ID J0N3E8_HELPX Unreviewed; 329 AA.
AC J0N3E8;
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:EJB81040.1};
GN ORFNames=HPHPH6_1419 {ECO:0000313|EMBL:EJB81040.1};
OS Helicobacter pylori Hp H-6.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=992061 {ECO:0000313|EMBL:EJB81040.1, ECO:0000313|Proteomes:UP000004177};
RN [1] {ECO:0000313|EMBL:EJB81040.1, ECO:0000313|Proteomes:UP000004177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hp H-6 {ECO:0000313|EMBL:EJB81040.1,
RC ECO:0000313|Proteomes:UP000004177};
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:EJB81040.1}.
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DR EMBL; AKOZ01000006; EJB81040.1; -; Genomic_DNA.
DR AlphaFoldDB; J0N3E8; -.
DR PATRIC; fig|992061.3.peg.1393; -.
DR Proteomes; UP000004177; 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; 1.10.1020.10; Adenine-specific Methyltransferase, Domain 2; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR023095; Ade_MeTrfase_dom_2.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR012327; MeTrfase_D12.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR30481; DNA ADENINE METHYLASE; 1.
DR PANTHER; PTHR30481:SF3; DNA ADENINE METHYLASE; 1.
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:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:EJB81040.1};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EJB81040.1}.
SQ SEQUENCE 329 AA; 37266 MW; 6D6BFA51C876A601 CRC64;
MNYIGSKYKL IPFIKENIHA VAGNNLSGAI FCDLFAGTGI VGRTFKKIVH KIISNDLEYY
SFVLNQNYIG NIQEIPNKEE LIDEINSVAL KKGFIYSHYS LGGSARQYFS ETNAQKIDAV
RLKIEELKLS QNIDNCAYYF LLASLLESAD KVANTASVYG AFLKRLKKSA QKELILKGAH
FDVSLNANEV YQQDSNDLIG KISGDILYLD PPYNARQYGA NYHLLNTIAA YTPFTPKGKT
GLPSYQKSSF CSRSQILNTF ENLIKKARFK YIFLSYNNEG LMSETEIKNI LKKYGAYSLV
TKTYMRFKAD NKRAHKAVHT KECLHVLIK
//