ID A0A1Y1JGR1_PLAGO Unreviewed; 621 AA. AC A0A1Y1JGR1; DT 30-AUG-2017, integrated into UniProtKB/TrEMBL. DT 30-AUG-2017, sequence version 1. DT 22-NOV-2017, entry version 4. 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; 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|EMBL:GAW79264.1, ECO:0000313|Proteomes:UP000195521} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 30045 {ECO:0000313|EMBL:GAW79264.1, RC 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 CC and 5'-3' exonuclease activities involved in DNA replication and CC repair. During DNA replication, cleaves the 5'-overhanging flap CC structure that is generated by displacement synthesis when DNA CC polymerase encounters the 5'-end of a downstream Okazaki fragment. CC It enters the flap from the 5'-end and then tracks to cleave the CC flap base, leaving a nick for ligation. Also involved in the long CC patch base excision repair (LP-BER) pathway, by cleaving within CC the apurinic/apyrimidinic (AP) site-terminated flap. Acts as a CC genome stabilization factor that prevents flaps from equilibrating CC into structurs that lead to duplications and deletions. Also CC possesses 5'-3' exonuclease activity on nicked or gapped double- CC stranded DNA, and exhibits RNase H activity. Also involved in CC replication and repair of rDNA and in repairing mitochondrial DNA. CC {ECO:0000256|HAMAP-Rule:MF_03140, ECO:0000256|SAAS:SAAS00725765}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_03140}; CC Note=Binds 2 magnesium ions per subunit. They probably participate CC in the reaction catalyzed by the enzyme. May bind an additional CC third magnesium ion after substrate binding. {ECO:0000256|HAMAP- CC Rule:MF_03140}; CC -!- SUBUNIT: Interacts with PCNA. Three molecules of FEN1 bind to one CC PCNA trimer with each molecule binding to one PCNA monomer. PCNA CC stimulates the nuclease activity without altering cleavage CC specificity. {ECO:0000256|HAMAP-Rule:MF_03140}. CC -!- SUBCELLULAR LOCATION: Mitochondrion CC {ECO:0000256|SAAS:SAAS00725520}. CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000256|HAMAP- CC Rule:MF_03140}. Nucleus, nucleoplasm {ECO:0000256|HAMAP- CC Rule:MF_03140}. Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03140}. CC Note=Resides mostly in the nucleoli and relocalizes to the CC nucleoplasm upon DNA damage. {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 CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_03140}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 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:0043137; P:DNA replication, removal of RNA primer; IEA:UniProtKB-UniRule. DR CDD; cd09867; PIN_FEN1; 1. DR Gene3D; 3.40.50.1010; -; 1. DR HAMAP; MF_00614; Fen; 1. DR InterPro; IPR036279; 5-3_exonuclease_C_sf. DR InterPro; IPR002421; 5-3_exonuclease_N. 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; 2. 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; 2. 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 Complete proteome {ECO:0000313|Proteomes:UP000195521}; KW DNA damage {ECO:0000256|HAMAP-Rule:MF_03140}; KW DNA repair {ECO:0000256|HAMAP-Rule:MF_03140}; KW DNA replication {ECO:0000256|HAMAP-Rule:MF_03140}; KW Endonuclease {ECO:0000256|HAMAP-Rule:MF_03140, KW ECO:0000313|EMBL:GAW79264.1}; KW Exonuclease {ECO:0000256|HAMAP-Rule:MF_03140}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_03140}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_03140}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_03140}; KW Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03140, KW ECO:0000256|SAAS:SAAS00725731}; KW Nuclease {ECO:0000256|HAMAP-Rule:MF_03140}; KW Nucleus {ECO:0000256|HAMAP-Rule:MF_03140, KW ECO:0000256|SAAS:SAAS00631924}; KW Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_03140}; KW Reference proteome {ECO:0000313|Proteomes:UP000195521}. FT DOMAIN 1 109 XPGN. {ECO:0000259|SMART:SM00485}. FT DOMAIN 28 327 53EXOc. {ECO:0000259|SMART:SM00475}. FT DOMAIN 148 233 XPGI. {ECO:0000259|SMART:SM00484}. FT REGION 351 359 Interaction with PCNA. FT {ECO:0000256|HAMAP-Rule:MF_03140}. FT COILED 99 128 {ECO:0000256|SAM:Coils}. FT METAL 34 34 Magnesium 1. {ECO:0000256|HAMAP-Rule: FT MF_03140}. FT METAL 88 88 Magnesium 1. {ECO:0000256|HAMAP-Rule: FT MF_03140}. FT METAL 160 160 Magnesium 1. {ECO:0000256|HAMAP-Rule: FT MF_03140}. FT METAL 162 162 Magnesium 1. {ECO:0000256|HAMAP-Rule: FT MF_03140}. FT METAL 181 181 Magnesium 2. {ECO:0000256|HAMAP-Rule: FT MF_03140}. FT METAL 183 183 Magnesium 2. {ECO:0000256|HAMAP-Rule: FT MF_03140}. FT METAL 248 248 Magnesium 2. {ECO:0000256|HAMAP-Rule: FT MF_03140}. FT BINDING 47 47 DNA substrate. {ECO:0000256|HAMAP-Rule: FT MF_03140}. FT BINDING 72 72 DNA substrate. {ECO:0000256|HAMAP-Rule: FT MF_03140}. FT BINDING 160 160 DNA substrate. {ECO:0000256|HAMAP-Rule: FT MF_03140}. FT BINDING 246 246 DNA substrate. {ECO:0000256|HAMAP-Rule: FT MF_03140}. FT BINDING 248 248 DNA substrate. {ECO:0000256|HAMAP-Rule: FT 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 //