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We are deeply saddened by the passing of Amos Bairoch (1957–2025), the creator of PROSITE. We wish to dedicate our latest paper, published shortly before his death, to him. He will always be a source of inspiration to us.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
Amos Bairoch

PROSITE documentation PDOC51358
Nop domain profile


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PURL: https://purl.expasy.org/prosite/documentation/PDOC51358

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.

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Technical section

PROSITE method (with tools and information) covered by this documentation:

NOP, PS51358; Nop domain profile  (MATRIX)


References

1AuthorsAittaleb M. Rashid R. Chen Q. Palmer J.R. Daniels C.J. Li H.
TitleStructure and function of archaeal box C/D sRNP core proteins.
SourceNat. Struct. Biol. 10:256-263(2003).
PubMed ID12598892
DOI10.1038/nsb905

2AuthorsLiu S. Li P. Dybkov O. Nottrott S. Hartmuth K. Luehrmann R. Carlomagno T. Wahl M.C.
TitleBinding of the human Prp31 Nop domain to a composite RNA-protein platform in U4 snRNP.
SourceScience 316:115-120(2007).
PubMed ID17412961
DOI10.1126/science.1137924



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