{PDOC51455} {PS51455; PIPK} {BEGIN} *************************************************************** * Phosphatidylinositol phosphate kinase (PIPK) domain profile * *************************************************************** Phosphoinositides (PIs) are central to signal transduction and membrane trafficking in all eukaryotes. They are derived from phosphatidylinositol (PtdIns) as the result of phosphorylation of hydroxyl groups at positions 3, 4 or 5 of the PtdIns head group. Phosphatidylinositol phosphate kinases (PIPKs) phosphorylate phosphatidylinositol phosphate (PtdInsP) to phosphatidylinositol bisphosphate (PtdInsP2). Three types of PIPKs are present throughout the eukaryotic kingdoms. Type I (PtdIns4P 5-kinase) and type II (PtdIns5P 4- kinase) generate PtdIns(4,5)P2 from PtdIns4P and PtdIns5P, respectively. Type III PIPK (PtdIns3P 5-kinases) are distinct from the type I and II PIPKs and synthesize PtdIns(3,5)P2 [1,2,3]. The basic structure of PIPKs shared by animals, yeast and plant PIPks consists of a highly conserved central kinase domain and a dimerization domain. PIPK domains have high sequence identity, well-defined motifs and conserved residues. They consist of two alpha+beta subdomains (see ]. The larger N-terminal subdomain contains a seven-stranded antiparallel beta sheet and four helices. The C-terminal subdomain contains a five-stranded antiparallel beta sheet and four helices [4]. The profile we developed covers the entire PIPK domain. -Sequences known to belong to this class detected by the profile: ALL. -Other sequence(s) detected in Swiss-Prot: NONE. -Last update: June 2009 / First entry. [ 1] Bakthavatsalam D., Meijer H.J.G., Noegel A.A., Govers F. "Novel phosphatidylinositol phosphate kinases with a G-protein coupled receptor signature are shared by Dictyostelium and Phytophthora." Trends Microbiol. 14:378-382(2006). PubMed=16876997; DOI=10.1016/j.tim.2006.07.006 [ 2] Heck J.N., Mellman D.L., Ling K., Sun Y., Wagoner M.P., Schill N.J., Anderson R.A. "A conspicuous connection: structure defines function for the phosphatidylinositol-phosphate kinase family." Crit. Rev. Biochem. Mol. Biol. 42:15-39(2007). PubMed=17364683; DOI=10.1080/10409230601162752 [ 3] Saavedra L., Balbi V., Dove S.K., Hiwatashi Y., Mikami K., Sommarin M. "Characterization of phosphatidylinositol phosphate kinases from the moss Physcomitrella patens: PpPIPK1 and PpPIPK2." Plant Cell Physiol. 50:595-609(2009). PubMed=19188261; DOI=10.1093/pcp/pcp018 [ 4] Rao V.D., Misra S., Boronenkov I.V., Anderson R.A., Hurley J.H. "Structure of type IIbeta phosphatidylinositol phosphate kinase: a protein kinase fold flattened for interfacial phosphorylation." Cell 94:829-839(1998). PubMed=9753329 -------------------------------------------------------------------------------- PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html -------------------------------------------------------------------------------- {END}