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Database: UniProt
Entry: F3CC70_PSESG
LinkDB: F3CC70_PSESG
Original site: F3CC70_PSESG 
ID   F3CC70_PSESG            Unreviewed;       495 AA.
AC   F3CC70;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE            EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
GN   ORFNames=Pgy4_27890 {ECO:0000313|EMBL:EGH16862.1};
OS   Pseudomonas savastanoi pv. glycinea str. race 4.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=875330 {ECO:0000313|EMBL:EGH16862.1, ECO:0000313|Proteomes:UP000005466};
RN   [1] {ECO:0000313|EMBL:EGH16862.1, ECO:0000313|Proteomes:UP000005466}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=race 4 {ECO:0000313|Proteomes:UP000005466};
RX   PubMed=21799664; DOI=10.1371/journal.ppat.1002132;
RA   Baltrus D.A., Nishimura M.T., Romanchuk A., Chang J.H., Mukhtar M.S.,
RA   Cherkis K., Roach J., Grant S.R., Jones C.D., Dangl J.L.;
RT   "Dynamic evolution of pathogenicity revealed by sequencing and comparative
RT   genomics of 19 Pseudomonas syringae isolates.";
RL   PLoS Pathog. 7:E1002132-e1002132(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}.
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:EGH16862.1}.
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DR   EMBL; ADWY01001380; EGH16862.1; -; Genomic_DNA.
DR   AlphaFoldDB; F3CC70; -.
DR   PATRIC; fig|875330.6.peg.4668; -.
DR   HOGENOM; CLU_020164_1_1_6; -.
DR   BioCyc; PSYR875330:G11XH-5325-MONOMER; -.
DR   Proteomes; UP000005466; 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   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   Pfam; PF01555; N6_N4_Mtase; 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:EGH16862.1};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          65..405
FT                   /note="DNA methylase N-4/N-6"
FT                   /evidence="ECO:0000259|Pfam:PF01555"
SQ   SEQUENCE   495 AA;  55866 MW;  7DB0B470DDF134B6 CRC64;
     MPTLHWIGKN KVVNHHHEVP FRVLNHQCRY RAPEGAPPNS TDNRIIHGDN LEALKSLLPE
     FEGQVDCIYI DPPYNTGNEG WAYNDNVNDP KLKKWLGEVV GKEGEDLSRH DKWLCMMYPR
     IKLLHKLLSN TGVIFVSLDE NEFCRMRLVL EEIFGESNFL AQIIVQSNKR GQTYKQIAKT
     HEYLICFGKT KDAALGELET NGENLPEVDS FGKYSSRELR NRNPKFGRFN RPNLFYPIYA
     HLSNPDENGL FPVSAIDSGE GVSILPYNSE GIESCWRWGK EKLARDNVSN NTQMLFAKQT
     RDGGWRVFEK YRKGSVKAKS IWFDTKHISE QGTTALNRLG LGEQFQFPKP VALIEDCISL
     ATEDDALILD SFAGSGTTAE AVLNLNAKNG GNRRFILIET LEYAETLTAE RVRRVMAGYE
     TGPKLTAGLG GQFDFFTVGE PLFLDPDTLN ETLDIAVIRD YVAYAEGVPV ADRINADNPF
     SPFLLGLNSD TAWIF
//
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