ID E1IY25_ECOLX Unreviewed; 520 AA.
AC E1IY25;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
GN Name=hsdM {ECO:0000313|EMBL:EFO55753.1};
GN ORFNames=HMPREF9348_05125 {ECO:0000313|EMBL:EFO55753.1};
OS Escherichia coli MS 145-7.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=679204 {ECO:0000313|EMBL:EFO55753.1, ECO:0000313|Proteomes:UP000003691};
RN [1] {ECO:0000313|EMBL:EFO55753.1, ECO:0000313|Proteomes:UP000003691}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS 145-7 {ECO:0000313|EMBL:EFO55753.1,
RC ECO:0000313|Proteomes:UP000003691};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
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 Evidence={ECO:0000256|ARBA:ARBA00001279};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFO55753.1}.
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DR EMBL; ADWS01000048; EFO55753.1; -; Genomic_DNA.
DR AlphaFoldDB; E1IY25; -.
DR Proteomes; UP000003691; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro.
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 CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 1.20.1260.30; -; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR022749; D12N6_MeTrfase_N.
DR InterPro; IPR003356; DNA_methylase_A-5.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR004546; Restrct_endonuc_T1M.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR038333; T1MK-like_N_sf.
DR NCBIfam; TIGR00497; hsdM; 1.
DR PANTHER; PTHR42933:SF1; SITE-SPECIFIC DNA-METHYLTRANSFERASE (ADENINE-SPECIFIC); 1.
DR PANTHER; PTHR42933; SLR6095 PROTEIN; 1.
DR Pfam; PF12161; HsdM_N; 1.
DR Pfam; PF02384; N6_Mtase; 1.
DR PRINTS; PR00507; N12N6MTFRASE.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:EFO55753.1};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EFO55753.1}.
FT DOMAIN 12..159
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 173..481
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
FT COILED 485..519
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 520 AA; 57942 MW; 77A01EC1690EB257 CRC64;
MKMTSIQQRA ELHRQIWQIA NDVRGSVDGW DFKQYVLGAL FYRFISENFS SYIEAGDDSI
CYAKLDDSVI TDDIKDDAIK TKGYFIYPSQ LFCNVAAKAN TNDRLNADLN SIFVAIESSA
YGYPSEADIK GLFADFDTTS NRLGNTVKDK NARLAAVLKG VEGLKLGDFN EHQIDLFGDA
YEFLISNYAA NAGKSGGEFF TPQHVSKLIA QLAMHGQTHV NKIYDPAAGS GSLLLQAKKQ
FDDHIIEEGF FGQEINHTTY NLARMNMFLH NINYDKFDIK LGNTLTEPHF RDEKPFDAIV
SNPPYSVKWI GSDDPTLIND ERFAPAGVLA PKSKADFAFV LHALNYLSAK GRAAIVCFPG
IFYRGGAEQK IRQYLVDNNY VETVISLAPN LFFGTTIAVN ILVLSKHKTD TKVQFIDASE
LFKKETNNNI LTDAHIEQIM QVFASKEDVA HLAKSVAFET VVANDYNLSV SSYVEAKDTR
EIIDIAELNA ELKTTVSKID QLRKDIDAIV AEIEGSEVQA
//
