A0A6B9TKE0 · A0A6B9TKE0_9EURY
- ProteinCCA-adding enzyme
- Genecca
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids452 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
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
- L-tyrosyl-[protein] + ATP = O-(5'-adenylyl)-L-tyrosyl-[protein] + diphosphate
- O-(5'-adenylyl)-L-tyrosyl-[protein] + ATP = O-[5'-(adenylyl-(5'->3')-adenylyl)]-L-tyrosyl-[protein] + 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 | 49 | ATP (UniProtKB | ChEBI) | |||
Binding site | 49 | CTP (UniProtKB | ChEBI) | |||
Binding site | 52 | ATP (UniProtKB | ChEBI) | |||
Binding site | 52 | CTP (UniProtKB | ChEBI) | |||
Binding site | 61 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 63 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 116 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 139 | ATP (UniProtKB | ChEBI) | |||
Binding site | 139 | CTP (UniProtKB | ChEBI) | |||
Binding site | 159 | ATP (UniProtKB | ChEBI) | |||
Binding site | 159 | CTP (UniProtKB | ChEBI) | |||
Binding site | 168 | ATP (UniProtKB | ChEBI) | |||
Binding site | 168 | CTP (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | AMPylase activity | |
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 lineageArchaea > Euryarchaeota > Methanomada group > Methanobacteria > Methanobacteriales > Methanobacteriaceae > Methanothermobacter
Accessions
- Primary accessionA0A6B9TKE0
Proteomes
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 33-139 | Polymerase nucleotidyl transferase | |||
Domain | 153-263 | tRNA nucleotidyltransferase substrate binding | |||
Domain | 282-422 | CCA-adding enzyme C-terminal | |||
Sequence similarities
Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. Archaeal CCA-adding enzyme subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length452
- Mass (Da)51,599
- Last updated2020-06-17 v1
- MD5 Checksum6CE8CCD7EB8CF118CDC6203EDA472091
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP043480 EMBL· GenBank· DDBJ | QHN08145.1 EMBL· GenBank· DDBJ | Genomic DNA |