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InterPro: IPR013320 Concanavalin A-like lectin/glucanase, subgroup

Protein matches Help

UniProtKB

Matches:

10075 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

IPR013320 ConA-like_subgrp

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Gene3D	G3DSA:2.60.120.200	ConA_like_subgrp	10075
Signatures in BioMart

InterPro Relationships Help

Parent

IPR008985 Concanavalin A-like lectin/glucanase

Children

IPR000757 Glycoside hydrolase, family 16
IPR001079 Galectin, carbohydrate recognition domain
IPR001220 Legume lectin, beta chain
IPR001791 Laminin G
IPR004124 Glycoside hydrolase, family 33, N-terminal
IPR008859 Thrombospondin, C-terminal
IPR012928 Clostridium neurotoxin, receptor binding N-terminal
IPR014895 Alginate lyase 2
IPR015185 Exotoxin A, binding
IPR015289 Alpha-L-arabinofuranosidase B, catalytic

Found in

IPR000416 Haemagglutinin outer capsid protein VP4
IPR001580 Calreticulin/calnexin
IPR001759 Pentaxin
IPR003129 Laminin G, thrombospondin-type, N-terminal
IPR005052 Legume-like lectin
IPR005629 Beta-glucan synthesis-associated, SKN1
IPR008377 Trypanosome sialidase
IPR009169 Calreticulin
IPR015305 Protein of unknown function DUF1961
IPR015447 Neurexin
IPR016287 Agarase
IPR016455 Xyloglucan endotransglucosylase/hydrolase
IPR016710 L-type lectin, fungi

Contains

IPR000985 Legume lectin, alpha chain, conserved site
IPR006558 LamG-like jellyroll fold
IPR008263 Glycoside hydrolase, family 16, active site
IPR010713 Xyloglucan endo-transglycosylase, C-terminal
IPR012679 Laminin G, subdomain 1
IPR012680 Laminin G, subdomain 2
IPR015344 Vibrio cholerae sialidase, lectin insertion
IPR018124 Calreticulin/calnexin, conserved site
IPR019825 Legume lectin, beta chain, Mn/Ca-binding site

InterPro annotation

Entry Details in BioMart

Abstract

Lectins and glucanases exhibit the common property of reversibly binding to specific complex carbohydrates. The lectins/glucanases are a diverse group of proteins found in a wide range of species from prokaryotes to humans. The different family members all contain a concanavalin A-like domain, which consists of a sandwich of 12-14 beta strands in two sheets with a complex topology. Members of this family are diverse, and include the lectins: legume lectins, cereal lectins, viral lectins, and animal lectins. Plant lectins function in the storage and transport of carbohydrates in seeds, the binding of nitrogen-fixing bacteria to root hairs, the inhibition of fungal growth or insect feeding, and in hormonally regulated plant growth [1]. Protein members include concanavalin A (Con A), favin, isolectin I, lectin IV, soybean agglutinin and lentil lectin. Animal lectins include the galectins, which are S-type lactose-binding and IgE-binding proteins such as S-lectin, CLC protein, galectin1, galectin2, galectin3 CRD, and Congerin I [2].

Other members with a Con A-like domain include the glucanases. Bacterial and fungal beta-glucanases, such as Bacillus 1-3,1-4-beta-glucanse, carry out the acid catalysis of beta-glucans found in microorganisms and plants [3]. Similarly, kappa-Carrageenase degrades kappa-carrageenans from marine red algae cell walls [4].

This entry differs from (IPR008985) by omitting the xylanases and glycosyl hydrolases.

Structural links Help

PDB - click here

SCOP: b.29.1.1 , b.29.1.12 , b.29.1.13 , b.29.1.14 , b.29.1.15 , b.29.1.16 , b.29.1.17 , b.29.1.18 , b.29.1.2 , b.29.1.21 , b.29.1.23 , b.29.1.3 , b.29.1.4 , b.29.1.5 , b.29.1.6 , b.29.1.8 , b.29.1.9 , b.42.4.2 , b.68.1.1 , h.4.2.1

