title: CASH--a beta-helix domain widespread among carbohydrate-binding proteins.
abstract: In this article, we describe a novel, widespread domain (CASH) that is shared by many carbohydrate-binding proteins and sugar hydrolases. This domain occurs in more than 1000 proteins distributed among all three kingdoms of life. The CASH domain is characterized 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.
authors.affiliation: Max-Delbrueck-Centrum, PO Box 740238, D-13092 Berlin, Germany. ciccarel@embl-heidelberg.de
authors.forename: Francesca D
authors.initials: FD
authors.lastname: Ciccarelli
authors.forename: Richard R
authors.initials: RR
authors.lastname: Copley
authors.forename: Tobias
authors.initials: T
authors.lastname: Doerks
authors.forename: Robert B
authors.initials: RB
authors.lastname: Russell
authors.forename: Peer
authors.initials: P
authors.lastname: Bork
mesh_terms: D020816:Amino Acid Motifs; D000818:Animals; D001665:Binding Sites; D050260:Carbohydrate Metabolism; D002352:Carrier Proteins / Q000378:metabolism; D006801:Humans; D011133:Polysaccharide-Lyases / Q000737:chemistry*; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary
chemical_list: D002352:Carrier Proteins; D011133:Polysaccharide-Lyases