The domain within your query sequence starts at position 219 and ends at position 464; the E-value for the Glyco_hydro_65m domain shown below is 3.8e-65.

RGSLYYLFSELPQPGTQGFISHGLSPGGLSNGSKEECYWGHIFWDQDIWMFPNILMFHPE
AARAILEYRVRTLGGALKNGQNLGYQGAKFAWESASTGLEVCPEDIYGTQEIHINGAVAL
AFQLYYYYTQDSKLFQEDGGWDVVSSVAEFWCSRVEWSSQDKMYHLKGVMPPDEYHSGVN
NSVYTNVLVQNSLHFAAALAKDLGLPIRKQWLEVADRIKIPFDSEQNFHPEFDGYEREHV
CCGLDG

Glyco_hydro_65m

Glyco_hydro_65m
PFAM accession number:PF03632
Interpro abstract (IPR005195):

O-Glycosyl hydrolases (EC 3.2.1.) are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families [(PUBMED:7624375), (PUBMED:8535779)]. This classification is available on the CAZy (CArbohydrate-Active EnZymes) web site.

The family of glycosyl hydrolases which contains this domain includes vacuolar acid trehalase and maltose phosphorylase. Maltose phosphorylase (MP) is a dimeric enzyme that catalyzes the conversion of maltose and inorganic phosphate into beta-D-glucose-1-phosphate and glucose. The central domain is the catalytic domain, which binds a phosphate ion that is proximal the the highly conserved Glu. The arrangement of the phosphate and the glutamate is thought to cause nucelophilic attack on the anomeric carbon atom [(PUBMED:11587643)]. The catalytic domain also forms the majority of the dimerisation interface.

GO process:carbohydrate metabolic process (GO:0005975)
GO function:catalytic activity (GO:0003824)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Glyco_hydro_65m