ID   MT1B_MORBO              Reviewed;         273 AA.
AC   P34721;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   RecName: Full=Type II methyltransferase M2.MboI {ECO:0000303|PubMed:12654995};
DE            Short=M2.MboI {ECO:0000303|PubMed:12654995};
DE            EC=2.1.1.72;
DE   AltName: Full=Adenine-specific methyltransferase MboIC;
DE   AltName: Full=M.MboC {ECO:0000303|PubMed:8506128};
DE   AltName: Full=Modification methylase MboIC;
DE            Short=M.MboIC;
GN   Name=mboIBM; Synonyms=mboC {ECO:0000303|PubMed:8506128};
OS   Moraxella bovis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Moraxella.
OX   NCBI_TaxID=476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=ATCC 10900 / DSM 6328 / CIP 70.40 / JCM 17254 / LMG 986 /
RC   NCTC 11013;
RX   PubMed=8506128; DOI=10.1093/nar/21.10.2309;
RA   Ueno T., Ito H., Kimizuka F., Kotani H., Nakajima K.;
RT   "Gene structure and expression of the MboI restriction-modification
RT   system.";
RL   Nucleic Acids Res. 21:2309-2313(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: A beta subtype methylase that recognizes the double-stranded
CC       sequence 5'-GATC-3', methylates A-2 on both strands, and protects the
CC       DNA from cleavage by the MboI endonuclease (PubMed:12654995)
CC       (Probable). This seems to be a weaker methylase than M1.MboI
CC       (Probable). {ECO:0000303|PubMed:12654995, ECO:0000305|PubMed:8506128}.
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   -!- MISCELLANEOUS: The MboI restriction system has two different
CC       methylases. {ECO:0000269|PubMed:8506128}.
CC   -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; D13968; BAA03073.1; -; Genomic_DNA.
DR   PIR; S35647; S35647.
DR   AlphaFoldDB; P34721; -.
DR   SMR; P34721; -.
DR   STRING; 476.B0182_10410; -.
DR   REBASE; 203780; M2.Lbr1106ORF1748P.
DR   REBASE; 204727; M.Bso1395ORF3951P.
DR   REBASE; 205333; M.Bso1395ORF1173P.
DR   REBASE; 3668; M2.MboI.
DR   PRO; PR:P34721; -.
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   3: Inferred from homology;
KW   DNA-binding; Methyltransferase; Restriction system;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..273
FT                   /note="Type II methyltransferase M2.MboI"
FT                   /id="PRO_0000087956"
SQ   SEQUENCE   273 AA;  31923 MW;  9571B82CB6B55D93 CRC64;
     MRIKPYFESD DKNFNIYQGN CIDFMSHFQD NSIDMIFADP PYFLSNDGLT FKNSIIQSVN
     KGEWDKNDNE ASIYNFNHEW IAQARQLLKD NGTIWISGTH HNIFTVGQVL KENNFKILNI
     ITWEKPNPPP NFSCRYFTYS SEWIIWARKH SKIPHYFNYD LMKKLNGDKQ QKDIWRLPAV
     GSWEKTQGKH PTQKPLGLLS RIILSSTQKD DLILDPFSGS GTTGIAGVLL DRNYIGIEQE
     LEFLELSKRR YHEITPVLKN EFKQKIRKQI SAI
//