ID A0A0K0Y016_9GAMM Unreviewed; 660 AA.
AC A0A0K0Y016;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=HNQ63_001575 {ECO:0000313|EMBL:MBB6087103.1}, WM2015_2854
GN {ECO:0000313|EMBL:AKS43211.1};
OS Wenzhouxiangella marina.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Wenzhouxiangellaceae; Wenzhouxiangella.
OX NCBI_TaxID=1579979 {ECO:0000313|EMBL:AKS43211.1, ECO:0000313|Proteomes:UP000066624};
RN [1] {ECO:0000313|EMBL:AKS43211.1, ECO:0000313|Proteomes:UP000066624}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 42284 {ECO:0000313|EMBL:AKS43211.1,
RC ECO:0000313|Proteomes:UP000066624};
RA Noorani M.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:MBB6087103.1, ECO:0000313|Proteomes:UP000581413}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 103414 {ECO:0000313|EMBL:MBB6087103.1,
RC ECO:0000313|Proteomes:UP000581413};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (AUG-2020) 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; CP012154; AKS43211.1; -; Genomic_DNA.
DR EMBL; JACHIC010000002; MBB6087103.1; -; Genomic_DNA.
DR RefSeq; WP_049726716.1; NZ_JACHIC010000002.1.
DR AlphaFoldDB; A0A0K0Y016; -.
DR STRING; 1579979.WM2015_2854; -.
DR REBASE; 116666; M.Wma42284ORF2854P.
DR KEGG; wma:WM2015_2854; -.
DR PATRIC; fig|1579979.3.peg.2919; -.
DR OrthoDB; 9784823at2; -.
DR Proteomes; UP000066624; Chromosome.
DR Proteomes; UP000581413; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0004519; F:endonuclease activity; 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 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 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 Endonuclease {ECO:0000313|EMBL:AKS43211.1};
KW Hydrolase {ECO:0000313|EMBL:AKS43211.1};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:MBB6087103.1}; Nuclease {ECO:0000313|EMBL:AKS43211.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000066624};
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:MBB6087103.1}.
FT DOMAIN 9..145
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 171..485
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 660 AA; 74153 MW; 5AB35DB8461CCAE0 CRC64;
MEQVQLNWIT NFIWGIADDV LRDLYVRGKY RDVILPMTVL RRLDAVLEPT KQAVLEMKAS
LDEAGIVQQD AALRQAAGQA FYNTSKFTLR DLRSRASQQQ LRADFEAYLD GFSPNVQDIL
ENFEFRNQIP RLSKADALGT LIEKFLSSDI NLSPNPVMNG NGSVKQAALD NHAMGTLFEE
LVRRFNEDNN EEAGEHWTPR DAVKLMAKLI FLPIADEIQS GTYLLYDGAC GTGGMLTVAE
ETLQQLAEDH GKQVATHLFG QEINAETYAI CKADLLLKGE GDAADNIIGG PEHSTLANDA
FPSREFDFML SNPPYGKSWK SDLERMGGKK GVKDPRFLIQ HAGDPEYSLL TRSNDGQMLF
LANMLAKMKQ GTKMGSRIAE VHNGSSLFTG DAGQGESNIR RWIIENDWLE AIVALPLNMF
YNTGIATYIW VLTNRKPEHR KGQVQLIDAT QWYKPLRKNL GKKNCELSEQ DIQRICDAFL
AFEETVQSKI FPNEAFGYWK VTVERPLRLA GIDPERAYKA AEIKKLKETC ERVDDAPPVI
KKIHKKGTEA DPLRGLFEAT IAGKTAVVEY EPDTELRDTE QVPLLEEGGI EAFIKREVLP
HAPDAWYVPG SVKTGYEISF TRYFYKPKPL RSLEEIRADI LALEKETEGL LGEIIGEKAP
//