ID   MTBF_BACIU              Reviewed;         409 AA.
AC   P17044;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   13-SEP-2023, entry version 97.
DE   RecName: Full=Type II methyltransferase M.BsuFI {ECO:0000303|PubMed:12654995};
DE            Short=M.BsuFI {ECO:0000303|PubMed:2108858};
DE            EC=2.1.1.37 {ECO:0000269|PubMed:2108858};
DE   AltName: Full=Cytosine-specific methyltransferase BsuFI;
DE   AltName: Full=Modification methylase BsuFI;
GN   Name=hsdFM; Synonyms=hsmFI {ECO:0000303|PubMed:2108858};
OS   Bacillus subtilis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=ISF18;
RX   PubMed=2108858; DOI=10.1002/j.1460-2075.1990.tb08203.x;
RA   Walter J., Noyer-Weidner M., Trautner T.A.;
RT   "The amino acid sequence of the CCGG recognizing DNA methyltransferase
RT   M.BsuFI: implications for the analysis of sequence recognition by cytosine
RT   DNA methyltransferases.";
RL   EMBO J. 9:1007-1013(1990).
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'-CCGG-
CC       3', methylates C-1 on both strands, and protects the DNA from cleavage
CC       by the BsuFI endonuclease. {ECO:0000269|PubMed:2108858,
CC       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         ECO:0000269|PubMed:2108858};
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   EMBL; X51515; CAA35888.1; -; Genomic_DNA.
DR   PIR; S09247; CTBSFI.
DR   AlphaFoldDB; P17044; -.
DR   SMR; P17044; -.
DR   REBASE; 203788; M.Bsu1444ORF756P.
DR   REBASE; 203791; M.Bsu757ORF755P.
DR   REBASE; 205274; M.Bsu761ORF757P.
DR   REBASE; 205287; M.Bsu333ORF764P.
DR   REBASE; 257163; M.Ssp9304ORF3154P.
DR   REBASE; 3338; M.BsuFI.
DR   PRO; PR:P17044; -.
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   CDD; cd00315; Cyt_C5_DNA_methylase; 1.
DR   Gene3D; 3.90.120.10; DNA Methylase, subunit A, domain 2; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR018117; C5_DNA_meth_AS.
DR   InterPro; IPR001525; C5_MeTfrase.
DR   InterPro; IPR031303; C5_meth_CS.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   NCBIfam; TIGR00675; dcm; 1.
DR   PANTHER; PTHR46098; TRNA (CYTOSINE(38)-C(5))-METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR46098:SF1; TRNA (CYTOSINE(38)-C(5))-METHYLTRANSFERASE; 1.
DR   Pfam; PF00145; DNA_methylase; 1.
DR   PRINTS; PR00105; C5METTRFRASE.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS00094; C5_MTASE_1; 1.
DR   PROSITE; PS00095; C5_MTASE_2; 1.
DR   PROSITE; PS51679; SAM_MT_C5; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Methyltransferase; Restriction system;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..409
FT                   /note="Type II methyltransferase M.BsuFI"
FT                   /id="PRO_0000087863"
FT   DOMAIN          101..402
FT                   /note="SAM-dependent MTase C5-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
FT   ACT_SITE        170
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016,
FT                   ECO:0000255|PROSITE-ProRule:PRU10018"
SQ   SEQUENCE   409 AA;  46911 MW;  9CBE3732596A3C20 CRC64;
     MRGGNRLGAG RKVIPESEKK KRKSVYITDK LYTRIMDTDI ENCNNFSQKC MALIELAMEN
     LNKNNQEHSV KRNNILMVRD TKSTYNKTNN NFEKQNRGIK LTFIDLFAGI GGIRLGFEDK
     YTKCVFSSEW DKYAAQTYEA NYGEKPHGDI TKINENDIPD QDVLLAGFPC QPFSNIGKRE
     GFAHERRNII FDVLRILKKK QPKMFLLENV KGLLTNDNGN TFRVILDNLK SLGYSVFYEV
     MDAQNFGLPQ RRERIVIVGF HPDLGINDFS FPKGNPDNKV PINAILEHNP TGYSISKRLQ
     ESYLFKKDDG KPQIVDFRCT YQVNTLVASY HKIQRLTGTF VKDGETGLRL FSELELKRLM
     GFPVDFKVPV SRTQMYRQFG NSVAVPMIKA VAGAMKERLL LAEMQVLKK
//