A0A2P7YFJ4 · A0A2P7YFJ4_9ASCO

Function

function

Polymerase that creates the 3'-poly(A) tail of mRNA's.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Binds 2 magnesium ions. Also active with manganese.
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site85-87ATP (UniProtKB | ChEBI)
Binding site98Mg2+ 2 (UniProtKB | ChEBI); catalytic
Binding site98Mg2+ 1 (UniProtKB | ChEBI); catalytic
Binding site98-100ATP (UniProtKB | ChEBI)
Binding site100Mg2+ 1 (UniProtKB | ChEBI); catalytic
Binding site100Mg2+ 2 (UniProtKB | ChEBI); catalytic
Binding site152ATP (UniProtKB | ChEBI)
Binding site152Mg2+ 2 (UniProtKB | ChEBI); catalytic
Binding site213ATP (UniProtKB | ChEBI)
Binding site222ATP (UniProtKB | ChEBI)
Binding site231-232ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Cellular ComponentMei2 nuclear dot complex
Cellular ComponentmRNA cleavage and polyadenylation specificity factor complex
Cellular Componentnuclear exosome focus
Molecular FunctionATP binding
Molecular Functionmetal ion binding
Molecular Functionpoly(A) RNA polymerase activity
Molecular FunctionRNA binding
Biological Processco-transcriptional mRNA 3'-end processing, cleavage and polyadenylation pathway
Biological Processnuclear-transcribed mRNA catabolic process, meiosis-specific transcripts

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Poly(A) polymerase
  • EC number

Gene names

    • ORF names
      C7M61_004932

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • B12108
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Metschnikowiaceae > Metschnikowiaceae incertae sedis > Candida/Metschnikowiaceae

Accessions

  • Primary accession
    A0A2P7YFJ4

Proteomes

Organism-specific databases

Subcellular Location

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, compositional bias, region.

TypeIDPosition(s)Description
Domain6-199Poly(A) polymerase nucleotidyltransferase
Domain204-348Poly(A) polymerase central
Domain351-519Poly(A) polymerase RNA-binding
Compositional bias517-531Basic and acidic residues
Region517-544Disordered

Sequence similarities

Belongs to the poly(A) polymerase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    544
  • Mass (Da)
    61,639
  • Last updated
    2018-05-23 v1
  • Checksum
    E97714B5E64EBBAE
MNSQLGVTPPISLANASPKDIELNDLLIKELKTRGSFESESATKKRVEVLNILQKMTEDFVYQVSKNKNMSDGMAKDAGGRIFTFGSYRLGVYGPGSDIDTLVVAPKHVSRSDFFEVYSSLLEKRPEVSEIAPVPDAFVPIIKIEFSGISIDLIFAKLDIPRVPRDLTLDNKNLLKNLDDKDLRALNGTRVTDEILTLVPKPTVFKHALRCIKMWAQQRAVYANVFGFPGGVAWAMLVARICQLYPNTVSAVIVEKFFQIYSKWNWPQPVLLKQIEDGPLQVRVWNPRLYPHDRQHRMPIITPAYPSMCATHNITQSTKEIILKELERGMNVMSQIVKGEALWGTLLQRHTFFHDYKFYLCIVAATKGASADHLKWSGLIESKVRFLVQKLELTEGIAMAHPYVKPFEVSLKCRDDEQVKQVIDGYGNLQGEKLTEGLDLMEENAENAKDVHLTKLYIGLSITEGHKKLDIQYPCSEFFNICKGWTEFSEEKNVVLIKNVKLYDLPNDVYVEGEQRPVKAPKRKKTNVASENIKRPKNAIPATT

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias517-531Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
PYFQ01000019
EMBL· GenBank· DDBJ
PSK34738.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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