MTR1_PBCVX
ID MTR1_PBCVX Reviewed; 379 AA.
AC P52284;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Type II methyltransferase M.CvrRI {ECO:0000303|PubMed:12654995};
DE Short=M.CviRI {ECO:0000303|PubMed:2014170};
DE EC=2.1.1.72;
DE AltName: Full=Adenine-specific methyltransferase CviRI;
DE AltName: Full=Modification methylase CviRI;
GN Name=CVIRIM;
OS Paramecium bursaria Chlorella virus XZ-6E (PBCV-XZ-6E).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC Algavirales; Phycodnaviridae; Chlorovirus; unclassified Chlorovirus.
OX NCBI_TaxID=36360;
OH NCBI_TaxID=114055; Chlorella.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=2014170; DOI=10.1093/nar/19.2.307;
RA Stefan G., Xia Y., van Etten J.L.;
RT "Molecular cloning and characterization of the gene encoding the adenine
RT methyltransferase M.CviRI from Chlorella virus XZ-6E.";
RL Nucleic Acids Res. 19:307-311(1991).
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 gamma subtype methylase, recognizes the double-stranded
CC sequence 5'-TGCA-3', methylates A-4 on both strands, and protects the
CC DNA from cleavage by the CviRI endonuclease.
CC {ECO:0000303|PubMed:12654995, ECO:0000305|PubMed:2014170}.
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; M38173; AAA42900.1; -; Genomic_DNA.
DR SMR; P52284; -.
DR REBASE; 3355; M.CviRI.
DR PRO; PR:P52284; -.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro.
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; 3.40.50.150; -; 1.
DR InterPro; IPR003356; DNA_methylase_A-5.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF02384; N6_Mtase; 1.
DR SUPFAM; SSF53335; SSF53335; 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..379
FT /note="Type II methyltransferase M.CvrRI"
FT /id="PRO_0000087949"
SQ SEQUENCE 379 AA; 42815 MW; 22758935BB702BFA CRC64;
MKLFEDKSVE FHKRLSKKER SDGGVFFTPK DIRDIVFEEL GDFEPTNILE PTCGTGEFIS
DCRKVYKNSR IIGVEIDPRS AELARDGSKN EIIVHDFMTW DTDEKFDLII GNPPYFTRPT
GFKHDPSVVK CRSNICIEVL HKCITRHLAD NGMLAMVLPV SILNSKFYTP TIDLITDTMD
VVSARAIKKN NFMGTNVRVM VFIIRKRTPG FVSKYTFKTS LGKVIINPDG ERLGSIVSGK
KTIGSLNVNI SFGVTLASVK EYFVDKSCSG SFPLICYNNI AKKGDLLFVS DKYSKKRFNG
RAILIPRGYA HGDYSFNFID YTNDYFIIEN HVIAITGEDC VLDIIAKSFA DHRTREFCRL
LCSSGDISKD YVKEIPVFG