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Flap endonuclease 1 (FEN-1) (EC 3.1.-.-) (Flap structure-specific endonuclease 1)

 FEN1_KLULA              Reviewed;         381 AA.
Q6CLH4;
11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
16-AUG-2004, sequence version 1.
16-JAN-2019, entry version 87.
RecName: Full=Flap endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140};
Short=FEN-1 {ECO:0000255|HAMAP-Rule:MF_03140};
EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_03140};
AltName: Full=Flap structure-specific endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_03140};
Name=FEN1 {ECO:0000255|HAMAP-Rule:MF_03140};
OrderedLocusNames=KLLA0F02992g;
Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC
1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
NCBI_TaxID=284590;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 /
WM37;
PubMed=15229592; DOI=10.1038/nature02579;
Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C.,
Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A.,
Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A.,
Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
Wincker P., Souciet J.-L.;
"Genome evolution in yeasts.";
Nature 430:35-44(2004).
-!- 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 structurs 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.
{ECO:0000255|HAMAP-Rule:MF_03140}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000255|HAMAP-Rule:MF_03140};
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. {ECO:0000255|HAMAP-
Rule:MF_03140};
-!- 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. {ECO:0000255|HAMAP-Rule:MF_03140}.
-!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000255|HAMAP-
Rule:MF_03140}. Nucleus, nucleoplasm {ECO:0000255|HAMAP-
Rule:MF_03140}. Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03140}.
Note=Resides mostly in the nucleoli and relocalizes to the
nucleoplasm upon DNA damage. {ECO:0000255|HAMAP-Rule:MF_03140}.
-!- PTM: Phosphorylated. Phosphorylation upon DNA damage induces
relocalization to the nuclear plasma. {ECO:0000255|HAMAP-
Rule:MF_03140}.
-!- SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. FEN1
subfamily. {ECO:0000255|HAMAP-Rule:MF_03140}.
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EMBL; CR382126; CAG97923.1; -; Genomic_DNA.
RefSeq; XP_455215.1; XM_455215.1.
ProteinModelPortal; Q6CLH4; -.
STRING; 284590.XP_455215.1; -.
PRIDE; Q6CLH4; -.
EnsemblFungi; CAG97923; CAG97923; KLLA0_F02992g.
GeneID; 2895779; -.
KEGG; kla:KLLA0_F02992g; -.
eggNOG; KOG2519; Eukaryota.
eggNOG; COG0258; LUCA.
HOGENOM; HOG000193853; -.
InParanoid; Q6CLH4; -.
KO; K04799; -.
OMA; GSQDYDS; -.
Proteomes; UP000000598; Chromosome F.
GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
GO; GO:0008409; F:5'-3' exonuclease activity; IEA:UniProtKB-UniRule.
GO; GO:0017108; F:5'-flap endonuclease activity; IEA:UniProtKB-UniRule.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
GO; GO:0006286; P:base-excision repair, base-free sugar-phosphate removal; IEA:EnsemblFungi.
GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
GO; GO:0043137; P:DNA replication, removal of RNA primer; IEA:UniProtKB-UniRule.
GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IEA:EnsemblFungi.
GO; GO:0000734; P:gene conversion at mating-type locus, DNA repair synthesis; IEA:EnsemblFungi.
GO; GO:0035753; P:maintenance of DNA trinucleotide repeats; IEA:EnsemblFungi.
GO; GO:0001302; P:replicative cell aging; IEA:EnsemblFungi.
CDD; cd09867; PIN_FEN1; 1.
HAMAP; MF_00614; Fen; 1.
InterPro; IPR036279; 5-3_exonuclease_C_sf.
InterPro; IPR023426; Flap_endonuc.
InterPro; IPR008918; HhH2.
InterPro; IPR029060; PIN-like_dom_sf.
InterPro; IPR006086; XPG-I_dom.
InterPro; IPR006084; XPG/Rad2.
InterPro; IPR019974; XPG_CS.
InterPro; IPR006085; XPG_DNA_repair_N.
PANTHER; PTHR11081; PTHR11081; 1.
Pfam; PF00867; XPG_I; 1.
Pfam; PF00752; XPG_N; 1.
PRINTS; PR00853; XPGRADSUPER.
SMART; SM00279; HhH2; 1.
SMART; SM00484; XPGI; 1.
SMART; SM00485; XPGN; 1.
SUPFAM; SSF47807; SSF47807; 1.
SUPFAM; SSF88723; SSF88723; 1.
PROSITE; PS00841; XPG_1; 1.
PROSITE; PS00842; XPG_2; 1.
3: Inferred from homology;
Complete proteome; DNA damage; DNA repair; DNA replication;
Endonuclease; Exonuclease; Hydrolase; Magnesium; Metal-binding;
Mitochondrion; Nuclease; Nucleus; Phosphoprotein; Reference proteome.
CHAIN 1 381 Flap endonuclease 1.
/FTId=PRO_0000403579.
REGION 1 105 N-domain.
REGION 120 251 I-domain.
REGION 339 347 Interaction with PCNA.
{ECO:0000255|HAMAP-Rule:MF_03140}.
METAL 34 34 Magnesium 1. {ECO:0000255|HAMAP-
Rule:MF_03140}.
METAL 87 87 Magnesium 1. {ECO:0000255|HAMAP-
Rule:MF_03140}.
METAL 156 156 Magnesium 1. {ECO:0000255|HAMAP-
Rule:MF_03140}.
METAL 158 158 Magnesium 1. {ECO:0000255|HAMAP-
Rule:MF_03140}.
METAL 177 177 Magnesium 2. {ECO:0000255|HAMAP-
Rule:MF_03140}.
METAL 179 179 Magnesium 2. {ECO:0000255|HAMAP-
Rule:MF_03140}.
METAL 231 231 Magnesium 2. {ECO:0000255|HAMAP-
Rule:MF_03140}.
BINDING 47 47 DNA substrate. {ECO:0000255|HAMAP-
Rule:MF_03140}.
BINDING 71 71 DNA substrate. {ECO:0000255|HAMAP-
Rule:MF_03140}.
BINDING 156 156 DNA substrate. {ECO:0000255|HAMAP-
Rule:MF_03140}.
BINDING 229 229 DNA substrate. {ECO:0000255|HAMAP-
Rule:MF_03140}.
BINDING 231 231 DNA substrate. {ECO:0000255|HAMAP-
Rule:MF_03140}.
SEQUENCE 381 AA; 43183 MW; 50194989AEEABA11 CRC64;
MGIKNLATLI SEQVPNAIKS RDIKYFHGRK VAIDASMSLY QFLIAVRQQD GVQLAGEDGE
TTSHLMGMFY RTLRMIDHGI KPCYVFDGSP PELKKYELDK RKVRREDTEA KLKEATEQAE
IIKHERRLVK VLPWHNEEAQ KLLSLMGIPY VVAPAEAEAQ CAELAKSGKV FAAASEDMDT
LCYQTPVLLR HLTFSEARKL PIQEFDTDVI YNTLDLTQTQ FIDLGIILGC DYCEGIKGVG
PVNALKLIKE HGSLEAIVEK FENGDISSGR WKIPEGWQFK EARDLFMQPD VIPSEEVTLK
WEEPKAEELI EFMVKEKGFN EDRIKSGIER LRKGLKVGVQ KRLDSFFKIQ PKTKEELATA
AKKAKDAKKK AAAKGKIAKR R


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