ID   MTC1_PBCVI              Reviewed;         367 AA.
AC   P36216;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   13-SEP-2023, entry version 84.
DE   RecName: Full=Type II methyltransferase M.CviJI {ECO:0000303|PubMed:12654995};
DE            Short=M.CviJI {ECO:0000303|PubMed:2158687};
DE            EC=2.1.1.37;
DE   AltName: Full=Cytosine-specific methyltransferase CviJI;
DE   AltName: Full=Modification methylase CviJI;
GN   Name=CVIJIM {ECO:0000303|PubMed:2158687};
OS   Paramecium bursaria Chlorella virus IL3A (PBCV-IL3A).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Algavirales; Phycodnaviridae; Chlorovirus.
OX   NCBI_TaxID=46019;
OH   NCBI_TaxID=3071; Chlorella.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2158687; DOI=10.1016/0042-6822(90)90225-g;
RA   Shields S.L., Burbank D.E., Grabherr R., van Etten J.L.;
RT   "Cloning and sequencing the cytosine methyltransferase gene M. CviJI from
RT   Chlorella virus IL-3A.";
RL   Virology 176:16-24(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 357-367, AND FUNCTION.
RX   PubMed=8692682; DOI=10.1093/nar/24.13.2463;
RA   Swaminathan N., Mead D.A., McMaster K., George D., van Etten J.L.,
RA   Skowron P.M.;
RT   "Molecular cloning of the three base restriction endonuclease R.CviJI from
RT   eukaryotic Chlorella virus IL-3A.";
RL   Nucleic Acids Res. 24:2463-2469(1996).
RN   [3]
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: A methylase that recognizes the double-stranded sequence 5'-
CC       RGCY-3', methylates C-3 on both strands, and protects the DNA from
CC       cleavage by the CviJI endonuclease. {ECO:0000269|PubMed:8692682,
CC       ECO:0000303|PubMed:12654995}.
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   -!- 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; M27265; AAA88826.1; -; Genomic_DNA.
DR   EMBL; U09001; AAC55063.1; -; Genomic_DNA.
DR   PIR; A46355; A46355.
DR   SMR; P36216; -.
DR   PRO; PR:P36216; -.
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:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR   CDD; cd00315; Cyt_C5_DNA_methylase; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR018117; C5_DNA_meth_AS.
DR   InterPro; IPR001525; C5_MeTfrase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   NCBIfam; TIGR00675; dcm; 1.
DR   PANTHER; PTHR46098; TRNA (CYTOSINE(38)-C(5))-METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR46098:SF1; TRNA (CYTOSINE(38)-C(5))-METHYLTRANSFERASE; 1.
DR   Pfam; PF00145; DNA_methylase; 1.
DR   PRINTS; PR00105; C5METTRFRASE.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS00094; C5_MTASE_1; 1.
DR   PROSITE; PS51679; SAM_MT_C5; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Methyltransferase; Restriction system;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..367
FT                   /note="Type II methyltransferase M.CviJI"
FT                   /id="PRO_0000087871"
FT   DOMAIN          3..367
FT                   /note="SAM-dependent MTase C5-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
FT   ACT_SITE        73
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016,
FT                   ECO:0000255|PROSITE-ProRule:PRU10018"
SQ   SEQUENCE   367 AA;  41861 MW;  15BD56B0354E2ECC CRC64;
     MSFRTLELFA GIAGISHGLR GISTPVAFVE INEDAQKFLK TKFSDASVFN DVTKFTKSDF
     PEDIDMITAG FPCTGFSIAG SRTGFEHKES GLFADVVRIT EEYKPKIVFL ENSHMLSHTY
     NLDVVVKKMD EIGYFCKWVT CRASIIGAHH QRHRWFCLAI RKDYEPEEII VSVNATKFDW
     ENNEPPCQVD NKSYENSTLV RLAGYSVVPD QIRYAFTGLF TGDFESSWKT TLTPGTIIGT
     EHKKMKGTYD KVINGYYEND VYYSFSRKEV HRAPLNISVK PRDIPEKHNG KTLVDREMIK
     KYWCTPCASY GTATAGCNVL TDRQSHALPT QVRFSYRGVC GRHLSGIWCA WLMGYDQEYL
     GYLVQYD
//