Ribonuclease III

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Ribonuclease III domain
Ribonuclease III structure interacting with double stranded RNA.
Identifiers
SymbolRNase_III
PfamPF00636
InterProIPR000999
PROSITEPDOC00448
SCOP21jfz / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
PDB1o0wB:51-141 2a11A:41-134 1jfzA:37-121

1rc7A:37-121 1yywA:37-121 1i4sA:37-121 1rc5B:37-121 1yyoA:37-121 1yykB:37-121

1yz9A:37-121 2fflA:333-418 1u61A:10-111

RNase III is a type of ribonuclease that specifically binds to and cleaves double-stranded RNA (dsRNA).[1] There are four subdivisions, known as Class 1, 2, 3, and 4.

Prokaryotic ribonuclease III (EC 3.1.26.3) (gene rnc)[2] is an enzyme that digests double-stranded RNA. It is involved in the processing of ribosomal RNA precursors and of some mRNAs.

Human proteins containing this domain

DICER1; MRPL44; RNASEN;

See also

External links

References

  1. ^ Lamontagne, B.; Larose, S.; Boulanger, J.; Elela, S. (2001). "The RNase III family: A conserved structure and expanding functions in eukaryotic dsRNA metabolism". Current issues in molecular biology. 3 (4): 71–78. PMID 11719970.
  2. ^ Nashimoto H, Uchida H (1985). "DNA sequencing of the Escherichia coli ribonuclease III gene and its mutations". Mol. Gen. Genet. 201 (1): 25–29. doi:10.1007/bf00397981. PMID 3903434.
  3. ^ Filippov V, Solovyev V, Filippova M, Gill SS (Mar 2000). "A novel type of RNase III family proteins in eukaryotes". Gene. 245 (1): 213–221. doi:10.1016/S0378-1119(99)00571-5. PMID 10713462.
  4. ^ Bernstein E, Caudy AA, Hammond SM, Hannon GJ (2001). "Role for a bidentate ribonuclease in the initiation step of RNA interference". Nature. 409 (6818): 363–6. doi:10.1038/35053110. PMID 11201747.
  5. ^ Glow, D.; Pianka, D.; Sulej, A. A.; Kozlowski, Lukasz P.; Czarnecka, J.; Chojnowski, G.; Skowronek, K. J.; Bujnicki, J. M. (2015). "Sequence-specific cleavage of dsRNA by Mini-III RNase". Nucleic Acids Research. 43 (5): 2864–2873. doi:10.1093/nar/gkv009. ISSN 0305-1048. PMID 25634891.
This article incorporates text from the public domain Pfam and InterPro: IPR000999