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InterPro: IPR000999 Ribonuclease III

Protein matchesHelp
UniProtKB
Matches:
3134 proteins
AccessionHelp IPR000999 RNase_III
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Found in IPR008226 Uncharacterised conserved protein UCP005520
IPR011907 Ribonuclease III, bacterial
GO Term annotationHelp
Process GO:0006396 RNA processing
Function GO:0003723 RNA binding
GO:0004525 ribonuclease III activity
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

Prokaryotic ribonuclease III (EC:3.1.26.3) (gene rnc) [1] is an enzyme that digests double-stranded RNA. It is involved in the processing of ribosomal RNA precursors and of some mRNAs. RNase III is evolutionary related to a number of proteins including [2]:

  • Saccharomyces cerevisiae (Baker's yeast) protein pac1, a ribonuclease that probably inhibits mating and meiosis by degrading a specific mRNA required for sexual development
  • yeast ribonuclease III (gene RNT1), a dsRNA-specific nuclease that cleaves eukaryotic preribosomal RNA at various sites
  • Caenorhabditis elegans hypothetical protein F26E4.13
  • Paramecium bursaria Chlorella virus 1 (PBCV-1) 1 protein A464R
  • Synechocystis sp. (strain PCC 6803) hypothetical protein slr0346
  • yeast hypothetical protein SpAC8A4.08c, a protein with a N-terminal helicase domain and a C-terminal RNase III domain
  • C. elegans hypothetical protein K12H4.8, a protein with the same structure as SpAC8A4.08c

Structural linksHelp
SCOP: a.149.1.1
CATH: 1.10.1520.10
Database linksHelp
PDBe-motif: PS00517
Enzyme: EC:3.1.26.3
PROSITE doc: PDOC00448
PANDIT: PF00636
Blocks: IPB000999
InteractionsHelp
This domain has been experimentally proven to be involved in Protein:Protein interactions.
Representative data is shown with the following example proteins:

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR000999 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
O01326 Ribonuclease 3

Q02555 Ribonuclease 3

Q8R418 Endoribonuclease Dicer

Q9UPY3 Endoribonuclease Dicer

Q9VCU9 Endoribonuclease Dcr-1

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR005034 Dicer double-stranded RNA-binding fold
IPR003100 Argonaute/Dicer protein, PAZ
IPR001159 Double-stranded RNA binding
IPR014021 Helicase, superfamily 1/2, ATP-binding domain
IPR000999 Ribonuclease III
IPR001650 DNA/RNA helicase, C-terminal
IPR011545 DNA/RNA helicase, DEAD/DEAH box type, N-terminal
IPR014001 DEAD-like helicase, N-terminal
IPR014720 Double-stranded RNA-binding-like
PDB Chain
ModBase
CATH Domain
SWISS-MODEL
SCOP Domain

PublicationsHelp
1. Nashimoto H, Uchida H.
DNA sequencing of the Escherichia coli ribonuclease III gene and its mutations.
Mol. Gen. Genet. 201 25-9 1985 [PubMed: 3903434]
http://dx.doi.org/10.1007/BF00397981
2. Mian IS.
Comparative sequence analysis of ribonucleases HII, III, II PH and D.
Nucleic Acids Res. 25 3187-95 1997 [PubMed: 9241229]
http://dx.doi.org/10.1093/nar/25.16.3187

Additional ReadingHelp
Gan J, Tropea JE, Austin BP, Court DL, Waugh DS, Ji X.
Intermediate states of ribonuclease III in complex with double-stranded RNA.
Structure 13 2005 1435-42 [PubMed: 16216575]
http://dx.doi.org/10.1016/j.str.2005.06.014
Blaszczyk J, Gan J, Tropea JE, Court DL, Waugh DS, Ji X.
Noncatalytic assembly of ribonuclease III with double-stranded RNA.
Structure 12 2004 457-66 [PubMed: 15016361]
http://dx.doi.org/10.1016/j.str.2004.02.004
Gan J, Shaw G, Tropea JE, Waugh DS, Court DL, Ji X.
A stepwise model for double-stranded RNA processing by ribonuclease III.
Mol. Microbiol. 67 2008 143-54 [PubMed: 18047582]
Gan J, Tropea JE, Austin BP, Court DL, Waugh DS, Ji X.
Structural insight into the mechanism of double-stranded RNA processing by ribonuclease III.
Cell 124 2006 355-66 [PubMed: 16439209]
http://dx.doi.org/10.1016/j.cell.2005.11.034
Tahbaz N, Kolb FA, Zhang H, Jaronczyk K, Filipowicz W, Hobman TC.
Characterization of the interactions between mammalian PAZ PIWI domain proteins and Dicer.
EMBO Rep. 5 2004 189-94 [PubMed: 14749716]
http://dx.doi.org/10.1038/sj.embor.7400070
Blaszczyk J, Tropea JE, Bubunenko M, Routzahn KM, Waugh DS, Court DL, Ji X.
Crystallographic and modeling studies of RNase III suggest a mechanism for double-stranded RNA cleavage.
Structure 9 2001 1225-36 [PubMed: 11738048]
http://dx.doi.org/10.1016/S0969-2126(01)00685-2
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InterPro 23.1