ID A0A1Y1JGR1_PLAGO Unreviewed; 621 AA. AC A0A1Y1JGR1; DT 30-AUG-2017, integrated into UniProtKB/TrEMBL. DT 30-AUG-2017, sequence version 1. DT 07-APR-2021, entry version 20. DE RecName: Full=Flap endonuclease 1 {ECO:0000256|HAMAP-Rule:MF_03140}; DE Short=FEN-1 {ECO:0000256|HAMAP-Rule:MF_03140}; DE EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_03140}; DE AltName: Full=Flap structure-specific endonuclease 1 {ECO:0000256|HAMAP-Rule:MF_03140}; GN Name=FEN1 {ECO:0000256|HAMAP-Rule:MF_03140}; GN ORFNames=PGO_030640 {ECO:0000313|EMBL:GAW79264.1}; OS Plasmodium gonderi. OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida; OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium). OX NCBI_TaxID=77519 {ECO:0000313|EMBL:GAW79264.1, ECO:0000313|Proteomes:UP000195521}; RN [1] {ECO:0000313|Proteomes:UP000195521} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 30045 {ECO:0000313|Proteomes:UP000195521}; RA Arisue N., Honma H., Kawai S., Tougan T., Tanabe K., Horii T.; RT "Plasmodium gonderi genome."; RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Structure-specific nuclease with 5'-flap endonuclease and 5'- CC 3' exonuclease activities involved in DNA replication and repair. CC During DNA replication, cleaves the 5'-overhanging flap structure that CC is generated by displacement synthesis when DNA polymerase encounters CC the 5'-end of a downstream Okazaki fragment. It enters the flap from CC the 5'-end and then tracks to cleave the flap base, leaving a nick for CC ligation. Also involved in the long patch base excision repair (LP-BER) CC pathway, by cleaving within the apurinic/apyrimidinic (AP) site- CC terminated flap. Acts as a genome stabilization factor that prevents CC flaps from equilibrating into structurs that lead to duplications and CC deletions. Also possesses 5'-3' exonuclease activity on nicked or CC gapped double-stranded DNA, and exhibits RNase H activity. Also CC involved in replication and repair of rDNA and in repairing CC mitochondrial DNA. {ECO:0000256|HAMAP-Rule:MF_03140}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_03140}; CC Note=Binds 2 magnesium ions per subunit. They probably participate in CC the reaction catalyzed by the enzyme. May bind an additional third CC magnesium ion after substrate binding. {ECO:0000256|HAMAP- CC Rule:MF_03140}; CC -!- SUBUNIT: Interacts with PCNA. Three molecules of FEN1 bind to one PCNA CC trimer with each molecule binding to one PCNA monomer. PCNA stimulates CC the nuclease activity without altering cleavage specificity. CC {ECO:0000256|HAMAP-Rule:MF_03140}. CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000256|HAMAP- CC Rule:MF_03140}. Nucleus, nucleoplasm {ECO:0000256|HAMAP-Rule:MF_03140}. CC Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03140}. Note=Resides mostly in CC the nucleoli and relocalizes to the nucleoplasm upon DNA damage. CC {ECO:0000256|HAMAP-Rule:MF_03140}. CC -!- PTM: Phosphorylated. Phosphorylation upon DNA damage induces CC relocalization to the nuclear plasma. {ECO:0000256|HAMAP- CC Rule:MF_03140}. CC -!- SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. FEN1 CC subfamily. {ECO:0000256|HAMAP-Rule:MF_03140}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03140}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:GAW79264.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BDQF01000003; GAW79264.1; -; Genomic_DNA. DR EnsemblProtists; GAW79264; GAW79264; PGO_030640. DR OrthoDB; 1094524at2759; -. DR Proteomes; UP000195521; Unassembled WGS sequence. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell. DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell. DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008409; F:5'-3' exonuclease activity; IEA:UniProtKB-UniRule. DR GO; GO:0017108; F:5'-flap endonuclease activity; IEA:UniProtKB-UniRule. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0006284; P:base-excision repair; IEA:UniProtKB-UniRule. