ID   MTT8_THET8              Reviewed;         428 AA.
AC   P29749; Q5SHZ7;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2005, sequence version 2.
DT   27-MAR-2024, entry version 131.
DE   RecName: Full=Type II methyltransferase M.TthHB8I {ECO:0000303|PubMed:12654995};
DE            Short=M.TthHB8I {ECO:0000303|PubMed:12654995};
DE            EC=2.1.1.72;
DE   AltName: Full=Adenine-specific methyltransferase TthHB8I;
DE   AltName: Full=Modification methylase TthHB8I;
GN   Name=tthHB8IM {ECO:0000303|PubMed:1339363};
GN   OrderedLocusNames=TTHA1583;
OS   Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC   Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=300852;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1339363; DOI=10.1016/0378-1119(92)90296-2;
RA   Barany F., Danzitz M., Zebala J., Mayer A.;
RT   "Cloning and sequencing of genes encoding the TthHB8I restriction and
RT   modification enzymes: comparison with the isoschizomeric TaqI enzymes.";
RL   Gene 112:3-12(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27634 / DSM 579 / HB8;
RA   Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA   Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT   "Complete genome sequence of Thermus thermophilus HB8.";
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NOMENCLATURE, AND SUBTYPE.
RX   PubMed=12654995; DOI=10.1093/nar/gkg274;
RA   Roberts R.J., Belfort M., Bestor T., Bhagwat A.S., Bickle T.A.,
RA   Bitinaite J., Blumenthal R.M., Degtyarev S.K., Dryden D.T., Dybvig K.,
RA   Firman K., Gromova E.S., Gumport R.I., Halford S.E., Hattman S.,
RA   Heitman J., Hornby D.P., Janulaitis A., Jeltsch A., Josephsen J., Kiss A.,
RA   Klaenhammer T.R., Kobayashi I., Kong H., Krueger D.H., Lacks S.,
RA   Marinus M.G., Miyahara M., Morgan R.D., Murray N.E., Nagaraja V.,
RA   Piekarowicz A., Pingoud A., Raleigh E., Rao D.N., Reich N., Repin V.E.,
RA   Selker E.U., Shaw P.C., Stein D.C., Stoddard B.L., Szybalski W.,
RA   Trautner T.A., Van Etten J.L., Vitor J.M., Wilson G.G., Xu S.Y.;
RT   "A nomenclature for restriction enzymes, DNA methyltransferases, homing
RT   endonucleases and their genes.";
RL   Nucleic Acids Res. 31:1805-1812(2003).
CC   -!- FUNCTION: A gamma subtype methylase, recognizes the double-stranded
CC       sequence 5'-TCGA-3', methylates A-4 on both strands and protects the
CC       DNA from cleavage by the TthHB8I endonuclease.
CC       {ECO:0000303|PubMed:12654995}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyadenosine in DNA + S-adenosyl-L-methionine = an
CC         N(6)-methyl-2'-deoxyadenosine in DNA + H(+) + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:15197, Rhea:RHEA-COMP:12418, Rhea:RHEA-
CC         COMP:12419, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:90615, ChEBI:CHEBI:90616; EC=2.1.1.72;
CC   -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; M74795; AAA27488.1; -; Genomic_DNA.
DR   EMBL; AP008226; BAD71406.1; -; Genomic_DNA.
DR   PIR; JH0634; JH0634.
DR   RefSeq; WP_011228786.1; NC_006461.1.
DR   RefSeq; YP_144849.1; NC_006461.1.
DR   AlphaFoldDB; P29749; -.
DR   SMR; P29749; -.
DR   REBASE; 3523; M.TthHB8I.
DR   EnsemblBacteria; BAD71406; BAD71406; BAD71406.
DR   GeneID; 3169149; -.
DR   KEGG; ttj:TTHA1583; -.
DR   PATRIC; fig|300852.9.peg.1554; -.
DR   eggNOG; COG0732; Bacteria.
DR   eggNOG; COG0827; Bacteria.
DR   HOGENOM; CLU_681415_0_0_0; -.
DR   PhylomeDB; P29749; -.
DR   PRO; PR:P29749; -.
DR   Proteomes; UP000000532; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC.
DR   GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.90.220.10; Adenine-n6-DNA-methyltransferase Taqi, Chain A, domain 2; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR011639; MethylTrfase_TaqI-like_dom.
DR   InterPro; IPR021188; N6_DNA_MeTrfase_TaqI.
DR   InterPro; IPR023135; N6_DNA_MeTrfase_TaqI_C.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR025931; TaqI_C.
DR   PANTHER; PTHR33841; DNA METHYLTRANSFERASE YEEA-RELATED; 1.
DR   PANTHER; PTHR33841:SF5; TYPE II METHYLTRANSFERASE M.HINDII; 1.
DR   Pfam; PF07669; Eco57I; 1.
DR   Pfam; PF12950; TaqI_C; 1.
DR   PIRSF; PIRSF037236; Ade-sp_methyltransferase_TaqI; 1.
DR   PRINTS; PR00507; N12N6MTFRASE.
DR   SUPFAM; SSF116734; DNA methylase specificity domain; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Methyltransferase; Reference proteome; Restriction system;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..428
FT                   /note="Type II methyltransferase M.TthHB8I"
FT                   /id="PRO_0000087981"
FT   REGION          407..428
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        36
FT                   /note="P -> R (in Ref. 1; AAA27488)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        39
FT                   /note="G -> V (in Ref. 1; AAA27488)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        56
FT                   /note="R -> P (in Ref. 1; AAA27488)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        235..241
FT                   /note="EWKGEII -> GMEGRDH (in Ref. 1; AAA27488)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        265
FT                   /note="R -> P (in Ref. 1; AAA27488)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   428 AA;  48408 MW;  6F1407F702D79B57 CRC64;
     MLFPPSLPPT ASGRSLGRVE TPPGLVRFMV GLAEAPKGGR VLEPACADGP FLRAFREAHG
     TGYRFVGVEI DPHALDLPPW AEGVVADFLL WEPGEAFDLI LGNPPYGIVG EASKYPIHVL
     REVKGLYKKT LSTWKGKYNL YGAFIEKSVR LLREGGTLVF VVPATWLVLD DFSLLRSFLA
     REGRTEVYYL GEVFPGRKVS AVVLRFRKGG KGLALWDTRR DGETFTPLLW SEKPEWKGEI
     IRFETGWTRE MEASGPPLGS LFHIRFAARS PEFKKHPAVQ KEPEPGLVPV LTGRNLKPGW
     IDYESNHSGL WMPKERAKEL RDFYATPHLV VAHTKGTKVV AAWDEKAYPW REEFHLLPKE
     GVELDPLFLV EWLNSDKIQE YVKTLYRDFV PHLTLRMLER IPALLPRKGN TERRKHGPYT
     SPESAGSF
//