R4G5E8 · R4G5E8_RHOPR
- ProteinDNA polymerase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids313 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score3/5
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
- 2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-phospho-2'-deoxyribonucleoside-DNA + H+
- a 5'-end 2'-deoxyribose-2'-deoxyribonucleotide-DNA = (2E,4S)-4-hydroxypenten-2-al-5-phosphate + a 5'-end 5'-phospho-2'-deoxyribonucleoside-DNA + H+
Cofactor
Features
Showing features for active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Active site | 73 | Nucleophile; Schiff-base intermediate with DNA; for 5'-dRP lyase activity | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | nucleus | |
Molecular Function | class I DNA-(apurinic or apyrimidinic site) endonuclease activity | |
Molecular Function | DNA binding | |
Molecular Function | DNA-directed DNA polymerase activity | |
Molecular Function | metal ion binding | |
Biological Process | base-excision repair | |
Biological Process | double-strand break repair via nonhomologous end joining |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDNA polymerase
- EC number
Organism names
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Paraneoptera > Hemiptera > Heteroptera > Panheteroptera > Cimicomorpha > Reduviidae > Triatominae > Rhodnius
Accessions
- Primary accessionR4G5E8
PTM/Processing
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 11-313 | DNA-directed DNA polymerase X | |||
Domain | 58-77 | Helix-hairpin-helix DNA-binding motif class 1 | |||
Domain | 99-118 | Helix-hairpin-helix DNA-binding motif class 1 | |||
Sequence similarities
Belongs to the DNA polymerase type-X family.
Family and domain databases
Sequence
- Sequence statusFragment
- Length313
- Mass (Da)35,512
- Last updated2013-06-26 v1
- ChecksumDE1EFC769DAB2E83
Features
Showing features for non-terminal residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Non-terminal residue | 313 | ||||
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
GAHY01000031 EMBL· GenBank· DDBJ | JAA77479.1 EMBL· GenBank· DDBJ | mRNA |