ID   NFI_THEAC               Reviewed;         323 AA.
AC   Q9HKY3;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-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=Ta0460;
OS   Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS   15155 / AMRC-C165).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Thermoplasmataceae; Thermoplasma.
OX   NCBI_TaxID=273075;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX   PubMed=11029001; DOI=10.1038/35035069;
RA   Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA   Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT   "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT   acidophilum.";
RL   Nature 407:508-513(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; AL445064; CAC11602.1; -; Genomic_DNA.
DR   RefSeq; WP_010900887.1; NC_002578.1.
DR   AlphaFoldDB; Q9HKY3; -.
DR   SMR; Q9HKY3; -.
DR   STRING; 273075.Ta0460; -.
DR   EnsemblBacteria; CAC11602; CAC11602; CAC11602.
DR   GeneID; 1456066; -.
DR   KEGG; tac:Ta0460; -.
DR   eggNOG; arCOG00929; Archaea.
DR   eggNOG; arCOG02724; Archaea.
DR   HOGENOM; CLU_047631_1_1_2; -.
DR   OMA; PPRIPCH; -.
DR   OrthoDB; 80668at2157; -.
DR   Proteomes; UP000001024; 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..323
FT                   /note="Bifunctional methyltransferase/endonuclease"
FT                   /id="PRO_0000159699"
FT   REGION          1..91
FT                   /note="Probable methylated-DNA--protein-cysteine
FT                   methyltransferase"
FT   REGION          92..323
FT                   /note="Endonuclease V"
FT   ACT_SITE        66
FT                   /evidence="ECO:0000255"
FT   BINDING         150
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         209
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   SITE            183
FT                   /note="Interaction with target DNA"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   323 AA;  36732 MW;  59A9C8A9F0E69A17 CRC64;
     MLGSIACSME FEDFDLYSYF YGLVKQIPEG YVTTYGDLAQ ALGDPIAARA VGYMLSINED
     PDTIPCYRVV LHDGTVGNYT HPLGPMEKVR RLRADGIPVV DGMIENFDRY RFRDFKTDQP
     LRKMQQYQEY IARKYSESGA GEFRTVAAFD VSYEERRAFA SMVIQDGSTI EAYVISDGIN
     FPYIPGYLAF REFRFIKKLY RKADLLLIDG NGILHPRFAG LATHAGVLLD RASIGVAKHL
     TRSTRHQDII YMQDRPVGVM IRKNMIVSPG NFIDVNGSAD TVRKMWNDRY PWPLKLAHQL
     STRHAETGGR VSEYSIESAH ELH