A0A059GBG5 · A0A059GBG5_9PROT

Function

function

Endoribonuclease that plays a central role in RNA processing and decay. Required for the maturation of 5S and 16S rRNAs and the majority of tRNAs. Also involved in the degradation of most mRNAs.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

  • Endonucleolytic cleavage of single-stranded RNA in A- and U-rich regions.
    EC:3.1.26.12 (UniProtKB | ENZYME | Rhea)

Cofactor

Protein has several cofactor binding sites:
Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Binds 1 Mg2+ ion per subunit.
Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 2 Zn2+ ions per homotetramer.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site387Mg2+ (UniProtKB | ChEBI); catalytic
Binding site430Mg2+ (UniProtKB | ChEBI); catalytic
Binding site488Zn2+ (UniProtKB | ChEBI); ligand shared between dimeric partners
Binding site491Zn2+ (UniProtKB | ChEBI); ligand shared between dimeric partners

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentcytoplasmic side of plasma membrane
Molecular Functionmagnesium ion binding
Molecular Functionribonuclease E activity
Molecular FunctionRNA endonuclease activity
Molecular FunctionrRNA binding
Molecular FunctiontRNA binding
Molecular Functionzinc ion binding
Biological ProcessmRNA catabolic process
Biological ProcessrRNA processing
Biological ProcesstRNA processing

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Ribonuclease E
  • EC number
  • Short names
    RNase E

Gene names

    • Name
      rne
    • ORF names
      HOC_02036

Organism names

  • Taxonomic identifier
  • Strain
    • SCH89
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Hyphomonadales > Hyphomonadaceae > Hyphomonas

Accessions

  • Primary accession
    A0A059GBG5

Proteomes

Subcellular Location

Cytoplasm
Cell inner membrane
; Peripheral membrane protein

Keywords

Interaction

Subunit

Homotetramer formed by a dimer of dimers.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, region, compositional bias.

TypeIDPosition(s)Description
Domain38-203S1 motif
Region96-172Disordered
Compositional bias98-143Acidic residues
Compositional bias144-172Basic and acidic residues
Region488-491Required for zinc-mediated homotetramerization and catalytic activity
Compositional bias567-581Basic and acidic residues
Region567-887Disordered
Compositional bias598-622Acidic residues
Compositional bias665-679Acidic residues
Compositional bias680-697Basic and acidic residues
Compositional bias773-790Basic and acidic residues
Compositional bias860-887Basic and acidic residues

Sequence similarities

Belongs to the RNase E/G family. RNase E subfamily.
Belongs to the RNase E/G family. RNase G subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    887
  • Mass (Da)
    96,924
  • Last updated
    2014-07-09 v1
  • Checksum
    32E6D78D983676C9
MSKLMLIDAAHPEETRVAIVNGGQVDDFDFETTGNEQLRGNIYLAKVTRVEPSLQAAFVEYGGNRHGFLAFSEIHPDYYQLPAEDREALLKEAAEEAAAQIEDEDDDDIEGDEDAHADADDSDDSDDDASDDDEDDGDDESEDGESKASAKPARGRRPARKESPRSSISKRYKIQEVIRRRQVMLVQVVKEERGNKGAALTTFLSLAGRYSVLMPNTPRGGGISRKIVNGADRKRLKSIVAELDVPDGMGLIVRTAGAKRTKAEIKRDYEYLSKLWETIVEKTLTSEAPMLINAEGGLVHRAMRDMFDKEIEEVWVQGDEAYREAKDLAKLIMPSQAKKVQQWKEGDPLFVSEAVEDQLDSIYSPTVQLKSGGYLVINQTEALVAIDVNSGKSTKERNIEQTAVRTNLEAAEEACRQMRLRDLAGLVVIDFIDMDENKNNRAVEKKLKECLKVDRARVQHGRISQFGLMEISRQRRRQGVLQATSDPCEACNGTGRRRSIPSAALQLIRAIEARASTGGLKSISVKAPTDVALYILNQKREALIEIERMAGFAVSIHSSEDLLPGDFMIDAERDPNSKPKKKSPPRSLSKSTKPAVSDEDDDEDIEDEDDEAVAETDDEAEDKAEDTQGKPRKRRRRRGGRGRNRDARDTGLEVIDGETAPAAASSDDDSDDDADDEGEGGNAPEARSDDSEEAGRKRRRRGRRGGRRRRRSGGEDRAEGAQEGAPTDGGAYLDGLSASAPEMLDAEAPSDAKPEEAPAPATEASEPAPAKAAEVEADTDTDEPVKAEKPKRARRSRAKPKPEAEAPAAEAAPAPVETKAAPEPKAEPKPAPDVTPAPVVEAVKETVAAEAAPAPEPKPEPKPEPAKAEAKDTGTKRKGWWARARGE

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias98-143Acidic residues
Compositional bias144-172Basic and acidic residues
Compositional bias567-581Basic and acidic residues
Compositional bias598-622Acidic residues
Compositional bias665-679Acidic residues
Compositional bias680-697Basic and acidic residues
Compositional bias773-790Basic and acidic residues
Compositional bias860-887Basic and acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
ARYL01000002
EMBL· GenBank· DDBJ
KDA04079.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp