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NFI_SHIF8
ID   NFI_SHIF8               Reviewed;         223 AA.
AC   Q0SY02;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Endonuclease V {ECO:0000255|HAMAP-Rule:MF_00801};
DE            EC=3.1.21.7 {ECO:0000255|HAMAP-Rule:MF_00801};
DE   AltName: Full=Deoxyinosine 3'endonuclease {ECO:0000255|HAMAP-Rule:MF_00801};
DE   AltName: Full=Deoxyribonuclease V {ECO:0000255|HAMAP-Rule:MF_00801};
DE            Short=DNase V {ECO:0000255|HAMAP-Rule:MF_00801};
GN   Name=nfi {ECO:0000255|HAMAP-Rule:MF_00801}; OrderedLocusNames=SFV_4070;
OS   Shigella flexneri serotype 5b (strain 8401).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=373384;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8401;
RX   PubMed=16822325; DOI=10.1186/1471-2164-7-173;
RA   Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., Peng J.,
RA   Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., Jin Q.;
RT   "Complete genome sequence of Shigella flexneri 5b and comparison with
RT   Shigella flexneri 2a.";
RL   BMC Genomics 7:173-173(2006).
CC   -!- FUNCTION: DNA repair enzyme involved in the repair of deaminated bases.
CC       Selectively cleaves double-stranded DNA at the second phosphodiester
CC       bond 3' to a deoxyinosine leaving behind the intact lesion on the
CC       nicked DNA. {ECO:0000255|HAMAP-Rule:MF_00801}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage at apurinic or apyrimidinic sites to
CC         products with a 5'-phosphate.; EC=3.1.21.7;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00801};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00801};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00801}.
CC   -!- SIMILARITY: Belongs to the endonuclease V family. {ECO:0000255|HAMAP-
CC       Rule:MF_00801}.
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DR   EMBL; CP000266; ABF06063.1; -; Genomic_DNA.
DR   RefSeq; WP_000362374.1; NC_008258.1.
DR   AlphaFoldDB; Q0SY02; -.
DR   SMR; Q0SY02; -.
DR   EnsemblBacteria; ABF06063; ABF06063; SFV_4070.
DR   KEGG; sfv:SFV_4070; -.
DR   HOGENOM; CLU_047631_1_0_6; -.
DR   OMA; RIHFRQA; -.
DR   BioCyc; SFLE373384:SFV_RS22405-MON; -.
DR   Proteomes; UP000000659; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0043737; F:deoxyribonuclease V activity; 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   CDD; cd06559; Endonuclease_V; 1.
DR   HAMAP; MF_00801; Endonuclease_5; 1.
DR   InterPro; IPR007581; Endonuclease-V.
DR   PANTHER; PTHR28511; PTHR28511; 1.
DR   Pfam; PF04493; Endonuclease_5; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; DNA damage; DNA repair; Endonuclease; Hydrolase; Magnesium;
KW   Metal-binding; Nuclease.
FT   CHAIN           1..223
FT                   /note="Endonuclease V"
FT                   /id="PRO_1000047002"
FT   BINDING         35
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00801"
FT   BINDING         103
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00801"
FT   SITE            73
FT                   /note="Interaction with target DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00801"
SQ   SEQUENCE   223 AA;  24619 MW;  44BCC9219BA4293A CRC64;
     MDLASLRAQQ IELASSVICE DRLDKDPPDL IAGADVGFEQ GGEVTRAAMV LLKYPSLELV
     EYKVARIATT MPYIPGFLSF REYPALLAAW EMLSQKPDLV FVDGHGISHP RRLGVASHFG
     LLVDVPTIGV AKKRLCGKFE PLSSKPGALA PLMDKGEQLA WVWRSKARCN PLFIATGHRV
     SVDSALAWVQ RCMKGYRLPE PTRWADAVAS ERPAFVRYTA NQP
 
 
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