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InterPro: IPR015364 Rhamnogalacturonase B, N-terminal

Protein matches Help

UniProtKB

Matches:

39 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

IPR015364 RhgB_N

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF09284	RhgB_N	39
Signatures in BioMart

InterPro Relationships Help

Parent

IPR011013 Glycoside hydrolase-type carbohydrate-binding

Found in

IPR016590 Rhamnogalacturonase B

GO Term annotation Help

Process

GO:0005975 carbohydrate metabolic process

Function

GO:0016837 carbon-oxygen lyase activity, acting on polysaccharides
GO:0030246 carbohydrate binding

InterPro annotation

Entry Details in BioMart

Abstract

This domain is found in prokaryotic enzyme rhamnogalacturonase B, it adopts a structure consisting of a beta supersandwich, with eighteen strands in two beta-sheets. The exact function of the domain is unknown, but a putative role includes carbohydrate-binding [1].

Structural links Help

PDB - click here

SCOP: b.30.5.10

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR015364

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

Q00019 Rhamnogalacturonase B

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR013784	Carbohydrate-binding-like fold
IPR016590	Rhamnogalacturonase B
IPR008979	Galactose-binding domain-like
IPR015364	Rhamnogalacturonase B, N-terminal
IPR011013	Glycoside hydrolase-type carbohydrate-binding
	PDB Chain
	ModBase
	SCOP Domain

Publications Open in usermanual
1.	McDonough MA, Kadirvelraj R, Harris P, Poulsen JC, Larsen S. Rhamnogalacturonan lyase reveals a unique three-domain modular structure for polysaccharide lyase family 4. FEBS Lett. 565 188-94 2004 [PubMed: 15135077] http://dx.doi.org/10.1016/j.febslet.2004.03.094

InterPro 23.1