ID M3NL52_HELPX Unreviewed; 201 AA.
AC M3NL52;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 28-JUN-2023, entry version 26.
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=HMPREF1421_00769 {ECO:0000313|EMBL:EMH28904.1};
OS Helicobacter pylori GAM265BSii.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1159049 {ECO:0000313|EMBL:EMH28904.1, ECO:0000313|Proteomes:UP000011872};
RN [1] {ECO:0000313|EMBL:EMH28904.1, ECO:0000313|Proteomes:UP000011872}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GAM265BSii {ECO:0000313|EMBL:EMH28904.1,
RC ECO:0000313|Proteomes:UP000011872};
RA Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA Pepin K.H., Bhonagiri V., Zhang X., Suruliraj S., Antonio M., Secka O.,
RA Thomas J., Warren W., Mitreva M., Mardis E.R., Wilson R.K.;
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
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:EMH28904.1}.
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DR EMBL; APDY01000043; EMH28904.1; -; Genomic_DNA.
DR AlphaFoldDB; M3NL52; -.
DR PATRIC; fig|1159049.3.peg.726; -.
DR HOGENOM; CLU_1400793_0_0_7; -.
DR Proteomes; UP000011872; Unassembled WGS sequence.
DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:InterPro.
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; 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.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:EMH28904.1};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EMH28904.1}.
SQ SEQUENCE 201 AA; 23631 MW; 48938EC73313E5E6 CRC64;
MKKSIRSPFF YVGDKYKLMP QLNKLFPNNI NQLIEPFVGG GSVFLNTKAK RYLANDIDTN
IINLHKTLSK FNACELFDEL SKIIIHYGLS FSFKGITAPS ELKKQYIKTY YAKYNKIAYE
KLRADFNSNQ NNMLYLYLLL IYGFNHMIRF NSKGLFNLPV GNVDFNENVY NALKNYLDFM
QQNTIIFHNN DYIDFLNHTT F
//
