FEN_SACS2
ID FEN_SACS2 Reviewed; 349 AA.
AC Q980U8;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 12-FEB-2003, sequence version 2.
DT 03-AUG-2022, entry version 122.
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=SSO0179;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [2]
RP FUNCTION, ACTIVITY REGULATION, INTERACTION WITH PCNA1, SUBUNIT, AND
RP MUTAGENESIS OF 341-ARG--PHE-349.
RX PubMed=12535540; DOI=10.1016/s1097-2765(02)00824-9;
RA Dionne I., Nookala R.K., Jackson S.P., Doherty A.J., Bell S.D.;
RT "A heterotrimeric PCNA in the hyperthermophilic archaeon Sulfolobus
RT solfataricus.";
RL Mol. Cell 11:275-282(2003).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 5-349 IN COMPLEX WITH PCNA.
RX PubMed=16945955; DOI=10.1093/nar/gkl623;
RA Dore A.S., Kilkenny M.L., Jones S.A., Oliver A.W., Roe S.M., Bell S.D.,
RA Pearl L.H.;
RT "Structure of an archaeal PCNA1-PCNA2-FEN1 complex: elucidating PCNA
RT subunit and client enzyme specificity.";
RL Nucleic Acids Res. 34:4515-4526(2006).
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). DNA polymerase
CC I, DNA ligase and the flap endonuclease may be constitutively
CC associated with the PCNA heterotrimer forming a scanning complex able
CC to couple DNA synthesis and Okazaki fragment maturation. {ECO:0000250,
CC ECO:0000269|PubMed:12535540}.
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 -!- ACTIVITY REGULATION: Heterotrimeric PCNA stimulates the nuclease
CC activity without altering cleavage specificity.
CC {ECO:0000269|PubMed:12535540}.
CC -!- SUBUNIT: Interacts with PCNA via subunit PCNA1.
CC {ECO:0000269|PubMed:12535540, ECO:0000269|PubMed:16945955}.
CC -!- SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. FEN1
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00614}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK40525.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE006641; AAK40525.1; ALT_INIT; Genomic_DNA.
DR PDB; 2IZO; X-ray; 2.90 A; A=5-349.
DR PDBsum; 2IZO; -.
DR AlphaFoldDB; Q980U8; -.
DR SMR; Q980U8; -.
DR STRING; 273057.SSO0179; -.
DR EnsemblBacteria; AAK40525; AAK40525; SSO0179.
DR KEGG; sso:SSO0179; -.
DR PATRIC; fig|273057.12.peg.176; -.
DR eggNOG; arCOG04050; Archaea.
DR HOGENOM; CLU_032444_0_0_2; -.
DR InParanoid; Q980U8; -.
DR OMA; GSQDYDS; -.
DR PhylomeDB; Q980U8; -.
DR BRENDA; 3.1.99.B1; 6163.
DR EvolutionaryTrace; Q980U8; -.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0008409; F:5'-3' exonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0017108; F:5'-flap endonuclease activity; IBA:GO_Central.
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..349
FT /note="Flap endonuclease 1"
FT /id="PRO_0000154065"
FT REGION 1..98
FT /note="N-domain"
FT REGION 116..258
FT /note="I-domain"
FT REGION 341..349
FT /note="Interaction with PCNA"
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 MUTAGEN 341..349
FT /note="Missing: No interaction with PCNA1."
FT /evidence="ECO:0000269|PubMed:12535540"
FT HELIX 16..19
FT /evidence="ECO:0007829|PDB:2IZO"
FT STRAND 22..27
FT /evidence="ECO:0007829|PDB:2IZO"
FT HELIX 28..37
FT /evidence="ECO:0007829|PDB:2IZO"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:2IZO"
FT HELIX 56..70
FT /evidence="ECO:0007829|PDB:2IZO"
FT STRAND 73..79
FT /evidence="ECO:0007829|PDB:2IZO"
FT HELIX 129..142
FT /evidence="ECO:0007829|PDB:2IZO"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:2IZO"
FT HELIX 153..162
FT /evidence="ECO:0007829|PDB:2IZO"
FT STRAND 165..170
FT /evidence="ECO:0007829|PDB:2IZO"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:2IZO"
FT HELIX 175..178
FT /evidence="ECO:0007829|PDB:2IZO"
FT STRAND 182..188
FT /evidence="ECO:0007829|PDB:2IZO"
FT STRAND 208..211
FT /evidence="ECO:0007829|PDB:2IZO"
FT HELIX 212..219
FT /evidence="ECO:0007829|PDB:2IZO"
FT HELIX 223..233
FT /evidence="ECO:0007829|PDB:2IZO"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:2IZO"
FT HELIX 247..256
FT /evidence="ECO:0007829|PDB:2IZO"
FT HELIX 281..286
FT /evidence="ECO:0007829|PDB:2IZO"
FT HELIX 304..310
FT /evidence="ECO:0007829|PDB:2IZO"
FT TURN 311..315
FT /evidence="ECO:0007829|PDB:2IZO"
FT HELIX 319..340
FT /evidence="ECO:0007829|PDB:2IZO"
FT HELIX 345..347
FT /evidence="ECO:0007829|PDB:2IZO"
SQ SEQUENCE 349 AA; 39598 MW; 7210395FD749C94C CRC64;
MDLADLVKDV KRELSFSELK GKRVSIDGYN ALYQFLAAIR QPDGTPLMDS QGRVTSHLSG
LFYRTINILE EGVIPIYVFD GKPPEQKSEE LERRRKAKEE AERKLERAKS EGKIEELRKY
SQAILRLSNI MVEESKKLLR AMGIPIVQAP SEGEAEAAYL NKLGLSWAAA SQDYDAILFG
AKRLVRNLTI TGKRKLPNKD VYVEIKPELI ETEILLKKLG ITREQLIDIG ILIGTDYNPD
GIRGIGPERA LKIIKKYGKI EKAMEYGEIS KKDINFNIDE IRGLFLNPQV VKPEEALDLN
EPNGEDIINI LVYEHNFSEE RVKNGIERLT KAIKEAKGAS RQTGLDRWF
