A0A2P6W285 · A0A2P6W285_9EURY
- ProteinCCA-adding enzyme
- Genecca
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids452 (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 + ATP + 2 CTP = a tRNA with a 3' CCA end + 3 diphosphate
- a tRNA with a 3' CCA end + ATP + 2 CTP = a tRNA with a 3' CCACCA end + 3 diphosphate
Cofactor
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 48 | ATP (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 48 | CTP (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 51 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 51 | CTP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 60 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 62 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 115 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 137 | ATP (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 137 | CTP (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 157 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 157 | CTP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 166 | ATP (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 166 | CTP (UniProtKB | ChEBI) | ||||
Sequence: Y |
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
- Strain
- Taxonomic lineageArchaea > Euryarchaeota > Stenosarchaea group > Candidatus Nanohaloarchaea
Accessions
- Primary accessionA0A2P6W285
Proteomes
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 30-135 | Polymerase nucleotidyl transferase | ||||
Sequence: EISDFIEREFGVATHFAGSASRGTCMKNDGDLDIFILFNKKIDELKLENKGLEIGKKTFRQFEEDFEVDYAEHPYTKGRIDDYEVEIVPCYETDPENIKSSVDRTP | ||||||
Domain | 152-270 | tRNA nucleotidyltransferase substrate binding | ||||
Sequence: DAVILKNFLDSKDLYGSSLKTQGFSGYLCEILINHYGGFHELVRSVTDWENEKLIDPENYHDGKLPERLEKKFNEEPLKVIDPVDKERNVASVLSLENYSKFIHLCWRFKRNPRMSFFE | ||||||
Domain | 291-422 | CCA-adding enzyme C-terminal | ||||
Sequence: FLVLEFGTIEEVDDIVYPQMRKTMRRLKSELKKKEFRIYESGFYVDQSTKIFFELDRELPEIREMEGPKVFHGEEHLSEFTSKYENVFIQENRVVAKTEREFTDAKKFLEAFLSDDLKEKGIPDNVSKKIEN |
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)53,751
- Last updated2018-05-23 v1
- Checksum31AD60B4C80AED88