The domain within your query sequence starts at position 48 and ends at position 495; the E-value for the Glyco_hydro_39 domain shown below is 2.4e-193.

STGFWKSPGQGLMYNFTHLDAFLDLLMENQLLPGFELMGSPSGYFTDFDDKQQVFEWKDL
VSLLARRYIGRYGLTHVSKWNFETWNEPDHHDFDNVSMTTQGFLNYYDACSEGLRIASPT
LKLGGPGDSFHPLPRSPMCWSLLGHCANGTNFFTGEVGVRLDYISLHKKGAGSSIAILEQ
EMAVVEQVQQLFPEFKDTPIYNDEADPLVGWSLPQPWRADVTYAALVVKVIAQHQNLLFA
NSSSSMRYVLLSNDNAFLSYHPYPFSQRTLTARFQVNNTHPPHVQLLRKPVLTVMGLMAL
LDGEQLWAEVSKAGAVLDSNHTVGVLASTHHPEGSAAAWSTTVLIYTSDDTHAHPNHSIP
VTLRLRGVPPGLDLVYIVLYLDNQLSSPYSAWQHMGQPVFPSAEQFRRMRMVEDPVAEAP
RPFPARGRLTLHRKLPVPSLLLVHVCTR

Glyco_hydro_39

Glyco_hydro_39
PFAM accession number:PF01229
Interpro abstract (IPR000514):

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) website.

Glycoside hydrolase family 39 comprises enzymes with several known activities; alpha-L-iduronidase ( EC 3.2.1.76 ); beta-xylosidase ( EC 3.2.1.37 ); and alpha-1,4-L-rhamnosidase [ (PUBMED:31285597) ].

The most highly conserved regions in these enzymes are located in their N-terminal sections. These contain a glutamic acid residue which, on the basis of similarities with other families of glycosyl hydrolases [ (PUBMED:7624375) ], probably acts as the proton donor in their catalytic mechanism.

GO process:carbohydrate metabolic process (GO:0005975)
GO function:hydrolase activity, hydrolyzing O-glycosyl compounds (GO:0004553)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Glyco_hydro_39