ID A0A1C6Q0S2_9BURK Unreviewed; 640 AA.
AC A0A1C6Q0S2;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
GN ORFNames=VAR608DRAFT_4893 {ECO:0000313|EMBL:SCK49183.1};
OS Variovorax sp. HW608.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=1034889 {ECO:0000313|EMBL:SCK49183.1, ECO:0000313|Proteomes:UP000198203};
RN [1] {ECO:0000313|Proteomes:UP000198203}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HW608 {ECO:0000313|Proteomes:UP000198203};
RA Varghese N., Submissions Spin;
RL Submitted (JUN-2016) 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};
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DR EMBL; LT607803; SCK49183.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C6Q0S2; -.
DR REBASE; 154918; M.Vsp608ORF4893P.
DR OrthoDB; 9784823at2; -.
DR Proteomes; UP000198203; Chromosome i.
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 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; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR038333; T1MK-like_N_sf.
DR PANTHER; PTHR42933; SLR6095 PROTEIN; 1.
DR PANTHER; PTHR42933:SF3; TYPE I RESTRICTION ENZYME MJAVIII METHYLASE SUBUNIT; 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 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 6..136
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 151..441
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 640 AA; 70684 MW; BB107150EB645AD9 CRC64;
MNQQNLADFI WNVADALRGP FKPSLYGRII LPFTVLRRLE CVLEPTREAV LERHAALIGS
GVELDLVLPA VAAAPFYNTS QYTLATLGST STRANLEEYL SRFSANARQV FDYFGFDNWL
VKLEEANLLY LVTQKFAAID LHPTRLSNAE MGLAFEHLIR KFAEAANDDA GEYFTPRDVV
RLVTTLVFAT DHEALNGEGV VRTVYDCAAG TGGFLSSAIE QVAEWNPAAR IVPYAQELNP
ETYAICVADK LIQGYDVRNL KRGNTLDDDQ LPGERFDYCL ANPPFGVKWE MVQKAVSDER
KNLGYAGRFG PGLPRVGDGS LLFLMHLLSK RKPVEQGGTR IGIVLSGSPL FNGGAGSGES
EVRRWILESD WLEAIVALPS DLFYNTGIGT YVWVLSNHKA PARKGKVQLI DATGLHTPMR
KSLGSKRKFI AHAQIDEIAG AQDTFAESEI SKLFDTADFG HRRITIERPL RMRFAVTEAA
LKAYAETKGA DHVDRFAALS GTSFDSLDVF LAAAKIKKLA KGTRKAVLDC FGTRDPAAEL
VTDADGALVP DAELREFENV PLKQDICDYF AREVLPHVPD AWIDDSKTDE KDGLVGVVGY
EINFNRHFYR YVPPRPLEEI DAELKAVEAE IAALLGEVTA
//
