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Q2KWY0 (RNC_BORA1) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 37. 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
Ordered Locus Names:BAV1131
OrganismBordetella avium (strain 197N) [Complete proteome] [HAMAP]
Taxonomic identifier360910 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella

Protein attributes

Sequence length251 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Digests double-stranded RNA. Involved in the processing of ribosomal RNA precursors and of some mRNAs By similarity. HAMAP MF_00104

Catalytic activity

Endonucleolytic cleavage to 5'-phosphomonoester. HAMAP MF_00104

Subcellular location

Cytoplasm By similarity HAMAP MF_00104.

Sequence similarities

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

Contains 1 RNase III domain.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandRNA-binding
   Molecular functionEndonuclease
Hydrolase
Nuclease
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processRNA processing

Inferred from electronic annotation. Source: InterPro

rRNA catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functiondouble-stranded RNA binding

Inferred from electronic annotation. Source: InterPro

ribonuclease III activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 251251Ribonuclease 3 HAMAP MF_00104
PRO_1000075727

Regions

Domain3 – 125123RNase III
Domain152 – 22271DRBM

Sequences

Sequence LengthMass (Da)Tools
Q2KWY0 [UniParc].

Last modified March 7, 2006. Version 1.
Checksum: 2822E847AD14BFFE

FASTA25127,144
        10         20         30         40         50         60 
MSLATLETRL GHHFGDQALL EQALTHRSHG ARHNERLEFL GDSVLNFVVA AMLFERYAKL 

        70         80         90        100        110        120 
DEGDLSRVRA NLVKQASLAD IAQRLELSPY LRLGEGEMKS GGFRRPSILA DAVEALFGAV 

       130        140        150        160        170        180 
FLDAGFDAAR KVIEQQYVPV LANVDPETLG KDAKTLLQEF LQGRKLALPL YTVVATHGAA 

       190        200        210        220        230        240 
HSQQFEVECA IPALEIKVTA AGASRRAAEQ SAAKLALEAA LVVSPRATRK GGRARKTAQL 

       250 
SLPVAVAQEV K 

« Hide

References

[1]"Comparison of the genome sequence of the poultry pathogen Bordetella avium with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals extensive diversity in surface structures associated with host interaction."
Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J., Parkhill J., Temple L.M.
J. Bacteriol. 188:6002-6015(2006) [PubMed: 16885469] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 197N.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM167904 Genomic DNA. Translation: CAJ48740.1.
RefSeqYP_785654.1. NC_010645.1.

3D structure databases

HSSPHSSP built from PDB template 1O0W based on UniProtKB Q9X0I6.
ProteinModelPortalQ2KWY0.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ2KWY0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6267285.
GenomeReviewsGene locus BAV1131 in contig AM167904_GR.
KEGGbav:BAV1131.
NMPDRfig|521.1.peg.618.
PATRIC21128470. VBIBorAvi43433_1159.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG744556.
OMAALTHKSF.
ProtClustDBPRK00102.

Enzyme and pathway databases

BioCycABAU360910:BAV1131-MONOMER.

Family and domain databases

HAMAPMF_00104. RNase_III.
[Tree]
InterProIPR001159. Ds-RNA-bd.
IPR014720. dsRNA-bd-like.
IPR000999. RNase_III.
IPR011907. RNase_III_bac.
[Graphical view]
Gene3DG3DSA:3.30.160.20. dsRNA-bd-like. 1 hit.
G3DSA:1.10.1520.10. RNase_III. 1 hit.
KOK03685.
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. RNase_III. 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_BORA1
AccessionPrimary (citable) accession number: Q2KWY0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: March 7, 2006
Last modified: January 25, 2012
This is version 37 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