ID D2A8W4_SHIF2 Unreviewed; 294 AA.
AC D2A8W4;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Methyltransferase {ECO:0000256|RuleBase:RU362026};
DE EC=2.1.1.- {ECO:0000256|RuleBase:RU362026};
GN Name=yhdJ {ECO:0000313|EMBL:ADA75623.1};
GN OrderedLocusNames=SFxv_3613 {ECO:0000313|EMBL:ADA75623.1};
OS Shigella flexneri serotype X (strain 2002017).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=591020 {ECO:0000313|EMBL:ADA75623.1, ECO:0000313|Proteomes:UP000001884};
RN [1] {ECO:0000313|EMBL:ADA75623.1, ECO:0000313|Proteomes:UP000001884}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2002017 {ECO:0000313|EMBL:ADA75623.1,
RC ECO:0000313|Proteomes:UP000001884};
RX PubMed=19955273; DOI=10.1128/JCM.00614-09;
RA Ye C., Lan R., Xia S., Zhang J., Sun Q., Zhang S., Jing H., Wang L., Li Z.,
RA Zhou Z., Zhao A., Cui Z., Cao J., Jin D., Huang L., Wang Y., Luo X.,
RA Bai X., Wang Y., Wang P., Xu Q., Xu J.;
RT "Emergence of a new multidrug-resistant serotype X variant in an epidemic
RT clone of Shigella flexneri.";
RL J. Clin. Microbiol. 48:419-426(2010).
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, ECO:0000256|RuleBase:RU362026}.
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DR EMBL; CP001383; ADA75623.1; -; Genomic_DNA.
DR RefSeq; WP_001258883.1; NC_017328.1.
DR AlphaFoldDB; D2A8W4; -.
DR REBASE; 23273; M.SflFORF3613P.
DR KEGG; sfe:SFxv_3613; -.
DR PATRIC; fig|591020.3.peg.3890; -.
DR HOGENOM; CLU_024927_5_2_6; -.
DR Proteomes; UP000001884; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro.
DR GO; GO:0006306; P:DNA methylation; IEA:InterPro.
DR CDD; cd02440; AdoMet_MTases; 1.
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; IPR001091; RM_Methyltransferase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR13370:SF32; DNA ADENINE METHYLTRANSFERASE YHDJ; 1.
DR PANTHER; PTHR13370; RNA METHYLASE-RELATED; 1.
DR Pfam; PF01555; N6_N4_Mtase; 1.
DR PRINTS; PR00508; S21N4MTFRASE.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:ADA75623.1};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ADA75623.1}.
FT DOMAIN 34..251
FT /note="DNA methylase N-4/N-6"
FT /evidence="ECO:0000259|Pfam:PF01555"
FT REGION 274..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 294 AA; 33431 MW; AA9F369A4804A0F0 CRC64;
MRTGCEPTRF GNEAKTIIHG DAFAELKKLP TESVDLLFAD PPYNIGKNFD GLIEAWKEDL
FIDWLFEVIA ECHRVLKKQG SMYIMNSTEN MPFIDLQCRK LFTIKSRIVW SYDSSGVQAK
KHYGSMYEPI LMMVKDAKNY TFNGDAILVE AKTGSQRALI DYRKNPPQPY NHQKVPGNVW
DFPRVRYLMD EYENHPTQKP KALLKRIILA SSNPGDIVLD PFAGSFTTGA VAIASGRKFI
GIEINSEYIK MGLRRLDVAS HYSAEELAKV KKRKTGNLSK RSRLSEVDPD LIAK
//
