ID   MTC2_PBCV1              Reviewed;         326 AA.
AC   P31118; O41015; Q84569;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   27-MAR-2024, sequence version 3.
DT   27-MAR-2024, entry version 98.
DE   RecName: Full=Type II methyltransferase M.CviAII {ECO:0000303|PubMed:12654995};
DE            Short=M.CviAII {ECO:0000303|PubMed:1437552};
DE            EC=2.1.1.72 {ECO:0000305|PubMed:1437552};
DE   AltName: Full=Adenine-specific methyltransferase CviAII;
DE   AltName: Full=Modification methylase CviAII;
GN   Name=CVIAIIM; OrderedLocusNames=A251R;
OS   Paramecium bursaria Chlorella virus 1 (PBCV-1).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Algavirales; Phycodnaviridae; Chlorovirus.
OX   NCBI_TaxID=10506;
OH   NCBI_TaxID=3071; Chlorella.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND BIOPHYSICOCHEMICAL
RP   PROPERTIES.
RX   PubMed=1437552; DOI=10.1093/nar/20.20.5351;
RA   Zhang Y., Nelson M., Nietfeldt J.W., Burbank D.E., van Etten J.L.;
RT   "Characterization of Chlorella virus PBCV-1 CviAII restriction and
RT   modification system.";
RL   Nucleic Acids Res. 20:5351-5356(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION.
RX   PubMed=7831789; DOI=10.1016/s0042-6822(95)80049-2;
RA   Lu Z., Li Y., Zhang Y., Kutish G.F., Rock D.L., van Etten J.L.;
RT   "Analysis of 45 kb of DNA located at the left end of the chlorella virus
RT   PBCV-1 genome.";
RL   Virology 206:339-352(1995).
RN   [3]
RP   SEQUENCE REVISION TO ASN-115 AND GLY-199.
RA   Dunigan D.D., Blanc G., Duncan G.A., Gurnon J.R., Jeanniard A.,
RA   McClung O.W., Upton C., van Etten J.L.;
RL   Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NOMENCLATURE, AND SUBTYPE.
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).
RN   [5]
RP   INDUCTION.
RX   PubMed=19828609; DOI=10.1128/jvi.01698-09;
RA   Yanai-Balser G.M., Duncan G.A., Eudy J.D., Wang D., Li X., Agarkova I.V.,
RA   Dunigan D.D., Van Etten J.L.;
RT   "Microarray analysis of Paramecium bursaria chlorella virus 1
RT   transcription.";
RL   J. Virol. 84:532-542(2010).
CC   -!- FUNCTION: An alpha subtype methylase that recognizes the double-
CC       stranded sequence 5'-CATG-3', methylates A-2 on both strands and
CC       protects the DNA from cleavage by the CviAII endonuclease.
CC       {ECO:0000303|PubMed:12654995, ECO:0000305|PubMed:1437552}.
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:0000305|PubMed:1437552};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 8.5-9.0. {ECO:0000269|PubMed:1437552};
CC   -!- INDUCTION: Expressed in the early phase of the viral replicative cycle.
CC       {ECO:0000269|PubMed:19828609}.
CC   -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; M86639; AAB92381.1; -; Genomic_DNA.
DR   EMBL; JF411744; AAC97062.2; -; Genomic_DNA.
DR   PIR; S35442; S27901.
DR   PIR; T17743; T17743.
DR   RefSeq; NP_048600.2; NC_000852.5.
DR   REBASE; 3542; M.CviAII.
DR   GeneID; 918436; -.
DR   KEGG; vg:918436; -.
DR   OrthoDB; 41175at10239; -.
DR   PRO; PR:P31118; -.
DR   Proteomes; UP000000862; Genome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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   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; IPR012327; MeTrfase_D12.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF02086; MethyltransfD12; 1.
DR   PRINTS; PR00505; D12N6MTFRASE.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Methyltransferase; Reference proteome; Restriction system;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..326
FT                   /note="Type II methyltransferase M.CviAII"
FT                   /id="PRO_0000087950"
SQ   SEQUENCE   326 AA;  37421 MW;  D590FC07DA794ADD CRC64;
     MNRIGYIGSK LKLKDWIFEE ISKRTDDTYT KFADLFAGSC IMTHEALEKK YECISNDLET
     YSYVIMNGLK CPFSDKLQNI IETLDDLDTK DMVIPGFVTL TYSPRGNRMY FTEDNAMRID
     IIRENIERMK ERVSTDEYNF LLASLLTSAD SVKNTSVVYG AYLKKFKKTA LKRMVFAPLH
     TRSTTVTLET FNEDATELGI KTDIAYVDPP YNSRQYGANY FVLNQILTPK EIGNGVTGLP
     EYKKSSFCRK QEVAMSFHKM LKNVSARLFV ISYSSESLLS KGDMVALLSQ YGKCEVVVRN
     HKRFKAQISA VGNDVEEYLF FVYIEQ
//