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Database: UniProt
Entry: T2T398_HELPX
LinkDB: T2T398_HELPX
Original site: T2T398_HELPX 
ID   T2T398_HELPX            Unreviewed;       345 AA.
AC   T2T398;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-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};
DE   Flags: Fragment;
GN   ORFNames=L931_07930 {ECO:0000313|EMBL:EQD99376.1};
OS   Helicobacter pylori PZ5024.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=1337391 {ECO:0000313|EMBL:EQD99376.1, ECO:0000313|Proteomes:UP000015645};
RN   [1] {ECO:0000313|EMBL:EQD99376.1, ECO:0000313|Proteomes:UP000015645}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PZ5024 {ECO:0000313|EMBL:EQD99376.1,
RC   ECO:0000313|Proteomes:UP000015645};
RX   PubMed=24051318;
RA   Sheh A., Piazuelo M.B., Wilson K.T., Correa P., Fox J.G.;
RT   "Draft Genome Sequences of Helicobacter pylori Strains Isolated from
RT   Regions of Low and High Gastric Cancer Risk in Colombia.";
RL   Genome Announc. 1:e00736-13(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:EQD99376.1}.
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DR   EMBL; ASYS01000049; EQD99376.1; -; Genomic_DNA.
DR   AlphaFoldDB; T2T398; -.
DR   REBASE; 72955; M.Hpy5024ORF7930P.
DR   Proteomes; UP000015645; 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   GO; GO:0009307; P:DNA restriction-modification system; IEA:InterPro.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 1.20.1260.30; -; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR022749; D12N6_MeTrfase_N.
DR   InterPro; IPR003356; DNA_methylase_A-5.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR004546; Restrct_endonuc_T1M.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR038333; T1MK-like_N_sf.
DR   NCBIfam; TIGR00497; hsdM; 1.
DR   PANTHER; PTHR42933:SF1; SITE-SPECIFIC DNA-METHYLTRANSFERASE (ADENINE-SPECIFIC); 1.
DR   PANTHER; PTHR42933; SLR6095 PROTEIN; 1.
DR   Pfam; PF12161; HsdM_N; 1.
DR   Pfam; PF02384; N6_Mtase; 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   Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT   DOMAIN          25..177
FT                   /note="N6 adenine-specific DNA methyltransferase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12161"
FT   DOMAIN          190..343
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         345
FT                   /evidence="ECO:0000313|EMBL:EQD99376.1"
SQ   SEQUENCE   345 AA;  39049 MW;  BF0BFB4C372810E1 CRC64;
     MENKNTQANE KNNEHASSSL ERNELHNTIW KVANELRGSV DGWDFKQYVL GILFYRYISE
     NMTDYINKEE RKHDPSFDYA LLSDEEAERA REELIKEKGF FIPPSALFCN ALKNARHNED
     LNVTLQNIFN EIEKSSLGTP SEENVKGLFA DLDVNSNKLG SSHKIRVEKL TKILQAIGGM
     QLGDYLKSGI DVFGDAYEYL MAMYASNAGK SGGEFFTPQE VSELLAKIAL HNQESINKVY
     DPCCGSGSLL LQFSKVLGDK NVSKGYFGQE INLTTYNLCR INMFLHDINY SKFHIALGDT
     LLDPKHEDDE PFDAIVSNPP YSTKWIGDNN PLLRNDERFS KAGTL
//
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