ID A9LZD8_NEIM0 Unreviewed; 533 AA.
AC A9LZD8;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
GN OrderedLocusNames=NMCC_1140 {ECO:0000313|EMBL:ABX73314.1};
OS Neisseria meningitidis serogroup C (strain 053442).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=374833 {ECO:0000313|EMBL:ABX73314.1, ECO:0000313|Proteomes:UP000001177};
RN [1] {ECO:0000313|EMBL:ABX73314.1, ECO:0000313|Proteomes:UP000001177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=053442 {ECO:0000313|EMBL:ABX73314.1,
RC ECO:0000313|Proteomes:UP000001177};
RX PubMed=18031983; DOI=10.1016/j.ygeno.2007.10.004;
RA Peng J., Yang L., Yang F., Yang J., Yan Y., Nie H., Zhang X., Xiong Z.,
RA Jiang Y., Cheng F., Xu X., Chen S., Sun L., Li W., Shen Y., Shao Z.,
RA Liang X., Xu J., Jin Q.;
RT "Characterization of ST-4821 complex, a unique Neisseria meningitidis
RT clone.";
RL Genomics 91:78-87(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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000381; ABX73314.1; -; Genomic_DNA.
DR RefSeq; WP_012221687.1; NC_010120.1.
DR AlphaFoldDB; A9LZD8; -.
DR SMR; A9LZD8; -.
DR REBASE; 16787; M.Nme53442ORF1140P.
DR KEGG; nmn:NMCC_1140; -.
DR HOGENOM; CLU_037306_0_0_4; -.
DR Proteomes; UP000001177; 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:0000256|ARBA:ARBA00022603};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 166..485
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 533 AA; 60177 MW; FADD94A124955F49 CRC64;
MTEQHFTEQT KSLIDSLKTI CANYGLGNDG NEFKIISQAF LYKFLNDKYD FEVKQIRKEN
PDEPIEFINM DIEGKTAVLK PEHSIKYLSE RQNGADFAKL FDDTLTDIAA HNAELFSVKT
EGGAKIVLFE RISQYITDEG RRDDFCRALI SKLAGFSFEA IFAQKFDFFA TIFEYLIKDY
NSNSGGKYAE YYTPHAVARI MADILVPEEV RGQIRSVDVY DPSAGSGTLL MNVAHAIGED
KCMIYTQDIS QKSSNLLRLN LILNNLVHSL NNVVQGNTIL SPAHKDASGR LKKFDFIVSN
PPFKLDFSDF RDQLEGEENR ERFFAGIPKI KAKDTDKMEI YQLFIQHILF SLKENGKAAI
VLPTGFITAQ SGIDKKIREH LVENKMLAGV VSMPSNIFAT TGTNVSILFI DKANKDKVVL
IDASGLGEKI KDGKNQKTVL SREEEQKICN TFTHKQAVED FSVVVGYDEI KAKNYSLSAG
QYFEVKIDYV DISAEEFKQR MAGFSADLDK LFAESAKLEK EIKDRLAMLK FNS
//
