ID   MTEC_ENTCL              Reviewed;         452 AA.
AC   P14827;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Type II methyltransferase M.EcaI {ECO:0000303|PubMed:12654995};
DE            Short=M.EcaI {ECO:0000303|PubMed:2183182};
DE            EC=2.1.1.72 {ECO:0000305|PubMed:2183182};
DE   AltName: Full=Adenine-specific methyltransferase EcaI;
DE   AltName: Full=Modification methylase EcaI;
GN   Name=ecaIM;
OS   Enterobacter cloacae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex.
OX   NCBI_TaxID=550;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PROBABLE CATALYTIC
RP   ACTIVITY.
RC   STRAIN=DSM 30056 / WS 10183;
RX   PubMed=2183182; DOI=10.1093/nar/18.2.355;
RA   Brenner V., Venetianer P., Kiss A.;
RT   "Cloning and nucleotide sequence of the gene encoding the EcaI DNA
RT   methyltransferase.";
RL   Nucleic Acids Res. 18:355-359(1990).
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 beta subtype methylase, recognizes the double-stranded
CC       sequence 5'-GGTNACC-3', methylates A-5 on both strands and protects the
CC       DNA from cleavage by the EcaI endonuclease.
CC       {ECO:0000303|PubMed:12654995, ECO:0000305|PubMed:2183182}.
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:2183182};
CC   -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X17111; CAA34968.1; -; Genomic_DNA.
DR   PIR; S07886; S07886.
DR   AlphaFoldDB; P14827; -.
DR   SMR; P14827; -.
DR   REBASE; 3365; M.EcaI.
DR   PRO; PR:P14827; -.
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; IPR002941; DNA_methylase_N4/N6.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR002295; N4/N6-MTase_EcoPI_Mod-like.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF01555; N6_N4_Mtase; 1.
DR   PRINTS; PR00506; D21N6MTFRASE.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Methyltransferase; Restriction system;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..452
FT                   /note="Type II methyltransferase M.EcaI"
FT                   /id="PRO_0000087958"
SQ   SEQUENCE   452 AA;  51112 MW;  C19D9582E4AE9535 CRC64;
     MAVGLNKKEI DGPASQRAVA CDLEPALPPI GARVTLNYPG KMDESIILQK KDTKYLRVGS
     DFAKESSLIL PNSFIWSDNS LALNRLMVEG KKAKLIYLDP PYATGMGFSS RSNEHAYDDC
     LTEAAYLEFM RRRLILMREI LDDDGTIYVH IGHQMLGELK CLLDEIFGRE RFINLITRRK
     CSSKNSTKNN FANLNDYILC YSKGKKYIWN RPLKKPDAEW LAKEYPKTDS KGQFKLVPIH
     APGVRHGATG GEWKGMLPPP GKHWQYTPEK LDILDASGDI HWSKTGNPRR KVYLTDDKSI
     GYTDYWEEFR DAHHQSILVT GYPTEKNFNM MKLIVGASSN PGDLVIDPFC GSGSTLHAAS
     LLQRKWIGID ESLFAAKTVM KRFAIGRAPM GDYVNTSLNK QTELPLSLNE TARHEYVSND
     FNIYVDELTA SVSKNELAEI QKAYRDLKAN QQ