ID   NFI_PICTO               Reviewed;         298 AA.
AC   Q6KZ38;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Bifunctional methyltransferase/endonuclease;
DE   Includes:
DE     RecName: Full=Probable methylated-DNA--protein-cysteine methyltransferase;
DE              EC=2.1.1.-;
DE     AltName: Full=O-6-methylbase-DNA-alkyltransferase;
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=PTO1429;
OS   Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC
OS   100828).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Picrophilaceae; Picrophilus.
OX   NCBI_TaxID=263820;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828;
RX   PubMed=15184674; DOI=10.1073/pnas.0401356101;
RA   Fuetterer O., Angelov A., Liesegang H., Gottschalk G., Schleper C.,
RA   Schepers B., Dock C., Antranikian G., Liebl W.;
RT   "Genome sequence of Picrophilus torridus and its implications for life
RT   around pH 0.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9091-9096(2004).
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;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
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}.
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DR   EMBL; AE017261; AAT44014.1; -; Genomic_DNA.
DR   RefSeq; WP_011178230.1; NC_005877.1.
DR   AlphaFoldDB; Q6KZ38; -.
DR   SMR; Q6KZ38; -.
DR   STRING; 263820.PTO1429; -.
DR   EnsemblBacteria; AAT44014; AAT44014; PTO1429.
DR   GeneID; 2843979; -.
DR   KEGG; pto:PTO1429; -.
DR   PATRIC; fig|263820.9.peg.1483; -.
DR   eggNOG; arCOG00929; Archaea.
DR   eggNOG; arCOG02724; Archaea.
DR   HOGENOM; CLU_047631_1_1_2; -.
DR   OMA; PPRIPCH; -.
DR   OrthoDB; 80668at2157; -.
DR   Proteomes; UP000000438; 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:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; 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.
DR   TIGRFAMs; TIGR00589; ogt; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; DNA damage; DNA repair; Endonuclease; Hydrolase; Magnesium;
KW   Metal-binding; Methyltransferase; Multifunctional enzyme; Nuclease;
KW   Reference proteome; Transferase.
FT   CHAIN           1..298
FT                   /note="Bifunctional methyltransferase/endonuclease"
FT                   /id="PRO_0000159698"
FT   REGION          1..79
FT                   /note="Probable methylated-DNA--protein-cysteine
FT                   methyltransferase"
FT   REGION          80..298
FT                   /note="Endonuclease V"
FT   ACT_SITE        56
FT                   /evidence="ECO:0000255"
FT   BINDING         137
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:0000250"
FT   SITE            170
FT                   /note="Interaction with target DNA"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   298 AA;  33854 MW;  981F625E8CB50864 CRC64;
     MQSIDLYSYL YSLLGQIPEG MVTTYGDLAV ALGDVKAARA CGYMLSRNND TENIPCYKVI
     MSDGSLGGYS LGIDEKIRRL RNDGIEINNG RIDLKRYRFN NFDSSYPLKR LQEEQEKIAG
     LAVYSDDYNE DKICAIDVSY KDEIGYSVMV SFENNEYDFK TFIKETRFPY IPGYLAYREF
     PYIKELGKNF DGTMIIDANG LLHPRRCGLA TYVGVIMNKP SIGVAKSLLT GSIKNGYVYY
     NNMPLGYMIN SRTIVSPGNR ISLESSINFI RNLGKDHYPE ILKIAHDRTV ALRRNNII