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Database: UniProt
Entry: E5Q8U0_GEOSE
LinkDB: E5Q8U0_GEOSE
Original site: E5Q8U0_GEOSE 
ID   E5Q8U0_GEOSE            Unreviewed;       389 AA.
AC   E5Q8U0;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=site-specific DNA-methyltransferase (cytosine-N(4)-specific) {ECO:0000256|ARBA:ARBA00012185};
DE            EC=2.1.1.113 {ECO:0000256|ARBA:ARBA00012185};
GN   Name=bsrIM2 {ECO:0000313|EMBL:ADR72995.1};
OS   Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=1422 {ECO:0000313|EMBL:ADR72995.1};
RN   [1] {ECO:0000313|EMBL:ADR72995.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NEBM140 {ECO:0000313|EMBL:ADR72995.1};
RA   Lunnen K.D., Wilson G.G.;
RT   "BsrI restriction-modification system genes.";
RL   Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00001893};
CC   -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family. N(4)
CC       subfamily. {ECO:0000256|ARBA:ARBA00010203}.
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DR   EMBL; HQ636105; ADR72995.1; -; Genomic_DNA.
DR   AlphaFoldDB; E5Q8U0; -.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
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; Vaccinia Virus protein VP39; 2.
DR   InterPro; IPR002941; DNA_methylase_N4/N6.
DR   InterPro; IPR017985; MeTrfase_CN4_CS.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF01555; N6_N4_Mtase; 2.
DR   PRINTS; PR00507; N12N6MTFRASE.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS00093; N4_MTASE; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          22..81
FT                   /note="DNA methylase N-4/N-6"
FT                   /evidence="ECO:0000259|Pfam:PF01555"
FT   DOMAIN          239..348
FT                   /note="DNA methylase N-4/N-6"
FT                   /evidence="ECO:0000259|Pfam:PF01555"
SQ   SEQUENCE   389 AA;  45556 MW;  6E3296F9B5EED359 CRC64;
     MVDITAIQNL KIFEEDYSNT TDLNHGIHSY PAKFPPQIPG KLLDKFAKDN YVVLDPFCGS
     GTTLVEASLR NLDSVGNDIN PIALLISTVK TTKYFDTDFE ELEKIIYDLK DDYMNNKNNL
     KSTIDFPNKD HWFQKNVQKE IELILKHINL CSNEKYRNLL KVVLSEIIVT VSNQESDTRY
     AAIDKNIPDG KTIELFEKRY FAIKDKILSF SQMVKDFEYE TKIISNDARN LIDIRSESID
     IIITSPPYAN TYDYYLYHKH RMNWLGYNFK ETQNIEIGSR NEYSSKKQKP EKWKHDLMLV
     LQEMYRVMKK DRLCFIIIGD SVINKEHIKI NDVIREIATK IGFEYLNEES VPLSKNSRKF
     NKKFGTDQTK LEHLISLYKP KLTIIMKAH
//
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