ID B5EWN8_SALA4 Unreviewed; 652 AA.
AC B5EWN8;
DT 14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2008, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
GN OrderedLocusNames=SeAg_B0392 {ECO:0000313|EMBL:ACH51680.1};
OS Salmonella agona (strain SL483).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=454166 {ECO:0000313|EMBL:ACH51680.1, ECO:0000313|Proteomes:UP000008819};
RN [1] {ECO:0000313|EMBL:ACH51680.1, ECO:0000313|Proteomes:UP000008819}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SL483 {ECO:0000313|EMBL:ACH51680.1,
RC ECO:0000313|Proteomes:UP000008819};
RX PubMed=21602358; DOI=10.1128/JB.00297-11;
RA Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA Leclerc J.E., Ravel J., Cebula T.A.;
RT "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT CRISPR-mediated adaptive sublineage evolution.";
RL J. Bacteriol. 193:3556-3568(2011).
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 -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC {ECO:0000256|ARBA:ARBA00006594}.
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DR EMBL; CP001138; ACH51680.1; -; Genomic_DNA.
DR RefSeq; WP_000910350.1; NC_011149.1.
DR AlphaFoldDB; B5EWN8; -.
DR REBASE; 18780; M.Sen483II.
DR KEGG; sea:SeAg_B0392; -.
DR HOGENOM; CLU_020164_2_0_6; -.
DR Proteomes; UP000008819; Chromosome.
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 Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR002941; DNA_methylase_N4/N6.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR002295; N4/N6-MTase_EcoPI_Mod-like.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR041405; T3RM_EcoP15I_C.
DR PANTHER; PTHR13370; RNA METHYLASE-RELATED; 1.
DR PANTHER; PTHR13370:SF16; TYPE III RESTRICTION-MODIFICATION ENZYME STYLTI MOD SUBUNIT; 1.
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; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:ACH51680.1};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ACH51680.1}.
FT DOMAIN 129..448
FT /note="DNA methylase N-4/N-6"
FT /evidence="ECO:0000259|Pfam:PF01555"
FT DOMAIN 553..648
FT /note="Type III R-M EcoP15I C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18273"
SQ SEQUENCE 652 AA; 73321 MW; B0BCEA3911080430 CRC64;
MLKDNQKHNE SVAPNSAFLS ELQRALPEFF IADRYNEQGE LIAKGGFDLA KFERALKARN
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
//
