ID   MTS1_SALIN              Reviewed;         461 AA.
AC   P09795;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Type II methyltransferase M.SinI {ECO:0000303|PubMed:12654995};
DE            Short=M.SinI {ECO:0000303|PubMed:2836359};
DE            EC=2.1.1.37;
DE   AltName: Full=Cytosine-specific methyltransferase SinI;
DE   AltName: Full=Modification methylase SinI;
GN   Name=sinIM;
OS   Salmonella infantis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX   PubMed=2836359; DOI=10.1128/jb.170.6.2527-2532.1988;
RA   Karreman C., de Waard A.;
RT   "Cloning and complete nucleotide sequences of the type II restriction-
RT   modification genes of Salmonella infantis.";
RL   J. Bacteriol. 170:2527-2532(1988).
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       GGWCC-3', methylates C-4 on both strands, and protects the DNA from
CC       cleavage by the SinI endonuclease. {ECO:0000269|PubMed:2836359,
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}.
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DR   EMBL; J03391; AAA27212.1; -; Genomic_DNA.
DR   AlphaFoldDB; P09795; -.
DR   SMR; P09795; -.
DR   REBASE; 3504; M.SinI.
DR   PRO; PR:P09795; -.
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; IPR031303; C5_meth_CS.
DR   InterPro; IPR041657; HTH_17.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR010093; SinI_DNA-bd.
DR   Pfam; PF00145; DNA_methylase; 1.
DR   Pfam; PF12728; HTH_17; 1.
DR   PRINTS; PR00105; C5METTRFRASE.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR00675; dcm; 1.
DR   TIGRFAMs; TIGR01764; excise; 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..461
FT                   /note="Type II methyltransferase M.SinI"
FT                   /id="PRO_0000087905"
FT   DOMAIN          75..435
FT                   /note="SAM-dependent MTase C5-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
FT   ACT_SITE        154
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016,
FT                   ECO:0000255|PROSITE-ProRule:PRU10018"
SQ   SEQUENCE   461 AA;  51767 MW;  5EA688C4F465BBC4 CRC64;
     MIMNDIITVT EAAQLLELTP QRVRTMCKQG SIDAYQSGRT WLIKSSSVEK LMLVNSLSDA
     QNSYSMLASE PKNKPKALSF FSGAMGLDLG IEQAGFETLL ASEIDKAARD TILSNRPNMA
     LIGDIRDYTT EDILKLAGVS SGNEIDLIMG GPPCQAFSTA GKRLGLEDER GNVFIKYLDV
     ALDIRPKYIV IENVRGLLSA PMKHRPHNER GEGLPPLKSE EQPGGVLHYI IRIIKSAGYS
     VSFNLYNSAN FGVPQIRERV IIICSRDGSR VPFLQPTHSE KGEYGLPKWI TLRETITNLK
     NITHEHVLFP EKRLKYYRLL KEGQYWKHLP EDLQKEALGK SFFLGGGKTG FLRRVAWDRP
     SPTLVTHPAM PATDLAHPDE LRPLSVQEYK VIQQFPEEWV IKGKLLDKYR QLGNAVPIGL
     GLAVGKNILD HMNGRKIESF PNFRYSRYKN TSDLDIFGEL V