ID I0ESY0_HELCM Unreviewed; 595 AA.
AC I0ESY0;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
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=HCD_05235 {ECO:0000313|EMBL:AFI06049.1};
OS Helicobacter cetorum (strain ATCC BAA-540 / MIT 99-5656).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1163745 {ECO:0000313|EMBL:AFI06049.1, ECO:0000313|Proteomes:UP000005013};
RN [1] {ECO:0000313|Proteomes:UP000005013}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-540 / MIT 99-5656 {ECO:0000313|Proteomes:UP000005013};
RA Kersulyte D., Berg D.E.;
RT "Complete genome sequence of Helicobacter cetorum strain MIT 99-5656.";
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AFI06049.1, ECO:0000313|Proteomes:UP000005013}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-540 / MIT 99-5656 {ECO:0000313|Proteomes:UP000005013};
RX PubMed=24358262;
RA Kersulyte D., Rossi M., Berg D.E.;
RT "Sequence Divergence and Conservation in Genomes ofHelicobacter cetorum
RT Strains from a Dolphin and a Whale.";
RL PLoS ONE 8:E83177-E83177(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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP003481; AFI06049.1; -; Genomic_DNA.
DR AlphaFoldDB; I0ESY0; -.
DR STRING; 1163745.HCD_05235; -.
DR KEGG; hcm:HCD_05235; -.
DR PATRIC; fig|1163745.3.peg.1107; -.
DR eggNOG; COG0286; Bacteria.
DR HOGENOM; CLU_015410_2_1_7; -.
DR Proteomes; UP000005013; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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:UniProtKB-KW.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.90.220.20; DNA methylase specificity domains; 1.
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; IPR044946; Restrct_endonuc_typeI_TRD_sf.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR42933; SLR6095 PROTEIN; 1.
DR PANTHER; PTHR42933:SF3; TYPE I RESTRICTION ENZYME MJAVIII METHYLASE SUBUNIT; 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 DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 114..342
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 595 AA; 67599 MW; E9594F121E38B818 CRC64;
MFRASKINKQ INVPFIGACL LCMQYGIDVD TTSTKTIIRS IQMGLETIID NKQPLTRKQK
KEFLKTTLGD PTLNKAKDTD LQDILREINT IYHFINTSYK DALGHDIMSN FLRIFRRWNS
VDANEKGEVF TPEHIADLMY DLAECSCENF ILDPACGSGT FLITAMNRMF KEVKNIPNGD
ELAKDIKQNQ LIGIEVNDFN ATLAGLNVML HGDGASYIYN EDCFKKLKTL INIYDRVLMN
PPFALSNEKE LEFVLETLKY LKNGGVLASI LPKTCLKGKD SKELLDECLK ISDLKMVVSL
PSDLFQPNAG ECTAIAIFHK TEKFHNSKTL LIDCSDDGFK LKDSNRECSP FWSQIRHEVL
EAAKGNYDEL RAIEVEIKSS DEILFEAFSL HRPLDISKDT FQKYLKEKIA SSILCNEALK
ENDFKLISNL KESEYKRFKI NDLLVKISNG CEKKSIERTL ENKFIQGVPL VIAKKDNNGI
GGLVEKPSVI FKDKFCIVTK GNGGGGKTFY LEKEFCATTL IMVCDLRESY SSMDKFAKFY
LSVVVSERLF KTVSEGRTIN EVPIIEVKLP IREDGNLNVE FMSDFIKQFE MARFL
//
