CASH

Domain present in carbohydrate binding proteins and sugar hydrolses
CASH
SMART accession number:SM00722
Description: -
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) ].

Family alignment:
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There are 11101 CASH domains in 5695 proteins in SMART's nrdb database.

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