A0A7L4PS66 · A0A7L4PS66_9EURY
- ProteinFlap endonuclease 1
- Genefen
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids332 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. Binds the unpaired 3'-DNA end and kinks the DNA to facilitate 5' cleavage specificity. Cleaves one nucleotide into the double-stranded DNA from the junction in flap DNA, leaving a nick for ligation. Also involved in the base excision repair (BER) pathway. Acts as a genome stabilization factor that prevents flaps from equilibrating into structures that lead to duplications and deletions. Also possesses 5'-3' exonuclease activity on nicked or gapped double-stranded DNA.
Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. Binds the unpaired 3'-DNA end and kinks the DNA to facilitate 5' cleavage specificity. Cleaves one nucleotide into the double-stranded DNA from the junction in flap DNA, leaving a nick for ligation. Also involved in the base excision repair (BER) pathway. Acts as a genome stabilization factor that prevents flaps from equilibrating into structurs that lead to duplications and deletions. Also possesses 5'-3' exonuclease activity on nicked or gapped double-stranded DNA.
Cofactor
Note: Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 27 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 80 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 152 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 154 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 173 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 175 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 236 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | 5'-3' exonuclease activity | |
Molecular Function | 5'-flap endonuclease activity | |
Molecular Function | DNA binding | |
Molecular Function | magnesium ion binding | |
Biological Process | DNA repair | |
Biological Process | DNA replication, removal of RNA primer |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameFlap endonuclease 1
- EC number
- Short namesFEN-1
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageArchaea > Euryarchaeota > Stenosarchaea group > Candidatus Methanofastidiosia
Accessions
- Primary accessionA0A7L4PS66
Proteomes
Interaction
Subunit
Interacts with PCNA. PCNA stimulates the nuclease activity without altering cleavage specificity.
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-98 | N-domain | ||||
Sequence: MGVNLGEIVPKKKIDISDLKGKSVAIDAYNALYQFLAIIRQRDGTPLKNSKGEVTSHLSGLFYRSVNFIEQGIRPIYVFDGKPPELKFQTIEKRKEIK | ||||||
Domain | 1-101 | XPG N-terminal | ||||
Sequence: MGVNLGEIVPKKKIDISDLKGKSVAIDAYNALYQFLAIIRQRDGTPLKNSKGEVTSHLSGLFYRSVNFIEQGIRPIYVFDGKPPELKFQTIEKRKEIKEEA | ||||||
Domain | 21-325 | 5'-3' exonuclease | ||||
Sequence: GKSVAIDAYNALYQFLAIIRQRDGTPLKNSKGEVTSHLSGLFYRSVNFIEQGIRPIYVFDGKPPELKFQTIEKRKEIKEEAREKYIDAKSRGDFKEAKKYSQMTSSLKGDMITSSKELLTSMGIPYIEAPSEGEAQAAYVVLKGDADLSASQDYDSILFGAPALVRNLTISGKRKIPGKDLFVDVVPEIIDNQDVLNTLNLSRKQLIEVAILIGTDYNLGGIKGIGPKKAIEIVKEGKFGEYGEFDQIINLFLNPEVSDNYNISFEKPDKDRIVKILCDKYEFSELRVEKGIERIDFSLENTLKQ | ||||||
Domain | 140-221 | XPG-I | ||||
Sequence: TSMGIPYIEAPSEGEAQAAYVVLKGDADLSASQDYDSILFGAPALVRNLTISGKRKIPGKDLFVDVVPEIIDNQDVLNTLNL | ||||||
Region | 324-332 | Interaction with PCNA | ||||
Sequence: KQKTLDMYF |
Sequence similarities
Belongs to the XPG/RAD2 endonuclease family. FEN1 subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length332
- Mass (Da)37,345
- Last updated2021-04-07 v1
- ChecksumCD39834E4EC4BAC2