ID K2L5Y7_HELPX Unreviewed; 404 AA.
AC K2L5Y7;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=OUI_1425 {ECO:0000313|EMBL:EKE85155.1};
OS Helicobacter pylori R036d.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1145113 {ECO:0000313|EMBL:EKE85155.1, ECO:0000313|Proteomes:UP000006759};
RN [1] {ECO:0000313|EMBL:EKE85155.1, ECO:0000313|Proteomes:UP000006759}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R036d {ECO:0000313|EMBL:EKE85155.1,
RC ECO:0000313|Proteomes:UP000006759};
RA Blanchard T.G., Czinn S.J., McCracken C.M., Abolude K.A., Shefchek K.S.,
RA Maroo A.M., Santana-Cruz I.S., Tallon L.J., Ficke F.W.F.;
RT "Comparative Sequence Analysis of H. pylori isolates.";
RL Submitted (AUG-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 -!- 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:EKE85155.1}.
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DR EMBL; AMOT01000005; EKE85155.1; -; Genomic_DNA.
DR AlphaFoldDB; K2L5Y7; -.
DR PATRIC; fig|1145113.3.peg.1393; -.
DR Proteomes; UP000006759; 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:0006306; P:DNA methylation; IEA:InterPro.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR003356; DNA_methylase_A-5.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR33841; DNA METHYLTRANSFERASE YEEA-RELATED; 1.
DR PANTHER; PTHR33841:SF5; TYPE II METHYLTRANSFERASE M.HINDII; 1.
DR Pfam; PF02384; N6_Mtase; 1.
DR PRINTS; PR00507; N12N6MTFRASE.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 4: Predicted;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:EKE85155.1};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 296..375
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 404 AA; 46715 MW; 595A80CFC8B7358A CRC64;
MLKEYLESIK DLTHEKNELT HRLFLHNLLK GLKDHFNKEF KIEHEPKKDK QGGQPDFSVS
YQGLNIGYIE NKRVGADLNK LLKSKQILKY LELNPNLMLT NYLNFMWVGK DENNAPLIKK
EISVASLDEL SKPLKPKPQI ERDLIELFKS FFNHEAVPIA NAKDFATHLS APTKYLKDAL
ITYQKDTQVS SIFNNFKEYL YEELSFEDFS DAFAQTLTYS LFLAKLNHPF EKINLDNVRS
SIPKNFAVIR EMADFLKKLD EIKEIQWLLN EILSSINHVD MDSILKDLND DKDPYLHFYE
TFLSAYDPKL RESKGVYYTP DSVVKFIINA LDSLLKTHFK DAPLGLKSAL DNENIKLLDF
ATGTGTFLLE AFRKALEVRK TSDGGISTKE DKYQNLLKQF FGSV
//
