A0AAE1HDE5 · A0AAE1HDE5_9NEOP

  • Protein
    Flap endonuclease 1
  • Gene
    Fen1
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

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.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
FAD (UniProtKB | Rhea| CHEBI:57692 )

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.
Mo-molybdopterin (UniProtKB | Rhea| CHEBI:71302 )

[2Fe-2S] cluster (UniProtKB | Rhea| CHEBI:190135 )

GO annotations

AspectTerm
Cellular Componentmitochondrion
Cellular Componentnucleolus
Cellular Componentnucleoplasm
Cellular Componentperoxisome
Molecular Function2 iron, 2 sulfur cluster binding
Molecular Function5'-3' exonuclease activity
Molecular Function5'-flap endonuclease activity
Molecular FunctionDNA binding
Molecular FunctionFAD binding
Molecular Functioniron ion binding
Molecular Functionmagnesium ion binding
Molecular Functionmolybdenum ion binding
Molecular Functionxanthine dehydrogenase 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

    • Name
      Fen1
    • ORF names
      KUF71_008361

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • PL_HMW_Pooled
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Paraneoptera > Thysanoptera > Terebrantia > Thripoidea > Thripidae > Frankliniella

Accessions

  • Primary accession
    A0AAE1HDE5

Proteomes

Subcellular Location

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

Keywords

PTM/Processing

Keywords

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for coiled coil, region, domain.

TypeIDPosition(s)Description
Coiled coil122-149
Region374-401Disordered
Domain420-5072Fe-2S ferredoxin-type
Region588-630Disordered
Domain709-895FAD-binding PCMH-type

Sequence similarities

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

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,829
  • Mass (Da)
    201,391
  • Last updated
    2024-05-29 v1
  • Checksum
    D83BFE923AB711E7
MFGARSKVVNLSLAVSRQFHSSSIAMGILGLSKLIADIAPGAVKENEIKNYFGRKVAIDASMSLYQFLIAVRSEGAQLTDSSGETTSHLMGTFYRTIRLIENGIKPVYVFDGKPPEMKSGELNKRAERREEAQKALQKAEEAGDAENIDKFNRRLVKVTRHHGEECKELLKLMGVPFIDAPCEAEAQCAAMVKSGKVFATATEDMDALTFGCSVLLRHLTFSEARKMPIQEFHLNKVLEELELSRDEFIDLCILLGCDYCDSIRGVGPKRAMDLIKQHRNIETIIEKLDKNKYPIPEDWPYKEARRLFIEPEVADPETIELKWSEPDEEGLVKYLCGDKNFNEERVRNGAKKLAKARSGTTQGRLDTFFKVLQSPSGGQKRKSEAAKNTPNKRGKKGGSFRGKPNALAIATMPGAQVVSSTLVFFVNGKKVVDDAVDPEWTLLYYLRNKLRLCGTKLGCAEGGCGACTVMVSKLDRTTKKIAHLAVNACLAPVCAMHGLAVTTVEGIGSTRTRLHPVQERIAKAHGSQCGFCTPGIVMSMYALLRTLPKPNMHDLEVAMQGNLCRCTGYRPIIEGFRTFTEEWEQMQSTVRTHSLSNGKANGGVNGQSNGQSNGQSNGHSNGVNGHSNGVNGNGVANGGCGMGSKCCKVTGKGCGAAEDGEEPEPMDRAGRPAKLFDHNEFAPYDASQEPIFPPELVASAVLDNQYLIIKGPRVTWHRPTSLDTLLELKAKHSDAKIIVGNTEVGVETKFKNCLYPVEIMPSRIPELTAIERLPDAVRVGASVTLRDMEDYFLGVMKEEPESRTRIMKAIVAMLHYFAGRQIRNVGAIGGNVMTGSPISDMLPILLASNVNMEVRSKERGSRQIKLDHTFFTGYRRNVVKPDEILVSLDVPFTHADQYFYAFKQAKRRDDDIAIVNIAMNVTFEPGTKTIQDIYIAYGGMAPMTVQARKTREALIGRTWDESLLDVAYAALVDDLPLAPSAPGGMIRYRSSLTLSLFYKGFLKITDQLGKRLAAGVVAPLPAHLRSAAGGFHSKPPKSSQYYFLETDESKGPVGQPMVHKSAMKQAAGEAVYIDDIPRYENELYLGLVLSQRAHARILSIDPSAALAVEGVHLFLSAKDLPGEKNEWGAIFHDDEVFASTEVQHFGQIVAAVVAVDQPTAQRAAKLVKIQYEDLPVIVTIEDAIRNNSFHTKPSVLQSGDVDKAFAEAKHIVEGEVHMGGQEHFYLETQACIAVPRNEDDELEIFSSTQNPAETQKLVAHMLGVSSNRVVVRTKRMGGGFGGKESKGNVVALPCALAATRLGRPVRIMLDRDEDMLITGTRHPFFMRYRVAHTPEGRLVAADAHIYNNAGYSKDLSTSVLDRAMSHFENAYYIENSRATGYVCKTNLPSNTAFRGFGGPQGMFLAEHMIRHVADAVGKDPIEVAEMNLYREGHRTHYNQELVHCTLQRCWTQCLRDADYSRRIQEVQAFNKQHRYRKRGLAIVPTKFGIAFTSLFLNQAGALVLVYADGSVLLSHGGTEMGQGLHTKMIQVASRALQIPESYIFISETATDKVPNTSPTAASAGSDLNGMAVLDACDQIMERLKPYKEANPKGTWKDWVNKAYFDRVQLSASGFHATPDIGFNRETRTGKMFNYFTFGAAVTEVEIDCLTGDHQVLRSDIVMDLGESLNPAIDIGQVEGGFIQGYGLFTLEEMVYSPTGVIFSRGPGVYKLPGFADIPQEFNVALLKGAPNPRAVYSSKAVGEPPLFLAASAFFAIWEAVKAAREEAGLTGYFTLHSPATSARIRMACPDHLTKHFPEPEPGTFQPWNTATKYLWTNELTSRIHVHADF

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JAHWGI010000971
EMBL· GenBank· DDBJ
KAK3919212.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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