ID   MTP7_PSEAI              Reviewed;         574 AA.
AC   P05103;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   19-FEB-2014, sequence version 3.
DT   02-SEP-2026, entry version 109.
DE   RecName: Full=Type II methyltransferase M.PaeR7I {ECO:0000303|PubMed:12654995};
DE            Short=M.PaeR7I {ECO:0000303|PubMed:12654995};
DE            EC=2.1.1.72;
DE   AltName: Full=Adenine-specific methyltransferase PaeR7I;
DE   AltName: Full=Modification methylase PaeR7I;
GN   Name=paeR7IM;
OS   Pseudomonas aeruginosa.
OG   Plasmid pMG7.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Pseudomonadales; Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION AS A MODIFICATION METHYLASE,
RP   AND SUBUNIT.
RX   PubMed=3001639; DOI=10.1093/nar/13.23.8441;
RA   Theriault G., Roy P.H., Howard K.A., Benner J.S., Brooks J.E., Waters A.F.,
RA   Gingeras T.R.;
RT   "Nucleotide sequence of the PaeR7 restriction/modification system and
RT   partial characterization of its protein products.";
RL   Nucleic Acids Res. 13:8441-8461(1985).
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'-CTCGAG-3', methylates A-5 on both strands, and protects the
CC       DNA from cleavage by the PaeR7I endonuclease.
CC       {ECO:0000269|PubMed:3001639, ECO:0000303|PubMed:12654995}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyadenosine in DNA + S-adenosyl-L-methionine = an
CC         N(6)-methyl-2'-deoxyadenosine in DNA + S-adenosyl-L-homocysteine +
CC         H(+); 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   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:3001639}.
CC   -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA27025.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAA27025.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; X03274; CAA27025.1; ALT_SEQ; Genomic_DNA.
DR   PIR; S07366; XYPS7A.
DR   AlphaFoldDB; P05103; -.
DR   SMR; P05103; -.
DR   REBASE; 191894; M.Apa1447ORF1853P.
DR   REBASE; 3477; M.PaeR7I.
DR   REBASE; 353101; M.LxyHY24ORF1216P.
DR   PRO; PR:P05103; -.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006304; P:DNA modification; IEA:InterPro.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR011639; MethylTrfase_TaqI-like_dom.
DR   InterPro; IPR050953; N4_N6_ade-DNA_methylase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR33841:SF5; DNA METHYLASE (MODIFICATION METHYLASE) (METHYLTRANSFERASE)-RELATED; 1.
DR   PANTHER; PTHR33841; DNA METHYLTRANSFERASE YEEA-RELATED; 1.
DR   Pfam; PF07669; Eco57I; 1.
DR   PRINTS; PR00507; N12N6MTFRASE.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Methyltransferase; Plasmid; Restriction system;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..574
FT                   /note="Type II methyltransferase M.PaeR7I"
FT                   /id="PRO_0000087977"
SQ   SEQUENCE   574 AA;  63229 MW;  31ABC8948DD1EFAD CRC64;
     MAFAPSVAHK PVAAAVCPVM AATEALATEG GLEARGAIFT RSEVVDFILD LAGYTEDQPL
     HEKRLLEPSF GGGDFLLPII QRLLSAWRAA RPNGTEVDDL GDAIRAVELH HDTFRSTYAA
     VVALLKREGL SANAATALAD RWLSQGDFLL APLEGQFDFV VGNPPYVRPE LIPAPLLAEY
     RSRYQTMYDR ADIYIPFIER SLTALSAGGN LGFICADRWM KNRYGGPLRS LVAERFHLKV
     YVDMVDTPAF HSDVIAYPAI TIISREGGGA TRIAHRPSID RATLTTLAGL LSAPTLPKDA
     GPVRELARVT NGAEPWLLES SDQMALIRRL EGAFPLLEEA GCKVGIGVAT GADKAFIGDF
     ESLDVEPDRK LPLVTTKDIM TGEVQWRGQG VINPFAESGG LVDLGEYPRL RRYLEARRDV
     IAGRHCAKKA PANWYRTIDR ITPALAARPK LLIPDIKGES HIVFEGGELY PSHNLYYVTS
     DDWDLRALQA VLLSAVSRLF VATYSTKMRG GFLRFQAQYL RRIRIPRWAD VPEPLRRELA
     EAAIKRDVQA CNRAVFRLYG LSHEERSALG GNGE
//