Q4QFL6 · Q4QFL6_LEIMA
- ProteinPoly(A) polymerase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids700 (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 | 99 | ATP (UniProtKB | ChEBI) | |||
Binding site | 103 | Mg2+ 2 (UniProtKB | ChEBI); catalytic | |||
Binding site | 103 | Mg2+ 1 (UniProtKB | ChEBI); catalytic | |||
Binding site | 103-105 | ATP (UniProtKB | ChEBI) | |||
Binding site | 105 | Mg2+ 1 (UniProtKB | ChEBI); catalytic | |||
Binding site | 105 | Mg2+ 2 (UniProtKB | ChEBI); catalytic | |||
Binding site | 157 | ATP (UniProtKB | ChEBI) | |||
Binding site | 157 | Mg2+ 2 (UniProtKB | ChEBI); catalytic | |||
Binding site | 215 | ATP (UniProtKB | ChEBI) | |||
Binding site | 224 | 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 > Discoba > Euglenozoa > Kinetoplastea > Metakinetoplastina > Trypanosomatida > Trypanosomatidae > Leishmaniinae > Leishmania
Accessions
- Primary accessionQ4QFL6
Proteomes
Organism-specific databases
Subcellular Location
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 41-201 | Poly(A) polymerase nucleotidyltransferase | |||
Domain | 206-346 | Poly(A) polymerase central | |||
Domain | 375-562 | Poly(A) polymerase RNA-binding | |||
Region | 452-488 | Disordered | |||
Compositional bias | 464-488 | Polar residues | |||
Region | 570-700 | Disordered | |||
Compositional bias | 601-624 | Polar residues | |||
Sequence similarities
Belongs to the poly(A) polymerase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length700
- Mass (Da)76,513
- Last updated2005-07-19 v1
- MD5 Checksum095B8D88D857000F0643A4AE9F962028
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 464-488 | Polar residues | |||
Compositional bias | 601-624 | Polar residues | |||
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
FR796410 EMBL· GenBank· DDBJ | CAJ03188.1 EMBL· GenBank· DDBJ | Genomic DNA |