A0A8J5CFR0 · A0A8J5CFR0_CHIOP
- ProteinDNA polymerase
- GenePoll
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids622 (go to sequence)
- Protein existenceInferred from homology
- 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.
Catalytic activity
- a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Cofactor
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 358 | Nucleophile; Schiff-base intermediate with DNA; for 5'-dRP lyase activity | ||||
Sequence: K |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | nucleus | |
Molecular Function | DNA binding | |
Molecular Function | DNA-directed DNA polymerase activity | |
Molecular Function | metal ion binding | |
Biological Process | double-strand break repair via nonhomologous end joining |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDNA polymerase
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Crustacea > Multicrustacea > Malacostraca > Eumalacostraca > Eucarida > Decapoda > Pleocyemata > Brachyura > Eubrachyura > Majoidea > Majidae > Chionoecetes
Accessions
- Primary accessionA0A8J5CFR0
Proteomes
Subcellular Location
Structure
Family & Domains
Features
Showing features for region, domain, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-22 | Disordered | ||||
Sequence: MKRRNKGSLPCAKRSKGECEAG | ||||||
Domain | 24-122 | BRCT | ||||
Sequence: PPPPFLDGVKCHVHPASFGLMRRRIFENHVTRYGGELVASLPLASDVAYHVVFEETVDQERLKRLLDPSALPKSLFLRCTWLVACVKAMAKAGTEDHLI | ||||||
Region | 128-160 | Disordered | ||||
Sequence: VEEQSPEETGATQPKGTNGTCLGVNTQAEETNR | ||||||
Compositional bias | 129-159 | Polar residues | ||||
Sequence: EEQSPEETGATQPKGTNGTCLGVNTQAEETN | ||||||
Region | 194-268 | Disordered | ||||
Sequence: PKVKDTFPSGDPLTRVASHPSPHEQMESLESQASTVVRRENTKLEDKKEPSNLMAGEEQGNTSVARREGGGSEED | ||||||
Compositional bias | 217-231 | Polar residues | ||||
Sequence: EQMESLESQASTVVR | ||||||
Compositional bias | 232-246 | Basic and acidic residues | ||||
Sequence: RENTKLEDKKEPSNL |
Sequence similarities
Belongs to the DNA polymerase type-X family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length622
- Mass (Da)69,310
- Last updated2022-05-25 v1
- Checksum35CDCD2237D93452
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 129-159 | Polar residues | ||||
Sequence: EEQSPEETGATQPKGTNGTCLGVNTQAEETN | ||||||
Compositional bias | 217-231 | Polar residues | ||||
Sequence: EQMESLESQASTVVR | ||||||
Compositional bias | 232-246 | Basic and acidic residues | ||||
Sequence: RENTKLEDKKEPSNL |
Keywords
- Technical term