ID A0A1X7BW15_9RHOB Unreviewed; 504 AA.
AC A0A1X7BW15;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
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:SMC13705.1};
GN ORFNames=ROA7745_03564 {ECO:0000313|EMBL:SMC13705.1};
OS Roseovarius aestuarii.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=475083 {ECO:0000313|EMBL:SMC13705.1, ECO:0000313|Proteomes:UP000193224};
RN [1] {ECO:0000313|EMBL:SMC13705.1, ECO:0000313|Proteomes:UP000193224}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7745 {ECO:0000313|EMBL:SMC13705.1,
RC ECO:0000313|Proteomes:UP000193224};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (MAR-2017) 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; FWXB01000016; SMC13705.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X7BW15; -.
DR OrthoDB; 9806213at2; -.
DR Proteomes; UP000193224; 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 GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
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; IPR004546; Restrct_endonuc_T1M.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR038333; T1MK-like_N_sf.
DR NCBIfam; TIGR00497; hsdM; 1.
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 Coiled coil {ECO:0000256|SAM:Coils};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:SMC13705.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000193224};
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:SMC13705.1}.
FT DOMAIN 10..144
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 158..468
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
FT COILED 465..492
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 504 AA; 57287 MW; F1EDE9D1273CB951 CRC64;
MTKQVNQAEI NQAVWAACDT FRGTVDPSIY KDFVLTMLFL KFLSDVWREH YEQYEADYGD
APELIAEMMK NERFVLPEGA SFYDLYGQRH APGNGERIDK ALHAIEEANI TKLRDVFQDI
SFNSTKLGDE KQKNDLLAHL LEDFVDERLD LRMAHIGNQD VIGNAYEYLI SRFASEGGKT
AGEFYTPAEV SELIAELVDP QEGDEICDPT CGSASLLMKC GRKVRAKGSK KYALFGQEAI
GSTWALAKMN LFLHGEDNHR VEWGDTIRNP KLLDEHDRLK HFDVVVANPP FSLDKWGHGT
AEDDRFSRFR RGIPPKSKGD YAFILHMIET MKPGSGRMGV VVPLGALFRG ASEGKIRRRL
VEEHKLDAVI GLPEKLFFGT GIPAAILIFK QDKEDGSVLF IDASREFIKG TNQNRLDPEK
HIKKIVETYR ARESETDKYS YLAQFEEMAE NDFNLNIPRY VDTFEEEEEI DLMAVRAERE
VLKKELADLD IQMAGCLKEL GYDA
//
