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Database: UniProt
Entry: Q9ZIJ7_HELPX
LinkDB: Q9ZIJ7_HELPX
Original site: Q9ZIJ7_HELPX 
ID   Q9ZIJ7_HELPX            Unreviewed;       170 AA.
AC   Q9ZIJ7;
DT   01-MAY-1999, integrated into UniProtKB/TrEMBL.
DT   01-MAY-1999, sequence version 1.
DT   24-JAN-2024, entry version 43.
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;
OS   Helicobacter pylori (Campylobacter pylori).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=210 {ECO:0000313|EMBL:AAC69266.1};
RN   [1] {ECO:0000313|EMBL:AAC69266.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=J166 {ECO:0000313|EMBL:AAC69266.1};
RX   PubMed=9789049; DOI=10.1073/pnas.95.22.13108;
RA   Akopyants N.S., Fradkov A., Diatchenko L., Hill J.E., Siebert P.D.,
RA   Lukyanov S.A., Sverdlov E.D., Berg D.E.;
RT   "PCR-based subtractive hybridization and differences in gene content among
RT   strains of Helicobacter pylori.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:13108-13113(1998).
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; AF025981; AAC69266.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9ZIJ7; -.
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   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000313|EMBL:AAC69266.1};
KW   Transferase {ECO:0000313|EMBL:AAC69266.1}.
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAC69266.1"
FT   NON_TER         170
FT                   /evidence="ECO:0000313|EMBL:AAC69266.1"
SQ   SEQUENCE   170 AA;  19291 MW;  087F9FA8D56A997C CRC64;
     IIKSYPTTLT NLVNSDNILD SLNEVFPYKE AFSPYLIEHL QHRFGCSIES VYDPFCGVGS
     SFLNTQTQVC YGFDTSPFAI NVAEAKLEKL DSNNLKKAEK HVGNFMGIAI ENIHFHMGNL
     LANILIKSDL ISSWILLESF KDLMKNLSFG GFPVFWQLGK MLNFKKEVWV
//
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