ID   MTE5_ECOLX              Reviewed;         298 AA.
AC   P04393;
DT   20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-1987, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Type II methyltransferase M.EcoRV {ECO:0000303|PubMed:12654995};
DE            Short=M.EcoRV {ECO:0000303|PubMed:12654995};
DE            EC=2.1.1.72;
DE   AltName: Full=Adenine-specific methyltransferase EcoRV;
DE   AltName: Full=Modification methylase EcoRV;
GN   Name=ecoRVM;
OS   Escherichia coli.
OG   Plasmid pLB1 {ECO:0000303|PubMed:6328432}, and
OG   Plasmid pLG13 {ECO:0000303|Ref.2}.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-11; 13-24 AND
RP   26-59, AND FUNCTION.
RC   STRAIN=J62; PLASMID=pLB1 {ECO:0000303|PubMed:6328432};
RX   PubMed=6328432; DOI=10.1093/nar/12.8.3659;
RA   Bougueleret L., Schwarzstein M., Tsugita A., Zabeau M.;
RT   "Characterization of the genes coding for the Eco RV restriction and
RT   modification system of Escherichia coli.";
RL   Nucleic Acids Res. 12:3659-3676(1984).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-45.
RC   PLASMID=pLG13 {ECO:0000303|Ref.2};
RA   Kraev A.S., Kravets A.N., Chernov B.K., Skryabin K.G., Baev A.A.;
RT   "The EcoRV restriction-modification system: genes, enzymes, synthetic
RT   substrates.";
RL   Mol. Biol. (Mosk.) 19:236-242(1985).
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'-GATATC-3', methylates A-2 on both strands, and
CC       protects the DNA from cleavage by the EcoRV endonuclease.
CC       {ECO:0000303|PubMed:12654995, ECO:0000305|PubMed:6328432}.
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; X00530; CAA25209.1; -; Genomic_DNA.
DR   EMBL; M19941; AAA24614.1; -; Genomic_DNA.
DR   PIR; A00557; XYECR5.
DR   RefSeq; NP_863581.1; NC_005019.1.
DR   RefSeq; WP_011117660.1; NC_005019.1.
DR   AlphaFoldDB; P04393; -.
DR   SMR; P04393; -.
DR   PRO; PR:P04393; -.
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; IPR012263; M_m6A_EcoRV.
DR   InterPro; IPR012327; MeTrfase_D12.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR30481; PTHR30481; 1.
DR   Pfam; PF02086; MethyltransfD12; 1.
DR   PIRSF; PIRSF000398; M_m6A_EcoRV; 1.
DR   PRINTS; PR00505; D12N6MTFRASE.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR00571; dam; 1.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; DNA-binding; Methyltransferase; Plasmid;
KW   Restriction system; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..298
FT                   /note="Type II methyltransferase M.EcoRV"
FT                   /id="PRO_0000087971"
FT   CONFLICT        22
FT                   /note="C -> W (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   298 AA;  34639 MW;  5FF2263E733574D5 CRC64;
     MKDKVFVPPI KSQGIKTKLV PCIKRIVPKN FNGVWVEPFM GTGVVAFNVA PKDALLCDTN
     PHLISFYNAL KNKDITGDLV KDFLYREGEK LLLSNGEYYY EVRERFNNYK EPLDFLFLNR
     SCFNGMIRFN SKGGFNVPFC KKPNRFAQAY ITKISNQVDR ISEIISKGNY TFLCQSFEKT
     IGMVNRDDVV YCDPPYIGRH VDYFNSWGER DERLLFETLS SLNATFITST WHHNDYRENK
     YVRDLWSSFR ILTKEHFYHV GASEKNRSPM VEALITNIAK DIIDHIEKSS GDILVIEE