The domain within your query sequence starts at position 295 and ends at position 633; the E-value for the Peptidase_M8 domain shown below is 5.2e-54.

PFNYSLGLYQWSDKVVRKVERLWNVRDNKIVRHTVYLLVTPRVVEEARKHFNCPVLEGME
LENQGGMGTELNHWEKRLLENEAMTGSHTQNRVLSRITLALMEDTGWYKANYSMAEKLDW
GRGLGCEFVRKSCKFWIDQHRQRRQVPSPYCDTLRSNPLQLTCRQDQRAVAVCNLQRFPN
PLPPEYQYFDELTGIPAEDLPYYGGSVEIADYCPFSQEFSWHLSGEYQRSSDCRILENQP
ELFKNYGAEQYGPHSVCLLQKSAFIMEQCERKLSYPDWGSGCYQVSCSPQGLKVWVQDTS
YLCSRAGQVLPVRIQMNGWIHNGNLLCPSCWDFCEQCPP

Peptidase_M8

Peptidase_M8
PFAM accession number:PF01457
Interpro abstract (IPR001577):

This group of metallopeptidases belong to the MEROPS peptidase family M8 (leishmanolysin family, clan MA(M)). The protein fold of the peptidase domain for members of this family resembles that of thermolysin, the type example for clan MA.

Leishmanolysin (EC 3.4.24.36) is an enzyme found in the eukaryotes including Leishmania and related parasitic protozoa [(PUBMED:7674922)]. The endopeptidase is the most abundant protein on the cell surface during the promastigote stage of the parasite, and is attached to the membrane by a glycosylphosphatidylinositol anchor [(PUBMED:7674922)]. In the amastigote form, the parasite lives in lysosomes of host macrophages, producing a form of the protease that has an acidic pH optimum [(PUBMED:7674922)]. This differs from most other metalloproteases and may be an adaptation to the environment in which the organism survives [(PUBMED:7674922)].

GO process:cell adhesion (GO:0007155), proteolysis (GO:0006508)
GO component:membrane (GO:0016020)
GO function:metalloendopeptidase activity (GO:0004222)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Peptidase_M8