A0A2P6W285 · A0A2P6W285_9EURY

Function

function

Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. tRNA 3'-terminal CCA addition is required both for tRNA processing and repair. Also involved in tRNA surveillance by mediating tandem CCA addition to generate a CCACCA at the 3' terminus of unstable tRNAs. While stable tRNAs receive only 3'-terminal CCA, unstable tRNAs are marked with CCACCA and rapidly degraded.

Miscellaneous

A single active site specifically recognizes both ATP and CTP and is responsible for their addition.

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 )

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site48ATP (UniProtKB | ChEBI)
Binding site48CTP (UniProtKB | ChEBI)
Binding site51ATP (UniProtKB | ChEBI)
Binding site51CTP (UniProtKB | ChEBI)
Binding site60Mg2+ (UniProtKB | ChEBI)
Binding site62Mg2+ (UniProtKB | ChEBI)
Binding site115Mg2+ (UniProtKB | ChEBI)
Binding site137ATP (UniProtKB | ChEBI)
Binding site137CTP (UniProtKB | ChEBI)
Binding site157ATP (UniProtKB | ChEBI)
Binding site157CTP (UniProtKB | ChEBI)
Binding site166ATP (UniProtKB | ChEBI)
Binding site166CTP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular FunctionATP binding
Molecular FunctionCCA tRNA nucleotidyltransferase activity
Molecular Functionmagnesium ion binding
Molecular FunctiontRNA binding
Biological ProcessRNA repair
Biological ProcesstRNA 3'-terminal CCA addition

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    CCA-adding enzyme
  • EC number
  • Alternative names
    • CCA tRNA nucleotidyltransferase
    • tRNA CCA-pyrophosphorylase
    • tRNA adenylyl-/cytidylyl- transferase
    • tRNA nucleotidyltransferase
    • tRNA-NT

Gene names

    • Name
      cca
    • ORF names
      BRC29_04280

Organism names

Accessions

  • Primary accession
    A0A2P6W285

Proteomes

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain30-135Polymerase nucleotidyl transferase
Domain152-270tRNA nucleotidyltransferase substrate binding
Domain291-422CCA-adding enzyme C-terminal

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    452
  • Mass (Da)
    53,751
  • Last updated
    2018-05-23 v1
  • Checksum
    31AD60B4C80AED88
MEWQGLREKVIEETYPEEQELGELRQKYKEISDFIEREFGVATHFAGSASRGTCMKNDGDLDIFILFNKKIDELKLENKGLEIGKKTFRQFEEDFEVDYAEHPYTKGRIDDYEVEIVPCYETDPENIKSSVDRTPHHSEWVKENLTEEERKDAVILKNFLDSKDLYGSSLKTQGFSGYLCEILINHYGGFHELVRSVTDWENEKLIDPENYHDGKLPERLEKKFNEEPLKVIDPVDKERNVASVLSLENYSKFIHLCWRFKRNPRMSFFESEQRNYSEFRIKQELKRRGNFLVLEFGTIEEVDDIVYPQMRKTMRRLKSELKKKEFRIYESGFYVDQSTKIFFELDRELPEIREMEGPKVFHGEEHLSEFTSKYENVFIQENRVVAKTEREFTDAKKFLEAFLSDDLKEKGIPDNVSKKIENYSFEDPMEGDSKWLNYLGEKLCLQHKGENK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
PXPE01000001
EMBL· GenBank· DDBJ
PSG99316.1
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.
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