ID   MTSB_LACLC              Reviewed;         360 AA.
AC   P34878;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   24-JAN-2024, entry version 99.
DE   RecName: Full=Type II methyltransferase M2.ScrFI {ECO:0000303|PubMed:12654995};
DE            Short=M2.ScrFI {ECO:0000303|PubMed:12654995};
DE            EC=2.1.1.37;
DE   AltName: Full=Cytosine-specific methyltransferase ScrFIB;
DE   AltName: Full=Modification methylase ScrFIB;
DE            Short=M.ScrFI-B {ECO:0000303|Ref.1};
DE            Short=M.ScrFIB;
GN   Name=scrFIBM;
OS   Lactococcus lactis subsp. cremoris (Streptococcus cremoris).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=1359;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=UC503;
RA   Twomey D.P., Davis R., Daly C., Fitzgerald G.F.;
RT   "Sequence of the gene encoding a second ScrFI m5C methyltransferase of
RT   Lactococcus lactis.";
RL   Gene 136:205-209(1993).
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       CCNGG-3', methylates C-2 on both strands, and protects the DNA from
CC       cleavage by the ScrFI endonuclease. {ECO:0000303|PubMed:12654995,
CC       ECO:0000305|Ref.1}.
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   -!- MISCELLANEOUS: The ScrFI restriction system has two different
CC       methylases. {ECO:0000269|PubMed:12654995}.
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; L12227; AAA16838.1; -; Unassigned_DNA.
DR   EMBL; U89998; AAB66694.1; -; Genomic_DNA.
DR   RefSeq; WP_015081858.1; NZ_CP068511.2.
DR   AlphaFoldDB; P34878; -.
DR   SMR; P34878; -.
DR   REBASE; 3682; M2.ScrFI.
DR   PRO; PR:P34878; -.
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   3: Inferred from homology;
KW   DNA-binding; Methyltransferase; Restriction system;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..360
FT                   /note="Type II methyltransferase M2.ScrFI"
FT                   /id="PRO_0000087893"
FT   DOMAIN          2..360
FT                   /note="SAM-dependent MTase C5-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
FT   ACT_SITE        127
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016,
FT                   ECO:0000255|PROSITE-ProRule:PRU10018"
SQ   SEQUENCE   360 AA;  41844 MW;  B51D60F72A22A7D7 CRC64;
     MLRVFEAFAG YGSQRLALIK ANIPHEIVGI SEIEGDVLLS YSAIHENLLE ERNKNIKLTD
     DEMRDYLKNI NIPLDYKTFE NRADKLGGQK LKDMYIANKL NKNFGDIRSI DPKKLPDFDF
     FTYSFPCQDI SVAGYQNGLV ADSGTRSSLL WECCKIIEHK KPKYLMMENV KNLVGKNHKV
     NFNKFLLYLE SLGYTNYWDI LNARDFGIPQ NRERVFCISI LNPNEDFTFP QKQNLTLSMN
     DLLEENVSEK FYLKNNQVSD EPILQDYIYC LDSNYWKGTF LKDFLSKKRR QLVSGKVRPD
     GKYPARRLTP RETWRFMGVE DTNFDKASIL VSNTSLYKQS GNSIVVPVLE SLFKELFKSQ
//