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- *****************************************
- * Cellulose-binding domain, fungal type *
- *****************************************
-
- The microbial degradation of cellulose and xylans requires several types of
- enzymes such as endoglucanases (EC 3.2.1.4), cellobiohydrolases (EC 3.2.1.91)
- (exoglucanases), or xylanases (EC 3.2.1.8) [1].
-
- Structurally, cellulases and xylanases generally consist of a catalytic
- domain joined to a cellulose-binding domain (CBD) by a short linker sequence
- rich in proline and/or hydroxy-amino acids.
-
- The CBD of a number of fungal cellulases has been shown to consist of 36 amino
- acid residues. Enzymes known to contain such a domain are:
-
- - Endoglucanase I (gene Egl-I) from Trichoderma reesei.
- - Endoglucanase II (gene Egl-II) from Trichoderma reesei.
- - Exocellobiohydrolase I (gene Cbh-I) from Humicola grisea, Phanerochaete
- chrysosporium, Trichoderma reesei, and Trichoderma viride.
- - Exocellobiohydrolase II (gene Cbh-II) from Trichoderma reesei.
-
- The CBD domain is found either at the N-terminal (Cbh-II or Egl-II) or at the
- C-terminal extremity (Cbh-I and Egl-I) of these enzymes. As it is shown in the
- following schematic representation, there are four conserved cysteines in this
- type of CBD domain, all involved in disulfide bonds.
-
- +----------------+
- | +-----|---------+
- | | | |
- xxxxxxxCxxxxxxxxxxCxxxxxCxxxxxxxxxCx
- ****************************
-
- 'C': conserved cysteine involved in a disulfide bond.
- '*': position of the pattern.
-
- -Consensus pattern: C-G-G-x(4)-G-x(3)-C-x(5)-C-x(3)-N-x-[YW]-Y-x-Q-C
- [The four C's are involved in disulfide bonds]
- -Sequences known to belong to this class detected by the pattern: ALL.
- -Other sequence(s) detected in SWISS-PROT: NONE.
-
- -Expert(s) to contact by email: Henrissat B.
- bernie@cermav.grenet.fr
-
- -Last update: December 1992 / Text revised.
-
- [ 1] Gilkes N.R., Henrissat B., Kilburn D.G., Miller R.C. Jr., Warren R.A.J.
- Microbiol. Rev. 55:303-315(1991).
-