ID A0A3A6PR23_9EURY Unreviewed; 326 AA.
AC A0A3A6PR23;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
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 ECO:0000313|EMBL:RJX42038.1};
GN ORFNames=DM826_10295 {ECO:0000313|EMBL:RJX42038.1};
OS Halonotius aquaticus.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halonotius.
OX NCBI_TaxID=2216978 {ECO:0000313|EMBL:RJX42038.1, ECO:0000313|Proteomes:UP000276588};
RN [1] {ECO:0000313|EMBL:RJX42038.1, ECO:0000313|Proteomes:UP000276588}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F13-13 {ECO:0000313|EMBL:RJX42038.1,
RC ECO:0000313|Proteomes:UP000276588};
RA Duran-Viseras A., Sanchez-Porro C., Ventosa A.;
RT "Halonotius sp. F13-13 a new haloarchaeeon isolated from a solar saltern
RT from Isla Cristina, Huelva, Spain.";
RL Submitted (JUN-2018) 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}.
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:RJX42038.1}.
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DR EMBL; QKNY01000018; RJX42038.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3A6PR23; -.
DR OrthoDB; 9593at2157; -.
DR Proteomes; UP000276588; Unassembled WGS sequence.
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; IPR019974; XPG_CS.
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.
DR PROSITE; PS00841; XPG_1; 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_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:UP000276588}.
FT DOMAIN 1..103
FT /note="XPG N-terminal"
FT /evidence="ECO:0000259|SMART:SM00485"
FT DOMAIN 142..217
FT /note="XPG-I"
FT /evidence="ECO:0000259|SMART:SM00484"
FT COILED 86..120
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 28
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00614"
FT BINDING 82
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00614"
FT BINDING 154
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00614"
FT BINDING 156
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00614"
FT BINDING 175
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00614"
FT BINDING 177
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00614"
FT BINDING 225
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00614"
SQ SEQUENCE 326 AA; 36251 MW; 55ED709D895C27A1 CRC64;
MGNSDLRSLA ALSECPFADI EGSTVAVDAH NWLYRYLTTT VKWTDDAIYT TDDGTEVANL
IGVVQGLPKF FEHDLTPIFV FDGGVTELKD DEVEKRREQR EQAEERLAEA EAAGDSIEAA
RLSARTVQLT ETIQETTRDL LALLDVPYID APAEGEAQAA YMNKIGDADY VGSEDYDTLL
FGAPSTLREL TSKGHPELME LQPTLDEHEI TYEQLVDVAM LCGTDFNEGI SGIGPKTGVK
LITEHGDLFG VLEARGEHIE FADRIRELFF DPPVTDDYEI ESDIDPDLDA ARAYVTEEWE
VDADEVERGF ERIESAVVQT GLDRWS
//