ID C6SD56_NEIME Unreviewed; 512 AA.
AC C6SD56;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 40.
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=hsdM7 {ECO:0000313|EMBL:CBA06718.1};
GN ORFNames=NME_1224 {ECO:0000313|EMBL:CBA06718.1};
OS Neisseria meningitidis alpha153.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=663926 {ECO:0000313|EMBL:CBA06718.1};
RN [1] {ECO:0000313|EMBL:CBA06718.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Alpha153 {ECO:0000313|EMBL:CBA06718.1};
RX PubMed=18305155; DOI=10.1073/pnas.0800151105;
RA Schoen C., Blom J., Claus H., Schramm-Glueck A., Brandt P., Mueller T.,
RA Goesmann A., Joseph B., Konietzny S., Kurzai O., Schmitt C., Friedrich T.,
RA Linke B., Vogel U., Frosch M.;
RT "Whole-genome comparison of disease and carriage strains provides insights
RT into virulence evolution in Neisseria meningitidis.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:3473-3478(2008).
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};
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DR EMBL; AM889137; CBA06718.1; -; Genomic_DNA.
DR AlphaFoldDB; C6SD56; -.
DR REBASE; 23152; M.NmeA153ORF1224P.
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:CBA06718.1};
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:CBA06718.1}.
FT DOMAIN 7..154
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 169..478
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
FT COILED 482..509
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 512 AA; 57032 MW; 01050B256848E63B CRC64;
MQQRAQLHRQ IWKIADEVRG AVDGWDFKQY VLGTLFYRFI SENFTDYMQA GDSSIDYAAM
PDSIITPEIK DDAVKVKGYF IYPGQLFCNI AAEAHQNEEL NTKLKEIFTA IESSASGYPS
EQDIKGLFDD FDTTSSRLGS TVADKNKRLA AVLKGVAELD FGSFEDHHID LFGDAYEYLI
SNYAANAGKS GGEFFTPQSV SVSKLIARLA VHGQEKVNKI YDPACGSGSL LLQAKKQFDE
HIIEEGFFGQ EINHTTYNLA RMNMFLHNVN YNKFHIELGD TLTNPKLKDS KPFDAVVSNP
PYSINWIGSG DPTLINDDRF APAGVLAPKS KADFAFILHA LNYLSGRGRA AIVSFPGIFY
RGGAEQKIRQ YLVEGNYVET VIALAPNLFY GTGIAVNILV LSKHKDNTDI QFIDAGGFFK
KETNNNVLTE EHIAEIVKLF ADKADVPHIA QNAAQQTVKD NGYNLAVSSY VEPEDTREII
DIKQLNAEIS ETVAKIERLR REIDEVIAEI EA
//
