ID   MTC2_PBCV1              Reviewed;         326 AA.
AC   P31118; Q84569;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 2.
DT   03-AUG-2022, entry version 95.
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=114055; 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   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).
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   -!- 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; AAC96619.1; -; Genomic_DNA.
DR   PIR; S35442; S27901.
DR   PIR; T17743; T17743.
DR   RefSeq; NP_048600.2; NC_000852.5.
DR   GeneID; 918436; -.
DR   KEGG; vg:918436; -.
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; -; 1.
DR   Gene3D; 3.40.50.150; -; 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; SSF53335; 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;  37492 MW;  8CC1FC75D85F0D89 CRC64;
     MNRIGYIGSK LKLKDWIFEE ISKRTDDTYT KFADLFAGSC IMTHEALEKK YECISNDLET
     YSYVIMNGLK CPFSDKLQNI IETLDDLDTK DMVIPGFVTL TYSPRGNRMY FTEDIAMRID
     IIRENIERMK ERVSTDEYNF LLASLLTSAD SVKNTSVVYG AYLKKFKKTA LKRMVFAPLH
     TRSTTVTLET FNEDATELEI KTDIAYVDPP YNSRQYGANY FVLNQILTPK EIGNGVTGLP
     EYKKSSFCRK QEVAMSFHKM LKNVSARLFV ISYSSESLLS KGDMVALLSQ YGKCEVVVRN
     HKRFKAQISA VGNDVEEYLF FVYIEQ