ID   MTSM_SERMA              Reviewed;         292 AA.
AC   P14230;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Type II methyltransferase M.SmaI {ECO:0000303|PubMed:12654995};
DE            Short=M.SmaI {ECO:0000303|PubMed:2690008};
DE            EC=2.1.1.113 {ECO:0000269|PubMed:2251121};
DE   AltName: Full=Modification methylase SmaI;
DE   AltName: Full=N-4 cytosine-specific methyltransferase SmaI;
GN   Name=smaIM;
OS   Serratia marcescens.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=BMTU 1373;
RX   PubMed=2690008; DOI=10.1093/nar/17.23.9783;
RA   Heidmann S., Seifert W., Kessler C., Domdey H.;
RT   "Cloning, characterization and heterologous expression of the SmaI
RT   restriction-modification system.";
RL   Nucleic Acids Res. 17:9783-9796(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=2251121; DOI=10.1093/nar/18.22.6607;
RA   Klimasauskas S., Steponaviciene D., Maneliene Z., Petrusyte M., Butkus V.,
RA   Janulaitis A.;
RT   "M.Smal is an N4-methylcytosine specific DNA-methylase.";
RL   Nucleic Acids Res. 18:6607-6609(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Dunbar J.C., Withers B.;
RT   "Characterization of the SmaI restriction and modification enzymes.";
RL   Submitted (AUG-1992) to the EMBL/GenBank/DDBJ databases.
RN   [4]
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 thatnrecognizes the double-stranded
CC       sequence 5'-CCCGGG-3', methylates C-2 on both strands, and protects the
CC       DNA from cleavage by the SmaI endonuclease.
CC       {ECO:0000269|PubMed:2251121, ECO:0000269|PubMed:2690008,
CC       ECO:0000303|PubMed:12654995}.
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         Evidence={ECO:0000269|PubMed:2251121};
CC   -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family. N(4)
CC       subfamily. {ECO:0000305}.
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DR   EMBL; X16458; CAA34479.1; -; Genomic_DNA.
DR   EMBL; M98769; AAA26570.1; -; Genomic_DNA.
DR   PIR; S06036; S06036.
DR   AlphaFoldDB; P14230; -.
DR   SMR; P14230; -.
DR   REBASE; 3505; M.SmaI.
DR   BRENDA; 2.1.1.113; 5690.
DR   PRO; PR:P14230; -.
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   1: Evidence at protein level;
KW   DNA-binding; Methyltransferase; Restriction system;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..292
FT                   /note="Type II methyltransferase M.SmaI"
FT                   /id="PRO_0000087932"
FT   REGION          110..130
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   292 AA;  33466 MW;  A923C42E5DBAB5AF CRC64;
     MKKHSNNLDL FDQTEECLES NLRSCKIIVG DAREAVQGLD SEIFDCVVTS PPYWGLRDYG
     NGGQIGAEDN INDYIKDLVD LFRDVRRTLK DDGTLWLNIG DSYTSGGRTW RDKDDKNKGR
     AMSYRPPTPE GLKPKDLIGV PWRLAFALQN DGWYLRTDII WNKPNCQPES VRDRPTRSHE
     YIFLLSKGKK YYYDWESIKE PASDPKMDKK NRRTVWNINT EPYPGSHFAV FPRAMARLCV
     LAGSRPGGKV LDPFFGSGTT GVVCQELDRE CVGIELNEEY ASLAKERILR RR