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Database: UniProt
Entry: L0JXP1_9EURY
LinkDB: L0JXP1_9EURY
Original site: L0JXP1_9EURY 
ID   L0JXP1_9EURY            Unreviewed;       325 AA.
AC   L0JXP1;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 55.
DE   RecName: Full=Flap endonuclease 1 {ECO:0000256|HAMAP-Rule:MF_00614};
DE            Short=FEN-1 {ECO:0000256|HAMAP-Rule:MF_00614};
DE            EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_00614};
DE   AltName: Full=Flap structure-specific endonuclease 1 {ECO:0000256|HAMAP-Rule:MF_00614};
GN   Name=fen {ECO:0000256|HAMAP-Rule:MF_00614};
GN   ORFNames=Natoc_1022 {ECO:0000313|EMBL:AGB36869.1};
OS   Natronococcus occultus SP4.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Natronococcus.
OX   NCBI_TaxID=694430 {ECO:0000313|EMBL:AGB36869.1, ECO:0000313|Proteomes:UP000010878};
RN   [1] {ECO:0000313|EMBL:AGB36869.1, ECO:0000313|Proteomes:UP000010878}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SP4 {ECO:0000313|EMBL:AGB36869.1,
RC   ECO:0000313|Proteomes:UP000010878};
RG   DOE Joint Genome Institute;
RA   Eisen J., Huntemann M., Wei C.-L., Han J., Detter J.C., Han C., Tapia R.,
RA   Chen A., Kyrpides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA   Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L.,
RA   Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Eisen J., Klenk H.-P.,
RA   Klenk H.-P.;
RT   "FINISHED of Natronococcus occultus SP4, DSM 3396.";
RL   Submitted (NOV-2012) 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. Binds the unpaired 3'-DNA
CC       end and kinks the DNA to facilitate 5' cleavage specificity. Cleaves
CC       one nucleotide into the double-stranded DNA from the junction in flap
CC       DNA, leaving a nick for ligation. Also involved in the base excision
CC       repair (BER) pathway. Acts as a genome stabilization factor that
CC       prevents flaps from equilibrating into structures that lead to
CC       duplications and deletions. Also possesses 5'-3' exonuclease activity
CC       on nicked or gapped double-stranded DNA.
CC       {ECO:0000256|ARBA:ARBA00024702}.
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. Binds the unpaired 3'-DNA
CC       end and kinks the DNA to facilitate 5' cleavage specificity. Cleaves
CC       one nucleotide into the double-stranded DNA from the junction in flap
CC       DNA, leaving a nick for ligation. Also involved in the base excision
CC       repair (BER) pathway. Acts as a genome stabilization factor that
CC       prevents flaps from equilibrating into structurs that lead to
CC       duplications and deletions. Also possesses 5'-3' exonuclease activity
CC       on nicked or gapped double-stranded DNA. {ECO:0000256|HAMAP-
CC       Rule:MF_00614}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00614};
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_00614};
CC   -!- SUBUNIT: Interacts with PCNA. PCNA stimulates the nuclease activity
CC       without altering cleavage specificity. {ECO:0000256|HAMAP-
CC       Rule:MF_00614}.
CC   -!- SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. FEN1
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00614}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00614}.
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DR   EMBL; CP003929; AGB36869.1; -; Genomic_DNA.
DR   RefSeq; WP_015320323.1; NC_019974.1.
DR   AlphaFoldDB; L0JXP1; -.
DR   STRING; 694430.Natoc_1022; -.
DR   GeneID; 14402301; -.
DR   KEGG; nou:Natoc_1022; -.
DR   eggNOG; arCOG04050; Archaea.
DR   HOGENOM; CLU_032444_0_0_2; -.
DR   OrthoDB; 9593at2157; -.
DR   Proteomes; UP000010878; Chromosome.
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:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR   GO; GO:0043137; P:DNA replication, removal of RNA primer; IEA:UniProtKB-UniRule.
DR   CDD; cd09903; H3TH_FEN1-Arc; 1.
DR   CDD; cd09867; PIN_FEN1; 1.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR   Gene3D; 3.40.50.1010; 5'-nuclease; 1.
DR   HAMAP; MF_00614; Fen; 1.
DR   InterPro; IPR036279; 5-3_exonuclease_C_sf.
DR   InterPro; IPR023426; Flap_endonuc.
DR   InterPro; IPR019973; Flap_endonuc_arc.
DR   InterPro; IPR008918; HhH2.
DR   InterPro; IPR029060; PIN-like_dom_sf.
DR   InterPro; IPR006086; XPG-I_dom.
DR   InterPro; IPR006084; XPG/Rad2.
DR   InterPro; IPR006085; XPG_DNA_repair_N.
DR   NCBIfam; TIGR03674; fen_arch; 1.
DR   PANTHER; PTHR11081:SF9; FLAP ENDONUCLEASE 1; 1.
DR   PANTHER; PTHR11081; FLAP ENDONUCLEASE FAMILY MEMBER; 1.
DR   Pfam; PF00867; XPG_I; 1.
DR   Pfam; PF00752; XPG_N; 1.
DR   PRINTS; PR00853; XPGRADSUPER.
DR   SMART; SM00279; HhH2; 1.
DR   SMART; SM00484; XPGI; 1.
DR   SMART; SM00485; XPGN; 1.
DR   SUPFAM; SSF47807; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR   SUPFAM; SSF88723; PIN domain-like; 1.
PE   3: Inferred from homology;
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW   Rule:MF_00614};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW   Rule:MF_00614};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW   Rule:MF_00614};
KW   Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|HAMAP-
KW   Rule:MF_00614};
KW   Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW   Rule:MF_00614};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00614};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00614};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00614};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00614};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010878}.
FT   DOMAIN          1..102
FT                   /note="XPG N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00485"
FT   DOMAIN          141..209
FT                   /note="XPG-I"
FT                   /evidence="ECO:0000259|SMART:SM00484"
FT   REGION          91..113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          317..325
FT                   /note="Interaction with PCNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00614"
FT   BINDING         27
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00614"
FT   BINDING         81
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00614"
FT   BINDING         153
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00614"
FT   BINDING         155
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00614"
FT   BINDING         174
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00614"
FT   BINDING         176
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00614"
FT   BINDING         224
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00614"
SQ   SEQUENCE   325 AA;  36294 MW;  BAB8B718D306CB7C CRC64;
     MGNAALRDIA VIEDVPFDEI EGTIAVDAHN WLYRYLTTTV KWTASEKYTT GDGTEVANLI
     GIVQGVARFF EHDVTPVMVF DGGPSQLKAD EIESRREQRR SYEEQLETAR EEGDEVAIAQ
     LESRTQRLTP TIQETSRELL ELLDVPVVEA PAEGEAQAAH IVKRGDADYV GSEDYDALLF
     GAPLTLRQLT SKGDPELMDL EATLERHELT LEQLIDAAIL IGTDFNEGVS GIGPKTAISE
     ITEHGDLWSV LEARGDTVEY GDRVRQLFRD PDVTDDYSFE TSLEPDLEDA RAYVTDEWGV
     AADEVERSFE RIEEHATQTG LDRWT
//
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