ID   T3MO_BPP1               Reviewed;         646 AA.
AC   P08763;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1988, sequence version 1.
DT   27-MAR-2024, entry version 107.
DE   RecName: Full=Type III restriction-modification enzyme EcoPI Mod subunit;
DE            Short=M.EcoPI;
DE            EC=2.1.1.72;
DE   AltName: Full=EcoPI methyltransferase;
DE   AltName: Full=Type III methyltransferase M.EcoPI {ECO:0000303|PubMed:12654995};
GN   Name=mod {ECO:0000303|PubMed:2837577};
OS   Escherichia phage P1 (Bacteriophage P1).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Punavirus; Punavirus P1.
OX   NCBI_TaxID=2886926;
OH   NCBI_TaxID=543; Enterobacteriaceae.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-5, FUNCTION, AND
RP   MUTAGENESIS OF THR-289 AND THR-316.
RX   PubMed=2837577; DOI=10.1016/0022-2836(88)90330-0;
RA   Huembelin M., Suri B., Rao D.N., Hornby D.P., Eberle H., Pripfl T.,
RA   Kenel S., Bickle T.A.;
RT   "Type III DNA restriction and modification systems EcoP1 and EcoP15.
RT   Nucleotide sequence of the EcoP1 operon, the EcoP15 mod gene and some EcoP1
RT   mod mutants.";
RL   J. Mol. Biol. 200:23-29(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND PRESENCE OF INSERTION
RP   SEQUENCE IS5.
RX   PubMed=15489417; DOI=10.1128/jb.186.21.7032-7068.2004;
RA   Lobocka M.B., Rose D.J., Plunkett G. III, Rusin M., Samojedny A.,
RA   Lehnherr H., Yarmolinsky M.B., Blattner F.R.;
RT   "Genome of bacteriophage P1.";
RL   J. Bacteriol. 186:7032-7068(2004).
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).
RN   [4]
RP   FUNCTION, AND SUBUNIT.
RX   PubMed=11178902; DOI=10.1006/jmbi.2000.4411;
RA   Janscak P., Sandmeier U., Szczelkun M.D., Bickle T.A.;
RT   "Subunit assembly and mode of DNA cleavage of the type III restriction
RT   endonucleases EcoP1I and EcoP15I.";
RL   J. Mol. Biol. 306:417-431(2001).
CC   -!- FUNCTION: A beta subtype methylase that binds the system-specific DNA
CC       recognition site 5'-AGACC-3' and methylates A-3 (of only 1 strand as
CC       the other does not have an A residue). DNA restriction requires both
CC       the Res and Mod subunits. {ECO:0000269|PubMed:11178902,
CC       ECO:0000269|PubMed:2837577, 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 + 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   -!- SUBUNIT: Homodimer. A heterotetramer with stoichiometry Res(2)Mod(2).
CC       {ECO:0000269|PubMed:11178902}.
CC   -!- MISCELLANEOUS: This R-M system is also called EcoP1 and EcoP1I.
CC       {ECO:0000303|PubMed:11178902, ECO:0000303|PubMed:2837577}.
CC   -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC       {ECO:0000305}.
CC   -!- CAUTION: This gene is interrupted by an IS5 insertion sequence in the
CC       phage P1 reference proteome UP000008091. {ECO:0000269|PubMed:15489417}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AF234172; Type=Miscellaneous discrepancy; Evidence={ECO:0000305};
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DR   EMBL; X06287; CAA29614.1; -; Genomic_DNA.
DR   EMBL; AF234172; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; S01351; S01351.
DR   SMR; P08763; -.
DR   REBASE; 3390; M.EcoPI.
DR   PRO; PR:P08763; -.
DR   Proteomes; UP000008091; Genome.
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   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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   InterPro; IPR041405; T3RM_EcoP15I_C.
DR   PANTHER; PTHR13370; RNA METHYLASE-RELATED; 1.
DR   PANTHER; PTHR13370:SF16; TYPE III RESTRICTION-MODIFICATION ENZYME STYLTI MOD SUBUNIT; 1.
DR   Pfam; PF01555; N6_N4_Mtase; 1.
DR   Pfam; PF18273; T3RM_EcoP15I_C; 1.
DR   PIRSF; PIRSF015855; TypeIII_Mtase_mKpnI; 1.
DR   PRINTS; PR00506; D21N6MTFRASE.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; DNA-binding; Methyltransferase;
KW   Reference proteome; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..646
FT                   /note="Type III restriction-modification enzyme EcoPI Mod
FT                   subunit"
FT                   /id="PRO_0000088030"
FT   REGION          123..126
FT                   /note="Binding of S-adenosyl methionine"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         289
FT                   /note="T->I: In c2-134; defective in DNA modification."
FT                   /evidence="ECO:0000269|PubMed:2837577"
FT   MUTAGEN         316
FT                   /note="T->I: In c2-440; defective in DNA modification."
FT                   /evidence="ECO:0000269|PubMed:2837577"
SQ   SEQUENCE   646 AA;  73486 MW;  DB2D8724777A5412 CRC64;
     MKKETIFSEV ETANSKQLAV LKANFPQCFD KNGAFIQEKL LEIIRASEVE LSKESYSLNW
     LGKSYARLLA NLPPKTLLAE DKTHNQQEEN KNSQNLLIKG DNLEVLKHMV NAYAEKVNMI
     YIDPPYNTGK DGFVYNDDRK FTPEQLSELA GIELDEANRI LEFTTKGSSS HSAWLTFIYP
     RLYIARELLK EDGVIFISID DNEDKQLGLL CDEVFGQGNF VAKLPTIMNL KGNHDNFGFS
     DTHEYIYVYA KNKDVCSLGQ FDIDESEVEK EWDEDEYGLF KRADTLKRTG QDASRKSRPK
     GWFPVFINSE NKVYVTDDDK PLNEDDYVLY PVSPTGEELS WSWGKKKIND EFYNLIVIDI
     KDGKNIYKKQ RPALGELPTK KPKSIWYKPE YSTSTATTEL KNLLGAKLFE GPKPVPLITD
     LVKIGTKKDS LVLDFFAGSG TTAEAVAYLN EKDSGCRNFI CIQKDEVINK TKNAYSLGYR
     SIFEITKKRI QEVFKKSTTT SDNAAKIGFK VIHTIDDFRA KVESELTLTN HTFFDDAVLT
     PEQYDALLTT WCVYDGSLLT TPIEDVDLSG YTAHFCNGRL YLIAPNFTSE ALKALLQKLD
     SDEDFAPNKV VFYGCNFESA KQRELNEALK SYANKKSIEL DLVVRN
//