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InterPro: IPR008144 Guanylate kinase

Protein matches Help

UniProtKB

Matches:

2825 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

IPR008144 Guanylate_kin

Secondary

IPR000619

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF00625	Guanylate_kin	2549
PROSITE profile	PS50052	GUANYLATE_KINASE_2	2824
Signatures in BioMart

InterPro Relationships Help

Parent

IPR008145 Guanylate kinase/L-type calcium channel

Children

IPR017665 Guanylate kinase, sub-group

Found in

IPR005417 Zona occludens protein
IPR005418 Zona occludens protein ZO-1
IPR005419 Zona occludens protein ZO-2
IPR005420 Zona occludens protein ZO-3
IPR016313 Membrane-associated guanylate kinase (MAGUK) scaffold protein

Contains

IPR019586 Guanylate kinase-associated, C-terminal
IPR020590 Guanylate kinase, conserved site

InterPro annotation

Entry Details in BioMart

Abstract

Guanylate kinase (EC:2.7.4.8) (GK) [1] catalyzes the ATP-dependent phosphorylation of GMP into GDP. It is essential for recycling GMP and indirectly, cGMP. In prokaryotes (such as Escherichia coli), lower eukaryotes (such as yeast) and in vertebrates, GK is a highly conserved monomeric protein of about 200 amino acids. GK has been shown [2, 3, 4] to be structurally similar to protein A57R (or SalG2R) from various strains of Vaccinia virus.

Proteins containing one or more copies of the DHR domain, an SH3 domain as well as a C-terminal GK-like domain, are collectively termed MAGUKs (membrane-associated guanylate kinase homologs) [5], and include Drosophila lethal(1)discs large-1 tumor suppressor protein (gene dlg1); mammalian tight junction protein Zo-1; a family of mammalian synaptic proteins that seem to interact with the cytoplasmic tail of NMDA receptor subunits (SAP90/PSD-95, CHAPSYN-110/PSD-93, SAP97/DLG1 and SAP102); vertebrate 55kDa erythrocyte membrane protein (p55); Caenorhabditis elegans protein lin-2; rat protein CASK; and human proteins DLG2 and DLG3. There is an ATP-binding site (P-loop) in the N-terminal section of GK, which is not conserved in the GK-like domain of the above proteins. However these proteins retain the residues known, in GK, to be involved in the binding of GMP.

Structural links Help

PDB - click here

SCOP: a.24.25.1 , c.37.1.1 , c.37.1.8

CATH: 1.20.120.430 , 3.30.63.10 , 3.40.50.300

Database links Help

PDBe-motif: PS00856

Enzyme: EC:2.7

PROSITE doc: PDOC00670

PANDIT: PF00625

Blocks: IPB008144

Pfam Clan: CL0023.30

AC	CL0023.30
ID	AAA
DE	P-loop containing nucleoside triphosphate hydrolase superfamily
PF00004	IPR003959	ATPase, AAA-type, core
PF00005	IPR003439	ABC transporter-like
PF00158	IPR002078	RNA polymerase sigma factor 54, interaction
PF00265	IPR001267	Thymidine kinase
PF00308	IPR013317	Chromosomal replication control, initiator (DnaA)/regulator (Hda)
PF00406	IPR000850	Adenylate kinase
PF00437	IPR001482	Type II secretion system protein E
PF00485	IPR006083	Phosphoribulokinase/uridine kinase
PF00488	IPR000432	DNA mismatch repair protein MutS, C-terminal
PF00493	IPR001208	DNA-dependent ATPase MCM
PF00625	IPR008144	Guanylate kinase
PF00685	IPR000863	Sulfotransferase
PF00931	IPR002182	NB-ARC
PF01078	IPR000523	Magnesium chelatase, ChlI subunit
PF01202	IPR000623	Shikimate kinase
PF01580	IPR002543	Cell divisionFtsK/SpoIIIE
PF01583	IPR002891	Adenylylsulphate kinase, C-terminal
PF01637	IPR011579	ATPase domain, prokaryote
PF01656	IPR002586	Cobyrinic acid a,c-diamide synthase
PF01695	IPR002611	IstB-like ATP-binding protein
PF01712	IPR002624	Deoxynucleoside kinase
PF01715	IPR002627	tRNA isopentenyltransferase
PF01745	IPR002648	Isopentenyl transferase
PF01935	IPR002789	Protein of unknown function DUF87
PF02223	IPR000062	Thymidylate kinase-like
PF02224	IPR011994	Cytidylate kinase domain
PF02367	IPR003442	Uncharacterised protein family UPF0079, ATPase bacteria
PF02374	IPR003348	ATPase, anion-transporting
PF02463	IPR003395	RecF/RecN/SMC protein, N-terminal
PF02492	IPR003495	Cobalamin (vitamin B12) biosynthesis CobW-like
PF02534	IPR003688	TRAG protein
PF03205	IPR004435	Molybdopterin-guanine dinucleotide biosynthesis protein B (MobB), conserved region
PF03215	IPR004582	Checkpoint protein Rad24
PF03308	IPR005129	ArgK protein
PF03668	IPR005337	ATPase, P-loop-containing
PF03969	IPR005654	ATPase, AFG1-like
PF05621	IPR008868	Bacterial TniB
PF05707	IPR008900	Zonular occludens toxin
PF05729	IPR007111	NACHT nucleoside triphosphatase
PF05872	IPR008571	Protein of unknown function DUF853, nucleotide triphosphate hydrolase, putative
PF06068	IPR010339	TIP49, C-terminal
PF06144	IPR010372	DNA polymerase III, delta
PF06309	IPR010448	Torsin
PF06431	IPR010932	Large T antigen, polyomavirus, C-terminal
PF07693	IPR011646	KAP P-loop
PF07724	IPR013093	ATPase associated with various cellular activities, AAA-2
PF07726	IPR011703	ATPase associated with various cellular activities, AAA-3
PF07728	IPR011704	ATPase associated with various cellular activities, AAA-5
PF07931	IPR012853	Chloramphenicol phosphotransferase-like
PF08298	IPR013153	PrkA AAA
PF08433	IPR013641	Chromatin associated protein KTI12
PF08542	IPR013748	Replication factor C
PF10443	IPR018850	Mitochondrial escape protein 2, putative NTP-binding domain
PF10609	IPR019591	ATPase-like, ParA/MinD

