A0A162IEV5 · A0A162IEV5_9HYPO
- ProteinFlap endonuclease 1
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids395 (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. It enters the flap from the 5'-end and then tracks to cleave the flap base, leaving a nick for ligation. Also involved in the long patch base excision repair (LP-BER) pathway, by cleaving within the apurinic/apyrimidinic (AP) site-terminated flap. 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, and exhibits RNase H activity. Also involved in replication and repair of rDNA and in repairing mitochondrial 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.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrion | |
Cellular Component | nucleolus | |
Cellular Component | nucleoplasm | |
Molecular Function | 5'-3' exonuclease activity | |
Molecular Function | 5'-flap endonuclease activity | |
Molecular Function | DNA binding | |
Molecular Function | magnesium ion binding | |
Biological Process | base-excision 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
- Organism
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Hypocreomycetidae > Hypocreales > Clavicipitaceae > Moelleriella
Accessions
- Primary accessionA0A162IEV5
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Note: Resides mostly in the nucleoli and relocalizes to the nucleoplasm upon DNA damage.
Keywords
- Cellular component
PTM/Processing
Keywords
- PTM
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 1-107 | XPG N-terminal | |||
Domain | 146-218 | XPG-I | |||
Region | 344-395 | Disordered | |||
Compositional bias | 351-389 | Basic and acidic residues | |||
Sequence similarities
Belongs to the XPG/RAD2 endonuclease family. FEN1 subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length395
- Mass (Da)44,884
- Last updated2016-07-06 v1
- Checksum42A8B133D3A0184C
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 351-389 | Basic and acidic residues | |||
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AZGY01000015 EMBL· GenBank· DDBJ | KZZ92423.1 EMBL· GenBank· DDBJ | Genomic DNA |