CBM10/dockerin domain (IPR002883)

Short name: CBM10/Dockerin_dom

Overlapping homologous superfamilies

Domain relationships


Plant cell wall hydrolases generally have a modular structure consisting of a catalytic domain linked to one or more noncatalytic carbohydrate-binding modules (CBMs). The majority of these CBMs interact with cellulose and are thus referred to as cellulose-binding domains or CBDs. CBM10s are small molecules, comprising only ca. 45 residues, that bind to insoluble forms of cellulose. CBM10s contain three tryptophan and two tyrosine residues which are completely conserved. The CBM10 domain is found in xylanases, mannanases and cellulases from aerobic bacteria and anaerobic fungi [PMID: 10653642, PMID: 10653641, PMID: 7493964, PMID: 11524680].

In aerobic bacteria, this domain binds cellulose (or other carbohydrates); but in anaerobic fungi this domain, also known as the dockerin domain, may be responsible for the assembly of a multiprotein cellulase/hemicellulase complex, similar to the cellulosome found in certain anaerobic bacteria [PMID: 7493964, PMID: 7492333].

This domain consists of two antiparallel beta-sheets, one with two strands and one with three, with a short alpha-helix across one face of the three-stranded sheet [PMID: 10653641, PMID: 11524680].

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE profiles