DNMT_FRG3G
ID DNMT_FRG3G Reviewed; 214 AA.
AC Q67472;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Probable DNA (cytosine-5)-methyltransferase;
DE EC=2.1.1.37;
DE AltName: Full=Orphan methyltransferase M.Fvi3IP {ECO:0000303|PubMed:12654995};
DE Short=M.Fvi3IP {ECO:0000303|PubMed:12654995};
GN ORFNames=FV3-083R;
OS Frog virus 3 (isolate Goorha) (FV-3).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC Pimascovirales; Iridoviridae; Alphairidovirinae; Ranavirus.
OX NCBI_TaxID=654924;
OH NCBI_TaxID=30343; Dryophytes versicolor (chameleon treefrog).
OH NCBI_TaxID=8404; Lithobates pipiens (Northern leopard frog) (Rana pipiens).
OH NCBI_TaxID=45438; Lithobates sylvaticus (Wood frog) (Rana sylvatica).
OH NCBI_TaxID=8316; Notophthalmus viridescens (Eastern newt) (Triturus viridescens).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROBABLE FUNCTION, SUBUNIT,
RP DEVELOPMENTAL STAGE, AND MUTAGENESIS OF CYS-17.
RX PubMed=7636474; DOI=10.1099/0022-1317-76-8-1937;
RA Kaur K., Rohozinski J., Goorha R.;
RT "Identification and characterization of the frog virus 3 DNA
RT methyltransferase gene.";
RL J. Gen. Virol. 76:1937-1943(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15165820; DOI=10.1016/j.virol.2004.02.019;
RA Tan W.G., Barkman T.J., Gregory Chinchar V., Essani K.;
RT "Comparative genomic analyses of frog virus 3, type species of the genus
RT Ranavirus (family Iridoviridae).";
RL Virology 323:70-84(2004).
RN [3]
RP DNA METHYLATION.
RX PubMed=6255678; DOI=10.1016/0042-6822(80)90290-1;
RA Willis D.B., Granoff A.;
RT "Frog virus 3 DNA is heavily methylated at CpG sequences.";
RL Virology 107:250-257(1980).
RN [4]
RP DNA METHYLATION, AND PROBABLE FUNCTION.
RX PubMed=2445102; DOI=10.1016/0042-6822(87)90187-5;
RA Essani K., Goorha R., Granoff A.;
RT "Mutation in a DNA-binding protein reveals an association between DNA-
RT methyltransferase activity and a 26,000-Da polypeptide in frog virus 3-
RT infected cells.";
RL Virology 161:211-217(1987).
RN [5]
RP NOMENCLATURE.
RX PubMed=12654995; DOI=10.1093/nar/gkg274;
RA Roberts R.J., Belfort M., Bestor T., Bhagwat A.S., Bickle T.A.,
RA Bitinaite J., Blumenthal R.M., Degtyarev S.K., Dryden D.T., Dybvig K.,
RA Firman K., Gromova E.S., Gumport R.I., Halford S.E., Hattman S.,
RA Heitman J., Hornby D.P., Janulaitis A., Jeltsch A., Josephsen J., Kiss A.,
RA Klaenhammer T.R., Kobayashi I., Kong H., Krueger D.H., Lacks S.,
RA Marinus M.G., Miyahara M., Morgan R.D., Murray N.E., Nagaraja V.,
RA Piekarowicz A., Pingoud A., Raleigh E., Rao D.N., Reich N., Repin V.E.,
RA Selker E.U., Shaw P.C., Stein D.C., Stoddard B.L., Szybalski W.,
RA Trautner T.A., Van Etten J.L., Vitor J.M., Wilson G.G., Xu S.Y.;
RT "A nomenclature for restriction enzymes, DNA methyltransferases, homing
RT endonucleases and their genes.";
RL Nucleic Acids Res. 31:1805-1812(2003).
CC -!- FUNCTION: This is probably the methylase that recognizes and modifies
CC 5'-CpG-3'. {ECO:0000305|PubMed:7636474}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-
CC methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:13681, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:11370,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:85452, ChEBI:CHEBI:85454; EC=2.1.1.37;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10018};
CC -!- SUBUNIT: Probably requires another subunit for function.
CC {ECO:0000305|PubMed:7636474}.
CC -!- DEVELOPMENTAL STAGE: Transcribed in the delayed early phase of
CC replication. {ECO:0000269|PubMed:7636474}.
CC -!- MISCELLANEOUS: About 20% of the cytosine bases in the genome are
CC methylated on 5'-CpG-3' sequences. {ECO:0000269|PubMed:2445102,
CC ECO:0000269|PubMed:6255678}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. C5-methyltransferase family. {ECO:0000255|PROSITE-
CC ProRule:PRU01016}.
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DR EMBL; U15575; AAA86959.1; -; Genomic_DNA.
DR EMBL; AY548484; AAT09743.1; -; Genomic_DNA.
DR RefSeq; YP_031662.1; NC_005946.1.
DR SMR; Q67472; -.
DR REBASE; 2843; M.Fvi3IP.
DR GeneID; 2947802; -.
DR KEGG; vg:2947802; -.
DR Proteomes; UP000008770; Genome.
DR GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR018117; C5_DNA_meth_AS.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS00094; C5_MTASE_1; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; DNA-binding; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..214
FT /note="Probable DNA (cytosine-5)-methyltransferase"
FT /id="PRO_0000410586"
FT ACT_SITE 62
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01016,
FT ECO:0000255|PROSITE-ProRule:PRU10018"
FT MUTAGEN 17
FT /note="C->W: Loss of methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:7636474"
SQ SEQUENCE 214 AA; 24730 MW; C0CB3D616F36A222 CRC64;
MRILDLFSGT HSVPKACAQR EGWSCVTVDL ADSDYNVDVL EWDYTKDLKP REFDVVWASP
PCRYFSKLRE SNIGRGGMTK KSVKEDLETK GLPLLRRAME IIAYLQPKKF IVENPDTGRM
KEYITEWPHY VVDYCAYSDW GYRKRTRLWT DIEGFVPKTC AGKESCPNME RNPSSGRWRH
VLATDAGGRG RKGTTRRLRY RVPPAIIVEL LDLC