CATH: 2.120.10.10 , 2.60.120.200

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR013320

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O00182 Galectin-9

O08573 Galectin-9

P24014 Protein slit

P27798 Calreticulin

P43555 Protein EMP47

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR001791	Laminin G
IPR006210	EGF-like
IPR000483	Cysteine-rich flanking region, C-terminal domain
IPR009169	Calreticulin
IPR001611	Leucine-rich repeat
IPR013032	EGF-like region, conserved site
IPR018097	EGF-like calcium-binding, conserved site
IPR006207	Cystine knot, C-terminal
IPR005052	Legume-like lectin
IPR001881	EGF-like calcium-binding
IPR001079	Galectin, carbohydrate recognition domain
IPR013320	Concanavalin A-like lectin/glucanase, subgroup
IPR012679	Laminin G, subdomain 1
IPR003591	Leucine-rich repeat, typical subtype
IPR018124	Calreticulin/calnexin, conserved site
IPR000372	Leucine-rich repeat-containing N-terminal domain
IPR016710	L-type lectin, fungi
IPR000152	EGF-type aspartate/asparagine hydroxylation site
IPR000742	EGF-like, type 3
IPR001580	Calreticulin/calnexin
IPR008985	Concanavalin A-like lectin/glucanase
IPR006209	EGF
	ModBase
	SWISS-MODEL
	PDB Chain
	CATH Domain
	SCOP Domain

Publications Open in usermanual
1.	Sanz-Aparicio J, Hermoso J, Grangeiro TB, Calvete JJ, Cavada BS. The crystal structure of Canavalia brasiliensis lectin suggests a correlation between its quaternary conformation and its distinct biological properties from Concanavalin A. FEBS Lett. 405 114-8 1997 [PubMed: 9094437] http://dx.doi.org/10.1016/S0014-5793(97)00137-3
2.	Ackerman SJ, Liu L, Kwatia MA, Savage MP, Leonidas DD, Swaminathan GJ, Acharya KR. Charcot-Leyden crystal protein (galectin-10) is not a dual function galectin with lysophospholipase activity but binds a lysophospholipase inhibitor in a novel structural fashion. J. Biol. Chem. 277 14859-68 2002 [PubMed: 11834744] http://dx.doi.org/10.1074/jbc.M200221200
3.	Hahn M, Pons J, Planas A, Querol E, Heinemann U. Crystal structure of Bacillus licheniformis 1,3-1,4-beta-D-glucan 4-glucanohydrolase at 1.8 A resolution. FEBS Lett. 374 221-4 1995 [PubMed: 7589539] http://dx.doi.org/10.1016/0014-5793(95)01111-Q
4.	Michel G, Chantalat L, Duee E, Barbeyron T, Henrissat B, Kloareg B, Dideberg O. The kappa-carrageenase of P. carrageenovora features a tunnel-shaped active site: a novel insight in the evolution of Clan-B glycoside hydrolases. Structure 9 513-25 2001 [PubMed: 11435116] http://dx.doi.org/10.1016/S0969-2126(01)00612-8

Additional Reading Open in usermanual
	Chen X, Liu H, Shim AH, Focia PJ, He X. Structural basis for synaptic adhesion mediated by neuroligin-neurexin interactions. Nat. Struct. Mol. Biol. 15 2008 50-6 [PubMed: 18084303] http://dx.doi.org/10.1038/nsmb1350
	Moreno FB, de Oliveira TM, Martil DE, Vicoti MM, Bezerra GA, Abrego JR, Cavada BS, Filgueira de Azevedo W Jr. Identification of a new quaternary association for legume lectins. J. Struct. Biol. 161 2008 133-43 [PubMed: 18068379] http://dx.doi.org/10.1016/j.jsb.2007.10.002
	Brunzelle JS, Jordan DB, McCaslin DR, Olczak A, Wawrzak Z. Structure of the two-subsite beta-d-xylosidase from Selenomonas ruminantium in complex with 1,3-bis[tris(hydroxymethyl)methylamino]propane. Arch. Biochem. Biophys. 474 2008 157-66 [PubMed: 18374656] http://dx.doi.org/10.1016/j.abb.2008.03.007
	Koehnke J, Jin X, Trbovic N, Katsamba PS, Brasch J, Ahlsen G, Scheiffele P, Honig B, Palmer AG 3rd, Shapiro L. Crystal structures of beta-neurexin 1 and beta-neurexin 2 ectodomains and dynamics of splice insertion sequence 4. Structure 16 2008 410-21 [PubMed: 18334216] http://dx.doi.org/10.1016/j.str.2007.12.024
	Buchini S, Buschiazzo A, Withers SG. A new generation of specific Trypanosoma cruzi trans-sialidase inhibitors. Angew. Chem. Int. Ed. Engl. 47 2008 2700-3 [PubMed: 18300214]

InterPro 23.1