ID M4SQ35_9CAUD Unreviewed; 302 AA.
AC M4SQ35;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=CPLG_00151 {ECO:0000313|EMBL:AGH57405.1};
OS Cyanophage S-SSM2.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Kyanoviridae; Ahtivirus; Ahtivirus sagseatwo.
OX NCBI_TaxID=536464 {ECO:0000313|EMBL:AGH57405.1, ECO:0000313|Proteomes:UP000225134};
RN [1] {ECO:0000313|EMBL:AGH57405.1, ECO:0000313|Proteomes:UP000225134}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S-SSM2 {ECO:0000313|EMBL:AGH57405.1,
RC ECO:0000313|Proteomes:UP000225134};
RG The Broad Institute Genome Sequencing Platform;
RA Henn M.R., Sullivan M.S., Osburne M.S., Levin J., Malboeuf C., Casali M.,
RA Russ C., Lennon N., Chapman S.B., Erlich R., Young S.K., Yandava C.,
RA Zeng Q., Alvarado L., Anderson S., Berlin A., Chen Z., Freedman E.,
RA Gellesch M., Goldberg J., Green L., Griggs A., Gujja S., Heilman E.R.,
RA Heiman D., Hollinger A., Howarth C., Larson L., Mehta T., Pearson M.,
RA Roberts A., Ryan E., Saif S., Shea T., Shenoy N., Sisk P., Stolte C.,
RA Sykes S., White J., Yu Q., Coleman M.L., Huang K.H., Weigele P.R.,
RA DeFrancesco A.S., Kern S.E., Thompson L.R., Fu R., Hombeck B.,
RA Chisholm S.W., Haas B., Nusbaum C., Birren B.;
RT "The Genome Sequence of Cyanophage S-SSM2.";
RL Submitted (NOV-2010) 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; JF974292; AGH57405.1; -; Genomic_DNA.
DR REBASE; 62396; M.CphSSM2ORF151P.
DR Proteomes; UP000225134; Genome.
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; IPR012263; M_m6A_EcoRV.
DR InterPro; IPR012327; MeTrfase_D12.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR30481; DNA ADENINE METHYLASE; 1.
DR PANTHER; PTHR30481:SF2; MODIFICATION 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.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
SQ SEQUENCE 302 AA; 35260 MW; 4028B9E3C444D556 CRC64;
MKKLKTPLRY PGGKSRATKK LAQFLPNMDE IREFREPFLG GGSVALYMTQ MYPHLSVWVN
DLYVPLVDFW QQLQSEGQQM RDQLIQLKYR YPDPTSAKVL FLEAKEYLSK DVRNTTALQR
AISFYIVNKC SFSGLTEASS FSKAASESNF SVRGIDNLPY YQQAIRNWKI TNYSYQQMIA
KGSDLFIYLD PPYDIKDNLY GRKGNMHARF NHDTFAADCN QYKDTVKMMV SYNTTNLIKE
RFVEWSPYEY DHTYTMRSVG DYMSDQKERK ELVLINYGIR SELPLEGLSE LNQSEQEESS
TQ
//
