The domain within your query sequence starts at position 251 and ends at position 510; the E-value for the Glyco_hydro_38 domain shown below is 2.8e-86.



PFAM accession number:PF18438
Interpro abstract (IPR041509):

The enzymatic hydrolysis of alpha-mannosides is catalyzed by glycoside hydrolases (GH), termed alpha-mannosidases. Streptococcal (Sp) GH38 alpha-mannosidase active on N-glycans and possibly O-glycans. SpGH38 structure can be considered as five domains: an N-terminal alpha/beta-domain, a three-helix bundle and three predominantly beta-sheet domains. This is the first of the three beta-sheet domains found in GH38, termed Beta-1. Structural analysis indicate that the beta-1 domain bows outward from the protein core, is involved in dimer interactions whilst also forming a lid 'above' and somewhat into the active centre of its dimer [ (PUBMED:20140249) ].

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