ID M3PJH2_HELPX Unreviewed; 518 AA.
AC M3PJH2;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=HMPREF1418_00317 {ECO:0000313|EMBL:EMH25198.1};
OS Helicobacter pylori GAM260BSi.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1159046 {ECO:0000313|EMBL:EMH25198.1, ECO:0000313|Proteomes:UP000012023};
RN [1] {ECO:0000313|EMBL:EMH25198.1, ECO:0000313|Proteomes:UP000012023}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GAM260BSi {ECO:0000313|EMBL:EMH25198.1,
RC ECO:0000313|Proteomes:UP000012023};
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 (NOV-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:EMH25198.1}.
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DR EMBL; APDV01000014; EMH25198.1; -; Genomic_DNA.
DR AlphaFoldDB; M3PJH2; -.
DR PATRIC; fig|1159046.3.peg.299; -.
DR HOGENOM; CLU_025115_2_0_7; -.
DR Proteomes; UP000012023; Unassembled WGS sequence.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; 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; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR011639; MethylTrfase_TaqI-like_dom.
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; PF07669; Eco57I; 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 3: Inferred from homology;
KW Endonuclease {ECO:0000313|EMBL:EMH25198.1};
KW Hydrolase {ECO:0000313|EMBL:EMH25198.1};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Nuclease {ECO:0000313|EMBL:EMH25198.1};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 78..187
FT /note="Type II methyltransferase M.TaqI-like"
FT /evidence="ECO:0000259|Pfam:PF07669"
FT DOMAIN 300..456
FT /note="TaqI-like C-terminal specificity"
FT /evidence="ECO:0000259|Pfam:PF12950"
SQ SEQUENCE 518 AA; 60186 MW; 6F6E7BD347513C33 CRC64;
MEALALEKKM AHEGLFHDYT PYPKLDKTDK VVGLEHFNRY VLTSYKDLQD ENERYANALE
WRFEFPEVLD DEGNFLGFDC IIGNPPYIRQ EHIKDLKPLL EKQYHDFYNS SSDIYTYFFA
LAFNLLKEKG FSAFITSNKY ARAKYGAKLR ELLLKKTTLV SYMELNALKV FESATVDTSI
IHFIKQAPLK ESVFNYYEPT PNDKDDLKNT PSLLMRQNAL QTESFIFANI TLLDLRDKME
NSGTPLKDWG IQIYRGILTG CNEAFIIPTE KRDEILKNCD DLQKDGKGMS ERERTIELIK
PILRGKDIKR YSYEWADLWV IATFPSLKLD IDDYPSLKTY LSQFRPRIDQ SGEKGCRKKT
SNQWFETQDT IAYHGDFEKE KIAYPCIMAK EPCFVYEEKG FYAPAPANII TGDKTEIKYL
TVLLNSKCIY FAMRKFYMGG GIEGELKTNN LEKIPIPKIT EKNQELADEI TDCAERILKS
KAKDPKANTQ ELEKEIDALV YQLYHLTDEE IKTIEDGQ
//
