The domain within your query sequence starts at position 34 and ends at position 471; the E-value for the Peptidase_S10 domain shown below is 1.7e-139.

PGLAKQPSFRQYSGYLRASDSKHFHYWFVESQNDPKNSPVVLWLNGGPGCSSLDGLLTEH
GPFLIQPDGVTLEYNPYAWNLIANVLYIESPAGVGFSYSDDKMYVTNDTEVAENNYEALK
DFFRLFPEYKDNKLFLTGESYAGIYIPTLAVLVMQDPSMNLQGLAVGNGLASYEQNDNSL
VYFAYYHGLLGNRLWTSLQTHCCAQNKCNFYDNKDPECVNNLLEVSRIVGKSGLNIYNLY
APCAGGVPGRHRYEDTLVVQDFGNIFTRLPLKRRFPEALMRSGDKVRLDPPCTNTTAPSN
YLNNPYVRKALHIPESLPRWDMCNFLVNLQYRRLYQSMNSQYLKLLSSQKYQILLYNGDV
DMACNFMGDEWFVDSLNQKMEVQRRPWLVDYGESGEQVAGFVKECSHITFLTIKGAGHMV
PTDKPRAAFTMFSRFLNK

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