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InterPro: IPR011650 Peptidase M20, dimerisation

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11576 proteins

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Accession List
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Accession

IPR011650 Peptidase_M20_dimer

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF07687	M20_dimer	10337
SuperFamily	SSF55031	Peptidase_M20_dimer	10700
Signatures in BioMart

InterPro Relationships Help

Found in

IPR001160 Peptidase M20C, Xaa-His dipeptidase
IPR002933 Peptidase M20
IPR005941 Succinyl-diaminopimelate desuccinylase, proteobacteria
IPR010158 Amidase, hydantoinase/carbamoylase
IPR010159 N-acyl-L-amino-acid amidohydrolase
IPR010161 Peptidase M20B, tripeptide aminopeptidase
IPR010162 Peptidase M20B, peptidase T
IPR010168 Peptidase M20D, amidohydrolase
IPR010169 Acetylornithine deacetylase (ArgE)
IPR010174 Succinyl-diaminopimelate desuccinylase
IPR010175 N-acetyl-ornithine/N-acetyl-lysine deacetylase
IPR010182 Acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase
IPR010964 Peptidase M20A, peptidase V related
IPR011291 Peptidase M20A, peptidase V
IPR017141 Peptidase M20, carboxypeptidase S
IPR017144 Peptidase M20D, amidohydrolase, predicted
IPR017145 Aminobenzoyl-glutamate utilization protein B
IPR017149 Glutathione degradosome, DUG2
IPR017150 Peptidase M20, glutamate carboxypeptidase
IPR017153 Glutathione degradosome, DUG1
IPR017591 Allantoate amidohydrolase
IPR017706 M20/DapE, YgeY

GO Term annotation Help

Function

GO:0016787 hydrolase activity
GO:0046983 protein dimerization activity

InterPro annotation

Entry Details in BioMart

Abstract

This domain consists of 4 beta strands and two alpha helices which make up the dimerisation surface of members of the MEROPS peptidase family M20 [1]. This family includes a range of zinc exopeptidases: carboxypeptidases, dipeptidases and specialised aminopeptidases [2].

Structural links Help

PDB - click here

SCOP: c.56.5.4 , d.58.19.1

CATH: 3.30.70.360 , 3.40.630.10

Database links Help

Enzyme: EC:3

PANDIT: PF07687

Blocks: IPB011650

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR011650

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P0C155 Putative carboxypeptidase YOL153C

P54970 IAA-amino acid hydrolase ILR1-like 2

Q03154 Aminoacylase-1

Q5N8F2 IAA-amino acid hydrolase ILR1-like 2

Q9D1A2 Cytosolic non-specific dipeptidase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR017439	Peptidase M20D, mername-AA028/carboxypeptidase Ss1
IPR010168	Peptidase M20D, amidohydrolase
IPR002933	Peptidase M20
IPR001261	ArgE/DapE/ACY1/CPG2/YscS, conserved site
IPR011650	Peptidase M20, dimerisation
IPR017153	Glutathione degradosome, DUG1
IPR017141	Peptidase M20, carboxypeptidase S
IPR010159	N-acyl-L-amino-acid amidohydrolase
	PDB Chain
	ModBase
	CATH Domain
	SWISS-MODEL
	SCOP Domain

Publications Open in usermanual
1.	Rowsell S, Pauptit RA, Tucker AD, Melton RG, Blow DM, Brick P. Crystal structure of carboxypeptidase G2, a bacterial enzyme with applications in cancer therapy. Structure 5 337-47 1997 [PubMed: 9083113] http://dx.doi.org/10.1016/S0969-2126(97)00191-3
2.	Rawlings ND, Barrett AJ. Evolutionary families of metallopeptidases. Meth. Enzymol. 248 183-228 1995 [PubMed: 7674922] http://dx.doi.org/10.1016/0076-6879(95)48015-3

Additional Reading Open in usermanual
	Andersen B, Lundgren S, Dobritzsch D, Piskur J. A recruited protease is involved in catabolism of pyrimidines. J. Mol. Biol. 379 2008 243-50 [PubMed: 18448119] http://dx.doi.org/10.1016/j.jmb.2008.03.073
	Levin EJ, Kondrashov DA, Wesenberg GE, Phillips GN Jr. Ensemble refinement of protein crystal structures: validation and application. Structure 15 2007 1040-52 [PubMed: 17850744] http://dx.doi.org/10.1016/j.str.2007.06.019
	Bitto E, Bingman CA, Bittova L, Houston NL, Boston RS, Fox BG, Phillips GN Jr. X-ray structure of ILL2, an auxin-conjugate amidohydrolase from Arabidopsis thaliana. Proteins 74 2009 61-71 [PubMed: 18543330] http://dx.doi.org/10.1002/prot.22124
	Lundgren S, Andersen B, Piskur J, Dobritzsch D. Crystal structures of yeast beta-alanine synthase complexes reveal the mode of substrate binding and large scale domain closure movements. J. Biol. Chem. 282 2007 36037-47 [PubMed: 17916556] http://dx.doi.org/10.1074/jbc.M705517200
	Agarwal R, Burley SK, Swaminathan S. Structural analysis of a ternary complex of allantoate amidohydrolase from Escherichia coli reveals its mechanics. J. Mol. Biol. 368 2007 450-63 [PubMed: 17362992] http://dx.doi.org/10.1016/j.jmb.2007.02.028

InterPro 23.1