Concanavalin A-like lectin/glucanase, subgroup <p> Lectins and glucanases exhibit the common property of reversibly binding to specific complex carbohydrates. The lectins/glucanases are a diverse group of proteins found in a wide range of species from prokaryotes to humans. The different family members all contain a concanavalin A-like domain, which consists of a sandwich of 12-14 beta strands in two sheets with a complex topology. Members of this family are diverse, and include the lectins: legume lectins, cereal lectins, viral lectins, and animal lectins. Plant lectins function in the storage and transport of carbohydrates in seeds, the binding of nitrogen-fixing bacteria to root hairs, the inhibition of fungal growth or insect feeding, and in hormonally regulated plant growth [<cite idref="PUB00010683"/>]. Protein members include concanavalin A (Con A), favin, isolectin I, lectin IV, soybean agglutinin and lentil lectin. Animal lectins include the galectins, which are S-type lactose-binding and IgE-binding proteins such as S-lectin, CLC protein, galectin1, galectin2, galectin3 CRD, and Congerin I [<cite idref="PUB00010684"/>]. </p><p> Other members with a Con A-like domain include the glucanases. Bacterial and fungal beta-glucanases, such as Bacillus 1-3,1-4-beta-glucanse, carry out the acid catalysis of beta-glucans found in microorganisms and plants [<cite idref="PUB00010685"/>]. Similarly, kappa-Carrageenase degrades kappa-carrageenans from marine red algae cell walls [<cite idref="PUB00010686"/>]. </p><p>This entry differs from (<db_xref db="INTERPRO" dbkey="IPR008985"/>) by omitting the xylanases and glycosyl hydrolases.</p>