ID   NFI_ARCFU               Reviewed;         221 AA.
AC   O30108;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 106.
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=AF_0129;
OS   Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS   100126 / VC-16).
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC   Archaeoglobus.
OX   NCBI_TaxID=224325;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX   PubMed=9389475; DOI=10.1038/37052;
RA   Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA   Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA   Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA   Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA   Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA   Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA   Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA   Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA   Smith H.O., Woese C.R., Venter J.C.;
RT   "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT   archaeon Archaeoglobus fulgidus.";
RL   Nature 390:364-370(1997).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=11056288; DOI=10.1016/s0921-8777(00)00054-9;
RA   Liu J., He B., Qing H., Kow Y.W.;
RT   "A deoxyinosine specific endonuclease from hyperthermophile, Archaeoglobus
RT   fulgidus: a homolog of Escherichia coli endonuclease V.";
RL   Mutat. Res. 461:169-177(2000).
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. Recognizes only deoxyinosine. {ECO:0000255|HAMAP-
CC       Rule:MF_00801, ECO:0000269|PubMed:11056288}.
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         ECO:0000269|PubMed:11056288};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00801,
CC         ECO:0000269|PubMed:11056288};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Optimum temperature is 85 degrees Celsius.
CC         {ECO:0000269|PubMed:11056288};
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; AE000782; AAB91100.1; -; Genomic_DNA.
DR   PIR; A69266; A69266.
DR   AlphaFoldDB; O30108; -.
DR   SMR; O30108; -.
DR   STRING; 224325.AF_0129; -.
DR   DNASU; 1483340; -.
DR   EnsemblBacteria; AAB91100; AAB91100; AF_0129.
DR   KEGG; afu:AF_0129; -.
DR   eggNOG; arCOG00929; Archaea.
DR   HOGENOM; CLU_047631_1_1_2; -.
DR   OMA; RIHFRQA; -.
DR   PhylomeDB; O30108; -.
DR   Proteomes; UP000002199; 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   1: Evidence at protein level;
KW   Cytoplasm; DNA damage; DNA repair; Endonuclease; Hydrolase; Magnesium;
KW   Metal-binding; Nuclease; Reference proteome.
FT   CHAIN           1..221
FT                   /note="Endonuclease V"
FT                   /id="PRO_0000159684"
FT   BINDING         38
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00801"
FT   BINDING         104
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00801"
FT   SITE            74
FT                   /note="Interaction with target DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00801"
SQ   SEQUENCE   221 AA;  24872 MW;  69F5DA504644A45C CRC64;
     MLQMNLEELR RIQEEMSRSV VLEDLIPLEE LEYVVGVDQA FISDEVVSCA VKLTFPELEV
     VDKAVRVEKV TFPYIPTFLM FREGEPAVNA VKGLVDDRAA IMVDGSGIAH PRRCGLATYI
     ALKLRKPTVG ITKKRLFGEM VEVEDGLWRL LDGSETIGYA LKSCRRCKPI FISPGSYISP
     DSALELTRKC LKGYKLPEPI RIADKLTKEV KRELTPTSKL K