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Q5X446 (RNC_LEGPA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 60. 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:lpp1834
OrganismLegionella pneumophila (strain Paris) [Complete proteome] [HAMAP]
Taxonomic identifier297246 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaLegionellalesLegionellaceaeLegionella

Protein attributes

Sequence length224 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 – 224224Ribonuclease 3 HAMAP-Rule MF_00104
PRO_0000228543

Regions

Domain5 – 127123RNase III
Domain154 – 22471DRBM

Sites

Active site441 Potential
Active site1161 By similarity
Metal binding401Magnesium By similarity
Metal binding1131Magnesium By similarity
Metal binding1161Magnesium By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5X446 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: 5F31B8993E74066C

FASTA22425,136
        10         20         30         40         50         60 
MKINLERLCR RLNYHFNNIA YLKQALTHCS AGSDNYERFE FLGDSILSFV IANELFNRFP 

        70         80         90        100        110        120 
LHSEGQLSRL RSFLVKGEML AEIAREIGLG DYLFLGQGEL RSGGFRRTSI LADALEAILA 

       130        140        150        160        170        180 
AIYLDGGMTA AKQIILMLYS SRLDDPDLNH CLKDAKTQLQ EFLQASKFAL PEYVLTKIEG 

       190        200        210        220 
DEHAQIFHVT CTIEGVSQVA YGTGPNRRKA EQLAAKAMLE QLQG 

« Hide

References

[1]"Evidence in the Legionella pneumophila genome for exploitation of host cell functions and high genome plasticity."
Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L., Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J., Glaser P., Buchrieser C.
Nat. Genet. 36:1165-1173(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Paris.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR628336 Genomic DNA. Translation: CAH12986.1.
RefSeqYP_124152.1. NC_006368.1.

3D structure databases

ProteinModelPortalQ5X446.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING297246.lpp1834.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAH12986; CAH12986; lpp1834.
GeneID3119653.
KEGGlpp:lpp1834.
PATRIC22324109. VBILegPne27771_2104.

Organism-specific databases

LegioListlpp1834.
CMRSearch...

Phylogenomic databases

eggNOGCOG0571.
HOGENOMHOG000246809.
KOK03685.
OMAAQKDPKT.
OrthoDBEOG6T1WVS.

Enzyme and pathway databases

BioCycLPNE297246:GCO9-2393-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_LEGPA
AccessionPrimary (citable) accession number: Q5X446
Entry history
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: November 23, 2004
Last modified: May 14, 2014
This is version 60 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