ID J0IR17_HELPX Unreviewed; 329 AA.
AC J0IR17;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=nlaIIIM {ECO:0000313|EMBL:EJB27910.1};
GN ORFNames=HPNQ4200_1127 {ECO:0000313|EMBL:EJB27910.1};
OS Helicobacter pylori NQ4200.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=992024 {ECO:0000313|EMBL:EJB27910.1, ECO:0000313|Proteomes:UP000003358};
RN [1] {ECO:0000313|EMBL:EJB27910.1, ECO:0000313|Proteomes:UP000003358}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NQ4200 {ECO:0000313|EMBL:EJB27910.1,
RC ECO:0000313|Proteomes:UP000003358};
RX PubMed=23661595; DOI=10.1111/2049-632X.12045;
RA Blanchard T.G., Czinn S.J., Correa P., Nakazawa T., Keelan M.,
RA Morningstar L., Santana-Cruz I., Maroo A., McCracken C., Shefchek K.,
RA Daugherty S., Song Y., Fraser C.M., Fricke W.F.;
RT "Genome sequences of 65 Helicobacter pylori strains isolated from
RT asymptomatic individuals and patients with gastric cancer, peptic ulcer
RT disease, or gastritis.";
RL Pathog. Dis. 68:39-43(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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EJB27910.1}.
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DR EMBL; AKNS01000009; EJB27910.1; -; Genomic_DNA.
DR RefSeq; WP_001106463.1; NZ_AKNS01000009.1.
DR AlphaFoldDB; J0IR17; -.
DR PATRIC; fig|992024.3.peg.1084; -.
DR Proteomes; UP000003358; Unassembled WGS sequence.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 2.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
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.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000313|EMBL:EJB27910.1};
KW Transferase {ECO:0000313|EMBL:EJB27910.1}.
SQ SEQUENCE 329 AA; 37123 MW; 3D797D5A1D73BEBF CRC64;
MNYIGSKYKL IPFIKENIHA VAGHDLSGAI FCDLFAGTGI VGRAFKKAVN KVISNDLEYY
SFVLNQNYIG NIQEIPNQEE LINGLNSVAL KKGFIHSHYS LGGSSRQYFS ETNAQKIDAM
RLKIEELKLS QNIDSHAYYF LLASLLESAD KVANTASVYG AFLKRLKKSA QKELILKGAH
FDVSLSANEV YQQDSNDLIG KISGDILYLD PPYNARQYGA NYHLLNTIAA YTPFTPKGKT
GLPNYQKSSF CSRSQILNAF ENLIKKARFK YIFLSYNNEG LMSETEIKNI LKKYGAYSLV
TKTYMRFKAD NKRTHKAAHT KECLHILIK
//