Protein Domain : CBM6/CBM35/CBM36-like 2 IPR033803

Type  Domain
Description  Carbohydrate binding module family 6 (CBM6, family 6 CBM), also known as cellulose binding domain family VI (CBD VI), and related CBMs (CBM35 and CBM36). These are non-catalytic carbohydrate binding domains found in a range of enzymes that display activities against a diverse range of carbohydrate targets, including mannan, xylan, beta-glucans, cellulose, agarose, and arabinans [ ]. These domains facilitate the strong binding of the appended catalytic modules to their dedicated, insoluble substrates. Many of these CBMs are associated with glycoside hydrolase (GH) domains. CBM6 is an unusual CBM as it represents a chimera of two distinct binding sites with different modes of binding: binding site I within the loop regions and binding site II on the concave face of the β-sandwich fold [, , ]. CBM36s are calcium-dependent xylan binding domains []. CBM35s display conserved specificity through extensive sequence similarity, but divergent function through their appended catalytic modules [, , ].This domain is related to carbohydrate binding modules CBM6/CBM35/CBM36 and is found in xanthan lyase, which cleaves the linkage between the terminal mannosyl and glucuronyl residues of the side chain of xanthan to liberate pyruvylated mannose [ ], and in golvesin, which is a membrane-bound protein from endosomes, vacuole and golgi found in Dictyostelium [].
Short Name  CBM6/CBM35/CBM36-like_2

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