MTS1_STRAH
ID MTS1_STRAH Reviewed; 390 AA.
AC O31073;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Type II methyltransferase M.SacI {ECO:0000303|PubMed:12654995};
DE Short=M.SacI {ECO:0000303|PubMed:9862476};
DE EC=2.1.1.37;
DE AltName: Full=Cytosine-specific methyltransferase SacI;
DE AltName: Full=Modification methylase SacI;
GN Name=sacIM {ECO:0000303|PubMed:9862476};
OS Streptomyces achromogenes.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=67255;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 12767 / CBS 458.68 / DSM 40028 / JCM 4121 / NBRC 12735 / NRRL
RC B-2120;
RX PubMed=9862476; DOI=10.1007/s004380050890;
RA Xu S.-Y., Xiao J.-P., Ettwiller L., Holden M., Aliotta J., Poh C.L.,
RA Dalton M., Robinson D.P., Petronzio T.R., Moran L., Ganatra M., Ware J.,
RA Slatko B., Benner J. II;
RT "Cloning and expression of the ApaLI, NspI, NspHI, SacI, ScaI, and SapI
RT restriction-modification systems in Escherichia coli.";
RL Mol. Gen. Genet. 260:226-231(1998).
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 methylase recognizes the double-stranded sequence 5'-
CC GAGCTC-3', methylates C-4 on both strands, and protects the DNA from
CC cleavage by the SacI endonuclease. {ECO:0000303|PubMed:12654995,
CC ECO:0000305|PubMed:9862476}.
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 -!- 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; AF027867; AAC97118.1; -; Genomic_DNA.
DR AlphaFoldDB; O31073; -.
DR SMR; O31073; -.
DR PRO; PR:O31073; -.
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; IPR001525; C5_MeTfrase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF00145; DNA_methylase; 1.
DR PRINTS; PR00105; C5METTRFRASE.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00675; dcm; 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..390
FT /note="Type II methyltransferase M.SacI"
FT /id="PRO_0000087909"
FT DOMAIN 5..371
FT /note="SAM-dependent MTase C5-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
FT ACT_SITE 96
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
SQ SEQUENCE 390 AA; 43293 MW; C7470D97BADFCE87 CRC64;
MNHELPVISL FSGAGGLDCA IESCAEPPLV QDGSGSPLRV AVATDYEQTA LDTLSANFPH
TKTLCGDIQT IPTAELLEAG GLKPGDPTLV IGGPPCTPFS KSGFWIEEKR NSADPNASLL
DEYVRVVRES KPEAFILENV QGLTYKTHQA QFDRLIAGLK DAGYNPTFRV LLAAEYGVPQ
LRRRVFVVGR RDGKAFHFPE TTHSGESERD RVIDHTKIPF TSLREALAGL PDVPEAGEVV
EGTYAELAAE VPPGQNYLWH TDRYGGRNEF KWRSRYWTFL LKADPDRPST TLQAQPGPWV
GPFHWENVKN ANGEERARRF RVAEMKRIMT FPDEFVFTGV KREVQRQIGN PVPVELGKVV
VRALMEQLGY LDSRGTTIPS QAGHEQLELI