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A8A377 (RNC_ECOHS) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 43. 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:EcHS_A2722
OrganismEscherichia coli O9:H4 (strain HS) [Complete proteome] [HAMAP]
Taxonomic identifier331112 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length226 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 – 226226Ribonuclease 3 HAMAP-Rule MF_00104
PRO_1000075746

Regions

Domain6 – 128123RNase III
Domain155 – 22571DRBM

Sites

Active site451 Potential
Active site1171 By similarity
Metal binding411Magnesium By similarity
Metal binding1141Magnesium By similarity
Metal binding1171Magnesium By similarity

Sequences

Sequence LengthMass (Da)Tools
A8A377 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: D9E2858F2E0AA3A5

FASTA22625,550
        10         20         30         40         50         60 
MNPIVINRLQ RKLGYTFNHQ ELLQQALTHR SASSKHNERL EFLGDSILSY VIANALYHRF 

        70         80         90        100        110        120 
PRVDEGDMSR MRATLVRGNT LAELAREFEL GECLRLGPGE LKSGGFRRES ILADTVEALI 

       130        140        150        160        170        180 
GGVFLDSDIQ TVEKLILNWY QTRLDEISPG DKQKDPKTRL QEYLQGRHLP LPTYLVVQVR 

       190        200        210        220 
GEAHDQEFTI HCQVSGLSEP VVGTGSSRRK AEQAAAEQAL KKLELE 

« Hide

References

[1]"The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates."
Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J.
J. Bacteriol. 190:6881-6893(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000802 Genomic DNA. Translation: ABV06981.1.
RefSeqYP_001459364.1. NC_009800.1.

3D structure databases

ProteinModelPortalA8A377.
SMRA8A377. Positions 5-224.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING331112.EcHS_A2722.

Proteomic databases

PRIDEA8A377.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABV06981; ABV06981; EcHS_A2722.
GeneID5592591.
KEGGecx:EcHS_A2722.
PATRIC18315425. VBIEscCol77814_2667.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0571.
HOGENOMHOG000246809.
KOK03685.
OMAAQKDPKT.
OrthoDBEOG6T1WVS.

Enzyme and pathway databases

BioCycECOL331112:GHHI-2707-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_ECOHS
AccessionPrimary (citable) accession number: A8A377
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: October 23, 2007
Last modified: May 14, 2014
This is version 43 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