ID M5D9U0_NEIME Unreviewed; 115 AA.
AC M5D9U0;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
DE Flags: Fragment;
GN Name=NEIS0061 {ECO:0000313|EMBL:CCP19746.1};
OS Neisseria meningitidis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=487 {ECO:0000313|EMBL:CCP19746.1};
RN [1] {ECO:0000313|EMBL:CCP19746.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ST-5594 {ECO:0000313|EMBL:CCP19746.1};
RA Aslett M.;
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CCP19746.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ST-5594 {ECO:0000313|EMBL:CCP19746.1};
RX PubMed=23628376; DOI=10.3201/eid1904.111799;
RA Harrison O.B., Claus H., Jiang Y., Bennett J.S., Bratcher H.B.,
RA Jolley K.A., Corton C., Care R., Poolman J.T., Zollinger W.L.D.,
RA Frasch C.E., Stephens D.S., Feavers I., Frosch M., Parkhill J., Vogel U.,
RA Quail M.A., Bentley S.D., Maiden M.C.J.;
RT "Description and Nomenclature of Neisseria meningitidis Capsule Locus.";
RL Emerg. Infect. Dis. 19:566-573(2013).
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; HF562984; CCP19746.1; -; Genomic_DNA.
DR AlphaFoldDB; M5D9U0; -.
DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:InterPro.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR012327; MeTrfase_D12.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF02086; MethyltransfD12; 1.
DR PRINTS; PR00505; D12N6MTFRASE.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000313|EMBL:CCP19746.1};
KW Transferase {ECO:0000313|EMBL:CCP19746.1}.
FT NON_TER 115
FT /evidence="ECO:0000313|EMBL:CCP19746.1"
SQ SEQUENCE 115 AA; 13233 MW; 40CFE6A5D24A069B CRC64;
MNKKYPKINY IGNKEKIVSW ICDQLPSDVD TIADVFSGGC SFAYEAKKRG YRVITNDILA
INYQIALALI ENNHETLNDD DVAMIFSGNP HAGFMSQHYA EKFYFYDECQ QLDLY
//
