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PROSITE documentation PDOC51327 [for PROSITE entry PS51327]

Dicer double-stranded RNA-binding fold domain profile





Description

RNA interference (RNAi) is an ancient gene-silencing process that plays a fundamental role in diverse eukaryotic functions including viral defense, chromatin remodeling, genome rearrangement, developmental timing, brain morphogenesis, and stem cell maintenance. All RNAi pathways require the multidomain ribonuclease Dicer, which initiates RNAi by cleaving double-stranded RNA (dsRNA) substrates into small fragments ~25 nuleotides in length. A typical eukaryotic Dicer consists of a helicase domain (see <PDOC51192>), a domain of unknown function, and a PAZ domain (see <PDOC50821>) at the amino (N)-terminus as well as two ribonuclease III domains (see <PDOC00448>) and a dsRNA-binding domain (dsRBD) (see <PDOC50137>) at the carboxy (C)-terminus. The domain of unknown function of ~100 amino acids is predicted to adopt the canonical α-β-β-β-α-fold found in all dsRBDs [1,2,3,4].

The profile we developed covers the entire Dicer dsRNA-binding fold domain.

Last update:

August 2007 / First entry.

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Technical section

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

DICER_DSRBF, PS51327; Dicer double-stranded RNA-binding fold domain profile  (MATRIX)


References

1AuthorsMacRae I.J. Zhou K. Li F. Repic A. Brooks A.N. Cande W.Z. Adams P.D. Doudna J.A.
TitleStructural basis for double-stranded RNA processing by Dicer.
SourceScience 311:195-198(2006).
PubMed ID16410517
DOI10.1126/science.1121638

2AuthorsDlakic M.
TitleDUF283 domain of Dicer proteins has a double-stranded RNA-binding fold.
SourceBioinformatics 22:2711-2714(2006).
PubMed ID16954143
DOI10.1093/bioinformatics/btl468

3AuthorsBateman A. Finn R.D.
TitleSCOOP: a simple method for identification of novel protein superfamily relationships.
SourceBioinformatics 23:809-814(2007).
PubMed ID17277330
DOI10.1093/bioinformatics/btm034

4AuthorsYe X. Paroo Z. Liu Q.
TitleFunctional anatomy of the Drosophila microRNA-generating enzyme.
SourceJ. Biol. Chem. 0:0-0(2007).
PubMed ID17666393
DOI10.1074/jbc.M705208200



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