A0A194Q6J6 · A0A194Q6J6_PAPXU

Function

Catalytic activity

  • Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.
    EC:3.1.11.2 (UniProtKB | ENZYME | Rhea)

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Note: Probably binds two magnesium or manganese ions per subunit.

Features

Showing features for binding site, active site, site.

165150100150200250300350400450500550600650
Type
IDPosition(s)Description
Binding site396Mg2+ 1 (UniProtKB | ChEBI)
Binding site424Mg2+ 1 (UniProtKB | ChEBI)
Active site497
Active site536Proton donor/acceptor
Binding site536Mg2+ 1 (UniProtKB | ChEBI)
Binding site538Mg2+ 1 (UniProtKB | ChEBI)
Site538Transition state stabilizer
Site608Important for catalytic activity
Binding site633Mg2+ 1 (UniProtKB | ChEBI)
Active site634Proton acceptor
Binding site634Mg2+ 1 (UniProtKB | ChEBI)
Site634Interaction 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
      RR46_05264

Organism names

  • Taxonomic identifier
  • Strain
    • Ya'a_city_454_Px
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Lepidoptera > Glossata > Ditrysia > Papilionoidea > Papilionidae > Papilioninae > Papilio

Accessions

  • Primary accession
    A0A194Q6J6

Proteomes

Subcellular Location

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, compositional bias, domain.

Type
IDPosition(s)Description
Region1-369Disordered
Compositional bias8-92Basic and acidic residues
Compositional bias112-195Basic and acidic residues
Compositional bias203-233Basic and acidic residues
Compositional bias243-316Basic and acidic residues
Compositional bias331-369Basic and acidic residues
Domain394-634Endonuclease/exonuclease/phosphatase

Sequence similarities

Belongs to the DNA repair enzymes AP/ExoA family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    651
  • Mass (Da)
    73,106
  • Last updated
    2016-10-05 v1
  • Checksum
    863FC8F0ECAD36A3
MAPRSAKGKKAADVKVAESAPAKKGRKGKQVAEPEPTEAEEVKTTVVEKKTKRGKKAKDEEIINGDNEEVCPPAKKSKKKISEDKAEEQSNGDNSSPEEEPNLDEQNEGGDDESETNGHTEEAKPAGGRGRKKQTKKETVPENKPKETGRGRKNAKQEVQEDVAKNSEVVEEKPKPSGRGRGKKAQAKPSNDLEEEDKAESVEEEVKPEPPATKGKKKQNKGSKEKIETDAAMSDQEKEEEDIVEEEPKKKETKSRKNQGKKAQPKEQEDKEEDIVEDTQTTKKRRGAKKDDKSKDSKEEEEVEEKAPEVKPAKGKRGAKNAAAKAAEAEQDIQDTGESNNKRRRKAADDKAGAEDSKKKAPAKNKTATKYEDIDFSSDSKTSQGKDWNFKISSWNVDGIRAWMDKGGLEYIQYEKPDILCLQEIKCSKEKLPEPIKNVPGYHAYWLCSEQDGYAGVGIYTTKLAMNVQYGLQDEELDSEGRIITAEYEQFYLICTYVPNAGRKLVTLPKRLKWNEEFRKHVKSLDKKKPVIICGDMNVSHNEIDLANPKTNRKNAGFTEEERTGMTELLGDGFVDTYRLLYPDKTSAYTFWTYMFNCRAKNVGWRLDYFIVSERLVTSVCDSIIRDSVYGSDHCPVTLLLHLSSADKPKE

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias8-92Basic and acidic residues
Compositional bias112-195Basic and acidic residues
Compositional bias203-233Basic and acidic residues
Compositional bias243-316Basic and acidic residues
Compositional bias331-369Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KQ459439
EMBL· GenBank· DDBJ
KPJ00999.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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