ID   MTS3_STAAU              Reviewed;         412 AA.
AC   P16668;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   13-SEP-2023, entry version 111.
DE   RecName: Full=Type II methyltransferase M.Sau3AI {ECO:0000303|PubMed:12654995};
DE            Short=M.Sau3AI {ECO:0000303|PubMed:2227451};
DE            EC=2.1.1.37;
DE   AltName: Full=Cytosine-specific methyltransferase Sau3AI;
DE   AltName: Full=Modification methylase Sau3AI;
GN   Name=sau3AIM;
OS   Staphylococcus aureus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=ATCC 49834 / 3A;
RX   PubMed=2227451; DOI=10.1016/0378-1119(90)90465-4;
RA   Seeber S., Kessler C., Goetz F.;
RT   "Cloning, expression and characterization of the Sau3AI restriction and
RT   modification genes in Staphylococcus carnosus TM300.";
RL   Gene 94:37-43(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 that recognizes the double-stranded sequence 5'-
CC       GATC-3', methylates C-4 on both strands and protects the DNA from
CC       cleavage by the Sau3AI endonuclease. {ECO:0000269|PubMed:2227451,
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   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. C5-methyltransferase family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01016}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M32470; AAA26673.1; -; Genomic_DNA.
DR   PIR; JQ0760; JQ0760.
DR   RefSeq; WP_001033636.1; NZ_WOUL01000015.1.
DR   AlphaFoldDB; P16668; -.
DR   SMR; P16668; -.
DR   REBASE; 252066; M.Psp7025ORF2592P.
DR   REBASE; 256731; M.Ssp9304ORF1496P.
DR   PRO; PR:P16668; -.
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..412
FT                   /note="Type II methyltransferase M.Sau3AI"
FT                   /id="PRO_0000087907"
FT   DOMAIN          4..402
FT                   /note="SAM-dependent MTase C5-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
FT   ACT_SITE        85
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016,
FT                   ECO:0000255|PROSITE-ProRule:PRU10018"
SQ   SEQUENCE   412 AA;  47295 MW;  E6F008248749F085 CRC64;
     MNKIKVVELF AGVGGFRLGL ENTKNGIFDI TWANQWEPSR KIQHAFDCYS KRFKNGIHSN
     KDIAQVSDEE MANTEADMIV GGFPCQDYSV ARSLNGELGI QGKKGVLFWQ IIRYIQNTFP
     KYLLLENVDR LLKSPSSQRG RDFAVMLSTL NELGYNVEWR VINAADYGNA QRRRRVFIFG
     YKQDLNYSKA MEESPLDKII YHNGLFAEAF PIEDYANKNR VNRTHITHDI VDISDNFSFQ
     FYNSGIMKNG EILTIDTIPK YEKSVTLGEI IESNVDDGFS LNQDQIDKFK YLRGPKKIKR
     TTKDGHEYYF SEGGMSETDS LELPARTMLT SESSINRSTH FLNVDGVYRT LTPIEAERLN
     GFPDNWTEGM PIKMRYFCMG NALVVPLITR IGNQIEKIDS ITNDEFSQLR LF
//