ID   NFI_THEVO               Reviewed;         321 AA.
AC   Q97AL5;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 108.
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=TV0795; ORFNames=TVG0795955;
OS   Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC
OS   15438 / GSS1).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Thermoplasmataceae; Thermoplasma.
OX   NCBI_TaxID=273116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1;
RX   PubMed=11121031; DOI=10.1073/pnas.97.26.14257;
RA   Kawashima T., Amano N., Koike H., Makino S., Higuchi S., Kawashima-Ohya Y.,
RA   Watanabe K., Yamazaki M., Kanehori K., Kawamoto T., Nunoshiba T.,
RA   Yamamoto Y., Aramaki H., Makino K., Suzuki M.;
RT   "Archaeal adaptation to higher temperatures revealed by genomic sequence of
RT   Thermoplasma volcanium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(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 (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}.
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DR   EMBL; BA000011; BAB59937.1; -; Genomic_DNA.
DR   RefSeq; WP_010917039.1; NC_002689.2.
DR   AlphaFoldDB; Q97AL5; -.
DR   SMR; Q97AL5; -.
DR   STRING; 273116.14325011; -.
DR   DNASU; 1441887; -.
DR   EnsemblBacteria; BAB59937; BAB59937; BAB59937.
DR   GeneID; 1441887; -.
DR   KEGG; tvo:TVG0795955; -.
DR   eggNOG; arCOG00929; Archaea.
DR   eggNOG; arCOG02724; Archaea.
DR   HOGENOM; CLU_047631_1_1_2; -.
DR   OMA; PPRIPCH; -.
DR   OrthoDB; 80668at2157; -.
DR   PhylomeDB; Q97AL5; -.
DR   Proteomes; UP000001017; 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   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   Transferase.
FT   CHAIN           1..321
FT                   /note="Bifunctional methyltransferase/endonuclease"
FT                   /id="PRO_0000159700"
FT   REGION          1..86
FT                   /note="Probable methylated-DNA--protein-cysteine
FT                   methyltransferase"
FT   REGION          87..318
FT                   /note="Endonuclease V"
FT   ACT_SITE        61
FT                   /evidence="ECO:0000255"
FT   BINDING         145
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         204
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   SITE            178
FT                   /note="Interaction with target DNA"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   321 AA;  36049 MW;  FC3220C1E37B7ACD CRC64;
     MLSVDYENFD LISYLYNLVR QIPDGMVSTY GDLAEALGDP VAARSVGFML SINKEPDYIP
     CYKVVPHDGS VGNYTHPLGS AEKMRRLIRD GITITNGHIS NFEKVRFREF KTDYPLRKLR
     ELQFKIGRLY DDRNDYSLDT IAAFDVSYKE TRGYASKVVY NKGKIGAYVY SSDSMFPYIP
     GYLAFKEFKF IRALYDNETM ILIDGNGILH PRFAGLATHA GVSLKTASIG IAKHLINCTV
     KGSDLLISGV VAGKMIGHHT IVSPGNRINV EEAGRLIEQR EGKEMRSLLR LAHNLTRLHI
     ETNGNIARYD FSTRNTAIQS S