A0A365TTV2 · A0A365TTV2_9GAMM

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 site300Mg2+ (UniProtKB | ChEBI); catalytic
Binding site343Mg2+ (UniProtKB | ChEBI); catalytic
Binding site401Zn2+ (UniProtKB | ChEBI); ligand shared between dimeric partners
Binding site404Zn2+ (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
      DQ400_01995

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • SST4
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Oceanospirillales > Halomonadaceae > Vreelandella

Accessions

  • Primary accession
    A0A365TTV2

Proteomes

Subcellular Location

Cytoplasm
Cell inner membrane
; Peripheral membrane protein

Keywords

Interaction

Subunit

Component of the RNA degradosome, which is a multiprotein complex involved in RNA processing and mRNA degradation. Within the RNA degradosome, RNase E assembles into a homotetramer formed by a dimer of dimers.

Family & Domains

Features

Showing features for domain, region, compositional bias.

TypeIDPosition(s)Description
Domain39-117S1 motif
Region401-404Required for zinc-mediated homotetramerization and catalytic activity
Region501-569Disordered
Region582-1119Disordered
Compositional bias599-625Basic and acidic residues
Compositional bias655-680Basic and acidic residues
Compositional bias691-753Basic and acidic residues
Compositional bias793-820Polar residues
Compositional bias871-892Polar residues
Compositional bias910-927Polar residues
Compositional bias957-1010Polar residues
Compositional bias1011-1034Basic and acidic residues
Compositional bias1047-1061Basic and acidic residues
Compositional bias1105-1119Basic 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
    1,119
  • Mass (Da)
    122,601
  • Last updated
    2018-11-07 v1
  • Checksum
    B7F920DDB7F59B16
MKRMLINATQPEELRVALVDGQRLYDLDIESGAREQKKANIYRGKITRVEPSLEAAFVDYGADRHGFLPLKEISKEYFVKDVSGRPSIREVLKEGQEVIVQVDKEERGNKGAALTTFVSLAGRFLVLMPNNPRAGGISRRIEGDERSQLKDAMGQLTVPDKMGLIVRTAGIGRNPEELQWDLDYLVQVWESITTEAAKRPAPFLIYRESNVIIRAMRDYLRQDIGEVLIDSPEIHAEALGFIRQVMPSYQQKIKLYADEVPLFSRFQIESQIETAYQREVKLPSGGSIVIDHTEALVSIDINSARATRGSDIEETALQTNSEAADEIARQLRLRDIGGLVVIDFIDMGPARNQREVENRMRDALKLDRARVQIGRISRFGLMEMSRQRLRPSLGETSGVVCPRCNGQGTIRDVRSLSLSIMRLIEEEAMKENSAQIRAILPVPVATYLLNEKRSVLADLESRQGVRVVLLPNPDMDTPHYDVQRLRDDHLDEDDTQSLSSFELSTDTEVGKEPTPSFVPPAQRAEAAVKSVTHNAPAPASLQTEEKAPAASSAPAAKATPATSEQPSVIGRFIRGFAKLLGSDESSAEPAPAPKAETPAPRKPSERKTNQRSNESRQKPSRGETTSRNARSDNSPQSEQKTEQKSDQRNTTQRAANEDSNDKRSGPSRTRNRRRHPQQDDTNGQEPANKVPRKETQTDSTAKDNAGKDSSAKEKEGKNAAQKEPRRDSSRDNQRNEAVNNTEAKDDGKPKRTRNNPRNRTRTQAINPQAEAEQLKLQAEAPSEAPEAVTQPSEMSAEAASNANVPNSADITSPSETSEKADNATTADRPVADNAKASKSTHQRRQPKVAPDAAPETAVATDVEKEAASKPSEPESTANDEPMATPTTGSTEAESEENEPKPLLSEAKTEPAATDQVSDSQPPVSDSESVTPEAIEPPAGNIVDPAASIDEAASPAALDTETTYQSNEERQPETPANAQEAHQESATPSDSKSVAAAPSVEEPSTNSEPKQEAAGKGDEPNNVEKSNDEESSVKEGSVELNSTEENSAEENSTEKSNDERVMTEAPATEAAPQLAQPIASEAPAEDAVTEEAPKPRRRRTRAHNDPREKRKQAQQDTYSE

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias599-625Basic and acidic residues
Compositional bias655-680Basic and acidic residues
Compositional bias691-753Basic and acidic residues
Compositional bias793-820Polar residues
Compositional bias871-892Polar residues
Compositional bias910-927Polar residues
Compositional bias957-1010Polar residues
Compositional bias1011-1034Basic and acidic residues
Compositional bias1047-1061Basic and acidic residues
Compositional bias1105-1119Basic and acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
QNTU01000001
EMBL· GenBank· DDBJ
RBI69484.1
EMBL· GenBank· DDBJ
Genomic DNA

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