A0AAJ1WCH0 · A0AAJ1WCH0_9ENTE

  • Protein
    Multifunctional fusion protein
  • Gene
    rph
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

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.
Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.

Caution

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

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Binds 1 Mg2+ ion per subunit.

Features

Showing features for binding site, active site.

Type
IDPosition(s)Description
Binding site86phosphate (UniProtKB | ChEBI); substrate
Binding site124-126phosphate (UniProtKB | ChEBI); substrate
Binding site258-263substrate
Binding site291Mg2+ (UniProtKB | ChEBI)
Active site320Proton acceptor
Binding site320Mg2+ (UniProtKB | ChEBI)
Binding site321substrate
Binding site403-406substrate
Binding site426substrate
Binding site431-432substrate

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Function3'-5'-RNA exonuclease activity
Molecular Functionmetal ion binding
Molecular Functionnucleoside triphosphate diphosphatase activity
Molecular Functionnucleotide binding
Molecular Functionribonucleoside triphosphate phosphatase activity
Molecular FunctiontRNA binding
Molecular FunctiontRNA nucleotidyltransferase activity
Biological Processnucleotide metabolic process
Biological Processpurine nucleoside triphosphate catabolic process
Biological ProcessrRNA catabolic process
Biological ProcessrRNA processing
Biological ProcesstRNA processing

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Multifunctional fusion protein

Including 2 domains:

  • Recommended name
    dITP/XTP pyrophosphatase
  • EC number
  • Alternative names
    • Non-canonical purine NTP pyrophosphatase
    • Non-standard purine NTP pyrophosphatase
    • Nucleoside-triphosphate diphosphatase
    • Nucleoside-triphosphate pyrophosphatase
      (NTPase
      )
  • Recommended name
    Ribonuclease PH
  • EC number
  • Short names
    RNase PH
  • Alternative names
    • tRNA nucleotidyltransferase

Gene names

    • Name
      rph
    • ORF names
      RAN64_10300

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • ENT3_CNKT_NWU
  • Taxonomic lineage
    Bacteria > Bacillota > Bacilli > Lactobacillales > Enterococcaceae > Enterococcus

Accessions

  • Primary accession
    A0AAJ1WCH0

Proteomes

Subcellular Location

Interaction

Subunit

Homodimer.
Homohexameric ring arranged as a trimer of dimers.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain10-140Exoribonuclease phosphorolytic
Domain160-224Exoribonuclease phosphorolytic

Sequence similarities

Belongs to the HAM1 NTPase family.
Belongs to the RNase PH family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    451
  • Mass (Da)
    50,118
  • Last updated
    2024-07-24 v1
  • Checksum
    DAB3E92F6E10AA37
MRHDGRKAQELRKLELQTNVFKYPEGSVVIRFGDTTVICSATVEDSVPPFLRETGTGWVTAEYSMLPRATSTRNRRESNKGKLSGRTMEIQRLIGRSLRAVIDLEKLGERSIIIDCDVIQADGGTRTASITGAFVALRLAIEKLLREKELSEDPIKEHLAAVSVGILPDGTCVTDLDYQEDSAALVDMNLVMTESGKFVEIQGTGEEATFDGEQLNEMLFFGKNAIEDLIKEQKHALLTEFAQDNERIEETKTIIIATRNPGKAEEFRNMFKEAGYHVKTLLDYPELPDVEETGSTFEENARLKAETIAQLLDQPVLADDSGLKVDALGGMPGIYSARFAGEQKSDAGNNAKLLYELTDVPDEKRTAQFHCTLVFAAPKKDSLVVEAEWPGRVARIPSGENGFGYDPLFIPEGKKQTAAELSSEEKNKISHRAQAMKKLSAEWKQWLEGER

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JAVBZS010000030
EMBL· GenBank· DDBJ
MDP8590409.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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