ID U3CBC2_9VIBR Unreviewed; 544 AA.
AC U3CBC2;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-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 Name=hsdM {ECO:0000313|EMBL:GAD78624.1};
GN ORFNames=VEZ01S_05_00110 {ECO:0000313|EMBL:GAD78624.1};
OS Vibrio ezurae NBRC 102218.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1219080 {ECO:0000313|EMBL:GAD78624.1, ECO:0000313|Proteomes:UP000016562};
RN [1] {ECO:0000313|EMBL:GAD78624.1, ECO:0000313|Proteomes:UP000016562}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 102218 {ECO:0000313|EMBL:GAD78624.1,
RC ECO:0000313|Proteomes:UP000016562};
RA Yoshida I., Hosoyama A., Numata M., Hashimoto M., Hosoyama Y.,
RA Tsuchikane K., Noguchi M., Hirakata S., Ichikawa N., Ohji S., Yamazoe A.,
RA Fujita N.;
RT "Whole genome shotgun sequence of Vibrio ezurae NBRC 102218.";
RL Submitted (SEP-2013) 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 -!- 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:GAD78624.1}.
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DR EMBL; BATM01000005; GAD78624.1; -; Genomic_DNA.
DR RefSeq; WP_021712347.1; NZ_BATM01000005.1.
DR AlphaFoldDB; U3CBC2; -.
DR STRING; 1219080.VEZ01S_05_00110; -.
DR eggNOG; COG0286; Bacteria.
DR OrthoDB; 9784823at2; -.
DR Proteomes; UP000016562; 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 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; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR038333; T1MK-like_N_sf.
DR PANTHER; PTHR42998:SF1; TYPE I RESTRICTION ENZYME HINDI METHYLASE SUBUNIT; 1.
DR PANTHER; PTHR42998; TYPE I RESTRICTION ENZYME HINDVIIP M PROTEIN-RELATED; 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.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000016562}.
FT DOMAIN 10..139
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 150..499
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
FT COILED 513..540
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 544 AA; 61059 MW; EC31A94BA04F86B6 CRC64;
MADFKKIEEL EKRLWSAADS LRANTGLTAQ EYSRPIQGLI FLKYAEYRFA LAKSKIEEQT
SSRRRGSGDI KSKIQAEGAM YVPDEALYTK LLALPEGANI GVKINDAMKA LEAENEAIKD
ALPKTFTRFE NDILKSLLKN FNDIDFSLGS DIFGRIYEYF LNEFAKTEGQ GGGEFFTPSA
LVKLITEIIE PYHGKVFDPA CGSGGMFVSS ADFVSSHNKS ASDELSVFGQ EKTGDTVRLS
KMNLAVHGLQ GDIREGNSYY EDPFELAKGP IVDGKQHGQF DYVMANPPFN VNEIQKDRLE
GDKHRFPYGM PRNDNGNYLW IQMFYTALNQ KGRAGFVMAN SASDARGSEQ EIRQQLIEDD
AVDVMVAVST NFFYTVTLPC ALWFLDKNKP AHNKDKVLFI DARHIFRQVT RSVRDYTSEQ
LNFIANIVRL YRGQDIDNTY LETHPDDGNV GKFKLEDFFT NDRGELAYQD IAGLCKVASK
ADIIEQGYSL NPGRYVGVAD GEVLDDVEFK LKFELLIEEL ESLSSEAHQL EADISKNAAQ
ILGL
//
