{PDOC51358} {PS51358; NOP} {BEGIN} ********************** * Nop domain profile * ********************** The ~120-residue Nop domain is present in various pre-RNA processing ribonucleoproteins (RNP): - Eukaryotic Prp31, part of a tri-snRNP complex. It is involved in pre-mRNA splicing. - Eukaryotic Nucleolar proteins 56 and 58 (Nop56 and Nop58), components of box C/D small nucleolar ribonucleoprotein (snoRNP) particles. - Archaeal Nop5, an homolog of Nop56/Nop58. The Nop domain is a RNP binding module, exhibiting RNA and protein binding surfaces. It is oval-shaped and exclusively alpha-helical (see ) [1,2]. The profile we developed covers the entire Nop domain. -Sequences known to belong to this class detected by the profile: ALL. -Other sequence(s) detected in Swiss-Prot: NONE. -Last update: June 2012 / First entry. [ 1] Aittaleb M., Rashid R., Chen Q., Palmer J.R., Daniels C.J., Li H. "Structure and function of archaeal box C/D sRNP core proteins." Nat. Struct. Biol. 10:256-263(2003). PubMed=12598892; DOI=10.1038/nsb905 [ 2] Liu S., Li P., Dybkov O., Nottrott S., Hartmuth K., Luehrmann R., Carlomagno T., Wahl M.C. "Binding of the human Prp31 Nop domain to a composite RNA-protein platform in U4 snRNP." Science 316:115-120(2007). PubMed=17412961; DOI=10.1126/science.1137924 -------------------------------------------------------------------------------- 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}