ID   MTV1_GEOSE              Reviewed;         561 AA.
AC   P43422;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Type II methyltransferase M.BstVI {ECO:0000303|PubMed:12654995};
DE            Short=M.BstVI {ECO:0000303|PubMed:8370531};
DE            EC=2.1.1.72;
DE   AltName: Full=Adenine-specific methyltransferase BstVI;
DE   AltName: Full=Modification methylase BstVI;
GN   Name=bstVIM {ECO:0000303|PubMed:8370531};
OS   Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=1422;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=V;
RX   PubMed=8370531; DOI=10.1016/0378-1119(93)90676-t;
RA   Gonzalez E., Vasquez C.;
RT   "Characterization of the bstVIRM genes encoding the Bacillus
RT   stearothermophilus V restriction-modification system.";
RL   Gene 131:103-106(1993).
RN   [2]
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'-CTCGAG-3', methylates A-5 on both strands, and protects the
CC       DNA from cleavage by the BstVI 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; L07642; AAA51408.1; -; Genomic_DNA.
DR   PIR; JN0797; JN0797.
DR   AlphaFoldDB; P43422; -.
DR   SMR; P43422; -.
DR   REBASE; 3331; M.BstVI.
DR   PRIDE; P43422; -.
DR   PRO; PR:P43422; -.
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   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
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   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Methyltransferase; Restriction system;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..561
FT                   /note="Type II methyltransferase M.BstVI"
FT                   /id="PRO_0000087945"
SQ   SEQUENCE   561 AA;  65702 MW;  4D463062E4941859 CRC64;
     MVTQHSYRMH GAVYTKPIIV DLILDLTGYT SDKNLENFKL LDPSFGDGVF LEAAVHRLMD
     SLIRRGYRPN ELIDHLGNCI RGIELRLEAY QAGRHRLQKV LEGYGFSKPE INWLINQWII
     QADFLLWQED TTEAIKFDFV VGNPPYVRQE LIQDELIKKY RKRYTTIYDR ADLYVPFIQH
     SLELLSEQGT LGIICSDRFT KNRYGKKLRK FITDNYKVRY IVDLHKTSPF ENEVTAYPAI
     YVIKTKNYDK SVVRAVYTEV ITSKVCQDAK DFLLSNQKPD QSSKEMKTYV FSEWFAGDEP
     WIIQSQECRE ILRRLENRFP LIEDDVHSCK IRIGVATGAD KVYIVDPQQV DIEPEVLLPL
     VTTADISSGR IIWSGKHVIN PFNSDGGLIN LDDFPRLKTY FQQHEEIIKN RNVAKKNPSQ
     WFRTIDRIYP EIVHQPKLLI PDMKNTNHIV KDDGAFYPHH NLYYILPGNW NIDILRAILL
     SSVVKFFIWS YATKMRGDTL RYQAQYLRKI RLPDPKSLTN DQKERLMDER VIQSQEYLDS
     IVAEIYQLSK TEIEIIKDAL E