A0A2P7YFJ4 · A0A2P7YFJ4_9ASCO
- ProteinPoly(A) polymerase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids544 (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 | 85-87 | ATP (UniProtKB | ChEBI) | ||||
Sequence: FGS | ||||||
Binding site | 98 | Mg2+ 2 (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 98 | Mg2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 98-100 | ATP (UniProtKB | ChEBI) | ||||
Sequence: DID | ||||||
Binding site | 100 | Mg2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 100 | Mg2+ 2 (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 152 | ATP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 152 | Mg2+ 2 (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 213 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 222 | ATP (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 231-232 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GV |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | Mei2 nuclear dot complex | |
Cellular Component | mRNA cleavage and polyadenylation specificity factor complex | |
Cellular Component | nuclear exosome focus | |
Molecular Function | ATP binding | |
Molecular Function | metal ion binding | |
Molecular Function | poly(A) RNA polymerase activity | |
Molecular Function | RNA binding | |
Biological Process | co-transcriptional mRNA 3'-end processing, cleavage and polyadenylation pathway | |
Biological Process | nuclear-transcribed mRNA catabolic process, meiosis-specific transcripts |
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 > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Metschnikowiaceae > Metschnikowiaceae incertae sedis > Candida/Metschnikowiaceae
Accessions
- Primary accessionA0A2P7YFJ4
Proteomes
Organism-specific databases
Subcellular Location
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 6-199 | Poly(A) polymerase nucleotidyltransferase | ||||
Sequence: GVTPPISLANASPKDIELNDLLIKELKTRGSFESESATKKRVEVLNILQKMTEDFVYQVSKNKNMSDGMAKDAGGRIFTFGSYRLGVYGPGSDIDTLVVAPKHVSRSDFFEVYSSLLEKRPEVSEIAPVPDAFVPIIKIEFSGISIDLIFAKLDIPRVPRDLTLDNKNLLKNLDDKDLRALNGTRVTDEILTLV | ||||||
Domain | 204-348 | Poly(A) polymerase central | ||||
Sequence: VFKHALRCIKMWAQQRAVYANVFGFPGGVAWAMLVARICQLYPNTVSAVIVEKFFQIYSKWNWPQPVLLKQIEDGPLQVRVWNPRLYPHDRQHRMPIITPAYPSMCATHNITQSTKEIILKELERGMNVMSQIVKGEALWGTLLQ | ||||||
Domain | 351-519 | Poly(A) polymerase RNA-binding | ||||
Sequence: TFFHDYKFYLCIVAATKGASADHLKWSGLIESKVRFLVQKLELTEGIAMAHPYVKPFEVSLKCRDDEQVKQVIDGYGNLQGEKLTEGLDLMEENAENAKDVHLTKLYIGLSITEGHKKLDIQYPCSEFFNICKGWTEFSEEKNVVLIKNVKLYDLPNDVYVEGEQRPVK | ||||||
Compositional bias | 517-531 | Basic and acidic residues | ||||
Sequence: PVKAPKRKKTNVASE | ||||||
Region | 517-544 | Disordered | ||||
Sequence: PVKAPKRKKTNVASENIKRPKNAIPATT |
Sequence similarities
Belongs to the poly(A) polymerase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length544
- Mass (Da)61,639
- Last updated2018-05-23 v1
- ChecksumE97714B5E64EBBAE
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 517-531 | Basic and acidic residues | ||||
Sequence: PVKAPKRKKTNVASE |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
PYFQ01000019 EMBL· GenBank· DDBJ | PSK34738.1 EMBL· GenBank· DDBJ | Genomic DNA |