ID   NFI_METKA               Reviewed;         229 AA.
AC   Q8X260; Q7LWW2;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 87.
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=MK1435;
OS   Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938).
OC   Archaea; Euryarchaeota; Methanopyri; Methanopyrales; Methanopyraceae;
OC   Methanopyrus.
OX   NCBI_TaxID=190192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11353838; DOI=10.1073/pnas.111040498;
RA   Belova G.I., Prasad R., Kozyavkin S.A., Lake J.A., Wilson S.H.,
RA   Slesarev A.I.;
RT   "A type IB topoisomerase with DNA repair activities.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:6015-6020(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX   PubMed=11930014; DOI=10.1073/pnas.032671499;
RA   Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA   Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A.,
RA   Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G.,
RA   Koonin E.V., Kozyavkin S.A.;
RT   "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and
RT   monophyly of archaeal methanogens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002).
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   -!- 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; AF311944; AAL61958.1; -; Genomic_DNA.
DR   EMBL; AE009439; AAM02648.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8X260; -.
DR   SMR; Q8X260; -.
DR   EnsemblBacteria; AAM02648; AAM02648; MK1435.
DR   KEGG; mka:MK1435; -.
DR   PATRIC; fig|190192.8.peg.1591; -.
DR   HOGENOM; CLU_047631_1_1_2; -.
DR   OMA; RIHFRQA; -.
DR   Proteomes; UP000001826; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0043737; F:deoxyribonuclease V activity; 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; Nuclease;
KW   Reference proteome.
FT   CHAIN           1..229
FT                   /note="Endonuclease V"
FT                   /id="PRO_0000159688"
FT   SITE            77
FT                   /note="Interaction with target DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00801"
SQ   SEQUENCE   229 AA;  25331 MW;  74881C35F5FAF924 CRC64;
     MKSAEWFEAS TEEERVEIQR KVARKVRLEP LDDVDAVAGV DVSYRGEEYR AAAVVLDPET
     YEVLDRRVVH GTTDVPYEPG FLAFREGPPA LEALEGLDFD LLFVHGHGVA HPRRAGLASH
     LGVALDVPTI GVARRPLVGR SKEEPSRIGD TTPLVHRGEV VGYLVRTDAE ARPVVVSPGH
     RCNLEDAVRW TLRLVRVGKW PEPLRLADLL SRRGASRVEG ESRGAGVRR