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Q2YN02 (RNC_BRUA2) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 50. 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:BAB1_0681
OrganismBrucella abortus (strain 2308) [Complete proteome] [HAMAP]
Taxonomic identifier359391 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella

Protein attributes

Sequence length245 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 By similarity. HAMAP-Rule MF_00104

Catalytic activity

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

Cofactor

Mg2+ By similarity. HAMAP-Rule MF_00104

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00104

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00104.

Sequence similarities

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

Contains 1 RNase III domain.

Ontologies

Keywords
   Biological processmRNA processing
rRNA processing
tRNA processing
   Cellular componentCytoplasm
   LigandMagnesium
Metal-binding
RNA-binding
rRNA-binding
   Molecular functionEndonuclease
Hydrolase
Nuclease
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processmRNA processing

Inferred from electronic annotation. Source: UniProtKB-HAMAP

rRNA catabolic process

Inferred from electronic annotation. Source: InterPro

rRNA processing

Inferred from electronic annotation. Source: UniProtKB-HAMAP

tRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

rRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

ribonuclease III activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 245245Ribonuclease 3 HAMAP-Rule MF_00104
PRO_0000228510

Regions

Domain19 – 144126RNase III
Domain169 – 23870DRBM

Sites

Active site611 Potential
Active site1331 By similarity
Metal binding571Magnesium By similarity
Metal binding1301Magnesium By similarity
Metal binding1331Magnesium By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2YN02 [UniParc].

Last modified February 7, 2006. Version 1.
Checksum: 084ED2D3A3F16BFC

FASTA24527,220
        10         20         30         40         50         60 
MNRTRPLPEI KMVSANKTAS ILEERTGHRF LNLKRLERAL THSSVQAPAR ANYERLEFLG 

        70         80         90        100        110        120 
DRVLGLTVAE MLFEAFPEAS EGELSVRLNA LVNAETCAAI ADEIGLADLI HTGSDIKSLN 

       130        140        150        160        170        180 
DKRLLNVRAD VVEALIATIY LDGGLEAARS FIQRYWKKRS LETGAARRDA KTELQEWAHQ 

       190        200        210        220        230        240 
QGNVHPVYAI LSRSGPDHDP LFLVEVTVKG FAPEKGEGRS KRIAEQSAAE AMLYREGVWK 


RDGSA 

« Hide

References

[1]"Whole-genome analyses of speciation events in pathogenic Brucellae."
Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A., Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.
Infect. Immun. 73:8353-8361(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 2308.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM040264 Genomic DNA. Translation: CAJ10637.1.
RefSeqYP_414123.1. NC_007618.1.

3D structure databases

ProteinModelPortalQ2YN02.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING359391.BAB1_0681.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAJ10637; CAJ10637; BAB1_0681.
GeneID3788905.
KEGGbmf:BAB1_0681.
PATRIC17844256. VBIBruMel86222_0711.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0571.
HOGENOMHOG000246809.
KOK03685.
OMAAQKDPKT.
OrthoDBEOG6T1WVS.

Enzyme and pathway databases

BioCycBABO359391:GKDV-690-MONOMER.
BMEL359391:GJOQ-690-MONOMER.

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_BRUA2
AccessionPrimary (citable) accession number: Q2YN02
Entry history
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: February 7, 2006
Last modified: May 14, 2014
This is version 50 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

Brucella abortus strain 2308

Brucella abortus (strain 2308): entries and gene names