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

 A0A084G9R7_9PEZI        Unreviewed;       395 AA.
A0A084G9R7;
29-OCT-2014, integrated into UniProtKB/TrEMBL.
29-OCT-2014, sequence version 1.
22-NOV-2017, entry version 26.
RecName: Full=Flap endonuclease 1 {ECO:0000256|HAMAP-Rule:MF_03140};
Short=FEN-1 {ECO:0000256|HAMAP-Rule:MF_03140};
EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_03140};
AltName: Full=Flap structure-specific endonuclease 1 {ECO:0000256|HAMAP-Rule:MF_03140};
Name=FEN1 {ECO:0000256|HAMAP-Rule:MF_03140};
ORFNames=SAPIO_CDS3832 {ECO:0000313|EMBL:KEZ44079.1};
Scedosporium apiospermum.
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
Sordariomycetes; Hypocreomycetidae; Microascales; Microascaceae;
Scedosporium.
NCBI_TaxID=563466 {ECO:0000313|EMBL:KEZ44079.1, ECO:0000313|Proteomes:UP000028545};
[1] {ECO:0000313|EMBL:KEZ44079.1, ECO:0000313|Proteomes:UP000028545}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=IHEM 14462 {ECO:0000313|EMBL:KEZ44079.1,
ECO:0000313|Proteomes:UP000028545};
Vandeputte P., Rechenmann M., Bouchara J.-P.;
Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
-!- 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:0000256|HAMAP-Rule:MF_03140, ECO:0000256|SAAS:SAAS00725765}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_03140}.
-!- SUBCELLULAR LOCATION: Mitochondrion
{ECO:0000256|SAAS:SAAS00725520}.
-!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000256|HAMAP-
Rule:MF_03140}. Nucleus, nucleoplasm {ECO:0000256|HAMAP-
Rule:MF_03140}. Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03140}.
Note=Resides mostly in the nucleoli and relocalizes to the
nucleoplasm upon DNA damage. {ECO:0000256|HAMAP-Rule:MF_03140}.
-!- PTM: Phosphorylated. Phosphorylation upon DNA damage induces
relocalization to the nuclear plasma. {ECO:0000256|HAMAP-
Rule:MF_03140}.
-!- SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. FEN1
subfamily. {ECO:0000256|HAMAP-Rule:MF_03140}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:KEZ44079.1}.
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EMBL; JOWA01000089; KEZ44079.1; -; Genomic_DNA.
RefSeq; XP_016643878.1; XM_016786535.1.
EnsemblFungi; KEZ44079; KEZ44079; SAPIO_CDS3832.
GeneID; 27722904; -.
Proteomes; UP000028545; Unassembled WGS sequence.
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:0006284; P:base-excision repair; IEA:UniProtKB-UniRule.
GO; GO:0043137; P:DNA replication, removal of RNA primer; IEA:UniProtKB-UniRule.
CDD; cd09867; PIN_FEN1; 1.
Gene3D; 3.40.50.1010; -; 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;
Coiled coil {ECO:0000256|SAM:Coils};
Complete proteome {ECO:0000313|Proteomes:UP000028545};
DNA damage {ECO:0000256|HAMAP-Rule:MF_03140};
DNA repair {ECO:0000256|HAMAP-Rule:MF_03140};
DNA replication {ECO:0000256|HAMAP-Rule:MF_03140};
Endonuclease {ECO:0000256|HAMAP-Rule:MF_03140,
ECO:0000313|EMBL:KEZ44079.1};
Exonuclease {ECO:0000256|HAMAP-Rule:MF_03140};
Hydrolase {ECO:0000256|HAMAP-Rule:MF_03140,
ECO:0000313|EMBL:KEZ44079.1};
Magnesium {ECO:0000256|HAMAP-Rule:MF_03140};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_03140};
Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03140,
ECO:0000256|SAAS:SAAS00725731};
Nuclease {ECO:0000256|HAMAP-Rule:MF_03140,
ECO:0000313|EMBL:KEZ44079.1};
Nucleus {ECO:0000256|HAMAP-Rule:MF_03140,
ECO:0000256|SAAS:SAAS00631924};
Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_03140};
Reference proteome {ECO:0000313|Proteomes:UP000028545}.
DOMAIN 1 107 XPGN. {ECO:0000259|SMART:SM00485}.
DOMAIN 146 218 XPGI. {ECO:0000259|SMART:SM00484}.
REGION 1 104 N-domain. {ECO:0000256|HAMAP-
Rule:MF_03140}.
REGION 122 253 I-domain. {ECO:0000256|HAMAP-
Rule:MF_03140}.
REGION 341 349 Interaction with PCNA.
{ECO:0000256|HAMAP-Rule:MF_03140}.
COILED 352 390 {ECO:0000256|SAM:Coils}.
METAL 34 34 Magnesium 1. {ECO:0000256|HAMAP-
Rule:MF_03140}.
METAL 86 86 Magnesium 1. {ECO:0000256|HAMAP-
Rule:MF_03140}.
METAL 158 158 Magnesium 1. {ECO:0000256|HAMAP-
Rule:MF_03140}.
METAL 160 160 Magnesium 1. {ECO:0000256|HAMAP-
Rule:MF_03140}.
METAL 179 179 Magnesium 2. {ECO:0000256|HAMAP-
Rule:MF_03140}.
METAL 181 181 Magnesium 2. {ECO:0000256|HAMAP-
Rule:MF_03140}.
METAL 233 233 Magnesium 2. {ECO:0000256|HAMAP-
Rule:MF_03140}.
BINDING 47 47 DNA substrate. {ECO:0000256|HAMAP-
Rule:MF_03140}.
BINDING 70 70 DNA substrate. {ECO:0000256|HAMAP-
Rule:MF_03140}.
BINDING 158 158 DNA substrate. {ECO:0000256|HAMAP-
Rule:MF_03140}.
BINDING 231 231 DNA substrate. {ECO:0000256|HAMAP-
Rule:MF_03140}.
BINDING 233 233 DNA substrate. {ECO:0000256|HAMAP-
Rule:MF_03140}.
SEQUENCE 395 AA; 44962 MW; 2F5F691E9B94A251 CRC64;
MGIKNLASII KEHAPDAIKE GEIKNHFGRK VAIDASMSIY SFLIAVRSEG QQLMDESGQT
TSHLMGMFYR TLRMVDNGIK PLYVFDGAPP KLKSGELAKR FQRKQEAHEG LEEAKETGTS
EDVEKFARRT VRVTREHNAE CQRLLKLMGI PYIVAPTEAE AQCAVLARAG KVFAAASEDM
DTLCFNSPIL LRHLTFSEQR KEPIQEIHLD KVLEGLDMSR DQFVDFCILL GCDYLDPIPK
VGPTTALKLI REHKTLEKVV EAIQKDPKER FKLPEDWPYE DARELFFHPD VRPASDPLCD
FKWDKPDIEG LVQFLVTEKG FSEDRVRAGG KRLEKNLKSA QQVRLDGFFK VIPKTEEEKA
ALKRKNEEKN VEKRKKLKEE KKEKAKAKAK PRAAG


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