ID   MTS1_STRAL              Reviewed;         587 AA.
AC   Q53609;
DT   08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Type II methyltransferase M.SalI {ECO:0000303|PubMed:12654995};
DE            Short=M.SalI {ECO:0000303|PubMed:7828868};
DE            EC=2.1.1.72;
DE   AltName: Full=Adenine-specific methyltransferase SalI;
DE   AltName: Full=Modification methylase SalI;
GN   Name=salIM {ECO:0000303|PubMed:7828868};
OS   Streptomyces albus G.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1962;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7828868; DOI=10.1016/0378-1119(94)90650-5;
RA   Rodicio M.R., Quinton-Jager T., Moran L.S., Slatko B.E., Wilson G.G.;
RT   "Organization and sequence of the SalI restriction-modification system.";
RL   Gene 151:167-172(1994).
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 gamma subtype methylase that recognizes the double-stranded
CC       sequence 5'-GTCGAC-3', methylates A-5 on both strands, and protects the
CC       DNA from cleavage by the SalI endonuclease.
CC       {ECO:0000303|PubMed:12654995}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyadenosine in DNA + S-adenosyl-L-methionine = an
CC         N(6)-methyl-2'-deoxyadenosine in DNA + H(+) + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:15197, Rhea:RHEA-COMP:12418, Rhea:RHEA-
CC         COMP:12419, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:90615, ChEBI:CHEBI:90616; EC=2.1.1.72;
CC   -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; U01232; AAA81887.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q53609; -.
DR   SMR; Q53609; -.
DR   REBASE; 3491; M.SalI.
DR   PRIDE; Q53609; -.
DR   PRO; PR:Q53609; -.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-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   Gene3D; 4.10.320.10; -; 1.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR036625; E3-bd_dom_sf.
DR   InterPro; IPR011639; RM_methylase_Eco57I-like.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF07669; Eco57I; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Methyltransferase; Restriction system;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..587
FT                   /note="Type II methyltransferase M.SalI"
FT                   /id="PRO_0000087979"
SQ   SEQUENCE   587 AA;  64975 MW;  B482F374397FF999 CRC64;
     MHSEAREAEA RRLLLQETLD AERTFLERNQ WGQFATPPSL AGEIMRYTID LHEETRINFL
     EPSCGSGSFF SALLRNLGDK KIEHAVGVEL DPRFSKAASD LWTGQGLRVI EGDFTSPSLV
     SGPVASLLVA NPPYVRHHHL GIDQKRDLVA RCADQLGIKP SGLSGLYLYF VLLSHRLLRA
     DAVSTWLIPS EFMDVNYGTA LKEYLATRVQ LVRIHQYDAA EVQFDDALVT SSVVVFRNSP
     PRPGHTAEFS FGGTLSEPKV THQIPSAALT PEAKWSRYVT GVMPADINLK QTGPKLSDFF
     KIRRGLATGS NAFFIIPRSE AERLGIKRNF LRPILPSPRK LKGDAITADA SGWPDIPEQL
     ALLDCPLPIE DLLLENPALA AYLSTADEKI RGGYLVSKRS PWYKQEQREP APILLTYMGR
     GKDDQHPLRF IRNDSDAVAT NMYLMLYPTA LLQRYLAGDP ERIKQVHKAL LAITAADLRG
     GGRVYGGGLH KMEPKELAAL PADGIATLDP VLREDISMVS VPPRKRTGRP QMPGPSASEV
     RAWARANGVC VPDRGRLRPE VWDAWRQAHA GEASPLNIDA GDQVALW