ID   MTC1_GEOSE              Reviewed;         579 AA.
AC   P43423;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Type II methyltransferase M.BseCI {ECO:0000303|PubMed:12654995};
DE            Short=M.BseCI {ECO:0000303|PubMed:12654995};
DE            EC=2.1.1.72;
DE   AltName: Full=Adenine-specific methyltransferase BseCI;
DE   AltName: Full=Modification methylase BseCI;
GN   Name=bseCIM {ECO:0000303|PubMed:7959066};
OS   Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=1422;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7959066; DOI=10.1016/0378-1119(94)90860-5;
RA   Rina M., Markaki M., Bouriotis V.;
RT   "Sequence of the cloned bseCIM gene: M.BseCI reveals high homology to
RT   M.BanIII.";
RL   Gene 150:71-73(1994).
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'-ATCGAT-3', methylation on A-5 on both strands, and protects
CC       the DNA from cleavage by the BanIII 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; X79509; CAA56041.1; -; Genomic_DNA.
DR   PIR; I40371; I40371.
DR   AlphaFoldDB; P43423; -.
DR   SMR; P43423; -.
DR   REBASE; 3536; M.BseCI.
DR   BRENDA; 2.1.1.72; 623.
DR   PRO; PR:P43423; -.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro.
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; IPR003356; DNA_methylase_A-5.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR025931; TaqI_C.
DR   Pfam; PF02384; N6_Mtase; 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..579
FT                   /note="Type II methyltransferase M.BseCI"
FT                   /id="PRO_0000087944"
SQ   SEQUENCE   579 AA;  66774 MW;  A4805FBEBA01835C CRC64;
     MMSVQKANTV SRQKATGAHF TPDKLAEVIA KRILDYFKGE KNRVIRVLDP ACGDGELLLA
     INKVAQSMNI QLELIGVDFD IDAINIANER LSRSGHKNFR LINKDFLEMV SEGDNYDLFN
     IEELEPVDII IANPPYVRTQ ILGAEKAQKL REKFNLKGRV DLYQAFLVAM TQQLKSNGII
     GVITSNRYLT TKGGGSTRKF LVSNFNILEI MDLGDSKFFE AAVLPAIFFG EKKNKEYQKE
     NSNVPKFFKI YEQSDIEASS SVNSEFNSLI ELLEVNKSGL YSVEDKTYSI SLGKIISPEN
     YKEPWILATE DEYEWFMKVN QNAYGFIEDF AHVKVGIKTT ADSVFIRSDW GELPEEQIPE
     DKLLRPIISA DQANKWSVSL VGNNKKVLYT HEIRDGQIKA INLEEFPRAK NYLESHKERL
     ASRKYVLKAN RNWYEIWVPH DPSLWDKPKI IFPDTSPEPK FFYEDKGSVV DGNCYWIIPK
     KENSNDILFL IMGICNSKFM SKYHDIAFQN KLYAGRRRYL TQYVNKYPIP DPESIYSKEI
     ISLVRELVNN KKETQDINEI ENRIEKLILR AFDIESLKY