ID   MTS1_STRFI              Reviewed;         421 AA.
AC   O52513;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Type II methyltransferase M.SfiI {ECO:0000303|PubMed:12654995};
DE            Short=M.SfiI {ECO:0000303|PubMed:12654995};
DE            EC=2.1.1.113;
DE   AltName: Full=Modification methylase SfiI;
DE   AltName: Full=N-4 cytosine-specific methyltransferase SfiI;
GN   Name=sfiIM {ECO:0000303|Ref.1};
OS   Streptomyces fimbriatus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=68197;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   van Cott E.M., Moran L.S., Slatko B.E., Wilson G.G.;
RT   "Characterization of the SfiI restriction and modification genes.";
RL   Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
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 beta subtype methylase, recognizes the double-stranded
CC       sequence 5'-GGCCNNNNNGGCC-3', methylates C-? on both strands, and
CC       protects the DNA from cleavage by the SfiI endonuclease.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = an N(4)-
CC         methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:16857, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:13674,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:85452, ChEBI:CHEBI:137933; EC=2.1.1.113;
CC   -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family. N(4)
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AF039750; AAB95366.1; -; Genomic_DNA.
DR   AlphaFoldDB; O52513; -.
DR   REBASE; 3502; M.SfiI.
DR   PRIDE; O52513; -.
DR   BRENDA; 2.1.1.113; 6011.
DR   PRO; PR:O52513; -.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0015667; F:site-specific DNA-methyltransferase (cytosine-N4-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; IPR002941; DNA_methylase_N4/N6.
DR   InterPro; IPR017985; MeTrfase_CN4_CS.
DR   InterPro; IPR001091; RM_Methyltransferase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF01555; N6_N4_Mtase; 1.
DR   PRINTS; PR00508; S21N4MTFRASE.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS00093; N4_MTASE; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Methyltransferase; Restriction system;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..421
FT                   /note="Type II methyltransferase M.SfiI"
FT                   /id="PRO_0000087934"
SQ   SEQUENCE   421 AA;  47624 MW;  54964454A28623C1 CRC64;
     MRKPSSGQPA GLDAWDETRS LATHAGPDFA LYVGDSLDCL AKLPDESINT VVTSPPYWAV
     RDYEHDEQLG LEDEVDDYVE RLVKIFREVY RVLATDGSAW LNIGDSYFNK QITVGGKPPR
     TGWKRNKQLS LVPFRVALAL QDDGWWIRNV AVWHKPNAMP ASVRDRLTVT WEPVFLLTKS
     ERYYFNLDEI RVPHQTSDAI ERRRAESGTV TGKAQGKKEL RKWLNSPRHR ATIEGIKEVE
     RRPNAPAAVE LASYLRTALK EKKRSIAWVA EQLDLPFERT RHYFRTDEIG SRLPPPEVWE
     QLKDLLELDA TYDEAMTVEV GDNVFRNHPN GKNPGDLLSI PTAPSGANHF AVMPRKLAHF
     ALKATLPMNG SCLDPFMGSG TTGRVVRELG GRFVGVDVNE HYMTDYLVES GVISPETETL
     W