A0A093BLI4 · A0A093BLI4_CHAPE

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

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

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

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentmitochondrion
Cellular Componentnucleolus
Cellular Componentnucleoplasm
Molecular Function5'-3' exonuclease activity
Molecular Function5'-flap endonuclease activity
Molecular FunctionDNA binding
Molecular Functionmagnesium ion binding
Molecular Functionmanganese ion binding
Molecular FunctionRNA-DNA hybrid ribonuclease activity
Biological Processbase-excision repair
Biological ProcessDNA replication, removal of RNA primer

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Flap endonuclease 1
  • EC number
  • Short names
    FEN-1
  • Alternative names
    • Flap structure-specific endonuclease 1

Gene names

    • ORF names
      M959_11883

Organism names

  • Taxonomic identifier
  • Strain
    • M959
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Archelosauria > Archosauria > Dinosauria > Saurischia > Theropoda > Coelurosauria > Aves > Neognathae > Neoaves > Strisores > Apodiformes > Apodidae > Apodinae > Chaetura

Accessions

  • Primary accession
    A0A093BLI4

Proteomes

Subcellular Location

Nucleus, nucleolus
Nucleus, nucleoplasm
Mitochondrion
Note: Resides mostly in the nucleoli and relocalizes to the nucleoplasm upon DNA damage.

Keywords

PTM/Processing

Keywords

Interaction

Subunit

Interacts with PCNA. Three molecules of FEN1 bind to one PCNA trimer with each molecule binding to one PCNA monomer. PCNA stimulates the nuclease activity without altering cleavage specificity. The C-terminal domain binds EP300; can bind simultaneously to both PCNA and EP300. Interacts with DDX11; this interaction is direct and increases flap endonuclease activity of FEN1. Interacts with WDR4; regulating its endonuclease activity. Interacts with POLB.

Family & Domains

Features

Showing features for domain, region, compositional bias.

TypeIDPosition(s)Description
Domain1-107XPG N-terminal
Region94-120Disordered
Domain146-218XPG-I
Region351-379Disordered
Compositional bias352-366Basic and acidic residues

Sequence similarities

Belongs to the XPG/RAD2 endonuclease family. FEN1 subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    379
  • Mass (Da)
    42,680
  • Last updated
    2014-11-26 v1
  • Checksum
    324C55E29527F8AA
MGIHGLAKLIAEVSPGAIREQDIKAYFGRKVAIDASMSIYQFLIAVRQGAEALQSQDGDTTSHLVGMFYRTIRMVESGIKPVYVFDGKPPQLKSGELAKRTERRAEAEKHLQEAQEAGEESNVEKYSKRLVKVTQQHTDECKKLLTLMGIPYVEAPGEAEASCATLVKAGKVYAAATEDMDCLTFGSPVLMRHLTASETKKLPIQEFHLNRILQDLELSWEQFVDLCILLGCDYCESIRGIGPKRAVELIREHKSIERIIQQIDTKKYPLPENWLHKEAQKLFLEPDVVDPEAVELKWTEPQEEQLVEFLCGEKQFNEERIRNGVKRLSKSRQGSTQGRLDDFFKVTGSITSAKRKEPETKGSAKKKAKTTNSKAKKGK

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias352-366Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KN127055
EMBL· GenBank· DDBJ
KFU94769.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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