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	PROSITE documentation PDOC51159

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 <PDOC00646>) [E2] or α 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 [2,3,4].

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.

Last update:

November 2005 / First entry.

PROSITE method (with tools and information) covered by this documentation:

CBM21, PS51159; CBM21 (carbohydrate binding type-21) domain profile  (MATRIX)

• Sequences in UniProtKB/Swiss-Prot known to belong to this class: 35
  • detected by PS51159: 35 (true positives)
  • undetected by PS51159: 0 (false negative or 'partial')
• Other sequence(s) in UniProtKB/Swiss-Prot detected by PS51159:
  NONE.
• Domain architecture view of Swiss-Prot proteins matching PS51159
  
• Retrieve an alignment of UniProtKB/Swiss-Prot true positive hits:
  Clustal format, color, condensed view  /  Clustal format, color  /  Clustal format, plain text  /  Fasta format
• Retrieve the sequence logo from the alignment
• Taxonomic distribution of all UniProtKB (Swiss-Prot + TrEMBL) entries matching PS51159
• Retrieve a list of all UniProtKB (Swiss-Prot + TrEMBL) entries matching PS51159
• Scan UniProtKB (Swiss-Prot and/or TrEMBL) entries against PS51159
• View ligand binding statistics of PS51159
• Matching PDB structures: 2DJM 2EEF 2M83 [ALL]

1	Authors	Rodriguez-Sanoja R., Oviedo N., Sanchez S.
	Title	Microbial starch-binding domain.
	Source	Curr. Opin. Microbiol. 8:260-267(2005).
	PubMed ID	15939348
	DOI	10.1016/j.mib.2005.04.013

2	Authors	Cheng C., Huang D., Roach P.J.
	Title	Yeast PIG genes: PIG1 encodes a putative type 1 phosphatase subunit that interacts with the yeast glycogen synthase Gsy2p.
	Source	Yeast 13:1-8(1997).
	PubMed ID	9046081
	DOI	10.1002/(SICI)1097-0061(199701)13:1<1::AID-YEA49>3.0.CO;2-F

3	Authors	Printen J.A., Brady M.J., Saltiel A.R.
	Title	PTG, a protein phosphatase 1-binding protein with a role in glycogen metabolism.
	Source	Science 275:1475-1478(1997).
	PubMed ID	9045612

4	Authors	Machovic M., Svensson B., Ann Macgregor E., Janecek S.
	Title	A new clan of CBM families based on bioinformatics of starch-binding domains from families CBM20 and CBM21.
	Source	FEBS J. 272:5497-5513(2005).
	PubMed ID	16262690
	DOI	10.1111/j.1742-4658.2005.04942.x

E1

Source

http://www.cazy.org/fam/CBM21.html

E2

Source

http://www.cazy.org/fam/GH13.html

E3

Source

http://www.cazy.org/fam/GH15.html

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