The domain within your query sequence starts at position 29 and ends at position 451; the E-value for the Peptidase_S10 domain shown below is 2e-99.

IDWREPEGKEVWDYVTVRKDAHMFWWLYYATNPCKNFSELPLVMWLQGGPGGSSTGFGNF
EEIGPLDTQLKPRNTTWLQWASLLFVDNPVGTGFSYVNTTDAYAKDLDTVASDMMVLLKS
FFDCHKEFQTVPFYIFSESYGGKMAAGISVELYKAVQQGTIKCNFSGVALGDSWISPVDS
VLSWGPYLYSMSLLDNQGLAEVSDIAEQVLDAVNKGFYKEATQLWGKAEMIIEKNTDGVN
FYNILTKSSPEKAMESSLEFLRSPLVRLCQRHVRHLQGDALSQLMNGPIKKKLKIIPEDI
SWGAQASYVFLSMEGDFMKPAIDVVDKLLAAGVNVTVYNGQLDLIVDTIGQESWVQKLKW
PQLSKFNQLKWKALYTDPKSSETAAFVKSYENLAFYWILKAGHMVPSDQGEMALKMMKLV
TKQ

Peptidase_S10

Peptidase_S10
PFAM accession number:PF00450
Interpro abstract (IPR001563):

This group of serine peptidases belong to MEROPS peptidase family S10 (clan SC). The type example is carboxypeptidase Y from Saccharomyces cerevisiae (Baker's yeast) [ (PUBMED:7845208) ].

All known carboxypeptidases are either metallo carboxypeptidases or serine carboxypeptidases ( EC 3.4.16.5 and EC 3.4.16.6 ). The catalytic activity of the serine carboxypeptidases, like that of the trypsin family serine proteases, is provided by a charge relay system involving an aspartic acid residue hydrogen-bonded to a histidine, which is itself hydrogen-bonded to a serine [ (PUBMED:2324088) ]. The sequences surrounding the active site serine and histidine residues are highly conserved in all the serine carboxypeptidases.

GO process:proteolysis (GO:0006508)
GO function:serine-type carboxypeptidase activity (GO:0004185)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Peptidase_S10