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW. DR GO; GO:0043137; P:DNA replication, removal of RNA primer; IEA:UniProtKB-UniRule. DR HAMAP; MF_00614; Fen; 1. DR InterPro; IPR002421; 5-3_exonuclease. DR InterPro; IPR036279; 5-3_exonuclease_C_sf. DR InterPro; IPR023426; Flap_endonuc. DR InterPro; IPR008918; HhH2. DR InterPro; IPR029060; PIN-like_dom_sf. DR InterPro; IPR006086; XPG-I_dom. DR InterPro; IPR006084; XPG/Rad2. DR InterPro; IPR019974; XPG_CS. DR InterPro; IPR006085; XPG_DNA_repair_N. DR PANTHER; PTHR11081; PTHR11081; 1. DR Pfam; PF00867; XPG_I; 1. DR Pfam; PF00752; XPG_N; 1. DR PRINTS; PR00853; XPGRADSUPER. DR SMART; SM00475; 53EXOc; 1. DR SMART; SM00279; HhH2; 1. DR SMART; SM00484; XPGI; 1. DR SMART; SM00485; XPGN; 1. DR SUPFAM; SSF47807; SSF47807; 1. DR SUPFAM; SSF88723; SSF88723; 1. DR PROSITE; PS00841; XPG_1; 1. DR PROSITE; PS00842; XPG_2; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP- KW Rule:MF_03140}; KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP- KW Rule:MF_03140}; KW DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP- KW Rule:MF_03140}; KW Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|HAMAP- KW Rule:MF_03140}; KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP- KW Rule:MF_03140}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_03140}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_03140}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_03140}; KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128, ECO:0000256|HAMAP- KW Rule:MF_03140}; KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_03140}; KW Nucleus {ECO:0000256|HAMAP-Rule:MF_03140}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|HAMAP- KW Rule:MF_03140}; Reference proteome {ECO:0000313|Proteomes:UP000195521}. FT DOMAIN 1..109 FT /note="XPGN" FT /evidence="ECO:0000259|SMART:SM00485" FT DOMAIN 28..327 FT /note="53EXOc" FT /evidence="ECO:0000259|SMART:SM00475" FT DOMAIN 148..233 FT /note="XPGI" FT /evidence="ECO:0000259|SMART:SM00484" FT REGION 351..359 FT /note="Interaction with PCNA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03140" FT REGION 373..484 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 523..544 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 99..128 FT /evidence="ECO:0000256|SAM:Coils" FT COMPBIAS 373..436 FT /note="Polyampholyte" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 437..454 FT /note="Acidic" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT METAL 34 FT /note="Magnesium 1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03140" FT METAL 88 FT /note="Magnesium 1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03140" FT METAL 160 FT /note="Magnesium 1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03140" FT METAL 162 FT /note="Magnesium 1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03140" FT METAL 181 FT /note="Magnesium 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03140" FT METAL 183 FT /note="Magnesium 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03140" FT METAL 248 FT /note="Magnesium 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03140" FT BINDING 47 FT /note="DNA substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03140" FT BINDING 72 FT /note="DNA substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03140" FT BINDING 160 FT /note="DNA substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03140" FT BINDING 246 FT /note="DNA substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03140" FT BINDING 248 FT /note="DNA substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03140" SQ SEQUENCE 621 AA; 70652 MW; 57E728FCE4FEDF6B CRC64; MGIKGLTKFI ADAAPNAIKE IKIENLMGRV VAIDASMSLY QFIIAIRDSE QYGNLTNELG ETTSHISGLM SRSIKLMENG LKPIYVFDGA PPELKGSELE KRGEKRQKAE ELLKKAKEEG NIEEIKKQSG RTVRVTKKQN EEAKKLLTLM GIPVVEAPCE AESQCAFLTK YNLAHATATE DADALVFGTK ILIRNLNANA SSSANQNKNK NSSKRGYILT EINLEQVLKG LNLNMNEFID FCILCGCDYC DTIKGIGSKT AYNLIKEYNC IEKIIENIDK NKYQVPANFR FVEARDSFIN PKVLSKEEVK IDWCEPKIEE LKNFLIKDYN FNEVRVTNYI NRLLKARKAT TQRRLDNFFT ACTKKSTKLI IEESQKELKP KRKGKKRDLP IDGSTKLNAK QKKEQNKKVK VENEDKKTSI KNESKEELQN HHMEEAEEGE VEEEVEEEVE EEKDDAMGLA PPFDEEQDEG DNPSPNFFHH KSDSESGNLK IAEMEKMEEI EEMEQNVKND NISPVYNCTN GNDTLGNNTH LSSNSTSYSR NSLNNNKKID ESVKHLTNDS PRDDNNHLCS SELFPHNTTD CLNNNSDMMQ SQVKKKNILF LLPYCPKNVT SVKKRKSIQR F //