(data stored in ACNUC7421 zone)

SWISSPROT: T3MO_SALTY

ID   T3MO_SALTY              Reviewed;         652 AA.
AC   P40814;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2002, sequence version 2.
DT   11-DEC-2019, entry version 119.
DE   RecName: Full=Type III restriction-modification system StyLTI enzyme mod;
DE            Short=M.StyLTI;
DE            EC=2.1.1.72;
DE   AltName: Full=StyLTI methyltransferase;
GN   Name=mod; OrderedLocusNames=STM0357;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=LT7;
RX   PubMed=8387444; DOI=10.1016/0378-1119(93)90623-b;
RA   Dartois V., de Backer O., Colson C.;
RT   "Sequence of the Salmonella typhimurium StyLT1 restriction-modification
RT   genes: homologies with EcoP1 and EcoP15 type-III R-M systems and presence
RT   of helicase domains.";
RL   Gene 127:105-110(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
CC   -!- FUNCTION: Binds the system-specific DNA recognition site 5'-CAGAG-3'.
CC       Necessary for restriction and for methylation of A-4.
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   -!- SUBUNIT: Contains two different subunits: res and mod. Mod is a
CC       homotetramer (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC       {ECO:0000305}.
DR   EMBL; M90544; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AE006468; AAL19311.1; -; Genomic_DNA.
DR   PIR; JN0657; JN0657.
DR   RefSeq; NP_459352.1; NC_003197.2.
DR   RefSeq; WP_000910371.1; NC_003197.2.
DR   SMR; P40814; -.
DR   REBASE; 203812; M.Keu1446ORF2697P.
DR   REBASE; 231846; M.Sen4024ORF3354P.
DR   REBASE; 233833; M.Sen4839ORF3406P.
DR   REBASE; 3515; M.StyLTI.
DR   PaxDb; P40814; -.
DR   PRIDE; P40814; -.
DR   EnsemblBacteria; AAL19311; AAL19311; STM0357.
DR   GeneID; 1251876; -.
DR   KEGG; stm:STM0357; -.
DR   PATRIC; fig|99287.12.peg.378; -.
DR   eggNOG; ENOG4107QMH; Bacteria.
DR   eggNOG; COG2189; LUCA.
DR   HOGENOM; HOG000253523; -.
DR   KO; K07316; -.
DR   OMA; DDRKFTP; -.
DR   BioCyc; SENT99287:STM0357-MONOMER; -.
DR   PRO; PR:P40814; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008168; F:methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IBA:GO_Central.
DR   GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR   InterPro; IPR002295; D21N6_MeTrfase.
DR   InterPro; IPR002941; DNA_methylase_N4/N6.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   InterPro; IPR041405; T3RM_EcoP15I_C.
DR   Pfam; PF01555; N6_N4_Mtase; 1.
DR   Pfam; PF18273; T3RM_EcoP15I_C; 1.
DR   PIRSF; PIRSF015855; TypeIII_Mtase_mKpnI; 1.
DR   PRINTS; PR00506; D21N6MTFRASE.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; P40814.
DR   SWISS-2DPAGE; P40814.
KW   DNA-binding; Methyltransferase; Reference proteome; Restriction system;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..652
FT                   /note="Type III restriction-modification system StyLTI
FT                   enzyme mod"
FT                   /id="PRO_0000088032"
FT   REGION          135..138
FT                   /note="Binding of S-adenosyl methionine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        55
FT                   /note="Missing (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        126
FT                   /note="A -> S (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        587..588
FT                   /note="DN -> ND (in Ref. 1)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   652 AA;  73336 MW;  385DE4851545C84E CRC64;
     MLKDNQKHNE SVAPNSAFLS ELQRALPEFF TADRYNEQGE LIAKGGFDLA RFERALKARN
     IDELTSGYQI DFIGKDYAKK QAGEKSVTVI VPDVEHNTLA ENKNSHNLFL TGDNLDVLRH
     LQNNYADTVD MIYIDPPYNT GSDGFVYPDH FEYSDRALQD MFGLNDTELA RLKSIQGKST
     HSAWLSFMYP RLFLARKLLK DTGFIFISID DNEYANLKLM MDEIFGEGGF VTNVMWKRKK
     EISNDSDNVS IQGEYILVYA KTGQGALRLE PLSKEYIQKS YKEPTEQFPE GKWRPVPLTV
     SKGLSGGGYT YKITTPNGTV HERLWAYPEA SYQKLVADNL VYFGKDNGGI PQRVMYAHHS
     KGQPTTNYWD NVASNKEGKK EILDLFGDNV FDTPKPTALL KKIIKLAIDK DGVVLDFFAG
     SGTTAHAVMA LNEEDGGQRT FILCTIDQAL SNNTIAKKAG YNTIDEISRE RITRVAAKIR
     ANNPATNSDL GFKHYRFATP TQQTLDDLDS FDIATGHFIN TSGQLAAFTE SGFTDMINPF
     SARGLGVPGG ASGEETLLTT WLVADGYKMD IDVQTVDFSG YCARYVDNTR LYLIDERWGT
     EQTRDLLNHI GTHQLPVQTI VIYGYSFDLE SIRELEIGLK QLDQKVNLVK RY
//

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