ID M1I3P8_9PHYC Unreviewed; 323 AA.
AC M1I3P8;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 13-SEP-2023, entry version 19.
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=NYs-1_810R {ECO:0000313|EMBL:AGE58892.1};
GN ORFNames=PBCVNYs1_810R {ECO:0000313|EMBL:AGE58892.1};
OS Paramecium bursaria Chlorella virus NYs1.
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC Algavirales; Phycodnaviridae; Chlorovirus.
OX NCBI_TaxID=83442 {ECO:0000313|EMBL:AGE58892.1};
RN [1] {ECO:0000313|EMBL:AGE58892.1}
RP NUCLEOTIDE SEQUENCE.
RA Jeanniard A., Dunigan D.D., Gurnon J.R., Agarkova I., Kang M., Vitek J.,
RA Duncan G., McClung O.W., Larsen M., Claverie J.-M., Van Etten J.L.,
RA Blanc G.;
RT "Towards defining the chloroviruses: a genomic journey through a genus of
RT large DNA viruses.";
RL Submitted (OCT-2012) 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};
CC -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC {ECO:0000256|ARBA:ARBA00006594}.
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DR EMBL; JX997183; AGE58892.1; -; Genomic_DNA.
DR REBASE; 60603; M.CviNYs1ORF810P.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC.
DR Gene3D; 1.10.1020.10; Adenine-specific Methyltransferase, Domain 2; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR023095; Ade_MeTrfase_dom_2.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR012263; M_m6A_EcoRV.
DR InterPro; IPR012327; MeTrfase_D12.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR NCBIfam; TIGR00571; dam; 1.
DR PANTHER; PTHR30481; DNA ADENINE METHYLASE; 1.
DR PANTHER; PTHR30481:SF3; DNA ADENINE METHYLASE; 1.
DR Pfam; PF02086; MethyltransfD12; 1.
DR PIRSF; PIRSF000398; M_m6A_EcoRV; 1.
DR PRINTS; PR00505; D12N6MTFRASE.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:AGE58892.1};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AGE58892.1}.
SQ SEQUENCE 323 AA; 37618 MW; 11EBD00896D35331 CRC64;
MLRAISISLL FLLGILFWNM SQDPSEPLFR PCNMSIYFIS TKSSFYFVYI DQFTVIAMSS
PFLKWVGGKQ KLTKEIIPLF PTNIDTYHEP FLGGGSVLLA VLNSDIKIKK IRANDLNAYL
VRTYIDVRDN TEELITSLKD LENSEEDYYK NRKLFNELKK NGHFSVKASA LFIYLNKTCF
RGLYRESPNG FNVSFGHYKN PDYIQADLLR DWSNKIKNVE FSCLPYQDFL HEVRENDFVY
LDPPYVPENK TSFTKYNISD FLDHDRLFSI VKSLPRFVMS NSKTEHTLSA FAEFEILEII
ARRSINSKKP GSTTTEIIIH NMR
//
