ID   NFI_NANEQ               Reviewed;         299 AA.
AC   Q74NK2;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Bifunctional methyltransferase-like/endonuclease;
DE   Includes:
DE     RecName: Full=Probable methylated-DNA--protein-cysteine methyltransferase-like;
DE   Includes:
DE     RecName: Full=Endonuclease V;
DE              EC=3.1.21.7;
DE     AltName: Full=Deoxyinosine 3'endonuclease;
DE     AltName: Full=Deoxyribonuclease V;
DE              Short=DNase V;
GN   OrderedLocusNames=NEQ345.1; ORFNames=NEQ345a;
OS   Nanoarchaeum equitans (strain Kin4-M).
OC   Archaea; Nanoarchaeota; Candidatus Nanoarchaeia; Nanoarchaeales;
OC   Nanoarchaeaceae; Nanoarchaeum.
OX   NCBI_TaxID=228908;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Kin4-M;
RX   PubMed=14566062; DOI=10.1073/pnas.1735403100;
RA   Waters E., Hohn M.J., Ahel I., Graham D.E., Adams M.D., Barnstead M.,
RA   Beeson K.Y., Bibbs L., Bolanos R., Keller M., Kretz K., Lin X., Mathur E.,
RA   Ni J., Podar M., Richardson T., Sutton G.G., Simon M., Soell D.,
RA   Stetter K.O., Short J.M., Noorderwier M.;
RT   "The genome of Nanoarchaeum equitans: insights into early archaeal
RT   evolution and derived parasitism.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:12984-12988(2003).
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 (By similarity). {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the MGMT family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the endonuclease V
CC       family. {ECO:0000305}.
CC   -!- CAUTION: Lacks the potential active site region of the MGMT family and
CC       therefore has probably lost the methyltransferase activity.
CC       {ECO:0000305}.
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DR   EMBL; AE017199; AAR39194.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q74NK2; -.
DR   SMR; Q74NK2; -.
DR   STRING; 228908.NEQ345a; -.
DR   EnsemblBacteria; AAR39194; AAR39194; NEQ345a.
DR   KEGG; neq:NEQ345a; -.
DR   HOGENOM; CLU_047631_1_1_2; -.
DR   OMA; PPRIPCH; -.
DR   Proteomes; UP000000578; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0043737; F:deoxyribonuclease V activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   CDD; cd06445; ATase; 1.
DR   CDD; cd06559; Endonuclease_V; 1.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR007581; Endonuclease-V.
DR   InterPro; IPR014048; MethylDNA_cys_MeTrfase_DNA-bd.
DR   InterPro; IPR036217; MethylDNA_cys_MeTrfase_DNAb.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   PANTHER; PTHR28511; PTHR28511; 1.
DR   Pfam; PF01035; DNA_binding_1; 1.
DR   Pfam; PF04493; Endonuclease_5; 1.
DR   SUPFAM; SSF46767; SSF46767; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; DNA damage; DNA repair; Endonuclease; Hydrolase; Magnesium;
KW   Metal-binding; Nuclease; Reference proteome.
FT   CHAIN           1..299
FT                   /note="Bifunctional methyltransferase-like/endonuclease"
FT                   /id="PRO_0000159697"
FT   REGION          1..80
FT                   /note="Probable methylated-DNA--protein-cysteine
FT                   methyltransferase-like"
FT   REGION          81..299
FT                   /note="Endonuclease V"
FT   BINDING         135
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         197
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255"
FT   SITE            168
FT                   /note="Interaction with target DNA"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   299 AA;  34366 MW;  A4513D0BDFFC50D4 CRC64;
     MLSSKLLDIN YWNKFGKRLI NELINLIEQI PKGYVTTFKE LAKALGDPIA TKFVAMYYKK
     APHWYRVVSS NLIVSPMQKA LLEKEVKIIG NKVYAPIFKD FKSSKPLLEL QKIQEYLVNK
     IKFDYPEYDY VIGIDIGYKN NIIALAIFDK NKKLIETKTC KHNIEFPYIP TYLSFREGIP
     IVNILKDLDY TALYIINGHG LSHPRKMGLA TFVGTVLDLP TIGDAKKLLY GKIKNNIIYA
     HNMPVGYFVG HYVTIGNRTN LEFLKEFIKE WNSKKYLLPI EVADKITKCG RGDSNPGRD