FEN_PYRFU
ID FEN_PYRFU Reviewed; 340 AA.
AC O93634;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 123.
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}; Synonyms=fen-1;
GN OrderedLocusNames=PF1414;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10486005; DOI=10.1007/pl00006570;
RA DiRuggiero J., Brown J.R., Bogert A.P., Robb F.T.;
RT "DNA repair systems in archaea: mementos from the last universal common
RT ancestor?";
RL J. Mol. Evol. 49:474-484(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=9778254; DOI=10.1016/s0092-8674(00)81789-4;
RA Hosfield D.J., Mol C.D., Shen B., Tainer J.A.;
RT "Structure of the DNA repair and replication endonuclease and exonuclease
RT FEN-1: coupling DNA and PCNA binding to FEN-1 activity.";
RL Cell 95:135-146(1998).
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. {ECO:0000269|PubMed:10486005}.
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}.
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DR EMBL; AF013497; AAD01514.1; -; Genomic_DNA.
DR EMBL; AE009950; AAL81538.1; -; Genomic_DNA.
DR PIR; T46893; T46893.
DR RefSeq; WP_011012561.1; NC_018092.1.
DR PDB; 1B43; X-ray; 2.00 A; A/B=1-340.
DR PDB; 6VBH; X-ray; 2.00 A; A=12-128.
DR PDBsum; 1B43; -.
DR PDBsum; 6VBH; -.
DR AlphaFoldDB; O93634; -.
DR SMR; O93634; -.
DR STRING; 186497.PF1414; -.
DR EnsemblBacteria; AAL81538; AAL81538; PF1414.
DR GeneID; 41713224; -.
DR KEGG; pfu:PF1414; -.
DR PATRIC; fig|186497.12.peg.1477; -.
DR eggNOG; arCOG04050; Archaea.
DR HOGENOM; CLU_032444_0_0_2; -.
DR OMA; GSQDYDS; -.
DR OrthoDB; 41214at2157; -.
DR PhylomeDB; O93634; -.
DR BRENDA; 3.1.99.B1; 5243.
DR EvolutionaryTrace; O93634; -.
DR Proteomes; UP000001013; 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..340
FT /note="Flap endonuclease 1"
FT /id="PRO_0000154061"
FT REGION 1..98
FT /note="N-domain"
FT REGION 116..258
FT /note="I-domain"
FT REGION 330..338
FT /note="Interaction with PCNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00614"
FT BINDING 27
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 152
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00614"
FT BINDING 154
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00614"
FT BINDING 173
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00614"
FT BINDING 175
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00614"
FT BINDING 236
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00614"
FT HELIX 6..8
FT /evidence="ECO:0007829|PDB:1B43"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:6VBH"
FT HELIX 16..19
FT /evidence="ECO:0007829|PDB:6VBH"
FT STRAND 23..27
FT /evidence="ECO:0007829|PDB:6VBH"
FT HELIX 28..32
FT /evidence="ECO:0007829|PDB:6VBH"
FT HELIX 57..70
FT /evidence="ECO:0007829|PDB:6VBH"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:6VBH"
FT HELIX 90..93
FT /evidence="ECO:0007829|PDB:6VBH"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:6VBH"
FT HELIX 101..111
FT /evidence="ECO:0007829|PDB:6VBH"
FT TURN 115..124
FT /evidence="ECO:0007829|PDB:6VBH"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:6VBH"
FT HELIX 129..142
FT /evidence="ECO:0007829|PDB:1B43"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:1B43"
FT HELIX 153..162
FT /evidence="ECO:0007829|PDB:1B43"
FT STRAND 165..170
FT /evidence="ECO:0007829|PDB:1B43"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:1B43"
FT HELIX 175..178
FT /evidence="ECO:0007829|PDB:1B43"
FT STRAND 182..187
FT /evidence="ECO:0007829|PDB:1B43"
FT TURN 188..190
FT /evidence="ECO:0007829|PDB:1B43"
FT STRAND 192..195
FT /evidence="ECO:0007829|PDB:1B43"
FT STRAND 202..205
FT /evidence="ECO:0007829|PDB:1B43"
FT STRAND 208..211
FT /evidence="ECO:0007829|PDB:1B43"
FT HELIX 212..219
FT /evidence="ECO:0007829|PDB:1B43"
FT HELIX 223..233
FT /evidence="ECO:0007829|PDB:1B43"
FT HELIX 247..255
FT /evidence="ECO:0007829|PDB:1B43"
FT HELIX 260..263
FT /evidence="ECO:0007829|PDB:1B43"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:1B43"
FT HELIX 272..280
FT /evidence="ECO:0007829|PDB:1B43"
FT HELIX 297..304
FT /evidence="ECO:0007829|PDB:1B43"
FT TURN 305..308
FT /evidence="ECO:0007829|PDB:1B43"
FT HELIX 312..328
FT /evidence="ECO:0007829|PDB:1B43"
FT HELIX 329..333
FT /evidence="ECO:0007829|PDB:1B43"
SQ SEQUENCE 340 AA; 38739 MW; D86D3D0F999E5D1E CRC64;
MGVPIGEIIP RKEIELENLY GKKIAIDALN AIYQFLSTIR QKDGTPLMDS KGRITSHLSG
LFYRTINLME AGIKPVYVFD GEPPEFKKKE LEKRREAREE AEEKWREALE KGEIEEARKY
AQRATRVNEM LIEDAKKLLE LMGIPIVQAP SEGEAQAAYM AAKGSVYASA SQDYDSLLFG
APRLVRNLTI TGKRKLPGKN VYVEIKPELI ILEEVLKELK LTREKLIELA ILVGTDYNPG
GIKGIGLKKA LEIVRHSKDP LAKFQKQSDV DLYAIKEFFL NPPVTDNYNL VWRDPDEEGI
LKFLCDEHDF SEERVKNGLE RLKKAIKSGK QSTLESWFKR
