ID Q5F8R1_NEIG1 Unreviewed; 533 AA.
AC Q5F8R1;
DT 15-MAR-2005, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2005, sequence version 1.
DT 24-JAN-2024, entry version 85.
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=NGO_0702 {ECO:0000313|EMBL:AAW89426.1};
OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89426.1, ECO:0000313|Proteomes:UP000000535};
RN [1] {ECO:0000313|Proteomes:UP000000535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535};
RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F.,
RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C.,
RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S.,
RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.;
RT "The complete genome sequence of Neisseria gonorrhoeae.";
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
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; AE004969; AAW89426.1; -; Genomic_DNA.
DR RefSeq; WP_003688773.1; NC_002946.2.
DR RefSeq; YP_207838.1; NC_002946.2.
DR AlphaFoldDB; Q5F8R1; -.
DR STRING; 242231.NGO_0702; -.
DR REBASE; 10860; M.NgoAXVII.
DR KEGG; ngo:NGO_0702; -.
DR PATRIC; fig|242231.10.peg.829; -.
DR HOGENOM; CLU_037306_0_0_4; -.
DR OMA; FFAPIFE; -.
DR Proteomes; UP000000535; 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; 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 PANTHER; PTHR42933:SF1; SITE-SPECIFIC DNA-METHYLTRANSFERASE (ADENINE-SPECIFIC); 1.
DR PANTHER; PTHR42933; SLR6095 PROTEIN; 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 Methyltransferase {ECO:0000313|EMBL:AAW89426.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000535};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW Transferase {ECO:0000313|EMBL:AAW89426.1}.
FT DOMAIN 166..485
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 533 AA; 60023 MW; 298C15FE16322A85 CRC64;
MTEQHFTEQI KSLIDSLKTI CANYGLGNDG NEFKIISQAF LYKFLNDKYD FEVKKIRKEK
PDEPIEFVNM DIDGKTAVLK PEHSIKYLSE RQNGADFAKL FDDTLTDIAA HNAELFSVKT
EGGAKIVLFE RISQYITDEG RRDDFCRALI SKLAGFSFEA IFAQKFDFFA TIFEYLIKDY
NSNSGGKYAE YYTPHAVARI MADILVPEDV RGQIRSVDVY DPSAGSGTLL MNVAHAIGED
KCMIYTQDIS QKSSNLLRLN LILNNLVHSL NNVVQGNTIL SPAHKDASGC LKKFDFIVSN
PPFKLDFSDF RDRLESDENH ERFFAGIPKI KPTKKEKMEI YQLFIQHILF SLKENGKAAI
VLPTGFITAK SGIDKKIREY LVENKMLAGV VSMPSNIFAT TGTNVSILFI DKTNKDKVVL
IDASGLGEKI KDGKNQKTVL SCEEEQKICN TFTNKQAVED FSVVVGYDEI KAKNHSLSAG
QYFEVKIDYV DISADEFAQK IAGFSADLDK LFAESAELEK EIKDRLAMLK FNS
//