A0A099CYD3 · A0A099CYD3_9GAMM
- ProteinMultifunctional CCA protein
- Genecca
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids410 (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
Protein has several cofactor binding sites:
Note: Magnesium is required for nucleotidyltransferase activity.
Note: Nickel for phosphatase activity.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 8 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 8 | CTP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 11 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 11 | CTP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 21 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 23 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 91 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 91 | CTP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 137 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 137 | CTP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 140 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 140 | CTP (UniProtKB | ChEBI) | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | ATP binding | |
Molecular Function | CCA tRNA nucleotidyltransferase activity | |
Molecular Function | cyclic-nucleotide phosphodiesterase activity | |
Molecular Function | magnesium ion binding | |
Molecular Function | phosphatase activity | |
Molecular Function | tRNA binding | |
Biological Process | RNA repair | |
Biological Process | tRNA 3'-terminal CCA addition |
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameMultifunctional CCA protein
Including 4 domains:
- Recommended nameCCA-adding enzyme
- EC number
- Alternative names
- Recommended name2'-nucleotidase
- EC number
- Recommended name2',3'-cyclic phosphodiesterase
- EC number
- Recommended namePhosphatase
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Lysobacterales > Rhodanobacteraceae > Oleiagrimonas
Accessions
- Primary accessionA0A099CYD3
Proteomes
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 228-330 | HD | ||||
Sequence: TGVHVELVVDMAARLAPGDDLVGFCALVHDLGKARTPEAEWPRHIMHEQRGTEPLRALAERLKLPTEHRELGLLVCREHLHAHRALQLKPKTVLGLLDKLDAL |
Domain
Comprises two domains: an N-terminal domain containing the nucleotidyltransferase activity and a C-terminal HD domain associated with both phosphodiesterase and phosphatase activities.
Sequence similarities
Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. Bacterial CCA-adding enzyme type 1 subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length410
- Mass (Da)45,387
- Last updated2015-01-07 v1
- Checksum6B3BA0B1131C59F6
Keywords
- Technical term