{PDOC51763} {PS51763; CBM10} {BEGIN} ******************************************************* * CBM10 (carbohydrate binding type-10) domain profile * ******************************************************* 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 [E1]. 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 [1,2,3,4]. The CBM10 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 (see ) [2,4]. Some proteins known to contain a CBM10 domain are listed below: - Cellvibrio japonicus endo-1,4-beta-xylanase A (xynA), endohydrolyses (1->4)-beta-D-xylosidic linkages in xylans. - Cellvibrio japonicus bifunctional xylanase/xylan deacetylase (xyn11A), endo-acting xylanase which specifically cleaves internal linkages on the xylan backbone, releasing xylooligosaccharides. - Cellvibrio japonicus endoglucanase A (celA), endohydrolyses (1->4)-beta-D- glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans. - Cellvibrio japonicus endoglucanase B (celB), catalyzes the endohydrolysis of 1,4-beta-glucosidic linkages in cellulose, lichenin and cereal beta-D- glucans. - Cellvibrio japonicus endoglucanase C (celC), endohydrolyses (1->4)-beta-D- glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans. - Neocallimastix patriciarum (Rumen fungus) endoglucanase B (CELB), endohydrolyse (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans. - Neocallimastix patriciarum (Rumen fungus) bifunctional endo-1,4-beta- xylanase A (XYNA), hydrolyzes xylans into xylobiose and xylose. - Piromyces sp. endo-1,4-beta-xylanase A (XYNA), hydrolyzes 1,4-beta linked polysaccharide backbones of xylans, one of the major hemicellulose components in hardwoods and softwoods. - Piromyces sp. mannan endo-1,4-beta-mannosidase A (MANA), hydrolyzes 1,4- beta linked polysaccharide backbones of mannans, one of the major hemicellulose components in hardwoods and softwoods. The profile we developed covers the entire CBM10 domain. -Sequences known to belong to this class detected by the profile: ALL. -Other sequence(s) detected in Swiss-Prot: NONE. -Last update: June 2015 / First entry. [ 1] Ponyi T., Szabo L., Nagy T., Orosz L., Simpson P.J., Williamson M.P., Gilbert H.J. "Trp22, Trp24, and Tyr8 play a pivotal role in the binding of the family 10 cellulose-binding module from Pseudomonas xylanase A to insoluble ligands." Biochemistry 39:985-991(2000). PubMed=10653642 [ 2] Raghothama S., Simpson P.J., Szabo L., Nagy T., Gilbert H.J., Williamson M.P. "Solution structure of the CBM10 cellulose binding module from Pseudomonas xylanase A." Biochemistry 39:978-984(2000). PubMed=10653641 [ 3] Fanutti C., Ponyi T., Black G.W., Hazlewood G.P., Gilbert H.J. "The conserved noncatalytic 40-residue sequence in cellulases and hemicellulases from anaerobic fungi functions as a protein docking domain." J. Biol. Chem. 270:29314-29322(1995). PubMed=7493964 [ 4] Raghothama S., Eberhardt R.Y., Simpson P., Wigelsworth D., White P., Hazlewood G.P., Nagy T., Gilbert H.J., Williamson M.P. "Characterization of a cellulosome dockerin domain from the anaerobic fungus Piromyces equi." Nat. Struct. Biol. 8:775-778(2001). PubMed=11524680; DOI=10.1038/nsb0901-775 [E1] http://www.cazy.org/CBM10.html -------------------------------------------------------------------------------- PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html -------------------------------------------------------------------------------- {END}