ID Q5GX54_XANOR Unreviewed; 514 AA.
AC Q5GX54;
DT 01-MAR-2005, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2005, sequence version 1.
DT 27-MAR-2024, entry version 93.
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-2 {ECO:0000313|EMBL:AAW76717.1};
GN OrderedLocusNames=XOO3463 {ECO:0000313|EMBL:AAW76717.1};
OS Xanthomonas oryzae pv. oryzae (strain KACC10331 / KXO85).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=291331 {ECO:0000313|EMBL:AAW76717.1, ECO:0000313|Proteomes:UP000006735};
RN [1] {ECO:0000313|EMBL:AAW76717.1, ECO:0000313|Proteomes:UP000006735}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KACC10331 / KXO85 {ECO:0000313|Proteomes:UP000006735};
RX PubMed=15673718; DOI=10.1093/nar/gki206;
RA Lee B.M., Park Y.J., Park D.S., Kang H.W., Kim J.G., Song E.S., Park I.C.,
RA Yoon U.H., Hahn J.H., Koo B.S., Lee G.B., Kim H., Park H.S., Yoon K.O.,
RA Kim J.H., Jung C.H., Koh N.H., Seo J.S., Go S.J.;
RT "The genome sequence of Xanthomonas oryzae pathovar oryzae KACC10331, the
RT bacterial blight pathogen of rice.";
RL Nucleic Acids Res. 33:577-586(2005).
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; AE013598; AAW76717.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5GX54; -.
DR STRING; 291331.XOO3463; -.
DR REBASE; 10820; M.XorKORF3462P.
DR KEGG; xoo:XOO3463; -.
DR PATRIC; fig|291331.8.peg.3832; -.
DR HOGENOM; CLU_018284_2_0_6; -.
DR Proteomes; UP000006735; 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 GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1260.30; -; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR003356; DNA_methylase_A-5.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR038333; T1MK-like_N_sf.
DR PANTHER; PTHR42933; SLR6095 PROTEIN; 1.
DR PANTHER; PTHR42933:SF4; TYPE I RESTRICTION ENZYME ECOKI METHYLASE SUBUNIT; 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 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Reference proteome {ECO:0000313|Proteomes:UP000006735};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 124..418
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 514 AA; 56139 MW; 1D7FBD1935398764 CRC64;
MTHNDIVQKL WNLCDVLRDD GINYSDYVTE LVLLLFVKME YEQVQNNPNF EHKLPAGSRW
PDLNGKSGLN LLNHYRQMLL DLGKSSDPMI AAIYADAQTR LKEPRHLETL VTALDGLDWF
SARQDGLGDL YEGLLQKNAN ETKSGAGQYF TPRALIDSII HCIKPQLGDV IQDPAAGTAG
FLIAADAYIK AQHDALYGPD VTAKKRSFQR EKAFVGMELV PGTRRLALMN CLLHGMHGEG
AGPIRLGNSL GTAGRDLPPA NIILSNPPFG TAKGGGGPTR DDLTYKTSNK QLAFLQHIYR
GLTPGGRAAV VLPDNVLFEA GLGTEIRRDL MDKCTLHTLL RLPTGIFYAQ GVKTNVLFFQ
KGTAANPRQD TGCTQATWVY DLRSNMPNFG KRTPFGPTHL KPFEEAYGTD PNGASPRTDA
GEQGRFRCFT RAQIAERGDS LDISWLKDAD SVDADSLPAP EVLAAEAMAE LSEALRELDA
LMQALGAGDE ALEQKRLLAE VMGLEVTSGE VDGE
//