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InterPro: IPR001956 Bacterial type 3a, cellulose-binding

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UniProtKB

Matches:

283 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR001956 CBD_3

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Gene3D	G3DSA:2.60.40.710	CBD_3	276
Pfam	PF00942	CBM_3	265
PROSITE profile	PS51172	CBM3	274
Signatures in BioMart

InterPro Relationships Help

Parent

IPR008965 Carbohydrate-binding

GO Term annotation Help

Process

GO:0005975 carbohydrate metabolic process

Function

GO:0030246 carbohydrate binding

InterPro annotation

Entry Details in BioMart

Abstract

This domain is involved in cellulose binding [1] and is found associated with a wide range of bacterial glycosyl hydrolases. The structure for this domain is known [2]; it forms a beta sandwich.

Structural links Help

PDB - click here

SCOP: a.102.1.2 , b.2.2.2

CATH: 2.60.40.710

Database links Help

Enzyme: EC:3.2.1

PROSITE doc: PDOC51172

PANDIT: PF00942

Blocks: IPB001956

Pfam Clan: CL0203.8

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR001956

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P26221 Endoglucanase E-4

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR001701	Glycoside hydrolase, family 9
IPR012341	Six-hairpin glycosidase
IPR008965	Carbohydrate-binding
IPR008928	Six-hairpin glycosidase-like
IPR008957	Fibronectin, type III-like fold
IPR001919	Cellulose-binding domain, family II, bacterial type
IPR018221	Glycoside hydrolase, family 9, active site
IPR001956	Bacterial type 3a, cellulose-binding
IPR018366	Carbohydrate-binding type-2, conserved site
IPR003961	Fibronectin, type III
	PDB Chain
	ModBase
	CATH Domain
	SWISS-MODEL
	SCOP Domain

Publications Open in usermanual
1.	Poole DM, Morag E, Lamed R, Bayer EA, Hazlewood GP, Gilbert HJ. Identification of the cellulose-binding domain of the cellulosome subunit S1 from Clostridium thermocellum YS. FEMS Microbiol. Lett. 78 181-6 1992 [PubMed: 1490597] http://dx.doi.org/10.1016/0378-1097(92)90022-G
2.	Tormo J, Lamed R, Chirino AJ, Morag E, Bayer EA, Shoham Y, Steitz TA. Crystal structure of a bacterial family-III cellulose-binding domain: a general mechanism for attachment to cellulose. EMBO J. 15 5739-51 1996 [PubMed: 8918451] http://ukpmc.ac.uk/articlerender.cgi?tool=EBI&pubmedid=8918451

Additional Reading Open in usermanual
	Gal L, Pages S, Gaudin C, Belaich A, Reverbel-Leroy C, Tardif C, Belaich JP. Characterization of the cellulolytic complex (cellulosome) produced by Clostridium cellulolyticum. Appl. Environ. Microbiol. 63 1997 903-9 [PubMed: 9055408] http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=9055408
	Irwin D, Shin DH, Zhang S, Barr BK, Sakon J, Karplus PA, Wilson DB. Roles of the catalytic domain and two cellulose binding domains of Thermomonospora fusca E4 in cellulose hydrolysis. J. Bacteriol. 180 1998 1709-14 [PubMed: 9537366] http://jb.asm.org/cgi/content/abstract/180/7/1709
	Carvalho AL, Dias FM, Prates JA, Nagy T, Gilbert HJ, Davies GJ, Ferreira LM, Romao MJ, Fontes CM. Cellulosome assembly revealed by the crystal structure of the cohesin-dockerin complex. Proc. Natl. Acad. Sci. U.S.A. 100 2003 13809-14 [PubMed: 14623971] http://dx.doi.org/10.1073/pnas.1936124100
	Spinelli S, Fierobe HP, Belaich A, Belaich JP, Henrissat B, Cambillau C. Crystal structure of a cohesin module from Clostridium cellulolyticum: implications for dockerin recognition. J. Mol. Biol. 304 2000 189-200 [PubMed: 11080455] http://dx.doi.org/10.1006/jmbi.2000.4191
	Shimon LJ, Pages S, Belaich A, Belaich JP, Bayer EA, Lamed R, Shoham Y, Frolow F. Structure of a family IIIa scaffoldin CBD from the cellulosome of Clostridium cellulolyticum at 2.2 A resolution. Acta Crystallogr. D Biol. Crystallogr. 56 2000 1560-8 [PubMed: 11092922] http://dx.doi.org/10.1107/S0907444900012889
	Carvalho AL, Dias FM, Nagy T, Prates JA, Proctor MR, Smith N, Bayer EA, Davies GJ, Ferreira LM, Romao MJ, Fontes CM, Gilbert HJ. Evidence for a dual binding mode of dockerin modules to cohesins. Proc. Natl. Acad. Sci. U.S.A. 104 2007 3089-94 [PubMed: 17360613] http://dx.doi.org/10.1073/pnas.0611173104
	Mandelman D, Belaich A, Belaich JP, Aghajari N, Driguez H, Haser R. X-Ray crystal structure of the multidomain endoglucanase Cel9G from Clostridium cellulolyticum complexed with natural and synthetic cello-oligosaccharides. J. Bacteriol. 185 2003 4127-35 [PubMed: 12837787] http://dx.doi.org/10.1128/JB.185.14.4127-4135.2003
	Pinheiro BA, Proctor MR, Martinez-Fleites C, Prates JA, Money VA, Davies GJ, Bayer EA, Fontesm CM, Fierobe HP, Gilbert HJ. The Clostridium cellulolyticum dockerin displays a dual binding mode for its cohesin partner. J. Biol. Chem. 283 2008 18422-30 [PubMed: 18445585] http://dx.doi.org/10.1074/jbc.M801533200

InterPro 23.1