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 27-MAR-2024, entry version 102. 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; Pseudomonadota; 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 / RC NCTC 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}. 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; 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; 767831; M.SspSPORF2370P. 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; Vaccinia Virus protein VP39; 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 PANTHER; PTHR13370; RNA METHYLASE-RELATED; 1. DR PANTHER; PTHR13370:SF33; TYPE II METHYLTRANSFERASE M.MJAV; 1. DR Pfam; PF01555; N6_N4_Mtase; 1. DR PRINTS; PR00508; S21N4MTFRASE. DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 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 //