FEN_METKA
ID FEN_METKA Reviewed; 348 AA.
AC Q8TXU4;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Flap endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_00614};
DE Short=FEN-1 {ECO:0000255|HAMAP-Rule:MF_00614};
DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_00614};
DE AltName: Full=Flap structure-specific endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_00614};
GN Name=fen {ECO:0000255|HAMAP-Rule:MF_00614}; OrderedLocusNames=MK0566;
OS Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938).
OC Archaea; Euryarchaeota; Methanopyri; Methanopyrales; Methanopyraceae;
OC Methanopyrus.
OX NCBI_TaxID=190192;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX PubMed=11930014; DOI=10.1073/pnas.032671499;
RA Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A.,
RA Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G.,
RA Koonin E.V., Kozyavkin S.A.;
RT "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and
RT monophyly of archaeal methanogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002).
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 (By similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|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:0000255|HAMAP-
CC Rule:MF_00614};
CC -!- SUBUNIT: Interacts with PCNA. PCNA stimulates the nuclease activity
CC without altering cleavage specificity. {ECO:0000255|HAMAP-
CC Rule:MF_00614}.
CC -!- SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. FEN1
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00614}.
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; AE009439; AAM01781.1; -; Genomic_DNA.
DR PDB; 4WA8; X-ray; 2.20 A; A/B=1-348.
DR PDBsum; 4WA8; -.
DR AlphaFoldDB; Q8TXU4; -.
DR SMR; Q8TXU4; -.
DR STRING; 190192.MK0566; -.
DR EnsemblBacteria; AAM01781; AAM01781; MK0566.
DR KEGG; mka:MK0566; -.
DR PATRIC; fig|190192.8.peg.601; -.
DR HOGENOM; CLU_032444_0_0_2; -.
DR OMA; GSQDYDS; -.
DR Proteomes; UP000001826; 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 HAMAP; MF_00614; Fen; 1.
DR InterPro; IPR036279; 5-3_exonuclease_C_sf.
DR InterPro; IPR023426; Flap_endonuc.
DR InterPro; IPR019973; Flap_structure-sp_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 PANTHER; PTHR11081; PTHR11081; 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; SSF47807; 1.
DR SUPFAM; SSF88723; SSF88723; 1.
DR TIGRFAMs; TIGR03674; fen_arch; 1.
DR PROSITE; PS00841; XPG_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA damage; DNA repair; DNA replication; Endonuclease;
KW Exonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease;
KW Reference proteome.
FT CHAIN 1..348
FT /note="Flap endonuclease 1"
FT /id="PRO_0000154054"
FT REGION 1..98
FT /note="N-domain"
FT REGION 113..256
FT /note="I-domain"
FT REGION 340..348
FT /note="Interaction with PCNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00614"
FT BINDING 28
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00614"
FT BINDING 80
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00614"
FT BINDING 149
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00614"
FT BINDING 151
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00614"
FT BINDING 170
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00614"
FT BINDING 172
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00614"
FT BINDING 234
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00614"
FT HELIX 3..6
FT /evidence="ECO:0007829|PDB:4WA8"
FT HELIX 7..10
FT /evidence="ECO:0007829|PDB:4WA8"
FT HELIX 17..20
FT /evidence="ECO:0007829|PDB:4WA8"
FT STRAND 24..28
FT /evidence="ECO:0007829|PDB:4WA8"
FT HELIX 29..39
FT /evidence="ECO:0007829|PDB:4WA8"
FT HELIX 56..70
FT /evidence="ECO:0007829|PDB:4WA8"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:4WA8"
FT HELIX 126..139
FT /evidence="ECO:0007829|PDB:4WA8"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:4WA8"
FT HELIX 150..159
FT /evidence="ECO:0007829|PDB:4WA8"
FT STRAND 162..167
FT /evidence="ECO:0007829|PDB:4WA8"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:4WA8"
FT HELIX 172..175
FT /evidence="ECO:0007829|PDB:4WA8"
FT STRAND 179..184
FT /evidence="ECO:0007829|PDB:4WA8"
FT STRAND 189..192
FT /evidence="ECO:0007829|PDB:4WA8"
FT TURN 194..196
FT /evidence="ECO:0007829|PDB:4WA8"
FT STRAND 199..202
FT /evidence="ECO:0007829|PDB:4WA8"
FT STRAND 205..208
FT /evidence="ECO:0007829|PDB:4WA8"
FT HELIX 209..216
FT /evidence="ECO:0007829|PDB:4WA8"
FT HELIX 221..231
FT /evidence="ECO:0007829|PDB:4WA8"
FT HELIX 245..255
FT /evidence="ECO:0007829|PDB:4WA8"
FT HELIX 259..263
FT /evidence="ECO:0007829|PDB:4WA8"
FT HELIX 267..273
FT /evidence="ECO:0007829|PDB:4WA8"
FT HELIX 278..286
FT /evidence="ECO:0007829|PDB:4WA8"
FT HELIX 303..310
FT /evidence="ECO:0007829|PDB:4WA8"
FT TURN 311..314
FT /evidence="ECO:0007829|PDB:4WA8"
FT HELIX 318..336
FT /evidence="ECO:0007829|PDB:4WA8"
SQ SEQUENCE 348 AA; 40252 MW; 2058C441900B7AF9 CRC64;
MGLAELRELI EPEETDLRAL AGREIAIDAF NALYQFLTTI MKDGRPLMDS RGRITSHLNG
LLYRTVNLVE EGIKPVYVFD GEPPDLKRET LERRRERKEE AMEKLRRAKT KEEREKYARQ
VARLDESLVE DAKRLLDLMG IPWVQAPSEG EAQCAYMARC GDVWATGSQD YDSLLFGSPR
LVRNITIVGK RKHPHTGEII EVKPEIMRLE DVLDQLGLES REQLVDLAIL LGTDYNPDGV
PGIGPKRALQ LIRKYGSLDE LKDTDIWPKI ERHLPVEPEK LRRLFLEPEV TDDYELDWDE
PDEEGLVEFL VEERDFSEDR VRRAVERLKE ALQELRKGGR QETLDAFF
