ID   NFI_AQUAE               Reviewed;         222 AA.
AC   O66824;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 3.
DT   03-AUG-2022, entry version 101.
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=aq_548;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(1998).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC06795.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE000657; AAC06795.1; ALT_INIT; Genomic_DNA.
DR   PIR; D70349; D70349.
DR   RefSeq; NP_213384.1; NC_000918.1.
DR   AlphaFoldDB; O66824; -.
DR   SMR; O66824; -.
DR   STRING; 224324.aq_548; -.
DR   EnsemblBacteria; AAC06795; AAC06795; aq_548.
DR   KEGG; aae:aq_548; -.
DR   PATRIC; fig|224324.8.peg.450; -.
DR   eggNOG; COG1515; Bacteria.
DR   HOGENOM; CLU_047631_1_1_0; -.
DR   InParanoid; O66824; -.
DR   OrthoDB; 1681607at2; -.
DR   Proteomes; UP000000798; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0043737; F:deoxyribonuclease V activity; IBA:GO_Central.
DR   GO; GO:0016891; F:endoribonuclease activity, producing 5'-phosphomonoesters; IBA:GO_Central.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003727; F:single-stranded RNA binding; IBA:GO_Central.
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; Reference proteome.
FT   CHAIN           1..222
FT                   /note="Endonuclease V"
FT                   /id="PRO_0000159656"
FT   BINDING         36
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00801"
FT   BINDING         107
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00801"
FT   SITE            77
FT                   /note="Interaction with target DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00801"
SQ   SEQUENCE   222 AA;  25085 MW;  F7FD35204ADBD8E4 CRC64;
     MNTELLEKLK KIQLECAKKV IARDDFEKVE TIGGMDLTFE KINENPTRAW ASLVVVELKT
     LKPVYQHVVK DIVDFPYIPT FLAFREMPLL LKLYETAKVK PDVYFIDGQG IAHPRGCGIA
     SHFGVETGEV TVGVAKSKLF GYAKEPAPQR GSYTYLKYKG KIIGAVVRTK DNTAPVYVSV
     GHRISLKTAI DLVLKTSKYR VPEPTRLAHN LLQVVRRKEL RR