A0A103QX79 · A0A103QX79_9BURK

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 site303Mg2+ (UniProtKB | ChEBI); catalytic
Binding site346Mg2+ (UniProtKB | ChEBI); catalytic
Binding site404Zn2+ (UniProtKB | ChEBI); ligand shared between dimeric partners
Binding site407Zn2+ (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
      WJ33_35530

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • MSMB2036
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Burkholderiaceae > Burkholderia > Burkholderia cepacia complex

Accessions

  • Primary accession
    A0A103QX79

Proteomes

Subcellular Location

Cytoplasm
Cell inner membrane
; Peripheral membrane protein

Keywords

Interaction

Subunit

Homotetramer formed by a dimer of dimers.

Family & Domains

Features

Showing features for domain, region, compositional bias.

TypeIDPosition(s)Description
Domain39-118S1 motif
Region404-407Required for zinc-mediated homotetramerization and catalytic activity
Compositional bias511-528Basic and acidic residues
Region511-560Disordered
Compositional bias540-557Pro residues
Region579-816Disordered
Compositional bias594-622Basic and acidic residues
Compositional bias644-737Basic and acidic residues
Region1005-1040Disordered

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
    1,040
  • Mass (Da)
    113,124
  • Last updated
    2016-04-13 v1
  • Checksum
    BED218A1C5957C3A
MKRMLFNATQQEELRVAIVDGQKLIDIDIETAGREQRKGNIYKGVITRIEPSLEACFVNYGEDRHGFLPFKEVARQYFKEGVDMRSARIQDALREGQELIVQVEKEERGNKGAALTTFISLAGRYLVLMPNNPRGGGVSRRIEGDERQELRETMAQLQIPDGMSMIARTAGIGRSAEELQWDLNYLLQLWRAIEAASQSGRSGEPMLIYLESSLVIRAIRDYFQPDIGEILIDTTEIHDQARAFMDIVMPDNVSKVKRYHDDVPLFSRFQIEHQIETAYSRTVPLPSGGAIVIDHTEALVAIDVNSARATKGADIEETATRTNLEAADEVARQLRLRDLGGLIVIDFIDMESAKSQREVEQRLKDALKHDRARVQMGKISRFGLMELSRQRLRPALSEGSHVTCPRCNGTGHIRDTESSALQVLRIIQEEAMKENTAAIHCQVPVEVTAFLLNEKRQEINKIESRFKVGIVLIPNKHLDTPHYKLERLRHDDARLDDPRASWKMAEEAARELESETGYSKRAAEVKPKQEAAVKGITPERPAPSPAPQRPAEPTPAPVPVAAASGGIIGWLKGLFGMQPAPAPAPAPAPVKEQAARPTRERTEKSEQRGERGGDRDRNRNRRGGAQQPQGGRDQAAAGRGGQPQRPEREGKEAREAREAREPREGREGREGREGREGRGQREPREAREGRETREPRESREPRERVEQPEAVEAAGRGERQERGERRERGERRKPTQHAATLETVTRGESHPELEADKAAAAALPGAEVMADAEAGARDGEERRRRRRGRRGGRREREEDGTIVAHAAEGAEGEAAVAPAAEPVVHAAPVAEAPHAAAPAVAAAVAAVGAVVAEAVAHAEPAAADTQPEPARVEPAPAVATVEPAVAAQPVETAAPVAAAEAGPTPVAVSPNDALEVPEAPAAVAAPQPAPVAEAAPVAMVETAPAVAAEPVRVEAAPVEAVVAAPVVEQAQPAAAAPASASLETVLTQAGLVWVNTDADKFRAAQDAAAQLPRPARVPRERKSLPPVDTTPMQQVETTHH

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias511-528Basic and acidic residues
Compositional bias540-557Pro residues
Compositional bias594-622Basic and acidic residues
Compositional bias644-737Basic and acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LOXM01000246
EMBL· GenBank· DDBJ
KVG57257.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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