ID M0AR56_NATA1 Unreviewed; 291 AA.
AC M0AR56;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Flap endonuclease-1 {ECO:0000313|EMBL:ELZ00423.1};
GN ORFNames=C481_12274 {ECO:0000313|EMBL:ELZ00423.1};
OS Natrialba asiatica (strain ATCC 700177 / DSM 12278 / JCM 9576 / FERM
OS P-10747 / NBRC 102637 / 172P1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natrialba.
OX NCBI_TaxID=29540 {ECO:0000313|EMBL:ELZ00423.1, ECO:0000313|Proteomes:UP000011554};
RN [1] {ECO:0000313|EMBL:ELZ00423.1, ECO:0000313|Proteomes:UP000011554}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12278 {ECO:0000313|EMBL:ELZ00423.1,
RC ECO:0000313|Proteomes:UP000011554};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ELZ00423.1}.
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DR EMBL; AOIO01000030; ELZ00423.1; -; Genomic_DNA.
DR STRING; 29540.C481_12274; -.
DR PATRIC; fig|29540.5.peg.2487; -.
DR eggNOG; arCOG04050; Archaea.
DR Proteomes; UP000011554; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 InterPro; IPR036279; 5-3_exonuclease_C_sf.
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 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.
PE 4: Predicted;
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000313|EMBL:ELZ00423.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Reference proteome {ECO:0000313|Proteomes:UP000011554}.
FT DOMAIN 1..102
FT /note="XPG N-terminal"
FT /evidence="ECO:0000259|SMART:SM00485"
FT DOMAIN 141..209
FT /note="XPG-I"
FT /evidence="ECO:0000259|SMART:SM00484"
SQ SEQUENCE 291 AA; 32124 MW; DCEDCF79C7103501 CRC64;
MGNAALRDIA VIEEVPFADI EGVVAVDAHN WLYRYLTTTV KWTNSAKYTT ADGTEVANLV
GIVQGLPKFF ENDVVPVMVF DGGPSELKED EIESRRDQRR TYEEQLETAR EEGDEVAIAQ
LESRTQRLTP TIQETSRELL ELLDVPIVEA PAEGEAQAAH MARRGDADYV GSEDYDALLF
GAPLTLRQLT SKGDPERMDL QATLDHHGLT LEQLIDAAIL IGTDFNEGVS GIGPKTAIAE
ITEHGDLWSV LEARGDSIRY GDRVRELFRE PNVTXHDARS GSGRGSGIRH R
//
