CASHDomain present in carbohydrate binding proteins and sugar hydrolses
|SMART accession number:||SM00722|
|Interpro abstract (IPR006633):|
The CASH domain is shared by many carbohydrate-binding proteins and sugar hydrolases. The CASH domain is characterised by internal repetitions of glycines and hydrophobic residues that correspond to the repetitive units of a predicted or observed right-handed beta-helix structure of the pectate lyase superfamily. The basic structural unit of this family consists of three beta-strands that form a single turn of the beta-helix. Each turn contains ~20 amino acids, and is normally repeated between 7 and 11 times to form the elongated helix structure. The repeats show a low degree of sequence identity when compared with each other. The region of homology with the CASH domain corresponds to the core region of the beta-helix, covering from the second to the sixth repeat [(PUBMED:11852237)].
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