ID A0A068QVL4_9GAMM Unreviewed; 251 AA.
AC A0A068QVL4;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=Flap endonuclease Xni {ECO:0000256|HAMAP-Rule:MF_01192};
DE Short=FEN {ECO:0000256|HAMAP-Rule:MF_01192};
DE EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_01192};
GN Name=xni {ECO:0000256|HAMAP-Rule:MF_01192,
GN ECO:0000313|EMBL:CDG19013.1};
GN Synonyms=ygdG {ECO:0000256|HAMAP-Rule:MF_01192};
GN ORFNames=XDD1_3323 {ECO:0000313|EMBL:CDG19013.1};
OS Xenorhabdus doucetiae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=351671 {ECO:0000313|EMBL:CDG19013.1, ECO:0000313|Proteomes:UP000032721};
RN [1] {ECO:0000313|EMBL:CDG19013.1, ECO:0000313|Proteomes:UP000032721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FRM16 / DSM 17909 {ECO:0000313|Proteomes:UP000032721};
RA Genoscope - CEA;
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Has flap endonuclease activity. During DNA replication, flap
CC endonucleases cleave the 5'-overhanging flap structure that is
CC generated by displacement synthesis when DNA polymerase encounters the
CC 5'-end of a downstream Okazaki fragment. {ECO:0000256|HAMAP-
CC Rule:MF_01192}.
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01192};
CC Note=Binds 1 K(+) per subunit. The potassium ion strongly increases the
CC affinity for DNA. {ECO:0000256|HAMAP-Rule:MF_01192};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01192};
CC Note=Binds 2 Mg(2+) per subunit. Only one magnesium ion has a direct
CC interaction with the protein, the other interactions are indirect.
CC {ECO:0000256|HAMAP-Rule:MF_01192};
CC -!- SIMILARITY: Belongs to the Xni family. {ECO:0000256|HAMAP-
CC Rule:MF_01192}.
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DR EMBL; FO704550; CDG19013.1; -; Genomic_DNA.
DR RefSeq; WP_045972532.1; NZ_VNHN01000022.1.
DR AlphaFoldDB; A0A068QVL4; -.
DR STRING; 351671.XDD1_3323; -.
DR KEGG; xdo:XDD1_3323; -.
DR HOGENOM; CLU_004675_1_2_6; -.
DR OrthoDB; 8070997at2; -.
DR Proteomes; UP000032721; Chromosome.
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:0030955; F:potassium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0033567; P:DNA replication, Okazaki fragment processing; IEA:UniProtKB-UniRule.
DR CDD; cd09898; H3TH_53EXO; 1.
DR CDD; cd09859; PIN_53EXO; 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_01192; Xni; 1.
DR InterPro; IPR020046; 5-3_exonucl_a-hlix_arch_N.
DR InterPro; IPR002421; 5-3_exonuclease.
DR InterPro; IPR036279; 5-3_exonuclease_C_sf.
DR InterPro; IPR020045; DNA_polI_H3TH.
DR InterPro; IPR038969; FEN.
DR InterPro; IPR008918; HhH2.
DR InterPro; IPR029060; PIN-like_dom_sf.
DR InterPro; IPR022895; Xni.
DR PANTHER; PTHR42646:SF2; DNA-DIRECTED DNA POLYMERASE; 1.
DR PANTHER; PTHR42646; FLAP ENDONUCLEASE XNI; 1.
DR Pfam; PF01367; 5_3_exonuc; 1.
DR Pfam; PF02739; 5_3_exonuc_N; 1.
DR SMART; SM00475; 53EXOc; 1.
DR SMART; SM00279; HhH2; 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 DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_01192};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|HAMAP-
KW Rule:MF_01192}; Hydrolase {ECO:0000256|HAMAP-Rule:MF_01192};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01192};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01192};
KW Nuclease {ECO:0000256|HAMAP-Rule:MF_01192};
KW Potassium {ECO:0000256|ARBA:ARBA00022958, ECO:0000256|HAMAP-Rule:MF_01192}.
FT DOMAIN 2..249
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT REGION 183..188
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01192"
FT BINDING 103
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01192"
FT BINDING 170
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01192"
FT BINDING 171
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01192"
FT BINDING 179
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01192"
FT BINDING 181
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01192"
FT BINDING 184
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01192"
SQ SEQUENCE 251 AA; 28115 MW; 7B58EDDC13424B7F CRC64;
MIHLLIVDAL NLIRRIHAVQ GSPCIPACEH ALKQLITHAS PTHAVAVFDE DDRSHSWRHQ
LFPDYKAGRA AMPDDLQQEM PFIKQAFDAL GVACWHIEGH EADDLAATLA TKVAKSGYHV
TIVSTDKGYC QLLSPHIQIR DYFQKRWLDL PFVQQAFGVA PHQLPDYWGL AGISSSKIPG
VQGIGPKTAA TLLQQAGSLD NLFQHLDTQP DKWRKKLAAH KEMAYISREI ASLRTDLLLQ
GNLQQLRLIK R
//
