ID   MTB1_BREBE              Reviewed;         374 AA.
AC   P34905;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Type II methyltransferase M.BbvI {ECO:0000303|PubMed:12654995};
DE            Short=M.BbvI {ECO:0000303|PubMed:12654995};
DE            EC=2.1.1.37;
DE   AltName: Full=Cytosine-specific methyltransferase BbvI;
DE   AltName: Full=Modification methylase BbvI;
GN   Name=bbvIM;
OS   Brevibacillus brevis (Bacillus brevis).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX   NCBI_TaxID=1393;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Barsomian J.M., Wilson G.G.;
RL   Submitted (FEB-1994) to UniProtKB.
RN   [2]
RP   NOMENCLATURE.
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 methylase, recognizes the double-stranded sequence 5'-
CC       GCAGC-3', methylates C-2 on both strands, and protects the DNA from
CC       cleavage by the BbvI endonuclease. {ECO:0000303|PubMed:12654995}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-
CC         methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:13681, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:11370,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:85452, ChEBI:CHEBI:85454; EC=2.1.1.37;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10018};
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. C5-methyltransferase family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01016}.
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DR   AlphaFoldDB; P34905; -.
DR   SMR; P34905; -.
DR   REBASE; 156149; M.BamRD77ORF3565P.
DR   REBASE; 162023; M.BsuBS38ORF4087P.
DR   REBASE; 182839; M.Bli14ORF3613P.
DR   REBASE; 251327; M.BliADL4ORF3338P.
DR   PRO; PR:P34905; -.
DR   GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR018117; C5_DNA_meth_AS.
DR   InterPro; IPR001525; C5_MeTfrase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF00145; DNA_methylase; 1.
DR   PRINTS; PR00105; C5METTRFRASE.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR00675; dcm; 1.
DR   PROSITE; PS00094; C5_MTASE_1; 1.
DR   PROSITE; PS51679; SAM_MT_C5; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Methyltransferase; Restriction system;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..374
FT                   /note="Type II methyltransferase M.BbvI"
FT                   /id="PRO_0000087861"
FT   DOMAIN          3..347
FT                   /note="SAM-dependent MTase C5-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
FT   ACT_SITE        92
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016,
FT                   ECO:0000255|PROSITE-ProRule:PRU10018"
SQ   SEQUENCE   374 AA;  42350 MW;  538127C7B761DC01 CRC64;
     MKFRKGELFC GPGGLALGAK EAKYMHPETG EVFEFEHAWA NDIDEWACET FRTNICPDRP
     DSVVCGDVRE LDIKSLGEKF GEIDAFTFGF PCNDYSIVGE HKGMEGNYGP LYSYGVKILN
     EYNPLVFIAE NVGGLQSANE GKAFLGILND LASAGKYGYK LVPHLYKFEE YGVPQRRHRI
     IIVGIRKDQD VAFRVPEPTH KEKYRTASEA LADIPEDALN HEFTRHKKKV VEMLNHIAPG
     GNAWSESIPE ELRLNVKKVR MSQIYRRLHP DQPSYTVTGS GGGGTHGYHW EEPRALTNRE
     RARLQTFPDD YEFIGKKEMV RKQIGMAVPP DGAKIILEAV LKTFARIEYP SINSKWDFES
     VSAEQVIEEV QEIM