XNI_VIBVU
ID XNI_VIBVU Reviewed; 259 AA.
AC Q8DFB4;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Flap endonuclease Xni {ECO:0000255|HAMAP-Rule:MF_01192};
DE Short=FEN {ECO:0000255|HAMAP-Rule:MF_01192};
DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_01192};
GN Name=xni {ECO:0000255|HAMAP-Rule:MF_01192};
GN Synonyms=ygdG {ECO:0000255|HAMAP-Rule:MF_01192};
GN OrderedLocusNames=VV1_0301;
OS Vibrio vulnificus (strain CMCP6).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=216895;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CMCP6;
RA Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.;
RT "Complete genome sequence of Vibrio vulnificus CMCP6.";
RL Submitted (DEC-2002) 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:0000255|HAMAP-
CC Rule:MF_01192}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|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:0000255|HAMAP-Rule:MF_01192};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01192};
CC Note=Binds 1 K(+) per subunit. The potassium ion strongly increases the
CC affinity for DNA. {ECO:0000255|HAMAP-Rule:MF_01192};
CC -!- SIMILARITY: Belongs to the Xni family. {ECO:0000255|HAMAP-
CC Rule:MF_01192}.
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DR EMBL; AE016795; AAO08834.1; -; Genomic_DNA.
DR RefSeq; WP_011078409.1; NC_004459.3.
DR AlphaFoldDB; Q8DFB4; -.
DR SMR; Q8DFB4; -.
DR PRIDE; Q8DFB4; -.
DR EnsemblBacteria; AAO08834; AAO08834; VV1_0301.
DR KEGG; vvu:VV1_0301; -.
DR HOGENOM; CLU_004675_1_2_6; -.
DR OMA; WRVDLIP; -.
DR Proteomes; UP000002275; Chromosome 1.
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 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; PTHR42646; 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; SSF47807; 1.
DR SUPFAM; SSF88723; SSF88723; 1.
PE 3: Inferred from homology;
KW DNA-binding; Endonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease;
KW Potassium.
FT CHAIN 1..259
FT /note="Flap endonuclease Xni"
FT /id="PRO_0000297890"
FT DOMAIN 165..255
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01192"
FT REGION 189..194
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01192"
FT BINDING 109
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01192"
FT BINDING 176
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01192"
FT BINDING 187
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01192"
FT BINDING 190
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01192"
SQ SEQUENCE 259 AA; 29402 MW; 672129B3A001D557 CRC64;
MAIHLVIIDA LNLIRRVHSA QPDPTDIANT IQNTRRTLQR IISESHPTHI VAVFDHLGSD
RGWRAEILPE YKQGRKPMPE PLLNGLEKIQ EAWWQLGIDS LLSEGDEADD LVATLACKVA
QHGEKVTIIS TDKGYCQLLS PTLQIRDYFQ HRWLDQPFIE QEFGVKPQQL SDYWGLTGIS
SSQVTGIPGI GPKAAKEILS QFDDIEQAFL SPDLPKKYRT KFDQHIELAR RCKRVSALKT
DIELGFNLQD LRFTANEAR