R4G5E8 · R4G5E8_RHOPR

Function

function

DNA polymerase that functions in several pathways of DNA repair. Involved in base excision repair (BER) responsible for repair of lesions that give rise to abasic (AP) sites in DNA. Also contributes to DNA double-strand break repair by non-homologous end joining and homologous recombination. Has both template-dependent and template-independent (terminal transferase) DNA polymerase activities. Has also a 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity.
Repair polymerase that plays a key role in base-excision repair. During this process, the damaged base is excised by specific DNA glycosylases, the DNA backbone is nicked at the abasic site by an apurinic/apyrimidic (AP) endonuclease, and POLB removes 5'-deoxyribose-phosphate from the preincised AP site acting as a 5'-deoxyribose-phosphate lyase (5'-dRP lyase); through its DNA polymerase activity, it adds one nucleotide to the 3' end of the arising single-nucleotide gap. Conducts 'gap-filling' DNA synthesis in a stepwise distributive fashion rather than in a processive fashion as for other DNA polymerases. It is also able to cleave sugar-phosphate bonds 3' to an intact AP site, acting as an AP lyase.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Features

Showing features for active site.

TypeIDPosition(s)Description
Active site73Nucleophile; Schiff-base intermediate with DNA; for 5'-dRP lyase activity

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentnucleus
Molecular Functionclass I DNA-(apurinic or apyrimidinic site) endonuclease activity
Molecular FunctionDNA binding
Molecular FunctionDNA-directed DNA polymerase activity
Molecular Functionmetal ion binding
Biological Processbase-excision repair
Biological Processdouble-strand break repair via nonhomologous end joining

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    DNA polymerase
  • EC number

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Paraneoptera > Hemiptera > Heteroptera > Panheteroptera > Cimicomorpha > Reduviidae > Triatominae > Rhodnius

Accessions

  • Primary accession
    R4G5E8

Subcellular Location

Keywords

  • Cellular component

PTM/Processing

Keywords

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain11-313DNA-directed DNA polymerase X
Domain58-77Helix-hairpin-helix DNA-binding motif class 1
Domain99-118Helix-hairpin-helix DNA-binding motif class 1

Sequence similarities

Belongs to the DNA polymerase type-X family.

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Length
    313
  • Mass (Da)
    35,512
  • Last updated
    2013-06-26 v1
  • Checksum
    DE1EFC769DAB2E83
MGKRKAPSDDNLNQDFCDFLNELADYEKNVNRNIHKHNAYRKAARVLAEHPVRIKSGEEAKKLNGIGAKIAAKIEEFIQTGKLRKLEVIREDDTTQAVNQLTRVSGIGPAKAQELLKMGIKTIEVLKNNKDKLNHHQLIGLKYLEDFEIKIPRKEIEIIENIIRKEIGTVDEDYLITICGSYRRGKTESGDVDVLITHPRFDSENTDKQRPTKLLKSVVSALEQKNLITDTISLGVCKADRLARRLDIRLTPHDQYHCAVLYFTGSDMFNKEMRAHALTQGFTLNEYCLRPIGSTGVPGKPLPVSSEKDVFDY

Features

Showing features for non-terminal residue.

TypeIDPosition(s)Description
Non-terminal residue313

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
GAHY01000031
EMBL· GenBank· DDBJ
JAA77479.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

Disclaimer

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