The domain within your query sequence starts at position 325 and ends at position 627; the E-value for the Glyco_hydro_2_C domain shown below is 9e-117.

VAVTKSKFLINGKPFYFQGVNKHEDSDIRGKGFDWPLLVKDFNLLRWLGANSFRTSHYPY
SEEVLQLCDRYGIVVIDECPGVGIVLPQSFGNESLRHHLEVMEELVRRDKNHPAVVMWSV
ANEPSSALKPAAYYFKTLITHTKALDLTRPVTFVSNAKYDADLGAPYVDVICVNSYFSWY
HDYGHLEVIQPQLNSQFENWYKTHQKPIIQSEYGADAIPGIHEDPPRMFSEEYQKAVLEN
YHSVLDQKRKEYVVGELIWNFADFMTNQSPLRVIGNKKGIFTRQRQPKTSAFILRERYWR
IAN

Glyco_hydro_2_C

• PFAM accession number: PF02836
• Interpro abstract (IPR006103):

  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 2 comprises enzymes with several known activities; beta-galactosidase ( EC 3.2.1.23 ); beta-mannosidase ( EC 3.2.1.25 ); beta-glucuronidase ( EC 3.2.1.31 ).

  These enzymes contain a conserved glutamic acid residue which has been shown [ (PUBMED:1350782) ], in Escherichia coli lacZ ( P00722 ), to be the general acid/base catalyst in the active site of the enzyme.

  Beta-galactosidase from E. coli has a TIM-barrel-like core surrounded by four other largely beta domains [ (PUBMED:8008071) ].

• 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_2_C