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Q52698 (RNC_RHOCA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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
OrganismRhodobacter capsulatus (Rhodopseudomonas capsulata)
Taxonomic identifier1061 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter

Protein attributes

Sequence length228 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Digests double-stranded RNA. Involved in the processing of ribosomal RNA precursors and of some mRNAs. Complements an E.coli disruption mutant, but the E.coli enzyme does not cleave R.capsulatus rRNA precursor, showing substrate recognition is different. Probably also processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Ref.1 Ref.2 Ref.3

Catalytic activity

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

Cofactor

Mg2+. Ref.3

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00104

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00104.

Disruption phenotype

Loss of processing of 23S rRNA. Full complementation requires both lep and rnc genes, suggesting they form an operon. Ref.1

Miscellaneous

The protein in strain DMS 938 / 37b4 has 5 other sequence differences. In Rhodobacter species, 23S rRNA is further processed to 16S and 14S rRNA species in vivo, probably by RNase III.

Sequence similarities

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

Contains 1 RNase III domain.

Biophysicochemical properties

pH dependence:

Optimum pH is 7.5 at 32 degrees Celsius. Ref.3

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 228228Ribonuclease 3 HAMAP-Rule MF_00104
PRO_0000180427

Regions

Domain7 – 132126RNase III
Domain157 – 22670DRBM

Sites

Active site491 Potential
Active site1211 By similarity
Metal binding451Magnesium By similarity
Metal binding1181Magnesium By similarity
Metal binding1211Magnesium By similarity

Natural variations

Natural variant621H → D in strain: DSM 938.

Sequences

Sequence LengthMass (Da)Tools
Q52698 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 8B4AEFF3434E699C

FASTA22824,663
        10         20         30         40         50         60 
MKVAADLSAF MDRLGHRFTT PEHLVRALTH SSLGSATRPD NQRLEFLGDR VLGLSMAEAL 

        70         80         90        100        110        120 
FHADGRASEG QLAPRFNALV RKETCAAVAR DIDLGAVLKL GRSEMMSGGR RKDALLGDAM 

       130        140        150        160        170        180 
EAVIAAVYLD AGFEVARALV LRLWAARIQS VDNDARDPKT ALQEWAQARG LPPPRYETLG 

       190        200        210        220 
RDGPDHAPQF RIAVVLASGE TEEAQAGSKR NAEQAAAKAL LERLERGA 

« Hide

References

[1]"Identification and analysis of the rnc gene for RNase III in Rhodobacter capsulatus."
Rauhut R., Jaeger A., Conrad C., Klug G.
Nucleic Acids Res. 24:1246-1251(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN RRNA PROCESSING, EXPRESSION IN E.COLI, DISRUPTION PHENOTYPE.
Strain: ATCC 33303 / B10 and DSM 938 / 37b4.
[2]"Cloning of a gene involved in rRNA precursor processing and 23S rRNA cleavage in Rhodobacter capsulatus."
Kordes E., Jock S., Fritsch J., Bosch F., Klug G.
J. Bacteriol. 176:1121-1127(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
Strain: DSM 938 / 37b4.
[3]"Different cleavage specificities of RNases III from Rhodobacter capsulatus and Escherichia coli."
Conrad C., Rauhut R., Klug G.
Nucleic Acids Res. 26:4446-4453(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, FUNCTION IN RRNA PROCESSING, RRNA-BINDING, SUBSTRATE SPECIFICITY.
Strain: ATCC 33303 / B10.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z68305 Genomic DNA. Translation: CAA92647.1.
PIRS66596.

3D structure databases

ProteinModelPortalQ52698.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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.
PF14622. Ribonucleas_3_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...

Entry information

Entry nameRNC_RHOCA
AccessionPrimary (citable) accession number: Q52698
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: May 14, 2014
This is version 73 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