| Type: | Repeat | Name: | Cellulosome enzyme, dockerin type I, calcium-binding motif |
| Description: | Gram-positive, thermophilic anaerobes such as Clostridium thermocellumor Clostridium cellulolyticumsecretes a highly active and thermostable cellulase complex (cellulosome) responsible for the degradation of crystalline cellulose [, ]. The cellulosome contains at least 30 polypeptides, the majority of the enzymes are endoglucanases (), but there are also some xylanases (), beta-glucosidases () and endo-beta-1,3-1,4-glucanases ().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 ). The cohesin-dockerin interaction is the crucial interaction for complex formation in the cellulosome []. 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. | Short Name: | Cellulos_enz_dockerin_1_Ca-bd |
