A0AAD9GH99 · A0AAD9GH99_BABDI
- ProteinPoly(A) polymerase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids514 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Polymerase that creates the 3'-poly(A) tail of mRNA's.
Catalytic activity
- RNA(n) + ATP = RNA(n)-3'-adenine ribonucleotide + diphosphate
RNA(n) RHEA-COMP:14527 + CHEBI:30616 = RNA(n)-3'-adenine ribonucleotide RHEA-COMP:17347 + CHEBI:33019
Cofactor
Protein has several cofactor binding sites:
Note: Binds 2 magnesium ions. Also active with manganese.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 94-96 | ATP (UniProtKB | ChEBI) | |||
Binding site | 107 | Mg2+ 2 (UniProtKB | ChEBI); catalytic | |||
Binding site | 107 | Mg2+ 1 (UniProtKB | ChEBI); catalytic | |||
Binding site | 107-109 | ATP (UniProtKB | ChEBI) | |||
Binding site | 109 | Mg2+ 1 (UniProtKB | ChEBI); catalytic | |||
Binding site | 109 | Mg2+ 2 (UniProtKB | ChEBI); catalytic | |||
Binding site | 161 | ATP (UniProtKB | ChEBI) | |||
Binding site | 161 | Mg2+ 2 (UniProtKB | ChEBI); catalytic | |||
Binding site | 222 | ATP (UniProtKB | ChEBI) | |||
Binding site | 231 | ATP (UniProtKB | ChEBI) | |||
Binding site | 240-241 | ATP (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | nucleus | |
Molecular Function | ATP binding | |
Molecular Function | metal ion binding | |
Molecular Function | poly(A) RNA polymerase activity | |
Molecular Function | RNA binding | |
Biological Process | mRNA processing | |
Biological Process | RNA 3'-end processing |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePoly(A) polymerase
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Sar > Alveolata > Apicomplexa > Aconoidasida > Piroplasmida > Babesiidae > Babesia
Accessions
- Primary accessionA0AAD9GH99
Proteomes
Subcellular Location
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 1-18 | Polar residues | |||
Region | 1-27 | Disordered | |||
Domain | 14-208 | Poly(A) polymerase nucleotidyltransferase | |||
Domain | 213-364 | Poly(A) polymerase central | |||
Domain | 369-426 | Poly(A) polymerase RNA-binding | |||
Sequence similarities
Belongs to the poly(A) polymerase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length514
- Mass (Da)59,193
- Last updated2024-05-29 v1
- ChecksumB52DEE22990B75B4
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 1-18 | Polar residues | |||
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JAHBMH010000024 EMBL· GenBank· DDBJ | KAK1938434.1 EMBL· GenBank· DDBJ | Genomic DNA |