The domain within your query sequence starts at position 83 and ends at position 404; the E-value for the Peptidase_M19 domain shown below is 1.2e-110.

ALMRDFPLVDGHNDLPLLLRELFQNQLQDVNLRNFTRGQTNLDRLRDGLVGAQFWSAYIP
CQTQDRDAVRLALEQIDLIRRMCSAYPELELVTSADGLNNTQKLACLIGVEGGHSLDTSL
AVLRSFYELGVRYLTLTFTCSTPWAESATKFRHHFYTNISGLTSFGEKVVEEMNRLGMMI
DLSHASDTLVKQTLEVSQAPVIFSHSAARSVCDNLLNIPDDILQLLKKNGGIVMVTLSMG
VLQCSLFANVSTVADHFDHIRTVIGSEFIGIGGSYDGSGRFPQGLEDVSTYPVLIEELLS
RGWDERELQGVLRGNLLRVFRQ

Peptidase_M19

Peptidase_M19
PFAM accession number:PF01244
Interpro abstract (IPR008257):

This group of peptidases belong to the MEROPS peptidase family M19 (membrane dipeptidase family, clan MJ). The protein fold of the peptidase domain for members of this family resembles that of Klebsiella urease, the type example for clan MJ [ (PUBMED:12144777) ].

Renal dipeptidase ( EC 3.4.13.19 ), also known as microsomal dipeptidase or membrane-bound dipeptidase, is a zinc-dependent metalloenzyme that hydrolyses a wide range of dipeptides. It is involved in renal metabolism of glutathione and its conjugates. It is a homodimeric disulphide-linked glycoprotein attached to the renal brush border microvilli membrane by a GPI-anchor. A glutamate residue has recently been shown [ (PUBMED:12144777) (PUBMED:8097406) ] to be important for the catalytic activity of renal dipeptidase. Renal dipeptidase seems to be evolutionary related to hypothetical proteins in the PQQ biosynthesis operons of Acinetobacter calcoaceticus and Klebsiella pneumoniae [ (PUBMED:7674922) ].

GO process:proteolysis (GO:0006508)
GO function:metallodipeptidase activity (GO:0070573)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Peptidase_M19