uncharacterized members of the carbohydrate binding module 6 (CBM6) and CBM35_like superfamily. 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 beta-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.

Right handed beta helix region. This region contains a parallel beta helix region that shares some similarity with Pectate lyases.

Right handed beta helix region. This region contains a parallel beta helix region that shares some similarity with Pectate lyases.

T1SS-143 repeat domain. This model represents a domain of about 143 amino acids that may occur singly or in up to 23 tandem repeats in very large proteins in the genus Vibrio, and in related species such as Legionella pneumophila, Photobacterium profundum, Rhodopseudomonas palustris, Shewanella pealeana, and Aeromonas hydrophila. Proteins with these domains represent a subset of a broader set of proteins with a particular signal for type 1 secretion, consisting of several glycine-rich repeats modeled by pfam00353, followed by a C-terminal domain modeled by TIGR03661. Proteins with this domain tend to share several properties with the RtxA (Repeats in Toxin) protein of Vibrio cholerae, including a large size often containing tandemly repeated domains and a C-terminal signal for type 1 secretion. [Cellular processes, Pathogenesis]

Right handed beta helix region. This region contains a parallel beta helix region that shares some similarity with Pectate lyases.

ChainA, Alpha-1,3-glucanase [Niallia circulans],5ZRU_C Chain C, Alpha-1,3-glucanase [Niallia circulans]

Catalyticdomain of GH87 alpha-1,3-glucanase from Paenibacillus glycanilyticus FH11 [Paenibacillus glycanilyticus],6K0N_A Catalytic domain of GH87 alpha-1,3-glucanase in complex with nigerose [Paenibacillus glycanilyticus]

Catalyticdomain of GH87 alpha-1,3-glucanase D1045A in complex with nigerose [Paenibacillus glycanilyticus]

Catalyticdomain of GH87 alpha-1,3-glucanase D1069A in complex with nigerose [Paenibacillus glycanilyticus],6K0V_A Catalytic domain of GH87 alpha-1,3-glucanase D1069A in complex with tetrasaccharides [Paenibacillus glycanilyticus],6K0V_B Catalytic domain of GH87 alpha-1,3-glucanase D1069A in complex with tetrasaccharides [Paenibacillus glycanilyticus],6K0V_C Catalytic domain of GH87 alpha-1,3-glucanase D1069A in complex with tetrasaccharides [Paenibacillus glycanilyticus],6K0V_D Catalytic domain of GH87 alpha-1,3-glucanase D1069A in complex with tetrasaccharides [Paenibacillus glycanilyticus]

Catalyticdomain of GH87 alpha-1,3-glucanase D1068A in complex with nigerose [Paenibacillus glycanilyticus],6K0U_A Catalytic domain of GH87 alpha-1,3-glucanase D1068A in complex with tetrasaccharides [Paenibacillus glycanilyticus]