ID A1TGB5_MYCVP Unreviewed; 552 AA.
AC A1TGB5;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
GN OrderedLocusNames=Mvan_5445 {ECO:0000313|EMBL:ABM16215.1};
OS Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 /
OS KCTC 9966 / NRRL B-24157 / PYR-1) (Mycobacterium vanbaalenii).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=350058 {ECO:0000313|EMBL:ABM16215.1, ECO:0000313|Proteomes:UP000009159};
RN [1] {ECO:0000313|EMBL:ABM16215.1, ECO:0000313|Proteomes:UP000009159}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 /
RC PYR-1 {ECO:0000313|Proteomes:UP000009159};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Anderson I.J., Miller C., Richardson P.;
RT "Complete sequence of Mycobacterium vanbaalenii PYR-1.";
RL Submitted (DEC-2006) 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; CP000511; ABM16215.1; -; Genomic_DNA.
DR AlphaFoldDB; A1TGB5; -.
DR STRING; 350058.Mvan_5445; -.
DR REBASE; 14480; M.MvaPORF5445P.
DR KEGG; mva:Mvan_5445; -.
DR eggNOG; COG0827; Bacteria.
DR HOGENOM; CLU_020255_1_0_11; -.
DR Proteomes; UP000009159; 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 CDD; cd02440; AdoMet_MTases; 1.
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; PTHR33841; DNA METHYLTRANSFERASE YEEA-RELATED; 1.
DR PANTHER; PTHR33841:SF5; TYPE II METHYLTRANSFERASE M.HINDII; 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:ABM16215.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009159};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABM16215.1}.
FT DOMAIN 12..203
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 552 AA; 60056 MW; 17D8766C22C198D6 CRC64;
MRMLPGDNAD LRKARGAFFT PTPVARFLTD WAVRHPEHSV LEPSCGEAVF LHEIGQRGGH
TGPLVGVEIH PGSAEESQRS LRARGIDATI HARDFFSHAE FGSYDAVVGN PPYVRYQDFA
GEARARARQA ALRAGVALSN LASSWAAFTV HSALHLRPGG RLGLVLPAEL LSVNYAAGVR
QYLMDHFGQV GLVLFDERVF PGVLEEVVLL LADGYQPDGG RGATHMRLSQ VRDAAGLARL
TGSRRWSPPG NGAKWSAGLM SAAGLSAFDS VVRGDAFTFL ETWGDTTLGM VTGSNRFFTL
SPDKVDALGL APSDLIPLSP PGSRHLRGLA LTPKALRALG EEGRSTYLFR PADEPSPAGW
HYIASGEDLD VHRAYKCRVR TPWWRVPYLR PADLFLTYMN ADTPRLTSNR ARTHHLNSVH
GVYLRDEFRQ DGMNLLPLAS LNSVTLLGAE TVGRAYGGGM LKIEPREADV LPVPSPDLVR
RNADQLRRIR PAVATCLRDA RLLDAVALVD EVLLLGTSTL SERALRAVRR DHAGLTARRI
TRGKVGKAHG GE
//
