ID   MTC1_PBCVC              Reviewed;         260 AA.
AC   Q01511;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   13-SEP-2023, entry version 94.
DE   RecName: Full=Type II methyltransferase M.CviBI {ECO:0000303|PubMed:12654995};
DE            Short=M.CviBI {ECO:0000303|PubMed:1427082};
DE            EC=2.1.1.72;
DE   AltName: Full=Adenine-specific methyltransferase CviBI;
DE   AltName: Full=Modification methylase CviBI;
GN   Name=CVIBIM {ECO:0000303|PubMed:1427082};
OS   Paramecium bursaria Chlorella virus NC1A (PBCV-NC1A).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Algavirales; Phycodnaviridae; Chlorovirus.
OX   NCBI_TaxID=46020;
OH   NCBI_TaxID=3071; Chlorella.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX   PubMed=1427082; DOI=10.1016/0378-1119(92)90155-i;
RA   Kan T.N., Li L., Chandrasegaran S.;
RT   "Cloning, sequencing, overproduction, and purification of M. CviBI (GANTC)
RT   methyltransferase from Chlorella virus NC-1A.";
RL   Gene 121:1-7(1992).
RN   [2]
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: A alpha subtype methylase, recognizes the double-stranded
CC       sequence 5'-GANTC-3', methylates A-2 on both strands, and protects the
CC       DNA from cleavage by the CviBI endonuclease.
CC       {ECO:0000303|PubMed:12654995, ECO:0000305|PubMed:1427082}.
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   -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; M96366; AAA88829.1; -; Genomic_DNA.
DR   SMR; Q01511; -.
DR   REBASE; 3352; M.CviBI.
DR   PRO; PR:Q01511; -.
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; IPR012263; M_m6A_EcoRV.
DR   InterPro; IPR012327; MeTrfase_D12.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   NCBIfam; TIGR00571; dam; 1.
DR   PANTHER; PTHR30481; DNA ADENINE METHYLASE; 1.
DR   PANTHER; PTHR30481:SF3; DNA ADENINE 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.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Methyltransferase; Restriction system;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..260
FT                   /note="Type II methyltransferase M.CviBI"
FT                   /id="PRO_0000087947"
FT   BINDING         7
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         11
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         54
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         177
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   260 AA;  30705 MW;  7AB57C5089EDD039 CRC64;
     MKPIVKWSGG KTDELKRFED YIPSDCSTFI EPFAGGAATF FHVGNQFENK VLSDVHVELV
     ALYRAIANGK SQAIYDFMKS HANDEKTYYE VRSWKPEDYV DVASRFYYLR KTCFRGMMRY
     NKNGGFNVPF GRYKTYNFED IINEEYYNIL KDTIILEKSF DYIFETYNDS SNFVFLDPPY
     DSVFTDYGYC SFGKEEHVRL SNFFKTTKNK CLMVIGATDF IRELYDGYIH TEYEKKYRFK
     LHSGRVGDEI NTTHLVIKNY
//