MTT8_THET8
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 03-AUG-2022, entry version 125.
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}; OrderedLocusNames=TTHA1583;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; 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 STRING; 300852.55772965; -.
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 OMA; AYPWREE; -.
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 Gene3D; 3.40.50.150; -; 1.
DR Gene3D; 3.90.220.10; -; 1.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR021188; N6_DNA_MeTrfase_TaqI.
DR InterPro; IPR023135; N6_DNA_MeTrfase_TaqI_C.
DR InterPro; IPR011639; RM_methylase_Eco57I-like.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR025931; TaqI_C.
DR Pfam; PF07669; Eco57I; 1.
DR Pfam; PF12950; TaqI_C; 1.
DR PIRSF; PIRSF037236; Ade-sp_methyltransferase_TaqI; 1.
DR SUPFAM; SSF53335; SSF53335; 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
