as probable protease htpX homologue (EC 3.4.24) or CAAX prenyl protease 1, which proteolytically removes the C-terminal three residues of farnesylated proteins. They are integral membrane proteins associated with the endoplasmic reticulum and Golgi, binding one zinc ion per subunit.

GO process:proteolysis (GO:0006508)
GO function:metalloendopeptidase activity (GO:0004222)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Peptidase_M48