ID Q17WV3_HELAH Unreviewed; 543 AA.
AC Q17WV3;
DT 25-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 25-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
GN Name=hsdM {ECO:0000313|EMBL:CAJ99873.1};
GN OrderedLocusNames=Hac_1111 {ECO:0000313|EMBL:CAJ99873.1};
OS Helicobacter acinonychis (strain Sheeba).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=382638 {ECO:0000313|EMBL:CAJ99873.1, ECO:0000313|Proteomes:UP000000775};
RN [1] {ECO:0000313|EMBL:CAJ99873.1, ECO:0000313|Proteomes:UP000000775}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sheeba {ECO:0000313|EMBL:CAJ99873.1,
RC ECO:0000313|Proteomes:UP000000775};
RX PubMed=16789826; DOI=10.1371/journal.pgen.0020120;
RA Eppinger M., Baar C., Linz B., Raddatz G., Lanz C., Keller H., Morelli G.,
RA Gressmann H., Achtman M., Schuster S.C.;
RT "Who ate whom? Adaptive Helicobacter genomic changes that accompanied a
RT host jump from early humans to large felines.";
RL PLoS Genet. 2:1097-1110(2006).
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; AM260522; CAJ99873.1; -; Genomic_DNA.
DR RefSeq; WP_011577980.1; NC_008229.1.
DR AlphaFoldDB; Q17WV3; -.
DR SMR; Q17WV3; -.
DR STRING; 382638.Hac_1111; -.
DR REBASE; 13260; M.HacSORF1111P.
DR KEGG; hac:Hac_1111; -.
DR eggNOG; COG0286; Bacteria.
DR HOGENOM; CLU_037306_0_0_7; -.
DR OrthoDB; 9761012at2; -.
DR BioCyc; HACI382638:HAC_RS04770-MONOMER; -.
DR Proteomes; UP000000775; 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 GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
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 PANTHER; PTHR42933:SF1; SITE-SPECIFIC DNA-METHYLTRANSFERASE (ADENINE-SPECIFIC); 1.
DR PANTHER; PTHR42933; SLR6095 PROTEIN; 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 Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:CAJ99873.1};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CAJ99873.1}.
FT DOMAIN 184..501
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 543 AA; 61823 MW; 12E82AD7B145547C CRC64;
MPNNALLQIK QDTFKLIDDL KVICTSFGLG NDGNEYKIIT QCFLYKFLCD KFEFLFEQEF
PNQTIQDYKD VTEEEKEDFF LTLSDKKLPK LSYDELLNHL FDKHFNDNDL HIKLDAIFNN
ISSNNAALFN TISTDKTTIA LFESISQHIN EESKRANFTK VLLDKLKNFN FKNAFLNLQN
QQGYDFFAPI FEYLLKDYNN AGGGKYAEYY TPLSIASIIA KLLVNEPVKS KKIYDPSAGT
GTLLIALAHQ IGTDSCTLYA QDISQKSLKM LKLNLILNDL THSLKNAIEG NTLTNPYHSK
DYKGKMDYIV SNPPFKLDFS NEHATISNNK SDFSLGVPNI PKNDKSKMPI YTLFFQHCLS
MLNPKSKGAI VVPTGFISAK SGVANKIVRH LVDEKLVYGV ICMPSQVFAN TGTNVSVIFF
QKTPSENEVI LIDASKLGEE YTENKNKKTR LRTSDMDLIL ETFKNKTQKS DFCAVVSFDE
IIEKNYSLNP GQYFTIEDVS ETISQTEFEN LMQQYSSELT SLFDESQHLQ QEILEVLGNL
NYD
//
