Bioinformatics. 2006 Nov 15;22(22):2711-4. Epub 2006 Sep 5.

DUF283 domain of Dicer proteins has a double-stranded RNA-binding fold.

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Department of Microbiology, Montana State University Bozeman, MT 59717, USA. mdlakic@montana.edu

Abstract

Two RNases, Dicer and Argonaute, are at the heart of the RNA interference (RNAi) molecular machinery responsible for gene silencing. Both RNases contain multiple domains, most of which have been characterized or have functions that can be predicted based on sequence comparisons. However, Dicers of higher eukaryotes contain the domain known as DUF283 which at present has no assigned role. Using sensitive profile-profile comparisons, we detected a divergent double-stranded RNA-binding domain coinciding with the DUF283 of Dicer. This finding has potential implications regarding the mechanistic role of Dicer in RNAi.

PMID:: 16954143; [PubMed - indexed for MEDLINE]

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DUF283 domain of Dicer proteins has a double-stranded RNA-binding fold.

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