Interactions Help

This domain has been experimentally proven to be involved in Protein:Protein interactions.
Representative data is shown with the following example proteins:

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR008144

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O14936 Peripheral plasma membrane protein CASK

O70589 Peripheral plasma membrane protein CASK

P15454 Guanylate kinase

P31007 Disks large 1 tumor suppressor protein

P54936 Protein lin-2

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR019586	Guanylate kinase-associated, C-terminal
IPR008145	Guanylate kinase/L-type calcium channel
IPR008144	Guanylate kinase
IPR017442	Serine/threonine-protein kinase-like domain
IPR001452	Src homology-3 domain
IPR004172	L27
IPR008266	Tyrosine-protein kinase, active site
IPR015143	L27-1
IPR017665	Guanylate kinase, sub-group
IPR011009	Protein kinase-like domain
IPR020590	Guanylate kinase, conserved site
IPR014775	L27, C-terminal
IPR001478	PDZ/DHR/GLGF
IPR000719	Protein kinase, catalytic domain
IPR002290	Serine/threonine-protein kinase domain
IPR011511	Variant SH3
	PDB Chain
	ModBase
	CATH Domain
	SWISS-MODEL
	SCOP Domain

Publications Open in usermanual
1.	Stehle T, Schulz GE. Refined structure of the complex between guanylate kinase and its substrate GMP at 2.0 A resolution. J. Mol. Biol. 224 1127-41 1992 [PubMed: 1314905] http://dx.doi.org/10.1016/0022-2836(92)90474-X
2.	Bryant PJ, Woods DF. A major palmitoylated membrane protein of human erythrocytes shows homology to yeast guanylate kinase and to the product of a Drosophila tumor suppressor gene. Cell 68 621-2 1992 [PubMed: 1310897] http://dx.doi.org/10.1016/0092-8674(92)90136-Z
3.	Zschocke PD, Schiltz E, Schulz GE. Purification and sequence determination of guanylate kinase from pig brain. Eur. J. Biochem. 213 263-9 1993 [PubMed: 8097461] http://dx.doi.org/10.1111/j.1432-1033.1993.tb17757.x
4.	Goebl MG. Is the erythrocyte protein p55 a membrane-bound guanylate kinase? Trends Biochem. Sci. 17 99 1992 [PubMed: 1329277] http://dx.doi.org/10.1016/0968-0004(92)90244-4
5.	Woods DF, Bryant PJ. ZO-1, DlgA and PSD-95/SAP90: homologous proteins in tight, septate and synaptic cell junctions. Mech. Dev. 44 85-9 1993 [PubMed: 8155583] http://dx.doi.org/10.1016/0925-4773(93)90059-7

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
	Brenman JE, Topinka JR, Cooper EC, McGee AW, Rosen J, Milroy T, Ralston HJ, Bredt DS. Localization of postsynaptic density-93 to dendritic microtubules and interaction with microtubule-associated protein 1A. J. Neurosci. 18 1998 8805-13 [PubMed: 9786987] http://www.jneurosci.org/cgi/content/abstract/18/21/8805
	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
	Scrima A, Vetter IR, Armengod ME, Wittinghofer A. The structure of the TrmE GTP-binding protein and its implications for tRNA modification. EMBO J. 24 2005 23-33 [PubMed: 15616586] http://dx.doi.org/10.1038/sj.emboj.7600507

InterPro 23.1