T1ME_ECOLX
ID T1ME_ECOLX Reviewed; 490 AA.
AC Q47282;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Type I restriction enzyme EcoEI methylase subunit {ECO:0000305};
DE Short=M protein;
DE EC=2.1.1.72 {ECO:0000250|UniProtKB:P08957};
DE AltName: Full=Type I methyltransferase M.EcoEI {ECO:0000303|PubMed:12654995};
DE Short=M.EcoEI {ECO:0000303|PubMed:12654995};
GN Name=hsdM;
OS Escherichia coli.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=A58;
RX PubMed=8412658; DOI=10.1111/j.1365-2958.1993.tb01675.x;
RA Murray N.E., Daniel A.S., Cowan G.M., Sharp P.M.;
RT "Conservation of motifs within the unusually variable polypeptide sequences
RT of type I restriction and modification enzymes.";
RL Mol. Microbiol. 9:133-143(1993).
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: The subtype gamma methyltransferase (M) subunit of a type I
CC restriction enzyme. The M and S subunits together form a
CC methyltransferase (MTase) that methylates two adenine residues of the
CC sequence 5'-GAGN(7)ATGC-3'. In the presence of the R subunit the
CC complex can also act as an endonuclease, binding to the same target
CC sequence but cutting the DNA some distance from this site. Whether the
CC DNA is cut or modified depends on the methylation state of the target
CC sequence. When the target site is unmodified, the DNA is cut. When the
CC target site is hemimethylated, the complex acts as a maintenance MTase
CC modifying the DNA so that both strands become methylated. After
CC locating a non-methylated recognition site, the enzyme complex serves
CC as a molecular motor that translocates DNA in an ATP-dependent manner
CC until a collision occurs that triggers cleavage.
CC {ECO:0000250|UniProtKB:P08957, 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 Evidence={ECO:0000250|UniProtKB:P08957};
CC -!- SUBUNIT: The type I restriction/modification system is composed of
CC three polypeptides R, M and S; the restriction enzyme has stoichiometry
CC R(2)M(2)S(1) while the methyltransferase is M(2)S(1).
CC {ECO:0000250|UniProtKB:P08957}.
CC -!- MISCELLANEOUS: Type I restriction and modification enzymes are complex,
CC multifunctional systems which require ATP, S-adenosyl methionine and
CC Mg(2+) as cofactors and, in addition to their endonucleolytic and
CC methylase activities, are potent DNA-dependent ATPases.
CC {ECO:0000250|UniProtKB:P08957}.
CC -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC {ECO:0000305}.
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DR EMBL; L18759; AAD15049.1; -; Genomic_DNA.
DR PIR; I41293; I41293.
DR RefSeq; WP_058649287.1; NZ_NMFU01000051.1.
DR AlphaFoldDB; Q47282; -.
DR SMR; Q47282; -.
DR REBASE; 101119; M.Rga602ORF2367P.
DR REBASE; 157593; M.Rso10709ORF3042P.
DR REBASE; 201010; M.RspNXC14ORF3392P.
DR REBASE; 205293; M.Bso1395ORF934P.
DR REBASE; 211745; M.RphB5ORF556P.
DR REBASE; 211757; M.RspL182ORF1057P.
DR REBASE; 233080; M.Sen4024ORF3807P.
DR REBASE; 256765; M.Ssp9304ORF612P.
DR REBASE; 3386; M.EcoEI.
DR PRO; PR:Q47282; -.
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; 1.20.1260.30; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR022749; D12N6_MeTrfase_N.
DR InterPro; IPR003356; DNA_methylase_A-5.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR038333; T1MK-like_N_sf.
DR Pfam; PF12161; HsdM_N; 1.
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..490
FT /note="Type I restriction enzyme EcoEI methylase subunit"
FT /id="PRO_0000088021"
FT BINDING 163..168
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q89Z59"
FT BINDING 193..195
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q89Z59"
FT BINDING 226
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q89Z59"
SQ SEQUENCE 490 AA; 55620 MW; A8643DEB39981FFB CRC64;
MSISSVIKSL QDIMRKDAGV DGDAQRLGQL SWLLFLKIFD TQEEELELEQ DDYQFPIPQR
YLWRSWAANS EGITGDALLE FVNDDLFPTL KNLTAPIDKN PRGFVVKQAF SDAYNYMKNG
TLLRQVINKL NEIDFSSSQE RHLFGDIYEQ ILRDLQSAGN AGEFYTPRAV TRFMVNRIDP
KLGESIMDPA CGTGGFLACA FDHVKDNYVK TTEDHKTLQQ QIYGVEKKQL PHLLCTTNML
LHGIEVPVQI RHDNTLNKPL SSWDEQVDVI VTNPPFGGTE EDGIEKNFPA EMQTRETADL
FLQLIIEVLA DKGRAAVVLP DGTLFGEGVK TKIKKLLTEE CNLHTIVRLP NGVFNPYTGI
KTNILFFTKG QPTKEVWFYE HPYPDGVKNY SKTKPMKFEE FQAEIDWWGN EADDFASREE
NNQAWKVGID DIIARNFNLD IKNPYQGETI SHDPDELLAQ YQTQQAEIGE LRNQLRDILG
AALAGNKGAN
