ID A0A380BGF1_9GAMM Unreviewed; 253 AA.
AC A0A380BGF1;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 28-JAN-2026, entry version 26.
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=ygdG {ECO:0000256|HAMAP-Rule:MF_01192,
GN ECO:0000313|EMBL:SUJ00156.1};
GN Synonyms=xni {ECO:0000256|HAMAP-Rule:MF_01192};
GN ORFNames=NCTC10738_03085 {ECO:0000313|EMBL:SUJ00156.1};
OS Shewanella algae.
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC Alteromonadales; Shewanellaceae; Shewanella.
OX NCBI_TaxID=38313 {ECO:0000313|EMBL:SUJ00156.1, ECO:0000313|Proteomes:UP000254069};
RN [1] {ECO:0000313|EMBL:SUJ00156.1, ECO:0000313|Proteomes:UP000254069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC10738 {ECO:0000313|EMBL:SUJ00156.1,
RC ECO:0000313|Proteomes:UP000254069};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) 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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01192}.
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DR EMBL; UGYO01000002; SUJ00156.1; -; Genomic_DNA.
DR RefSeq; WP_101059815.1; NZ_CP032415.1.
DR AlphaFoldDB; A0A380BGF1; -.
DR KEGG; salg:BS332_00345; -.
DR Proteomes; UP000254069; Unassembled WGS sequence.
DR GO; GO:0008409; F:5'-3' exonuclease activity; IEA:InterPro.
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 FunFam; 1.10.150.20:FF:000003; DNA polymerase I; 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 NCBIfam; NF007017; PRK09482.1; 1.
DR PANTHER; PTHR42646:SF2; 5'-3' EXONUCLEASE FAMILY PROTEIN; 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}; Exonuclease {ECO:0000313|EMBL:SUJ00156.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01192};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01192};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01192};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_01192};
KW Potassium {ECO:0000256|ARBA:ARBA00022958, ECO:0000256|HAMAP-Rule:MF_01192};
KW Reference proteome {ECO:0000313|Proteomes:UP000254069}.
FT DOMAIN 2..251
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT REGION 185..190
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01192"
FT BINDING 105
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01192"
FT BINDING 172
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 183
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01192"
FT BINDING 186
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01192"
SQ SEQUENCE 253 AA; 28014 MW; B1262BACBAD4A942 CRC64;
MNRLLIIDGM NLVRRLHAAQ PDEADMQGLT ERSRNACQKL IRQHCPSHVA IVWDGDEESW
RKRLYPDYKK GRKPMPQALA DGLPALKQAL AEAGIGSINA LSEADDVIAT LASKLCLRGG
EAIIVSTDKG FCQLRLPRLL LWDHFNGAAM DIAALEQKLG IEQSQLLDFM ALSGDSGNKI
PGIQGIGPKT AGELLRSFRT LANVYNALDT LGAKQAKKLT EGKEMARLSY RLAKLRTDLE
LNIRLNQYRV KEN
//
