ID X2ILU1_HELPX Unreviewed; 299 AA.
AC X2ILU1;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900, ECO:0000256|RuleBase:RU361257};
DE EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900, ECO:0000256|RuleBase:RU361257};
GN ORFNames=HPOKI673_07495 {ECO:0000313|EMBL:AHN42596.1};
OS Helicobacter pylori oki673.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1382925 {ECO:0000313|EMBL:AHN42596.1, ECO:0000313|Proteomes:UP000019661};
RN [1] {ECO:0000313|EMBL:AHN42596.1, ECO:0000313|Proteomes:UP000019661}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Oki673 {ECO:0000313|EMBL:AHN42596.1};
RX PubMed=24744331;
RA Satou K., Shiroma A., Teruya K., Shimoji M., Nakano K., Juan A.,
RA Tamotsu H., Terabayashi Y., Aoyama M., Teruya M., Suzuki R., Matsuda M.,
RA Sekine A., Kinjo N., Kinjo F., Yamaoka Y., Hirano T.;
RT "Complete Genome Sequences of Eight Helicobacter pylori Strains with
RT Different Virulence Factor Genotypes and Methylation Profiles, Isolated
RT from Patients with Diverse Gastrointestinal Diseases on Okinawa Island,
RT Japan, Determined Using PacBio Single-Molecule Real-Time Technology.";
RL Genome Announc. 2:e00286-14(2014).
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 ECO:0000256|RuleBase:RU361257};
CC -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC {ECO:0000256|ARBA:ARBA00006594, ECO:0000256|RuleBase:RU361257}.
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DR EMBL; CP006825; AHN42596.1; -; Genomic_DNA.
DR AlphaFoldDB; X2ILU1; -.
DR REBASE; 81538; M2.Hpy673ORF7490P.
DR KEGG; hpyg:HPOKI673_07495; -.
DR HOGENOM; CLU_077381_0_0_7; -.
DR Proteomes; UP000019661; Chromosome.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-UniRule.
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; IPR012263; M_m6A_EcoRV.
DR InterPro; IPR012327; MeTrfase_D12.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR NCBIfam; TIGR00571; dam; 1.
DR PANTHER; PTHR30481; DNA ADENINE METHYLASE; 1.
DR PANTHER; PTHR30481:SF3; DNA ADENINE METHYLASE; 1.
DR Pfam; PF02086; MethyltransfD12; 1.
DR PIRSF; PIRSF000398; M_m6A_EcoRV; 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:0000256|RuleBase:RU361257};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|RuleBase:RU361257};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361257}.
SQ SEQUENCE 299 AA; 35371 MW; FB3B4EEE06D7B7D0 CRC64;
MKKGIRSPFF YVGDKYKLMP QLNKLFPNNI NQFIEPFVGG GSVFLNTKAK RYLANDIDTN
IINLHKTLSK FNTCELFDEL SKIIIHYGLS FSFKGITAPD ELKKQYIKTY YAKYNKIAYE
KLRADFNSNQ NNMLYLYLLL IYGFNHMIRF NSKGLFNLPV GNVDFNENVY NALKNYIDFM
QQNTIIFHND DYIDFLNHTT YLKDDYVYFD PPYLISSSEY NKLWDSDNEI ALYGVLDSLD
KKGVLFGITN LVYRKGETNF ILKEWAKKYY IFNIKSNYIS YNDNTIKEDS QEIFVTNYR
//
