The domain within your query sequence starts at position 24 and ends at position 462; the E-value for the Peptidase_M18 domain shown below is 2e-190.

FVNRSPSPFHVVAECRSRLLQAGFRELKETEGWDIVPENKYFLTRNSSSIIAFAVGGQYV
PGNGFSLIGAHTDSPCLRVKRKSRRSQVGYHQVGVETYGGGIWSTWFDRDLTLAGRVIIK
CPTSGRLEQRLVHIERPILRIPHLAIHLQRNINENFGPNTEIHLVPILATAVQEELEKGT
PEPGPLGATDERHHSVLMSLLCTHLGLSPDSIMEMELCLADTQPAVLGGAYEEFIFAPRL
DNLHSCFCALQALIDSCASPASLARDPHVRMVTLYDNEEVGSESAQGAQSLLTELILRRI
SASPQRLTAFEEAIPKSFMISADMAHAVHPNYSDKHEENHRPLFHKGPVIKVNSKQRYAS
NAVSESMIREVAGQVGVPLQDLMVRNDSPCGTTIGPILASRLGLRVLDLGSPQLAMHSIR
ETACTTGVLQTLTLFKGFF

Peptidase_M18

Peptidase_M18
PFAM accession number:PF02127
Interpro abstract (IPR001948):

This group of metallopeptidases belong to the MEROPS peptidase family M18, (clan MH). The proteins have two catalytic zinc ions at the active site, bound by His/Asp, Asp, Glu, Asp/Glu and His. The catalysed reaction involves the release of an N-terminal aminoacid, usually neutral or hydrophobic, from a polypeptide [(PUBMED:7674922)].

The type example is aminopeptidase I from Saccharomyces cerevisiae (Baker's yeast), the sequence of which has been deduced, and the mature protein shown to consist of 469 amino acids [(PUBMED:2651436)]. A 45-residue presequence contains both positively- and negatively-charged and hydrophobic residues, which could be arranged in an N-terminal amphiphilic alpha-helix [(PUBMED:2651436)]. The presequence differs from signal sequences that direct proteins across bacterial plasma membranes and endoplasmic reticulum or into mitochondria. It is unclear how this unique presequence targets aminopeptidase I to yeast vacuoles, and how this sorting utilises classical protein secretory pathways [(PUBMED:2651436)].

GO process:proteolysis (GO:0006508)
GO function:zinc ion binding (GO:0008270), aminopeptidase activity (GO:0004177)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Peptidase_M18