ID   T2SM_SERMA              Reviewed;         247 AA.
AC   P14229;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Type II restriction enzyme SmaI {ECO:0000303|Ref.2};
DE            Short=R.SmaI {ECO:0000303|PubMed:2690008};
DE            EC=3.1.21.4 {ECO:0000269|PubMed:2690008};
DE   AltName: Full=Endonuclease SmaI;
DE   AltName: Full=Type-2 restriction enzyme SmaI;
GN   Name=smaIR;
OS   Serratia marcescens.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
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].
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   [3]
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 P subtype restriction enzyme that recognizes the double-
CC       stranded sequence 5'-CCCGGG-3' and cleaves after C-3.
CC       {ECO:0000269|PubMed:2690008, ECO:0000303|PubMed:12654995}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage of DNA to give specific double-
CC         stranded fragments with terminal 5'-phosphates.; EC=3.1.21.4;
CC         Evidence={ECO:0000269|PubMed:2690008};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC   -!- COFACTOR:
CC       Name=K(+); Xref=ChEBI:CHEBI:29103;
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DR   EMBL; X16458; CAA34478.1; -; Genomic_DNA.
DR   EMBL; M98769; AAA26569.1; -; Genomic_DNA.
DR   PIR; S06035; S06035.
DR   AlphaFoldDB; P14229; -.
DR   REBASE; 1704; SmaI.
DR   BRENDA; 3.1.21.4; 5690.
DR   PRO; PR:P14229; -.
DR   GO; GO:0009036; F:type II site-specific deoxyribonuclease activity; IEA:UniProtKB-EC.
DR   GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Endonuclease; Hydrolase; Magnesium; Nuclease; Restriction system.
FT   CHAIN           1..247
FT                   /note="Type II restriction enzyme SmaI"
FT                   /id="PRO_0000077362"
SQ   SEQUENCE   247 AA;  28782 MW;  DBE6CD66362DCF93 CRC64;
     MSRDDQLFTL WGKLNDRQKD NFLKWMKAFD VEKTYQKTSG DIFNDDFFDI FGDRLITHHF
     SSTQALTKTL FEHAFNDSLN ESGVISSLAE SRTNPGHDIT IDSIKVALKT EAAKNISKSY
     IHVSKWMELG KGEWILELLL ERFLEHLENY ERIFTLRYFK ISEYKFSYQL VEIPKSLLLE
     AKNAKLEIMS GSKQSPKPGY GYVLDENENK KFSLYFDGGA ERKLQIKHLN LEHCIVHGVW
     DFILPPP