Essential maintenance is planned to begin on Fri Jan 24 2025. The website may be temporarily unavailable. Please use our fallback: https://wwwdev.ebi.ac.uk/uniprot/front-end/fallback/ in case of any outage.

A0A366CWD4 · A0A366CWD4_9NOCA

  • Protein
    Ribonuclease PH
  • Gene
    rph
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation.

Caution

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

Catalytic activity

Features

Showing features for binding site.

125720406080100120140160180200220240
TypeIDPosition(s)Description
Binding site88phosphate (UniProtKB | ChEBI); substrate
Binding site126-128phosphate (UniProtKB | ChEBI); substrate

GO annotations

AspectTerm
Molecular Function3'-5'-RNA exonuclease activity
Molecular FunctiontRNA binding
Molecular FunctiontRNA nucleotidyltransferase activity
Biological ProcessrRNA catabolic process
Biological ProcessrRNA processing
Biological ProcesstRNA processing

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Ribonuclease PH
  • EC number
  • Short names
    RNase PH
  • Alternative names
    • tRNA nucleotidyltransferase

Gene names

    • Name
      rph
    • ORF names
      DFR74_12429

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • DSM 44599
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Nocardiaceae > Nocardia

Accessions

  • Primary accession
    A0A366CWD4

Proteomes

Interaction

Subunit

Homohexameric ring arranged as a trimer of dimers.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain12-142Exoribonuclease phosphorolytic
Domain161-226Exoribonuclease phosphorolytic

Sequence similarities

Belongs to the RNase PH family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    257
  • Mass (Da)
    27,098
  • Last updated
    2018-11-07 v1
  • MD5 Checksum
    5A85FDE097A6E94763A072A9FBE59368
MSRRADGRADDELREVRITRGFTTHPAGSVLVEFGQTRVMCTASVTEGVPPWRRDSGLGWLTAEYAMLPAATHTRSGRESVKGKVGGRTQEISRLIGRSLRACIDLAAIGENTIAIDCDVLQADGGTRTAAITGAYVALSDAVTWLGAAGRLADPQPISCAIAAVSVGVVDGRVRLDLPYEEDSRAEVDMNVVATDTGTLVEVQGTGEGATFPRSTLDKLLDSALAGCEQLFAIQKEALALPYPGGLPEPAETSKKK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
QNRE01000024
EMBL· GenBank· DDBJ
RBO82151.1
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.
Help