A0A7S0DQ90 · A0A7S0DQ90_9EUKA

  • Protein
    DNA-(apurinic or apyrimidinic site) endonuclease
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

Cofactor

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

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Note: Probably binds two magnesium or manganese ions per subunit.
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Features

Showing features for binding site, active site, site.

143050100150200250300350400
Type
IDPosition(s)Description
Binding site140Mg2+ 1 (UniProtKB | ChEBI)
Binding site173Mg2+ 1 (UniProtKB | ChEBI)
Active site258
Active site295Proton donor/acceptor
Binding site295Mg2+ 1 (UniProtKB | ChEBI)
Binding site297Mg2+ 1 (UniProtKB | ChEBI)
Site297Transition state stabilizer
Site370Important for catalytic activity
Binding site416Mg2+ 1 (UniProtKB | ChEBI)
Active site417Proton acceptor
Binding site417Mg2+ 1 (UniProtKB | ChEBI)
Site417Interaction with DNA substrate

GO annotations

AspectTerm
Cellular Componentnucleus
Molecular FunctionDNA binding
Molecular FunctionDNA-(apurinic or apyrimidinic site) endonuclease activity
Molecular Functiondouble-stranded DNA 3'-5' DNA exonuclease activity
Molecular Functionendonuclease activity
Molecular Functionmetal ion binding
Molecular Functionphosphoric diester hydrolase activity
Biological Processbase-excision repair

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    DNA-(apurinic or apyrimidinic site) endonuclease
  • EC number

Gene names

    • ORF names
      LAMO00422_LOCUS21062

Organism names

Accessions

  • Primary accession
    A0A7S0DQ90

Subcellular Location

PTM/Processing

Features

Showing features for signal, chain.

Type
IDPosition(s)Description
Signal1-17
ChainPRO_503073909418-430DNA-(apurinic or apyrimidinic site) endonuclease

Family & Domains

Features

Showing features for compositional bias, region, domain.

Type
IDPosition(s)Description
Compositional bias51-82Basic and acidic residues
Region51-118Disordered
Compositional bias92-108Polar residues
Domain137-417Endonuclease/exonuclease/phosphatase

Sequence similarities

Belongs to the DNA repair enzymes AP/ExoA family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Length
    430
  • Mass (Da)
    47,975
  • Last updated
    2021-06-02 v1
  • Checksum
    3EF375D7B8A03659
AGMKSALFLMLIPSTLARFGKVCGRFQRVTHPPRRPLPLAAREHVRFVHRATLRGGGEDGDEVEERKGRKRGRKDEDSTNPQPKPKRNPNSKPRSSDTGKISSKTRRTGVSAGRERIARDHTQRFPLLQGEIGIKIVSWNVAGLRSILNKPEKLKVLKRLIDEENPDIVCLQETKLQDSHVDKIAEELNREIGMSGFWACSTERKGYSGVATLLKNGYESLGIPSPAHRVVHGPGEGGAEGRIVETTFGPNLRLLNLYVPNSGAGLKRLDYRVNTWDTWLQDNISGDINVVICGDLNVAHKDSDFFCPENKAYETQAGTTPAERESFGRMLKECELIDTFRHLHPKAKGVYSYWSQRARNRDWNRGLRLDYFVVNKKLVEGTHDISVDNAADGSKSTKIRVVDSFVLDSSTLGVSDHAPVGLLLGVKRLD

Features

Showing features for non-terminal residue, compositional bias.

Type
IDPosition(s)Description
Non-terminal residue1
Compositional bias51-82Basic and acidic residues
Compositional bias92-108Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
HBEM01030920
EMBL· GenBank· DDBJ
CAD8462102.1
EMBL· GenBank· DDBJ
Transcribed RNA

Similar Proteins

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