Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O67082 (RNC_AQUAE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribonuclease 3

EC=3.1.26.3
Alternative name(s):
Ribonuclease III
Short name=RNase III
Gene names
Name:rnc
Ordered Locus Names:aq_946
OrganismAquifex aeolicus (strain VF5) [Reference proteome] [HAMAP]
Taxonomic identifier224324 [NCBI]
Taxonomic lineageBacteriaAquificaeAquificalesAquificaceaeAquifex

Protein attributes

Sequence length221 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Also processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Ref.2 Ref.6

Catalytic activity

Endonucleolytic cleavage to 5'-phosphomonoester. HAMAP-Rule MF_00104

Cofactor

Binds 2 Mg2+ per subunit. Mn2+ also supports catalytic activity. Ref.2 Ref.3 Ref.4 Ref.6 Ref.7

Subunit structure

Homodimer. Ref.3 Ref.4 Ref.6

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00104.

Sequence similarities

Contains 1 DRBM (double-stranded RNA-binding) domain.

Contains 1 RNase III domain.

Biophysicochemical properties

Kinetic parameters:

KM=98 nM for 16S-u-hp RNA Ref.2

pH dependence:

Optimum pH is 8-9.

Temperature dependence:

Optimum temperature is 70-85 degrees Celsius.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 221221Ribonuclease 3 HAMAP-Rule MF_00104
PRO_0000180371

Regions

Domain4 – 121118RNase III
Domain151 – 21969DRBM

Sites

Active site441 Potential
Active site1101 Probable
Metal binding401Magnesium
Metal binding1071Magnesium
Metal binding1101Magnesium

Experimental info

Mutagenesis441D → N: Very low catalytic activity, binds RNA normally. Ref.6
Mutagenesis1101E → K: Loss of magnesium, alters ds-RNA binding, loss of activity. Ref.4 Ref.7
Mutagenesis1571Q → A: No RNase activity, no RNA binding. Ref.2

Secondary structure

.................................. 221
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O67082 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: ACB69735DB49641D

FASTA22126,100
        10         20         30         40         50         60 
MKMLEQLEKK LGYTFKDKSL LEKALTHVSY SKKEHYETLE FLGDALVNFF IVDLLVQYSP 

        70         80         90        100        110        120 
NKREGFLSPL KAYLISEEFF NLLAQKLELH KFIRIKRGKI NETIIGDVFE ALWAAVYIDS 

       130        140        150        160        170        180 
GRDANFTREL FYKLFKEDIL SAIKEGRVKK DYKTILQEIT QKRWKERPEY RLISVEGPHH 

       190        200        210        220 
KKKFIVEAKI KEYRTLGEGK SKKEAEQRAA EELIKLLEES E 

« Hide

References

« Hide 'large scale' references
[1]"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus."
Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.
Nature 392:353-358(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: VF5.
[2]"Characterization of Aquifex aeolicus ribonuclease III and the reactivity epitopes of its pre-ribosomal RNA substrates."
Shi Z., Nicholson R.H., Jaggi R., Nicholson A.W.
Nucleic Acids Res. 39:2756-2768(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: BIOPHYSICOCHEMICAL PROPERTIES, FUNCTION AS AN ENDORIBONUCLEASE, FUNCTION IN RRNA PRECURSOR PROCESSING, COFACTOR, RNA-BINDING, MUTAGENESIS OF GLN-157.
[3]"Crystallographic and modeling studies of RNase III suggest a mechanism for double-stranded RNA cleavage."
Blaszczyk J., Tropea J.E., Bubunenko M., Routzahn K.M., Waugh D.S., Court D.L., Ji X.
Structure 9:1225-1236(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-147 WITH AND WITHOUT MANGANESE, COFACTOR, SUBUNIT.
Strain: VF5.
[4]"Noncatalytic assembly of ribonuclease III with double-stranded RNA."
Blaszczyk J., Gan J., Tropea J.E., Court D.L., Waugh D.S., Ji X.
Structure 12:457-466(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-147 WITH MAGNESIUM, X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 1-220 WITH DS-RNA, RNA-BINDING, COFACTOR, SUBUNIT, MUTAGENESIS OF GLU-110.
Strain: VF5.
[5]"Intermediate states of ribonuclease III in complex with double-stranded RNA."
Gan J., Tropea J.E., Austin B.P., Court D.L., Waugh D.S., Ji X.
Structure 13:1435-1442(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH DS-RNA.
[6]"Structural insight into the mechanism of double-stranded RNA processing by ribonuclease III."
Gan J., Tropea J.E., Austin B.P., Court D.L., Waugh D.S., Ji X.
Cell 124:355-366(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH PRODUCT, FUNCTION AS AN RNASE, COFACTOR, SUBUNIT, RNA-BINDING, MUTAGENESIS OF ASP-44.
[7]"A stepwise model for double-stranded RNA processing by ribonuclease III."
Gan J., Shaw G., Tropea J.E., Waugh D.S., Court D.L., Ji X.
Mol. Microbiol. 67:143-154(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH PRODUCT AND MAGNESIUM, COFACTOR, MUTAGENESIS OF GLU-110.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000657 Genomic DNA. Translation: AAC07049.1.
PIRG70381.
RefSeqNP_213645.1. NC_000918.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1I4SX-ray2.15A/B1-147[»]
1JFZX-ray2.10A/B/C/D1-147[»]
1RC5X-ray2.30A/B/C/D1-147[»]
1RC7X-ray2.15A1-220[»]
1YYKX-ray2.50A/B1-221[»]
1YYOX-ray2.90A/B1-221[»]
1YYWX-ray2.80A/B/C/D1-221[»]
1YZ9X-ray2.10A/B1-221[»]
2EZ6X-ray2.05A/B1-221[»]
2NUEX-ray2.90A/B1-221[»]
2NUFX-ray2.50A/B1-221[»]
2NUGX-ray1.70A/B1-221[»]
4M2ZX-ray2.85A/B1-221[»]
4M30X-ray2.50A/B1-221[»]
ProteinModelPortalO67082.
SMRO67082. Positions 1-221.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-48455N.
STRING224324.aq_946.

Proteomic databases

PRIDEO67082.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC07049; AAC07049; aq_946.
GeneID1193624.
KEGGaae:aq_946.
PATRIC20959242. VBIAquAeo85532_0743.

Phylogenomic databases

eggNOGCOG0571.
HOGENOMHOG000246808.
KOK03685.
OMALTHKSCK.
OrthoDBEOG6T1WVS.
ProtClustDBCLSK2748388.

Enzyme and pathway databases

BioCycAAEO224324:GJBH-678-MONOMER.
BRENDA3.1.26.3. 396.

Family and domain databases

Gene3D1.10.1520.10. 1 hit.
3.30.160.20. 1 hit.
HAMAPMF_00104. RNase_III.
InterProIPR014720. dsRNA-bd_dom.
IPR011907. RNase_III.
IPR000999. RNase_III_dom.
[Graphical view]
PANTHERPTHR11207. PTHR11207. 1 hit.
PfamPF00035. dsrm. 1 hit.
PF00636. Ribonuclease_3. 1 hit.
[Graphical view]
SMARTSM00358. DSRM. 1 hit.
SM00535. RIBOc. 1 hit.
[Graphical view]
SUPFAMSSF69065. SSF69065. 1 hit.
TIGRFAMsTIGR02191. RNaseIII. 1 hit.
PROSITEPS50137. DS_RBD. 1 hit.
PS00517. RNASE_3_1. 1 hit.
PS50142. RNASE_3_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO67082.

Entry information

Entry nameRNC_AQUAE
AccessionPrimary (citable) accession number: O67082
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: April 16, 2014
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references