The domain within your query sequence starts at position 22 and ends at position 542; the E-value for the Glyco_hydro_39 domain shown below is 1.4e-223.

LALAESPYLVRVDAARPLRPLLPFWRSTGFCPPLPHDQADQYDLSWDQQLNLAYIGAVPH
SGIEQVRIHWLLDLITARKSPGQGLMYNFTHLDAFLDLLMENQLLPGFELMGSPSGYFTD
FDDKQQVFEWKDLVSLLARRYIGRYGLTHVSKWNFETWNEPDHHDFDNVSMTTQGFLNYY
DACSEGLRIASPTLKLGGPGDSFHPLPRSPMCWSLLGHCANGTNFFTGEVGVRLDYISLH
KKGAGSSIAILEQEMAVVEQVQQLFPEFKDTPIYNDEADPLVGWSLPQPWRADVTYAALV
VKVIAQHQNLLFANSSSSMRYVLLSNDNAFLSYHPYPFSQRTLTARFQVNNTHPPHVQLL
RKPVLTVMGLMALLDGEQLWAEVSKAGAVLDSNHTVGVLASTHHPEGSAAAWSTTVLIYT
SDDTHAHPNHSIPVTLRLRGVPPGLDLVYIVLYLDNQLSSPYSAWQHMGQPVFPSAEQFR
RMRMVEDPVAEAPRPFPARGRLTLHRKLPVPSLLLVHVCTR

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) web site.

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).

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