ID B5Z740_HELPG Unreviewed; 887 AA.
AC B5Z740;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 70.
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=HPG27_630 {ECO:0000313|EMBL:ACI27389.1};
OS Helicobacter pylori (strain G27).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=563041 {ECO:0000313|EMBL:ACI27389.1, ECO:0000313|Proteomes:UP000001735};
RN [1] {ECO:0000313|EMBL:ACI27389.1, ECO:0000313|Proteomes:UP000001735}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G27 {ECO:0000313|EMBL:ACI27389.1,
RC ECO:0000313|Proteomes:UP000001735};
RX PubMed=18952803; DOI=10.1128/JB.01416-08;
RA Baltrus D.A., Amieva M.R., Covacci A., Lowe T.M., Merrell D.S.,
RA Ottemann K.M., Stein M., Salama N.R., Guillemin K.;
RT "The complete genome sequence of Helicobacter pylori strain G27.";
RL J. Bacteriol. 191:447-448(2009).
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};
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DR EMBL; CP001173; ACI27389.1; -; Genomic_DNA.
DR AlphaFoldDB; B5Z740; -.
DR REBASE; 19048; HpyGORF629P.
DR KEGG; hpg:HPG27_630; -.
DR HOGENOM; CLU_002151_1_1_7; -.
DR Proteomes; UP000001735; Chromosome.
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; IPR041635; Type_ISP_LLaBIII_C.
DR Pfam; PF02384; N6_Mtase; 1.
DR Pfam; PF18135; Type_ISP_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;
FT DOMAIN 134..322
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
FT DOMAIN 509..856
FT /note="Type ISP restriction-modification enzyme LLaBIII C-
FT terminal specificity"
FT /evidence="ECO:0000259|Pfam:PF18135"
SQ SEQUENCE 887 AA; 102220 MW; 688BE1B7C901ED1E CRC64;
MYNVMPTKLG DRNYWENFTK KTGNIARTLN NRLKMIFDKN PEFFHDFLNS LRDNIHQNIR
EDEALDMITS HIITKPIFDA LFGDNIKNPI AKALDKMVLK LSTLGLEGET KDLKNLYESV
KTEATHAKSP KSQQELIKNL YNTFFKEAFK KQSEKLGIVY TPIEVVDFIL RATNGILKKH
FNTDFNDQSI TIFDPFTGTG SFIARLLSKE NKLISDEALK EKFQKNLFAF DIVLLSYYIA
LINITQAAQN RDSSLKNFKN IALTDSLDYL EEKTNKGALP LYEDLKENKE IKDTLADQNI
RVIIGNPPYS SGAKSQNDNN QNLSHPKLKK LVYEKYGKNS TAKVGKATRD ALIQSIRMAS
DVVKDKGVIG FVVNGSFIDS KSTDGFRKCV AKEFSHLYVL NLRGNTRTSG EERKKQGDGI
FDSGSRATVA IVFFVKDNSV KNNTIDYYDI GDYLKREEKL HKLAQFENLE SVPFKEITPN
AKGDWINQRN DDFEKLIPLK RDKTLQNDSI FDINSGGVVS GRDPWVYNFS PKILMQSVQN
CIDTYNADLK RFNARFREAF KQRTKGVKSG DLYKHLNDKE ITTDKTKIAW VQNLKTQLIK
GKKLDDFSQE KISVSLYRPF NKQWLYWDKD WINTQGKFSK IFPDKSARNV VINTTTRNFC
SLIGDAIPDT HFIGDTQAYP LYYYDDLGNR YDAISGYALN LFRRHYQDDS IVEEEIFYYI
YAIFHHKGYL EKYKNSLAKE APRIALSEDF KELSTLGKEL AELHLNYESG EMHESVKHNL
LENAGMEGYY DVVQMKKDKK GDRIIYNKNI AITKIPQKAF DYVVNGKSAI DWVIERYQKT
MDKDSLIENN PNDYAGGKYV FELLCRVITL SVKSVDLIEK ISEKRFE
//
