ID A7RAG0_PBCVA Unreviewed; 373 AA.
AC A7RAG0;
DT 02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 46.
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=C011L {ECO:0000313|EMBL:ABU43557.1};
GN ORFNames=AR158_C011L {ECO:0000313|EMBL:ABU43557.1};
OS Paramecium bursaria Chlorella virus AR158 (PBCV-AR158).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC Algavirales; Phycodnaviridae; Chlorovirus.
OX NCBI_TaxID=380598 {ECO:0000313|EMBL:ABU43557.1, ECO:0000313|Proteomes:UP000203485};
OH NCBI_TaxID=74790; Paramecium bursaria.
RN [1] {ECO:0000313|EMBL:ABU43557.1, ECO:0000313|Proteomes:UP000203485}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AR158 {ECO:0000313|EMBL:ABU43557.1,
RC ECO:0000313|Proteomes:UP000203485};
RX PubMed=17027058; DOI=10.1016/j.virol.2006.08.033;
RA Fitzgerald L.A., Graves M.V., Li X., Feldblyum T., Nierman W.C.,
RA Van Etten J.L.;
RT "Sequence and annotation of the 369-kb NY-2A and the 345-kb AR158 viruses
RT that infect Chlorella NC64A.";
RL Virology 358:472-484(2007).
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; DQ491003; ABU43557.1; -; Genomic_DNA.
DR RefSeq; YP_001498093.1; NC_009899.1.
DR GeneID; 5660087; -.
DR KEGG; vg:5660087; -.
DR Proteomes; UP000203485; Genome.
DR GO; GO:0003677; F:DNA binding; 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 CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.90.220.20; DNA methylase specificity domains; 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; IPR044946; Restrct_endonuc_typeI_TRD_sf.
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; SSF116734; DNA methylase specificity domain; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Reference proteome {ECO:0000313|Proteomes:UP000203485};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 21..186
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 373 AA; 42902 MW; C357EB1B5227AFB9 CRC64;
MYYTIMEYSQ ITKDFEKTLD KEKKSKQGIF FTPKSVREKL FGYVDEPKNI LEPSCGTGEI
ISDCIERFPS ANITGVELDK DIYDVCKRSY TRENVNIIND DFLAWKGGKF DFIVGNPPFV
VRPKGHKNDD RIVRGRSNLY VEFLFKCITE HLKEDGILAF IIPSTIGNSK FYEPIRKLII
TLDILSFEIL DKHEFCDTNT RLCSIVIKNS PGTGKYTYKD YICDREIPHH EGETIGDLDL
TFKTGFTWSS VKKFFIDKSD IPFFTSGNIK FDEVIIGEKT KYVSEEMTKF FTGKALLIKT
ASGGKRGGRF EFGFSMYEND KWAADNDIII IQGSDDDLSR VRYVLLKEET LNFIDVLVNN
AHIDMKLLKS IPM
//
