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

Q46Z18 (RNC_CUPPJ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 54. 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:Reut_A2252
OrganismCupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Ralstonia eutropha (strain JMP 134)) [Complete proteome] [HAMAP]
Taxonomic identifier264198 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus

Protein attributes

Sequence length256 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 – 256256Ribonuclease 3 HAMAP-Rule MF_00104
PRO_0000228571

Regions

Domain3 – 125123RNase III
Domain152 – 22271DRBM

Sites

Active site421 Potential
Active site1141 By similarity
Metal binding381Magnesium By similarity
Metal binding1111Magnesium By similarity
Metal binding1141Magnesium By similarity

Sequences

Sequence LengthMass (Da)Tools
Q46Z18 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: E392B0948A1538D2

FASTA25628,529
        10         20         30         40         50         60 
MNLDALQQRL GYRFSKPELL QQALTHRSHS AQHNERLEFL GDSVLNCAVA DMLFGMFGKL 

        70         80         90        100        110        120 
DEGDLSRVRA NLVKQQALYE IAQMLQLSEV LRLGEGELKS GGFRRPSILA DALEAIVGAV 

       130        140        150        160        170        180 
FLDAGFEAAR TLIRKLYIPI LEQVDPRTLG KDAKTLLQEY LQGHKIALPQ YNVIATHGAA 

       190        200        210        220        230        240 
HSQQFEVECM VPKLEVRVFG TGASRRAAEQ AAAKLALDEV QKLVPQLLKR SRAERTGKTR 

       250 
KQPVPPDPQL SLRLKE 

« Hide

References

[1]"Complete sequence of chromosome 1 of Ralstonia eutropha JMP134."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Goltsman E., Martinez M., Schmutz J., Larimer F., Land M., Lykidis A., Richardson P.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JMP134 / LMG 1197.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000090 Genomic DNA. Translation: AAZ61615.1.
RefSeqYP_296459.1. NC_007347.1.

3D structure databases

ProteinModelPortalQ46Z18.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING264198.Reut_A2252.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ61615; AAZ61615; Reut_A2252.
GeneID3610595.
KEGGreu:Reut_A2252.
PATRIC20230119. VBIRalEut24049_2901.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0571.
HOGENOMHOG000246809.
KOK03685.
OMAHRFPKVN.
OrthoDBEOG6T1WVS.

Enzyme and pathway databases

BioCycCPIN264198:GIW3-2290-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_CUPPJ
AccessionPrimary (citable) accession number: Q46Z18
Entry history
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: September 13, 2005
Last modified: May 14, 2014
This is version 54 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