A0A6A8V9G2 · A0A6A8V9G2_STRPA

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 site32ATP (UniProtKB | ChEBI)
Binding site32CTP (UniProtKB | ChEBI)
Binding site35ATP (UniProtKB | ChEBI)
Binding site35CTP (UniProtKB | ChEBI)
Binding site45Mg2+ (UniProtKB | ChEBI)
Binding site47Mg2+ (UniProtKB | ChEBI)
Binding site116ATP (UniProtKB | ChEBI)
Binding site116CTP (UniProtKB | ChEBI)
Binding site159ATP (UniProtKB | ChEBI)
Binding site159CTP (UniProtKB | ChEBI)
Binding site162ATP (UniProtKB | ChEBI)
Binding site162CTP (UniProtKB | ChEBI)
Binding site165ATP (UniProtKB | ChEBI)
Binding site165CTP (UniProtKB | ChEBI)
Binding site168ATP (UniProtKB | ChEBI)
Binding site168CTP (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
      GMC73_02205
      , GMC90_04240

Organism names

  • Taxonomic identifier
  • Strains
    • BIOML-A12
    • BIOML-A6
  • Taxonomic lineage
    Bacteria > Bacillota > Bacilli > Lactobacillales > Streptococcaceae > Streptococcus

Accessions

  • Primary accession
    A0A6A8V9G2

Proteomes

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain27-147Poly A polymerase head
Domain174-233tRNA nucleotidyltransferase/poly(A) polymerase RNA and SrmB- binding
Domain250-394CCA-adding enzyme C-terminal

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    403
  • Mass (Da)
    46,460
  • Last updated
    2020-06-17 v1
  • Checksum
    640C92125231DB04
MRLEKMPSEFQEALPILEKIKAAGFEAYFVGGSVRDALLDRPIHDVDIASSSYPEETKAIFDRTVDIGIEHGTVLVLENGQEYEITTFRTEDVYVDYRRPSSVSFVRSLEEDLKRRDFTVNAFALNEKGEIVDLFHGLEDLENKVLRAVGLPHERFNEDALRIMRGFRFQASLGFELEEATFDAMKKCAPLLEKISVERTFIEFDKLLLSPYWRQGLEAMLASGAYHYLPEMKDRKEAIERLFDIELEYTFSTSEQAWAALVLALEIQDIPKFFKKWKTSREFAKTVEQIVEILKLRENGSLDKRACYKYEKRLLLVAEELREAYALSVDYLAIERVYDSLTIHDKHEVVVNGGMLIKEYGFQPGPALGEILTKIEYAIVDGELANEKEAIMAYIQQAKEEEK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
WMYY01000002
EMBL· GenBank· DDBJ
MTR66097.1
EMBL· GenBank· DDBJ
Genomic DNA
WMZE01000002
EMBL· GenBank· DDBJ
MTS01041.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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