A0AAD9GH99 · A0AAD9GH99_BABDI

  • Protein
    Poly(A) polymerase
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

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 site94-96ATP (UniProtKB | ChEBI)
Binding site107Mg2+ 2 (UniProtKB | ChEBI); catalytic
Binding site107Mg2+ 1 (UniProtKB | ChEBI); catalytic
Binding site107-109ATP (UniProtKB | ChEBI)
Binding site109Mg2+ 1 (UniProtKB | ChEBI); catalytic
Binding site109Mg2+ 2 (UniProtKB | ChEBI); catalytic
Binding site161ATP (UniProtKB | ChEBI)
Binding site161Mg2+ 2 (UniProtKB | ChEBI); catalytic
Binding site222ATP (UniProtKB | ChEBI)
Binding site231ATP (UniProtKB | ChEBI)
Binding site240-241ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentnucleus
Molecular FunctionATP binding
Molecular Functionmetal ion binding
Molecular Functionpoly(A) RNA polymerase activity
Molecular FunctionRNA binding
Biological ProcessmRNA processing
Biological ProcessRNA 3'-end processing

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Poly(A) polymerase
  • EC number

Gene names

    • ORF names
      X943_001176

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • 1802A
  • Taxonomic lineage
    Eukaryota > Sar > Alveolata > Apicomplexa > Aconoidasida > Piroplasmida > Babesiidae > Babesia

Accessions

  • Primary accession
    A0AAD9GH99

Proteomes

Subcellular Location

Keywords

  • Cellular component

Family & Domains

Features

Showing features for compositional bias, region, domain.

Type
IDPosition(s)Description
Compositional bias1-18Polar residues
Region1-27Disordered
Domain14-208Poly(A) polymerase nucleotidyltransferase
Domain213-364Poly(A) polymerase central
Domain369-426Poly(A) polymerase RNA-binding

Sequence similarities

Belongs to the poly(A) polymerase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    514
  • Mass (Da)
    59,193
  • Last updated
    2024-05-29 v1
  • Checksum
    B52DEE22990B75B4
MNNAQPAKNLQRYGITDPVSTNGPAEGDREATEEFVKLLKSHSLFETDEGKRKRERVLEALNRALQQFVRRTSKRALGIEGADASKISAKLLTFGSYRLGIVAPDSDIDCLCLCPQSVTREAFFGDFYASLKLIPAITKLHAVPDAYTPVIKLIYDGVDIDLLFANLPAPSVPEELDILDDSILRNMNEATARSVNGCRVAALILSLVPNKDNFRTTLRYVKLWANRRGLYTTVMGYMGGVAWAILTARVCQLYPNYLPNQLIQRFFKVYAQWNWKYPVMLCKIKEVPNVPGYMSFKVWDPRTNHTDRQHLMPVITPAFPSMNSTHNITLTTKRILTDEFKRADEMLKSHRNTKDMRKVWNQVLEKEDMFASHKHFLVIEAMATTEHIHGKWEGWIGSRMRYLIKKLEVVPDILVRPWPEFFKYKHDEWDYASCVFFGFKCKSAEATQPATRGETTTKTFDMRMSIKGFKEIINTWTEMDTYKDQIAVNIKYLKNSQLPYFVSPRHKRTAEEMA

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias1-18Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JAHBMH010000024
EMBL· GenBank· DDBJ
KAK1938434.1
EMBL· GenBank· DDBJ
Genomic DNA

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.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp