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Ribonuclease-III-like
Members of this family are involved in rDNA transcription and rRNA processing. They probably also cleave a stem-loop structure at the 3' end of U2 snRNA to ensure formation of the correct U2 3' end; they are involved in polyadenylation-independent transcription termination. Some members may be mitochondrial ribosomal protein subunit L15, others may be 60S ribosomal protein L3. (from Pfam)
putative dsRNA-binding protein
Sequences gathered for seed by HMM_iterative_training Putative motif shared by proteins that bind to dsRNA. At least some DSRM proteins seem to bind to specific RNA targets. Exemplified by Staufen, which is involved in localisation of at least five different mRNAs in the early Drosophila embryo. Also by interferon-induced protein kinase in humans, which is part of the cellular response to dsRNA. [1]. 8036511. Conserved structures and diversity of functions of RNA-binding proteins. Burd CG, Dreyfuss G;. Science 1994;265:615-621. (from Pfam)
ribonuclease III domain-containing protein
ribonuclease III family protein
ribonuclease III family protein similar to ribonuclease III, which digests double-stranded RNA in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S)
ribonuclease III
This family consists of bacterial examples of ribonuclease III. This enzyme cleaves double-stranded rRNA. It is involved in processing ribosomal RNA precursors. It is found even in minimal genones such as Mycoplasma genitalium and Buchnera aphidicola, and in some cases has been shown to be an essential gene. These bacterial proteins contain a double-stranded RNA binding motif (PF00035) and a ribonuclease III domain (PF00636). Eukaryotic homologs tend to be much longer proteins with additional domains, localized to the nucleus, and not included in this family.
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