P48561 · TRF5_YEAST

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.

Caution

Was originally thought to have DNA polymerase activity.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site233Mg2+ (UniProtKB | ChEBI); catalytic
Binding site235Mg2+ (UniProtKB | ChEBI); catalytic
Binding site298ATP (UniProtKB | ChEBI)
Binding site323ATP (UniProtKB | ChEBI)
Binding site428ATP (UniProtKB | ChEBI)
Binding site432ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentnucleolus
Cellular ComponentTRAMP complex
Molecular FunctionATP binding
Molecular Functionmetal ion binding
Molecular Functionpoly(A) RNA polymerase activity
Biological Processcell division
Biological Processhistone mRNA catabolic process
Biological Processnuclear polyadenylation-dependent CUT catabolic process
Biological Processnuclear polyadenylation-dependent mRNA catabolic process
Biological Processnuclear polyadenylation-dependent rRNA catabolic process
Biological Processnuclear polyadenylation-dependent snoRNA catabolic process
Biological Processnuclear polyadenylation-dependent snRNA catabolic process
Biological Processpoly(A)-dependent snoRNA 3'-end processing
Biological Processpolyadenylation-dependent ncRNA catabolic process
Biological ProcessRNA 3'-end processing
Biological ProcessRNA fragment catabolic process
Biological ProcessTRAMP-dependent tRNA surveillance pathway
Biological ProcessU4 snRNA 3'-end processing

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Poly(A) RNA polymerase protein 1
  • EC number
  • Alternative names
    • Topoisomerase 1-related protein TRF5

Gene names

    • Name
      TRF5
    • ORF names
      N0440
    • Ordered locus names
      YNL299W

Organism names

Accessions

  • Primary accession
    P48561
  • Secondary accessions
    • D6W0P5

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00001203161-642Poly(A) RNA polymerase protein 1
Modified residue596Phosphoserine
Modified residue602Phosphoserine

Keywords

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

TypeEntry 1Entry 2Number of experimentsIntact
BINARY P48561MTR4 P470478EBI-19525, EBI-11592

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for region, compositional bias, domain.

TypeIDPosition(s)Description
Region1-29Disordered
Compositional bias84-100Basic and acidic residues
Region84-104Disordered
Domain368-428PAP-associated
Compositional bias535-552Basic and acidic residues
Region535-642Disordered
Compositional bias579-595Polar residues
Compositional bias600-631Basic and acidic residues

Sequence similarities

Belongs to the DNA polymerase type-B-like family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    642
  • Mass (Da)
    74,179
  • Last updated
    2007-05-29 v2
  • Checksum
    67D4CD75AEBAE1A4
MTRLKAKYSPTKGKRKEDKHTKRMRKSSFTRTQKMLEVFNDNRSHFNKYESLAIDVEDDDTFGNLVLMENDKSDVDIPVIEEVTSSEDEQRAESSKRNNSLEDNQDFIAFSDSSEDETEQIKEDDDERSSFLLTDEHEVSKLTSQQSLNTESACNVEYPWIRNHCHSKQRRIADWLTSEIKDFVHYISPSKNEIKCRNRTIDKLRRAVKELWSDADLHVFGSFATDLYLPGSDIDCVVNSRNRDKEDRNYIYELARHLKNKGLAIRMEVIVKTRVPIIKFIEPQSQLHIDVSFERTNGLEAAKLIREWLRDSPGLRELVLIIKQFLHSRRLNNVHTGGLGGFTVICLVYSFLNMHPRIKSNDIDVLDNLGVLLIDFFELYGKNFGYDDVAISISDGYASYIPKSCWRTLEPSRSKFSLAIQDPGDPNNNISRGSFNMKDIKKAFAGAFELLVNKCWELNSATFKDRVGKSILGNVIKYRGQKRDFNDERDLVQNKAIIENERYHKRRTRIVQEDLFINDTEDLPVEEIYKLDEPAKKKQKAKKDKREGEIKKSAIPSPPPDFGVSRSKLKRKVKKTDQGSLLHQNNLSIDDLMGLSENDQESDQDQKGRDTPSGQDEKSPLETKTVDAQTRRDYWLSKGQAL

Sequence caution

The sequence AAC49099.1 differs from that shown. Reason: Frameshift
The sequence AAC49397.1 differs from that shown. Reason: Frameshift
The sequence CAA96217.1 differs from that shown. Reason: Frameshift

Features

Showing features for compositional bias, sequence conflict.

TypeIDPosition(s)Description
Compositional bias84-100Basic and acidic residues
Sequence conflict354-355in Ref. 1; AAC49397
Compositional bias535-552Basic and acidic residues
Compositional bias579-595Polar residues
Compositional bias600-631Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

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