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InterPro: IPR017665 Guanylate kinase, sub-group

Protein matches Help

UniProtKB

Matches:

1880 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

IPR017665 Guanylate_kinase_sub

Type

Family

Signatures Help

Database	ID	Name	Proteins
HAMAP	MF_00328	Guanylate_kinase_sub	1433
TIGRFAMs	TIGR03263	guanyl_kin	1880
Signatures in BioMart

InterPro Relationships Help

Parent

IPR008144 Guanylate kinase

Contains

IPR020590 Guanylate kinase, conserved site

GO Term annotation Help

Process

GO:0006163 purine nucleotide metabolic process

Function

GO:0004385 guanylate kinase activity

InterPro annotation

Entry Details in BioMart

Abstract

Members of this family contain the enzyme guanylate kinase, also called GMP kinase and is essential for recycling GMP and indirectly, cGMP. This enzyme transfers a phosphate from ATP to GMP, yielding ADP and GDP [1]. Guanylate kinase is a highly conserved monomer and is important for the activation of various antiviral drugs.

Structural links Help

PDB - click here

SCOP: c.37.1.1

CATH: 3.30.63.10 , 3.40.50.300

Database links Help

Enzyme: EC:2.7.4.8

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR017665

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P0A5I4 Guanylate kinase

P15454 Guanylate kinase

P72648 Guanylate kinase

Q16774 Guanylate kinase

Q64520 Guanylate kinase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR017665	Guanylate kinase, sub-group
IPR020590	Guanylate kinase, conserved site
IPR008145	Guanylate kinase/L-type calcium channel
IPR008144	Guanylate kinase
	SWISS-MODEL
	PDB Chain
	ModBase
	CATH Domain
	SCOP Domain

Publications Open in usermanual
1.	Sekulic N, Shuvalova L, Spangenberg O, Konrad M, Lavie A. Structural characterization of the closed conformation of mouse guanylate kinase. J. Biol. Chem. 277 30236-43 2002 [PubMed: 12036965] http://dx.doi.org/10.1074/jbc.M204668200

Additional Reading Open in usermanual
	Hible G, Renault L, Schaeffer F, Christova P, Zoe Radulescu A, Evrin C, Gilles AM, Cherfils J. Calorimetric and crystallographic analysis of the oligomeric structure of Escherichia coli GMP kinase. J. Mol. Biol. 352 2005 1044-59 [PubMed: 16140325] http://dx.doi.org/10.1016/j.jmb.2005.07.042
	Hible G, Christova P, Renault L, Seclaman E, Thompson A, Girard E, Munier-Lehmann H, Cherfils J. Unique GMP-binding site in Mycobacterium tuberculosis guanosine monophosphate kinase. Proteins 62 2006 489-500 [PubMed: 16288457] http://dx.doi.org/10.1002/prot.20662
	Vedadi M, Lew J, Artz J, Amani M, Zhao Y, Dong A, Wasney GA, Gao M, Hills T, Brokx S, Qiu W, Sharma S, Diassiti A, Alam Z, Melone M, Mulichak A, Wernimont A, Bray J, Loppnau P, Plotnikova O, Newberry K, Sundararajan E, Houston S, Walker J, Tempel W, Bochkarev A, Kozieradzki I, Edwards A, Arrowsmith C, Roos D, Kain K, Hui R. Genome-scale protein expression and structural biology of Plasmodium falciparum and related Apicomplexan organisms. Mol. Biochem. Parasitol. 151 2007 100-10 [PubMed: 17125854] http://dx.doi.org/10.1016/j.molbiopara.2006.10.011
	Hible G, Daalova P, Gilles AM, Cherfils J. Crystal structures of GMP kinase in complex with ganciclovir monophosphate and Ap5G. Biochimie 88 2006 1157-64 [PubMed: 16690197] http://dx.doi.org/10.1016/j.biochi.2006.04.002

InterPro 23.1