ID E1PYT7_HELPM Unreviewed; 309 AA.
AC E1PYT7;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
GN OrderedLocusNames=HPSJM_02410 {ECO:0000313|EMBL:ADO02078.1};
OS Helicobacter pylori (strain SJM180).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=765962 {ECO:0000313|EMBL:ADO02078.1, ECO:0000313|Proteomes:UP000006862};
RN [1] {ECO:0000313|Proteomes:UP000006862}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SJM180 {ECO:0000313|Proteomes:UP000006862};
RA Kersulyte D., Velapatino B., Gilman R.H., Berg D.E.;
RT "Complete genome sequence of Helicobacter pylori strain SJM180.";
RL Submitted (JUN-2010) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002073; ADO02078.1; -; Genomic_DNA.
DR RefSeq; WP_000543212.1; NC_014560.1.
DR AlphaFoldDB; E1PYT7; -.
DR REBASE; 28113; M.Hpy180ORF2410P.
DR KEGG; hpm:HPSJM_02410; -.
DR HOGENOM; CLU_996664_0_0_7; -.
DR Proteomes; UP000006862; Chromosome.
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;
KW Methyltransferase {ECO:0000313|EMBL:ADO02078.1};
KW Transferase {ECO:0000313|EMBL:ADO02078.1}.
SQ SEQUENCE 309 AA; 35877 MW; CB1A3E18697B60DD CRC64;
MHANLFNQNA SKKDVFLHHL RSNNGRYKRY IKAPLRYGGG KSLAVGLIVE YIPNGVRRII
SPFIGGGSVE IACATELGLE VLGFDIFDIL VNFYQVLLKD KQALYNHLLS LEPNQETYST
IKQELKAHYK KECVLDPLIL ARDYYFNFNL SYGPGFLGWM SKIYTDKQRY LNALLKIKGF
NAPSLKVECS SFEEVLLAYP NDFFYLDPPY VLENSKMFKG IYPMRNFPIH HNGFKHEVLA
HMLKRHKGPF ILSYNDCEFV RNAYKDFKIL EPSWQYTMGQ GETRMGKNRL ERGDNNHVKQ
SHELLIIKE
//