A0A3G5FJ32 · A0A3G5FJ32_TETHA

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

Lacks conserved residue(s) required for the propagation of feature annotation.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Binds 1 Mg2+ ion per subunit.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site86phosphate (UniProtKB | ChEBI); substrate
Binding site124-126phosphate (UniProtKB | ChEBI); substrate
Binding site256-261substrate
Active site318Proton acceptor
Binding site318Mg2+ (UniProtKB | ChEBI)
Binding site319substrate
Binding site401-404substrate
Binding site424substrate
Binding site429-430substrate

GO annotations

AspectTerm
Molecular Function3'-5'-RNA exonuclease activity
Molecular FunctiondITP diphosphatase activity
Molecular FunctionITP diphosphatase activity
Molecular Functionmetal ion binding
Molecular Functionnucleotide binding
Molecular Functionribonucleoside triphosphate phosphatase activity
Molecular FunctiontRNA binding
Molecular FunctiontRNA nucleotidyltransferase activity
Molecular FunctionXTP diphosphatase 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
      C7H83_07765

Organism names

Accessions

  • Primary accession
    A0A3G5FJ32

Proteomes

Interaction

Subunit

Homodimer.
Homohexameric ring arranged as a trimer of dimers.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain10-140Exoribonuclease phosphorolytic
Domain160-225Exoribonuclease phosphorolytic

Sequence similarities

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

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    449
  • Mass (Da)
    49,602
  • Last updated
    2019-02-13 v1
  • Checksum
    6A2411371E5D6D06
MRHDGRYFDQLRNIKIKTNVYKQPEGSVVINFGDTQVICSATIENTVPPFLKDSNTGWVTAEYSMLPRATQIRNKRESTKGKLKGRTMEIQRLIGRCLRAVVDLDKLGERSIIIDCDVVQADGGTRTASITGAFTALRLAIDKLLQTNELSEDPIKEFCAAISVGILADGSCVLDLDYEEDSRCAVDMNIAMTESGRFIEIQGNGEQATFDRSQLNELLLLAKQGIDTLVTRQKEALYANPEQNQGVDAQTIVIATGNPGKAREFSTMFYAAGYKVKTMKDFPELPEVAETGTTFEENARLKAETIANILQCPVLADDSGLKVDILNGMPGIYSARFAGAEKNDAANNAKLLHELTNIADEQRRAQFHCTLVFAVPKKESLVVEADWPGRIARIPQGDNGFGYDPLFIPEGLNESAAEMSESEKNKVSHRAQALNKLQEQWQDWLEGGN

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP027768
EMBL· GenBank· DDBJ
AYW50363.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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