ID M1Y129_NATM8 Unreviewed; 327 AA.
AC M1Y129;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 59.
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=fen1 {ECO:0000313|EMBL:CCQ36195.1};
GN Synonyms=fen {ECO:0000256|HAMAP-Rule:MF_00614};
GN OrderedLocusNames=Nmlp_2011 {ECO:0000313|EMBL:CCQ36195.1};
OS Natronomonas moolapensis (strain DSM 18674 / CECT 7526 / JCM 14361 /
OS 8.8.11).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Natronomonas.
OX NCBI_TaxID=268739 {ECO:0000313|EMBL:CCQ36195.1, ECO:0000313|Proteomes:UP000011867};
RN [1] {ECO:0000313|EMBL:CCQ36195.1, ECO:0000313|Proteomes:UP000011867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18674 / JCM 14361 / 8.8.11
RC {ECO:0000313|Proteomes:UP000011867};
RX PubMed=23516216; DOI=10.1128/genomeA.00095-13;
RA Dyall-Smith M.L., Pfeiffer F., Oberwinkler T., Klee K., Rampp M., Palm P.,
RA Gross K., Schuster S.C., Oesterhelt D.;
RT "Genome of the haloarchaeon Natronomonas moolapensis, a neutrophilic member
RT of a previously haloalkaliphilic genus.";
RL Genome Announc. 1:e0009513-e0009513(2013).
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.
CC {ECO:0000256|ARBA:ARBA00024702}.
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; HF582854; CCQ36195.1; -; Genomic_DNA.
DR RefSeq; WP_015409012.1; NC_020388.1.
DR AlphaFoldDB; M1Y129; -.
DR STRING; 268739.Nmlp_2011; -.
DR GeneID; 14652187; -.
DR KEGG; nmo:Nmlp_2011; -.
DR eggNOG; arCOG04050; Archaea.
DR HOGENOM; CLU_032444_0_0_2; -.
DR OrthoDB; 9593at2157; -.
DR Proteomes; UP000011867; 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 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; IPR002421; 5-3_exonuclease.
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; 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; SM00475; 53EXOc; 1.
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.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA damage {ECO:0000256|HAMAP-Rule:MF_00614};
KW DNA repair {ECO:0000256|HAMAP-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:UP000011867}.
FT DOMAIN 1..103
FT /note="XPG N-terminal"
FT /evidence="ECO:0000259|SMART:SM00485"
FT DOMAIN 22..294
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 143..211
FT /note="XPG-I"
FT /evidence="ECO:0000259|SMART:SM00484"
FT COILED 86..140
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 28
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00614"
FT BINDING 82
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00614"
FT BINDING 155
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00614"
FT BINDING 157
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00614"
FT BINDING 176
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00614"
FT BINDING 178
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00614"
FT BINDING 226
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00614"
SQ SEQUENCE 327 AA; 36317 MW; AD5B8641F7A68847 CRC64;
MGNADLRSLA VIEPKPFGEL AGSVVAVDAH NWLYRYLTTT VRFTSSDTYT TESGEEVANL
VGVVQGLPKF FEADVTPVFV FDGGVAELKD DEVESRREQR ERYEDELDAA RAGEADAAEI
ATLESRTQRL TETIQTTTRE LLSLLDVPVV EAPAEGEAQA AYMARYGDVD YAGSEDYDTL
LLGAPYTLRG LTSKGDPECM DFERTLEDLG LTWEELVDAA ILMGTDFNEG IDGIGPKTAV
KLLREHGDLW GALDARGESI PNADRIREMF LDPAVTDEYD YDTEIEPDMD AARQYVTDTW
EVPAEEVARG FERIEESVVQ TGLDRWR
//
