ID J0PML1_HELPX Unreviewed; 532 AA.
AC J0PML1;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
GN Name=vspIM {ECO:0000313|EMBL:EJB99852.1};
GN ORFNames=HPHPP2_0564 {ECO:0000313|EMBL:EJB99852.1};
OS Helicobacter pylori Hp P-2.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=992073 {ECO:0000313|EMBL:EJB99852.1, ECO:0000313|Proteomes:UP000004326};
RN [1] {ECO:0000313|EMBL:EJB99852.1, ECO:0000313|Proteomes:UP000004326}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hp P-2 {ECO:0000313|EMBL:EJB99852.1,
RC ECO:0000313|Proteomes:UP000004326};
RX PubMed=23661595; DOI=10.1111/2049-632X.12045;
RA Blanchard T.G., Czinn S.J., Correa P., Nakazawa T., Keelan M.,
RA Morningstar L., Santana-Cruz I., Maroo A., McCracken C., Shefchek K.,
RA Daugherty S., Song Y., Fraser C.M., Fricke W.F.;
RT "Genome sequences of 65 Helicobacter pylori strains isolated from
RT asymptomatic individuals and patients with gastric cancer, peptic ulcer
RT disease, or gastritis.";
RL Pathog. Dis. 68:39-43(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 -!- 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:EJB99852.1}.
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DR EMBL; AKPJ01000001; EJB99852.1; -; Genomic_DNA.
DR RefSeq; WP_001139764.1; NZ_AKPJ01000001.1.
DR AlphaFoldDB; J0PML1; -.
DR PATRIC; fig|992073.3.peg.552; -.
DR Proteomes; UP000004326; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro.
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; 1.
DR InterPro; IPR003356; DNA_methylase_A-5.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR025931; TaqI_C.
DR PANTHER; PTHR33841:SF1; ADENINE-SPECIFIC METHYLTRANSFERASE PGLX; 1.
DR PANTHER; PTHR33841; DNA METHYLTRANSFERASE YEEA-RELATED; 1.
DR Pfam; PF02384; N6_Mtase; 1.
DR Pfam; PF12950; TaqI_C; 1.
DR PRINTS; PR00507; N12N6MTFRASE.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 4: Predicted;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:EJB99852.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EJB99852.1}.
FT DOMAIN 93..264
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
FT DOMAIN 375..488
FT /note="TaqI-like C-terminal specificity"
FT /evidence="ECO:0000259|Pfam:PF12950"
SQ SEQUENCE 532 AA; 61528 MW; 2653E2E92EBC34B2 CRC64;
MPSNALSVGE IAHLINVSHS SVRNWIKTNL LEKLEIDHKI YVKTSSFLDF CRNHLGKNKL
NKYANKSLKS AHNHQELILK YLEMLENSSD LENLGSYYEK ELSNTTRNLE GIYYTPNRIV
EQLFTLPKDF DTTQAIFCDP AVGSGNFVMH ALKLGFKVEN IYGYDTDAFA VALTKKRIKE
RYRLDCPNIV QKDFLSLKHA PQFDCIFTNP PWGKKYNQNQ KENFKLQFNL PQSLDSASLF
FMASLNCLKE NAHLGLLLPE SCLNIDAFSK MREMALKFQM RSLIDFDKPF KNLMTKAVGL
ALKKTPNFER SPSSFFNNPK KIFNIHCSHQ KNKILDHLFS IPHTTLKNNA HFALGIVTGN
NEEKLHPKQE KNTIPIFRGS DILKDGLKAP SQFINADLKD CQQVAPLSLY QAREKIVYKF
ISSKLVFFYD NEQRLFLNSA NMFVLKENFP INAHALKELL NSDLMQFIFE SLFKTHKILR
KDLECLPLFA QFINNGFDEK FYLKNLGIEK KDPKHFTIRK NHAHRLSFGF RG
//
