{PDOC51641} {PS51641; AGENET_LIKE} {BEGIN} ****************************** * Agenet-like domain profile * ****************************** Fragile X Mental Retardation Protein (FMRP), and its autosomal paralogues, Fragile X mental Retardation syndrome-related protein 1 and 2 (FXR1 and FXR2), comprise a family of RNA-binding proteins. It is thought that the FRMP family of proteins contributes to the regulation of protein synthesis at sites where mRNAs are locally translated in response to stimuli. These proteins are highly similar to one another and also retain highly conserved domain architecture. The two ribonucleoprotein K homology (KH) domains (see ) and the cluster of arginine and glycine residues that constitute the RGG box, comprise a large region that is important for RNA binding and polyribosome association. In addition, two Agenet-like domains exist in tandem within the N-terminal regions of FMRP family proteins. The Agenet-like domain belongs to the "Royal" domain superfamilly which contains also the Tudor (see ), chromo (see ), MBT (see ), PWWP (see ) and plant Agenet domains. Biochemical analysis of the tandem Agenet-like domains reveals their ability to preferentially recognize trimethylated peptides in a sequence-specific manner [1,2,3,4]. The Agenet-like domain folds into a bent four-stranded antiparallel beta sheet with a fifth strand closing the cavity of the sheet, similar to a thumb accross a semiclosed hand (see ) [3,4]. The profile we developed covers the entire Agenet-like domain. -Sequences known to belong to this class detected by the profile: ALL. -Other sequence(s) detected in Swiss-Prot: NONE. -Last update: March 2012 / First entry. [ 1] Maurer-Stroh S., Dickens N.J., Hughes-Davies L., Kouzarides T., Eisenhaber F., Ponting C.P. "The Tudor domain 'Royal Family': Tudor, plant Agenet, Chromo, PWWP and MBT domains." Trends Biochem. Sci. 28:69-74(2003). PubMed=12575993 [ 2] Adinolfi S., Ramos A., Martin S.R., Dal Piaz F., Pucci P., Bardoni B., Mandel J.L., Pastore A. "The N-terminus of the fragile X mental retardation protein contains a novel domain involved in dimerization and RNA binding." Biochemistry 42:10437-10444(2003). PubMed=12950170; DOI=10.1021/bi034909g [ 3] Ramos A., Hollingworth D., Adinolfi S., Castets M., Kelly G., Frenkiel T.A., Bardoni B., Pastore A. "The structure of the N-terminal domain of the fragile X mental retardation protein: a platform for protein-protein interaction." Structure 14:21-31(2006). PubMed=16407062; DOI=10.1016/j.str.2005.09.018 [ 4] Adams-Cioaba M.A., Guo Y., Bian C., Amaya M.F., Lam R., Wasney G.A., Vedadi M., Xu C., Min J. "Structural studies of the tandem Tudor domains of fragile X mental retardation related proteins FXR1 and FXR2." PLoS ONE 5:E13559-E13559(2010). PubMed=21072162; DOI=10.1371/journal.pone.0013559 -------------------------------------------------------------------------------- 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}