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InterPro: IPR003137 Protease-associated PA

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UniProtKB

Matches:

2468 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
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Architectures
Accession List
Matches in BioMart

Accession

IPR003137 PA

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF02225	PA	2468
Signatures in BioMart

InterPro Relationships Help

Found in

IPR000209 Peptidase S8/S53, subtilisin/kexin/sedolisin
IPR015500 Peptidase S8, subtilisin-related
IPR017292 Peptidase S8A, Vpr
IPR017296 Peptidase S8A, SAM-P45
IPR017311 Peptidase S8A, subtilisin-related, shewanella
IPR017312 Peptidase S8A, subtilisin-related, shewanella-2

InterPro annotation

Entry Details in BioMart

Abstract

The PA (Protease associated) domain is found as an insert domain in diverse proteases, which include the MEROPS peptidase families A22B, M28, and S8A [1]. The PA domain is also found in a plant vacuolar sorting receptor O22925 and members of the RZF family, e.g. O43567.

Structural links Help

PDB - click here

SCOP: c.41.1.1 , c.8.4.1

CATH: 3.50.30.30

Database links Help

PANDIT: PF02225

Blocks: IPB003137

MEROPS: A22 , M28 , S8

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR003137

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O35409 Glutamate carboxypeptidase 2

P02786 Transferrin receptor protein 1

P37302 Aminopeptidase Y

P91406 Glutamate carboxypeptidase 2 homolog

Q06003 Protein goliath

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR007365	Transferrin receptor-like, dimerisation
IPR018957	Zinc finger, C3HC4 RING-type
IPR007484	Peptidase M28
IPR001841	Zinc finger, RING-type
IPR003137	Protease-associated PA
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Open in usermanual
1.	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
	Mesters JR, Henning K, Hilgenfeld R. Human glutamate carboxypeptidase II inhibition: structures of GCPII in complex with two potent inhibitors, quisqualate and 2-PMPA. Acta Crystallogr. D Biol. Crystallogr. 63 2007 508-13 [PubMed: 17372356] http://dx.doi.org/10.1107/S090744490700902X
	Barinka C, Hlouchova K, Rovenska M, Majer P, Dauter M, Hin N, Ko YS, Tsukamoto T, Slusher BS, Konvalinka J, Lubkowski J. Structural basis of interactions between human glutamate carboxypeptidase II and its substrate analogs. J. Mol. Biol. 376 2008 1438-50 [PubMed: 18234225] http://dx.doi.org/10.1016/j.jmb.2007.12.066
	Mesters JR, Barinka C, Li W, Tsukamoto T, Majer P, Slusher BS, Konvalinka J, Hilgenfeld R. Structure of glutamate carboxypeptidase II, a drug target in neuronal damage and prostate cancer. EMBO J. 25 2006 1375-84 [PubMed: 16467855] http://dx.doi.org/10.1038/sj.emboj.7600969
	Barinka C, Starkova J, Konvalinka J, Lubkowski J. A high-resolution structure of ligand-free human glutamate carboxypeptidase II. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 63 2007 150-3 [PubMed: 17329803]
	Barinka C, Rovenska M, Mlcochova P, Hlouchova K, Plechanovova A, Majer P, Tsukamoto T, Slusher BS, Konvalinka J, Lubkowski J. Structural insight into the pharmacophore pocket of human glutamate carboxypeptidase II. J. Med. Chem. 50 2007 3267-73 [PubMed: 17567119] http://dx.doi.org/10.1021/jm070133w
	Luo X, Hofmann K. The protease-associated domain: a homology domain associated with multiple classes of proteases. Trends Biochem. Sci. 26 2001 147-8 [PubMed: 11246007] http://dx.doi.org/10.1016/S0968-0004(00)01768-0

InterPro 23.1