The domain within your query sequence starts at position 166 and ends at position 496; the E-value for the Glyco_hydro_38 domain shown below is 2.3e-111.

QVFVVPHSHNDPGWLKTFNDYFRDKTQYIFNNMVLKLKEDSSRKFMWSEISYLAKWWDII
DIPKKEAVKSLLQNGQLEIVTGGWVMPDEATPHYFALIDQLIEGHQWLEKNLGVKPRSGW
AIDPFGHSPTMAYLLKRAGFSHMLIQRVHYAIKKHFSLHKTLEFFWRQNWDLGSATDILC
HMMPFYSYDIPHTCGPDPKICCQFDFKRLPGGRYGCPWGVPPEAISPGNVQSRAQMLLDQ
YRKKSKLFRTKVLLAPLGDDFRFSEYTEWDLQCRNYEQLFSYMNSQPHLKVKIQFGTLSD
YFDALEKAVAAEKKSSQSVFPALSGDFFTYA

Glyco_hydro_38

Glyco_hydro_38
PFAM accession number:PF01074
Interpro abstract (IPR000602):

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.

Glycoside hydrolase family 38 comprises enzymes with only one known activity; alpha-mannosidase (EC 3.2.1.24) (EC 3.2.1.114).

Lysosomal alpha-mannosidase is necessary for the catabolism of N-linked carbohydrates released during glycoprotein turnover. The enzyme catalyses the hydrolysis of terminal, non-reducing alpha-D-mannose residues in alpha-D-mannosides, and can cleave all known types of alpha-mannosidic linkages. Defects in the gene cause lysosomal alpha-mannosidosis (AM), a lysosomal storage disease characterised by the accumulation of unbranched oligo-saccharide chains.

This entry represents the N-terminal domain of the glycoside hydrolase 38 family protein.

GO process:mannose metabolic process (GO:0006013)
GO function:alpha-mannosidase activity (GO:0004559)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Glyco_hydro_38