A0A556UC68 · A0A556UC68_9LACO
- ProteinCCA-adding enzyme
- Genecca
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids399 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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.
Catalytic activity
- a tRNA precursor + 2 CTP + ATP = a tRNA with a 3' CCA end + 3 diphosphate
- a tRNA with a 3' CCA end + 2 CTP + ATP = a tRNA with a 3' CCACCA end + 3 diphosphate
Cofactor
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 33 | ATP (UniProtKB | ChEBI) | |||
Binding site | 33 | CTP (UniProtKB | ChEBI) | |||
Binding site | 36 | ATP (UniProtKB | ChEBI) | |||
Binding site | 36 | CTP (UniProtKB | ChEBI) | |||
Binding site | 46 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 48 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 117 | ATP (UniProtKB | ChEBI) | |||
Binding site | 117 | CTP (UniProtKB | ChEBI) | |||
Binding site | 160 | ATP (UniProtKB | ChEBI) | |||
Binding site | 160 | CTP (UniProtKB | ChEBI) | |||
Binding site | 163 | ATP (UniProtKB | ChEBI) | |||
Binding site | 163 | CTP (UniProtKB | ChEBI) | |||
Binding site | 166 | ATP (UniProtKB | ChEBI) | |||
Binding site | 166 | CTP (UniProtKB | ChEBI) | |||
Binding site | 169 | ATP (UniProtKB | ChEBI) | |||
Binding site | 169 | CTP (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | ATP binding | |
Molecular Function | CCA tRNA nucleotidyltransferase activity | |
Molecular Function | magnesium ion binding | |
Molecular Function | tRNA binding | |
Biological Process | RNA repair | |
Biological Process | tRNA 3'-terminal CCA addition |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCCA-adding enzyme
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Lactobacillales > Lactobacillaceae > Lactobacillus
Accessions
- Primary accessionA0A556UC68
Proteomes
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 28-148 | Poly A polymerase head | |||
Domain | 176-233 | tRNA nucleotidyltransferase/poly(A) polymerase RNA and SrmB- binding | |||
Domain | 251-394 | CCA-adding enzyme C-terminal | |||
Sequence similarities
Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. Bacterial CCA-adding enzyme type 3 subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length399
- Mass (Da)45,760
- Last updated2019-10-16 v1
- MD5 ChecksumCD488EB9639631EF3474FAF00B4823BB
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
VLLR01000001 EMBL· GenBank· DDBJ | TSO26265.1 EMBL· GenBank· DDBJ | Genomic DNA |