The domain within your query sequence starts at position 1 and ends at position 57; the E-value for the Gal-bind_lectin domain shown below is 4e-16.



PFAM accession number:PF00337
Interpro abstract (IPR001079):

Galectins (also known as galaptins or S-lectin) are a family of proteins defined by having at least one characteristic carbohydrate recognition domain (CRD) with an affinity for beta-galactosides and sharing certain sequence elements. Members of the galectins family are found in mammals, birds, amphibians, fish, nematodes, sponges, and some fungi. Galectins are known to carry out intra- and extracellular functions through glycoconjugate-mediated recogntion. From the cytosol they may be secreted by non-classical pathways, but they may also be targeted to the nucleus or specific sub-cytosolic sites. Within the same peptide chain some galectins have a CRD with only a few additional amino acids, whereas others have two CRDs joined by a link peptide, and one (galectin-3) has one CRD joined to a different type of domain [ (PUBMED:16051274) (PUBMED:14758066) ].

The galectin carbohydrate recognition domain (CRD) is a beta-sandwich of about 135 amino acid. The two sheets are slightly bent with 6 strands forming the concave side and 5 strands forming the convex side. The concave side forms a groove in which carbohydrate is bound, and which is long enough to hold about a linear tetrasaccharide [ (PUBMED:8262940) (PUBMED:8747464) ].

GO function:carbohydrate binding (GO:0030246)

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