PROSITE documentation PDOC51358Nop domain profile
Description
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 α-helical (see <PDB:2OZB>) [1,2].
The profile we developed covers the entire Nop domain.
Last update:June 2012 / First entry.
-------------------------------------------------------------------------------
Technical section
PROSITE method (with tools and information) covered by this documentation:
References
1 | Authors | Aittaleb M. Rashid R. Chen Q. Palmer J.R. Daniels C.J. Li H. |
Title | Structure and function of archaeal box C/D sRNP core proteins. | |
Source | Nat. Struct. Biol. 10:256-263(2003). | |
PubMed ID | 12598892 | |
DOI | 10.1038/nsb905 |
2 | Authors | Liu S. Li P. Dybkov O. Nottrott S. Hartmuth K. Luehrmann R. Carlomagno T. Wahl M.C. |
Title | Binding of the human Prp31 Nop domain to a composite RNA-protein platform in U4 snRNP. | |
Source | Science 316:115-120(2007). | |
PubMed ID | 17412961 | |
DOI | 10.1126/science.1137924 |
Copyright
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 prosite_license.html.
Miscellaneous
View entry in original PROSITE document format
View entry in raw text format (no links)