Schultz et al. (1998) Proc. Natl. Acad. Sci. USA 95, 5857-5864
Letunic et al. (2012) Nucleic Acids Res , doi:10.1093/nar/gkr931

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CASH Domain present in carbohydrate binding proteins and sugar hydrolses

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:	View or CHROMA formatCLUSTALW formatMSF formatFASTA formatPIR format

There are 1050 CASH domains in 549 proteins in SMART's nrdb database.

Click on the following links for more information.

• Evolution (species in which this domain is found)

• Click on to expand nodes. To display all proteins with a CASH domain in a specific node, click on it.

  This tree shows only several representative species. The complete taxonomic breakdown of all proteins with CASH domain is also avaliable.

  Useful shortcuts: Expand all nodes or Collapse tree
  Go to specific node: Anopheles gambiae, Arabidopsis thaliana, Caenorhabditis elegans, Drosophila melanogaster, Homo sapiens, Mus musculus, Rattus norvegicus, Takifugu rubripes

• Literature (relevant references for this domain)

• Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.

  • Ciccarelli FD, Copley RR, Doerks T, Russell RB, Bork P
  • CASH--a beta-helix domain widespread among carbohydrate-binding proteins.
  • Trends Biochem Sci. 2002; 27: 59-62
  • Display 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.

• Structure (3D structures containing this domain)

• 3D Structures of CASH domains in PDB

  PDB code	Main view	Title
  1gq8		Pectin methylesterase from carrot
  2pyg		Azotobacter vinelandii mannuronan c-5 epimerase alge4 a- module
  2pyh		Azotobacter vinelandii mannuronan c-5 epimerase alge4 a- module complexed with mannuronan trisaccharide

• Links (links to other resources describing this domain)

• INTERPRO	IPR006633

Send comments to Ivica Letunic