P48561 · TRF5_YEAST
- ProteinPoly(A) RNA polymerase protein 1
- GeneTRF5
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids642 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalytic subunit of the TRAMP5 complex which has a poly(A) RNA polymerase activity and is involved in a post-transcriptional quality control mechanism limiting inappropriate expression of genetic information. Polyadenylation is required for the degradative activity of the exosome on several of its nuclear RNA substrates like cryptic transcripts generated by RNA polymerase II and III, or hypomethylated pre-tRNAi-Met. Polyadenylates RNA processing and degradation intermediates of snRNAs, snoRNAs and mRNAs that accumulate in strains lacking a functional exosome. TRF5 is also required for proper nuclear division in mitosis and sister chromatid cohesion. Involved in the regulation of histone mRNA levels. May mediate mitotic chromosome condensation.
Miscellaneous
Present with 2240 molecules/cell in log phase SD medium.
Catalytic activity
- ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide
Cofactor
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 233 | Mg2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 235 | Mg2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 298 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 323 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 428 | ATP (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 432 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | nucleolus | |
Cellular Component | TRAMP complex | |
Molecular Function | ATP binding | |
Molecular Function | metal ion binding | |
Molecular Function | poly(A) RNA polymerase activity | |
Biological Process | cell division | |
Biological Process | histone mRNA catabolic process | |
Biological Process | nuclear polyadenylation-dependent CUT catabolic process | |
Biological Process | nuclear polyadenylation-dependent mRNA catabolic process | |
Biological Process | nuclear polyadenylation-dependent rRNA catabolic process | |
Biological Process | nuclear polyadenylation-dependent snoRNA catabolic process | |
Biological Process | nuclear polyadenylation-dependent snRNA catabolic process | |
Biological Process | poly(A)-dependent snoRNA 3'-end processing | |
Biological Process | polyadenylation-dependent ncRNA catabolic process | |
Biological Process | RNA 3'-end processing | |
Biological Process | RNA fragment catabolic process | |
Biological Process | TRAMP-dependent tRNA surveillance pathway | |
Biological Process | U4 snRNA 3'-end processing |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePoly(A) RNA polymerase protein 1
- EC number
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP48561
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000120316 | 1-642 | Poly(A) RNA polymerase protein 1 | |||
Sequence: MTRLKAKYSPTKGKRKEDKHTKRMRKSSFTRTQKMLEVFNDNRSHFNKYESLAIDVEDDDTFGNLVLMENDKSDVDIPVIEEVTSSEDEQRAESSKRNNSLEDNQDFIAFSDSSEDETEQIKEDDDERSSFLLTDEHEVSKLTSQQSLNTESACNVEYPWIRNHCHSKQRRIADWLTSEIKDFVHYISPSKNEIKCRNRTIDKLRRAVKELWSDADLHVFGSFATDLYLPGSDIDCVVNSRNRDKEDRNYIYELARHLKNKGLAIRMEVIVKTRVPIIKFIEPQSQLHIDVSFERTNGLEAAKLIREWLRDSPGLRELVLIIKQFLHSRRLNNVHTGGLGGFTVICLVYSFLNMHPRIKSNDIDVLDNLGVLLIDFFELYGKNFGYDDVAISISDGYASYIPKSCWRTLEPSRSKFSLAIQDPGDPNNNISRGSFNMKDIKKAFAGAFELLVNKCWELNSATFKDRVGKSILGNVIKYRGQKRDFNDERDLVQNKAIIENERYHKRRTRIVQEDLFINDTEDLPVEEIYKLDEPAKKKQKAKKDKREGEIKKSAIPSPPPDFGVSRSKLKRKVKKTDQGSLLHQNNLSIDDLMGLSENDQESDQDQKGRDTPSGQDEKSPLETKTVDAQTRRDYWLSKGQAL | ||||||
Modified residue | 596 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 602 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Component of the TRAMP5 complex composed of at least AIR1, MTR4 and TFR5. Interacts with POL2, DPB2 and DPB11.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P48561 | MTR4 P47047 | 8 | EBI-19525, EBI-11592 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-29 | Disordered | ||||
Sequence: MTRLKAKYSPTKGKRKEDKHTKRMRKSSF | ||||||
Compositional bias | 84-100 | Basic and acidic residues | ||||
Sequence: TSSEDEQRAESSKRNNS | ||||||
Region | 84-104 | Disordered | ||||
Sequence: TSSEDEQRAESSKRNNSLEDN | ||||||
Domain | 368-428 | PAP-associated | ||||
Sequence: NLGVLLIDFFELYGKNFGYDDVAISISDGYASYIPKSCWRTLEPSRSKFSLAIQDPGDPNN | ||||||
Compositional bias | 535-552 | Basic and acidic residues | ||||
Sequence: AKKKQKAKKDKREGEIKK | ||||||
Region | 535-642 | Disordered | ||||
Sequence: AKKKQKAKKDKREGEIKKSAIPSPPPDFGVSRSKLKRKVKKTDQGSLLHQNNLSIDDLMGLSENDQESDQDQKGRDTPSGQDEKSPLETKTVDAQTRRDYWLSKGQAL | ||||||
Compositional bias | 579-595 | Polar residues | ||||
Sequence: GSLLHQNNLSIDDLMGL | ||||||
Compositional bias | 600-631 | Basic and acidic residues | ||||
Sequence: QESDQDQKGRDTPSGQDEKSPLETKTVDAQTR |
Sequence similarities
Belongs to the DNA polymerase type-B-like family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length642
- Mass (Da)74,179
- Last updated2007-05-29 v2
- Checksum67D4CD75AEBAE1A4
Sequence caution
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 84-100 | Basic and acidic residues | ||||
Sequence: TSSEDEQRAESSKRNNS | ||||||
Sequence conflict | 354-355 | in Ref. 1; AAC49397 | ||||
Sequence: MH → ID | ||||||
Compositional bias | 535-552 | Basic and acidic residues | ||||
Sequence: AKKKQKAKKDKREGEIKK | ||||||
Compositional bias | 579-595 | Polar residues | ||||
Sequence: GSLLHQNNLSIDDLMGL | ||||||
Compositional bias | 600-631 | Basic and acidic residues | ||||
Sequence: QESDQDQKGRDTPSGQDEKSPLETKTVDAQTR |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U47282 EMBL· GenBank· DDBJ | AAC49397.1 EMBL· GenBank· DDBJ | Genomic DNA | Frameshift | |
U23084 EMBL· GenBank· DDBJ | AAC49099.1 EMBL· GenBank· DDBJ | Genomic DNA | Frameshift | |
Z71575 EMBL· GenBank· DDBJ | CAA96217.1 EMBL· GenBank· DDBJ | Genomic DNA | Frameshift | |
BK006947 EMBL· GenBank· DDBJ | DAA10261.1 EMBL· GenBank· DDBJ | Genomic DNA |