AC MF_00614; DC Protein; auto c? TR HAMAP; MF_00614; -; 1; level=0 XX Names: Fen XX ID FEN DE RecName: Full=Flap endonuclease 1; DE Short=FEN-1; DE EC=3.1.-.-; DE AltName: Full=Flap structure-specific endonuclease 1; GN Name=fen; XX 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. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; 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.; CC -!- SUBUNIT: Interacts with PCNA. PCNA stimulates the nuclease activity CC without altering cleavage specificity. CC -!- SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. FEN1 CC subfamily. XX DR Pfam; PF00867; XPG_I; 1; trigger=no DR Pfam; PF00752; XPG_N; 1; trigger=no DR PRINTS; PR00853; XPGRADSUPER; 1; trigger=no DR NCBIfam; TIGR03674; Fen_arch; 1; trigger=no DR PROSITE; PS00841; XPG_1; 1; trigger=no XX KW DNA damage KW DNA repair KW DNA replication KW Endonuclease KW Exonuclease KW Hydrolase KW Magnesium KW Metal-binding KW Nuclease XX GO GO:0003677; F:DNA binding GO GO:0008409; F:5'-3' exonuclease activity GO GO:0017108; F:5'-flap endonuclease activity GO GO:0000287; F:magnesium ion binding GO GO:0043137; P:DNA replication, removal of RNA primer GO GO:0006281; P:DNA repair XX FT From: FEN_METJA (Q58839) FT REGION 1..98 FT /note="N-domain" FT REGION 116..245 FT /note="I-domain" FT REGION 317..325 FT /note="Interaction with PCNA" FT Optional; Condition: x-Q-x(2)-[ILM]-x(2)-[FYW]-[FYILAT] FT BINDING 27 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT Condition: D FT BINDING 80 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT Condition: D FT BINDING 152 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT Condition: E FT BINDING 154 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT Condition: E FT BINDING 173 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT Condition: D FT BINDING 175 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT Condition: D FT BINDING 224 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT Condition: D XX Size: 326-351; Related: None; Template: Q58839; O93634; Scope: Archaea Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: None XX # Revision 1.23 2023/06/01 //