The domain within your query sequence starts at position 28 and ends at position 351; the E-value for the Glyco_hydro_38 domain shown below is 4e-100.
RAFVVPHSHMDVGWVFTVQESMRAYAANVYTTVVAELVRGGQRRFIAVEQEFFRLWWDGV ASEQQKQQVRQLLHEGRLEFVLGGQVMHDEAVTHLDDQILQLTEGHGFLYETFGIRPQFS WHVDPFGASATTPTLFALAGFNAHLISRIDYDLKDAMQEAQMLQFVWHGSPSLSGQQEIF THVMDHYSYCTPSHIPFSNRSGFYWNGVAVFPEPPPDGVYPNMSEPVTGANIHLYAEALV ANVKQRAAWFRTPHVLWPWGCDKQFFNASVQFDNMDPLLDYINQRTAQFGISVQYATLND YFQALHATNMTWGIRDHQDFLPYS
Glyco_hydro_38 |
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PFAM accession number: | PF18438 |
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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