ID T5CX31_HELPX Unreviewed; 309 AA.
AC T5CX31;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, 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};
GN ORFNames=N405_08480 {ECO:0000313|EMBL:EQL61050.1};
OS Helicobacter pylori FD568.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1191282 {ECO:0000313|EMBL:EQL61050.1, ECO:0000313|Proteomes:UP000015965};
RN [1] {ECO:0000313|EMBL:EQL61050.1, ECO:0000313|Proteomes:UP000015965}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FD568 {ECO:0000313|EMBL:EQL61050.1,
RC ECO:0000313|Proteomes:UP000015965};
RX PubMed=23012278; DOI=10.1128/JB.01278-12;
RA Gunaletchumy S.P., Teh X., Khosravi Y., Ramli N.S., Chua E.G., Kavitha T.,
RA Mason J.N., Lee H.T., Alias H., Zaidan N.Z., Yassin N.B., Tay L.C.,
RA Rudd S., Mitchell H.M., Kaakoush N.O., Loke M.F., Goh K.L., Vadivelu J.;
RT "Draft genome sequences of Helicobacter pylori isolates from Malaysia,
RT cultured from patients with functional dyspepsia and gastric cancer.";
RL J. Bacteriol. 194:5695-5696(2012).
RN [2] {ECO:0000313|EMBL:EQL61050.1, ECO:0000313|Proteomes:UP000015965}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FD568 {ECO:0000313|EMBL:EQL61050.1,
RC ECO:0000313|Proteomes:UP000015965};
RX PubMed=24051312;
RA Rehvathy V., Tan M.H., Gunaletchumy S.P., Teh X., Wang S., Baybayan P.,
RA Singh S., Ashby M., Kaakoush N.O., Mitchell H.M., Croft L.J., Goh K.L.,
RA Loke M.F., Vadivelu J.;
RT "Multiple genome sequences of Helicobacter pylori strains of diverse
RT disease and antibiotic resistance backgrounds from malaysia.";
RL Genome Announc. 1:E00687-E00713(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:EQL61050.1}.
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DR EMBL; AKHQ02000006; EQL61050.1; -; Genomic_DNA.
DR RefSeq; WP_000543224.1; NZ_AKHQ02000006.1.
DR AlphaFoldDB; T5CX31; -.
DR PATRIC; fig|1191282.4.peg.1689; -.
DR Proteomes; UP000015965; Unassembled WGS sequence.
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; IPR012263; M_m6A_EcoRV.
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 PIRSF; PIRSF000398; M_m6A_EcoRV; 1.
DR PRINTS; PR00505; D12N6MTFRASE.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
SQ SEQUENCE 309 AA; 35995 MW; C7D82A8AABB90228 CRC64;
MHANLFNQNA SKKDVFLHNL RSNNGRYKRY IKAPLRYGGG KSLAVGLIVE YIPNGVRRII
SPFIGGGSVE IACATELGLE VLGFDIFDIL VNFYQVLLKD KQALYNNLLS LEPTQETYNI
IKQELKAHYK KECVLDPLIL ARDYYFNFNL SYGPGFLGWM SKIYTDKQHY LNALLKIKDF
NAPSLKVECS SFEEVLLAYP NDFFYLDPPY VLENSKMFKG IYPMRNFPIH HNGFKHEILA
HMLKRHKGPF ILSYNDCEFV RNAYKDFKIL EPFWQYIMGQ GEIRMGKNRL ERGDNNHVKQ
SHELLIIKE
//
