MTM2_MORBO
ID MTM2_MORBO Reviewed; 260 AA.
AC P23192;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Type II methyltransferase M1.MboII {ECO:0000303|PubMed:12654995};
DE Short=M1.MboII {ECO:0000303|PubMed:12654995};
DE EC=2.1.1.72;
DE AltName: Full=Adenine-specific methyltransferase MboII;
DE AltName: Full=DNA MTase MboIIA;
DE AltName: Full=Modification methylase MboII;
DE Short=M.MboII {ECO:0000303|PubMed:2020540};
GN Name=mboIIM {ECO:0000303|PubMed:2020540};
OS Moraxella bovis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Moraxella.
OX NCBI_TaxID=476;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 10900 / DSM 6328 / CIP 70.40 / JCM 17254 / LMG 986 / NCTC
RC 11013;
RX PubMed=2020540; DOI=10.1093/nar/19.5.1007;
RA Bocklage H., Heeger K., Mueller-Hill B.;
RT "Cloning and characterization of the MboII restriction-modification
RT system.";
RL Nucleic Acids Res. 19:1007-1013(1991).
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).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) IN COMPLEX WITH
RP S-ADENOSYL-L-METHIONINE, AND SUBUNIT.
RX PubMed=12954781; DOI=10.1093/nar/gkg713;
RA Osipiuk J., Walsh M.A., Joachimiak A.;
RT "Crystal structure of MboIIA methyltransferase.";
RL Nucleic Acids Res. 31:5440-5448(2003).
CC -!- FUNCTION: A beta subtype methylase that recognizes the double-stranded
CC sequence 5'-GAAGA-3', methylates A-5 on the top strand, and protects
CC the DNA from cleavage by the MboII endonuclease. It is not known if the
CC cytosine of the complementary sequence TCTTC is also methylated by this
CC enzyme. {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: At low concentration exists as a monomer and homodimer
CC (PubMed:12954781). Probably binds to DNA as a monomer (Probable).
CC {ECO:0000269|PubMed:12954781, ECO:0000305|PubMed:12954781}.
CC -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC {ECO:0000305}.
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DR EMBL; X56977; CAA40297.1; -; Genomic_DNA.
DR PIR; S26835; S26835.
DR PDB; 1G60; X-ray; 1.74 A; A/B=1-260.
DR PDBsum; 1G60; -.
DR AlphaFoldDB; P23192; -.
DR SMR; P23192; -.
DR STRING; 476.B0182_06905; -.
DR REBASE; 3441; M1.MboII.
DR BRENDA; 2.1.1.72; 3416.
DR EvolutionaryTrace; P23192; -.
DR PRO; PR:P23192; -.
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; IPR001091; RM_Methyltransferase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF01555; N6_N4_Mtase; 1.
DR PRINTS; PR00508; S21N4MTFRASE.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Methyltransferase; Restriction system;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..260
FT /note="Type II methyltransferase M1.MboII"
FT /id="PRO_0000087967"
FT BINDING 12
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:12954781,
FT ECO:0007744|PDB:1G60"
FT BINDING 30
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:12954781,
FT ECO:0007744|PDB:1G60"
FT BINDING 197
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:12954781,
FT ECO:0007744|PDB:1G60"
FT BINDING 223..225
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:12954781,
FT ECO:0007744|PDB:1G60"
FT BINDING 241..242
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:12954781,
FT ECO:0007744|PDB:1G60"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:1G60"
FT HELIX 12..18
FT /evidence="ECO:0007829|PDB:1G60"
FT STRAND 24..29
FT /evidence="ECO:0007829|PDB:1G60"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:1G60"
FT HELIX 46..63
FT /evidence="ECO:0007829|PDB:1G60"
FT STRAND 64..74
FT /evidence="ECO:0007829|PDB:1G60"
FT HELIX 76..88
FT /evidence="ECO:0007829|PDB:1G60"
FT STRAND 92..99
FT /evidence="ECO:0007829|PDB:1G60"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:1G60"
FT STRAND 117..125
FT /evidence="ECO:0007829|PDB:1G60"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:1G60"
FT HELIX 141..151
FT /evidence="ECO:0007829|PDB:1G60"
FT STRAND 170..173
FT /evidence="ECO:0007829|PDB:1G60"
FT HELIX 199..209
FT /evidence="ECO:0007829|PDB:1G60"
FT STRAND 215..220
FT /evidence="ECO:0007829|PDB:1G60"
FT HELIX 225..232
FT /evidence="ECO:0007829|PDB:1G60"
FT STRAND 236..242
FT /evidence="ECO:0007829|PDB:1G60"
FT HELIX 244..255
FT /evidence="ECO:0007829|PDB:1G60"
SQ SEQUENCE 260 AA; 30077 MW; E53354DCA12DBE7C CRC64;
MLEINKIHQM NCFDFLDQVE NKSVQLAVID PPYNLSKADW DSFDSHNEFL PFTYRWIDKV
LDKLDKDGSL YIFNTPFNCA FICQYLVSKG MIFQNWITWD KRDGMGSAKR GFSTGQETIL
FFSKSKNHTF NYDEVRVPYE STDRIKHASE KGILKNGKRW FPNPNGRLCG EVWHFSSQRH
KEKVNGKTVK LTHITPKPRD LIERIIRASS NPNDLVLDCF MGSGTTAIVA KKLGRNFIGC
DMNAEYVNQA NFVLNQLEIN
