{PDOC51159} {PS51159; CBM21} {BEGIN} ******************************************************* * CBM21 (carbohydrate binding type-21) domain profile * ******************************************************* The carbohydrate binding type-21 or CBM21 domain is a 90-130 amino acid carbohydrate binding domain. The domain is named after proteins classified in carbohydrate-binding module (CBM) family 21 and is sometimes called starch-binding domain (SBD) [E1,1]. The CBM21 domain occurs in several eukaryotic proteins implicated in glycogen metabolism. A glucoamylase active site region (see ) [E2] or alpha amylase catalytic domain [E3] can occur C-terminal to the CBM21 domain. The CBM21 domain of Rhizopus oryzae glucoamylase can bind to raw starch. Most conserved residues are located in a region with a length of 35 in the N-terminal part [2] and in a 15-25 residue motif II at the C-terminus of the domain [2-4]. Some proteins known to contain a CBM21 domain: - Mammalian protein phosphatase 1 (PP1) regulatory subunit 3A, which seems to target PP1 to glycogen. - Mammalian protein phosphatase 1 binding protein PTG, which binds the 3 key enzymes for the regulation of glycogen metabolism: phosphorylase kinase, phosphorylase A and glycogen synthase. - Yeast protein phosphatase 1 regulatory subunits GAC1 and PIG1, which are regulators of glycogen synthase. - Yeast GLC7-interacting protein 2 (GIP2), which interacts with the catalytic subunit (GLC7) of PP1. - Yeast protein 2 interacting with GSY2 (PIG2), which interacts with glycogen synthase 2 (GSY2), a nutritionally regulated form. - Rhizopus oryzae glucoamylase, which binds and hydrolyzes granular starch. R. oryzae is a fungus from e.g. decaying vegetables and it causes mucormycosis. The profile we developed covers the entire CBM21 domain. -Sequences known to belong to this class detected by the profile: ALL. -Other sequence(s) detected in Swiss-Prot: NONE. -Last update: November 2005 / First entry. [ 1] Rodriguez-Sanoja R., Oviedo N., Sanchez S. "Microbial starch-binding domain." Curr. Opin. Microbiol. 8:260-267(2005). PubMed=15939348; DOI=10.1016/j.mib.2005.04.013 [ 2] Cheng C., Huang D., Roach P.J. "Yeast PIG genes: PIG1 encodes a putative type 1 phosphatase subunit that interacts with the yeast glycogen synthase Gsy2p." Yeast 13:1-8(1997). PubMed=9046081; DOI=10.1002/(SICI)1097-0061(199701)13:1<1::AID-YEA49>3.0.CO;2-F [ 3] Printen J.A., Brady M.J., Saltiel A.R. "PTG, a protein phosphatase 1-binding protein with a role in glycogen metabolism." Science 275:1475-1478(1997). PubMed=9045612 [ 4] Machovic M., Svensson B., Ann Macgregor E., Janecek S. "A new clan of CBM families based on bioinformatics of starch-binding domains from families CBM20 and CBM21." FEBS J. 272:5497-5513(2005). PubMed=16262690; DOI=10.1111/j.1742-4658.2005.04942.x [E1] http://www.cazy.org/CBM21.html [E2] http://www.cazy.org/GH13.html [E3] http://www.cazy.org/GH15.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}