| Type: | Domain | Name: | Fungal dockerin domain |
| Description: | In anaerobic microorganisms, the degradation of plant cell walls in order to recycle the photosynthetically fixed carbon is carried out by a multifunctional complex termed the cellulosome. This consists of a number of independent enzyme components, each of which contains a conserved dockerin domain, which functions to bind the enzyme to a cohesin domain within the protein scaffoldin protein []. The sequences of dockerin domains from bacterial and fungal enzymes are completely different. Fungal enzymes contain one, two or three copies of the dockerin domain in tandem within the catalytic polypeptide, while in bacteria such as Clostridium thermocellum, the cellulosome catalytic components contain a single dockerin domain. The tandem dockerin domains, seen in the majority of anaerobic fungal plant cell wall degrading enzymes, could present multiple simultaneous binding sites and, therefore, permit tailoring of binding to catalytic demands. Furthermore, fungal dockerin domains have broad interspecies specificity, while bacterial dockerin domains appear species-specific. The structure of the N-terminal dockerin domain of Cel45A from the anaerobic fungus Piromyces equi displays an alpha/beta fold that is disulphide-rich []. This entry represents fungal dockerin domains. | Short Name: | Dockerin_dom_fun |
