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A0A556UC68 · A0A556UC68_9LACO

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 site33ATP (UniProtKB | ChEBI)
Binding site33CTP (UniProtKB | ChEBI)
Binding site36ATP (UniProtKB | ChEBI)
Binding site36CTP (UniProtKB | ChEBI)
Binding site46Mg2+ (UniProtKB | ChEBI)
Binding site48Mg2+ (UniProtKB | ChEBI)
Binding site117ATP (UniProtKB | ChEBI)
Binding site117CTP (UniProtKB | ChEBI)
Binding site160ATP (UniProtKB | ChEBI)
Binding site160CTP (UniProtKB | ChEBI)
Binding site163ATP (UniProtKB | ChEBI)
Binding site163CTP (UniProtKB | ChEBI)
Binding site166ATP (UniProtKB | ChEBI)
Binding site166CTP (UniProtKB | ChEBI)
Binding site169ATP (UniProtKB | ChEBI)
Binding site169CTP (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
      FOD82_04120

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • LL6
  • Taxonomic lineage
    Bacteria > Bacillota > Bacilli > Lactobacillales > Lactobacillaceae > Lactobacillus

Accessions

  • Primary accession
    A0A556UC68

Proteomes

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain28-148Poly A polymerase head
Domain176-233tRNA nucleotidyltransferase/poly(A) polymerase RNA and SrmB- binding
Domain251-394CCA-adding enzyme C-terminal

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    399
  • Mass (Da)
    45,760
  • Last updated
    2019-10-16 v1
  • MD5 Checksum
    CD488EB9639631EF3474FAF00B4823BB
MMKIENLPKIFMQAMPVLKKLEDAGFEAYFVGGSVRDLLLNRHIHDVDIATSAYPEEVKELFEKTIDTGIKHGTVTVLFNRESYEITTFRTESGYQDYRRPDHVTFVQNLDEDLKRRDFTINALAMNTDGEVIDLFNGLEDLKKRVIRAVGNPETRFHEDALRMMRAVRFMSQLEFNLEENTQQAIKDNHKLLQKISVERIRDEFVKMGLGPHSRQAFQIFLDTKLSENVPDFAGKSNLLAVFPSLKFNPTLETSLWSIIIILLKLPNNKITGFMRDWKNSNATTDSVERIVELFDLLAERIPSDYELFKIGQDTLLNTIDVAHILGQPIDSKVLVDRYTSLPIKNASELAIDGRFLIQQGVRPGPKLGIMLDKIKEKVVSNELDNSEVAIKKFIKEQN

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
VLLR01000001
EMBL· GenBank· DDBJ
TSO26265.1
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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