ID A4YD87_METS5 Unreviewed; 300 AA.
AC A4YD87;
DT 29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 88.
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 OrderedLocusNames=Msed_0212 {ECO:0000313|EMBL:ABP94389.1};
OS Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509
OS / TH2).
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Metallosphaera.
OX NCBI_TaxID=399549 {ECO:0000313|EMBL:ABP94389.1, ECO:0000313|Proteomes:UP000000242};
RN [1] {ECO:0000313|EMBL:ABP94389.1, ECO:0000313|Proteomes:UP000000242}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2
RC {ECO:0000313|Proteomes:UP000000242};
RX PubMed=18083856; DOI=10.1128/AEM.02019-07;
RA Auernik K.S., Maezato Y., Blum P.H., Kelly R.M.;
RT "The genome sequence of the metal-mobilizing, extremely thermoacidophilic
RT archaeon Metallosphaera sedula provides insights into bioleaching-
RT associated metabolism.";
RL Appl. Environ. Microbiol. 74:682-692(2008).
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}.
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DR EMBL; CP000682; ABP94389.1; -; Genomic_DNA.
DR AlphaFoldDB; A4YD87; -.
DR STRING; 399549.Msed_0212; -.
DR KEGG; mse:Msed_0212; -.
DR eggNOG; arCOG04050; Archaea.
DR HOGENOM; CLU_032444_0_0_2; -.
DR Proteomes; UP000000242; 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 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 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:UP000000242}.
FT DOMAIN 1..54
FT /note="XPG N-terminal"
FT /evidence="ECO:0000259|SMART:SM00485"
FT DOMAIN 93..174
FT /note="XPG-I"
FT /evidence="ECO:0000259|SMART:SM00484"
FT REGION 50..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 292..300
FT /note="Interaction with PCNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00614"
FT COMPBIAS 50..73
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 33
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00614"
FT BINDING 105
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00614"
FT BINDING 107
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00614"
FT BINDING 126
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00614"
FT BINDING 128
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00614"
FT BINDING 189
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00614"
SQ SEQUENCE 300 AA; 34493 MW; 7D0E5813EC22C97A CRC64;
MNRQGKVTSH LNGVFYRTVN LLEEGIIPIY VFDGKPPELK AQELENRRKM KEEAEKKLEK
AKESGKVEEM RKYSQMTSRL TTDMAKESKE LLEYMGVPTV QAPSEGEAEA AYLNAKGITY
ASASQDYDSL LFGAEKLIRN LTISGKRKLP NKDVYVEVKP ELIETASLLK KLEITREQLI
DIAILVGTDY NPDGVRGIGP KKAYKLIKTY KKIENIDKRE LPEPIYFDYE KIRELFLKPQ
VTLPSTPLEL SDPDPSKIIQ FLVNENDFNE ERVRGTIERL QKAMKEIKDI KRQTGLDQWF
//
