Dockerin type I repeat (IPR002105)

Short name: Dockerin_1_rpt


Gram-positive, thermophilic anaerobes such as Clostridium thermocellum or Clostridium cellulolyticum secretes a highly active and thermostable cellulase complex (cellulosome) responsible for the degradation of crystalline cellulose [PMID: 2252383, PMID: 1478480]. The cellulosome contains at least 30 polypeptides, the majority of the enzymes are endoglucanases (EC:, but there are also some xylanases (EC:, beta-glucosidases (EC: and endo-beta-1,3-1,4-glucanases (EC:

Complete sequence data for many of these enzymes has been obtained. A majority of these proteins contain a highly conserved type I dockerin domain of about 65 to 70 residues, which is generally (but not always) located in the C terminus. The dockerin domain is the binding partner of the cohesin domain (see IPR002102). The cohesin-dockerin interaction is the crucial interaction for complex formation in the cellulosome [PMID: 10390637]. The dockerin domain contains a tandem repeat of two calcium-binding loop-helix motifs (distinct from EF-hand Ca-binding motifs). These motifs are about 24 amino acids in length. This entry represents these repeated Ca-binding motifs.

GO terms

Biological Process

GO:0000272 polysaccharide catabolic process

Molecular Function

GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds

Cellular Component

No terms assigned in this category.

Contributing signatures

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