The domain within your query sequence starts at position 52 and ends at position 277; the E-value for the Lectin_leg-like domain shown below is 2.2e-95.

RRFEYKYSFKGPHLVQSDGTVPFWAHAGNAIPSADQIRIAPSLKSQRGSVWTKAKAAFEN
WEVEVTFRVTGRGRIGADGLAIWYTENQGLDGPVFGSADTWNGVGIFFDSFDNDGKKNNP
AIVVIGNNGQINYDHQNDGATQALASCQRDFRNKPYPVRAKITYYQKTLTVMINNGFTPD
KNDYEFCAKVENMVIPTQGHFGISAATGGLADDHDVLSFLTFQLTE

Lectin_leg-like

Lectin_leg-like
PFAM accession number:PF03388
Interpro abstract (IPR005052):

Lectins are structurally diverse proteins that bind to specific carbohydrates. This family includes the VIP36 and ERGIC-53 lectins. These two proteins were the first members of the family of animal lectins similar to the leguminous plant lectins [(PUBMED:8205612)]. The alignment for this family is towards the N terminus, where the similarity of VIP36 and ERGIC-53 is greatest. Although they have been identified as a family of animal lectins, this alignment also includes yeast sequences[(PUBMED:8205612)].

ERGIC-53 is a 53kDa protein, localised to the intermediate region between the endoplasmic reticulum and the Golgi apparatus (ER-Golgi-Intermediate Compartment, ERGIC). It was identified as a calcium-dependent, mannose-specific lectin [(PUBMED:8868475)]. Its dysfunction has been associated with combined factors V and VIII deficiency, suggesting an important and substrate-specific role for ERGIC-53 in the glycoprotein-secreting pathway [(PUBMED:8868475),(PUBMED:10090935)].

The L-type lectin-like domain has an overall globular shape composed of a beta-sandwich of two major twisted antiparallel beta-sheets. The beta-sandwich comprises a major concave beta-sheet and a minor convex beta-sheet, in a variation of the jelly roll fold [(PUBMED:11850423), (PUBMED:14643651), (PUBMED:16439369), (PUBMED:17652092)].

GO component:membrane (GO:0016020)

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