ID   MT1A_MORBO              Reviewed;         294 AA.
AC   P34720;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   13-SEP-2023, entry version 91.
DE   RecName: Full=Type II methyltransferase M1.MboI {ECO:0000303|PubMed:12654995};
DE            Short=M1.MboI {ECO:0000303|PubMed:12654995};
DE            EC=2.1.1.72;
DE   AltName: Full=Adenine-specific methyltransferase MboIA;
DE   AltName: Full=M.MboA {ECO:0000303|PubMed:8506128};
DE   AltName: Full=Modification methylase MboIA;
DE            Short=M.MboIA;
GN   Name=mboIAM; Synonyms=mboA {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: An alpha subtype methylase that recognizes the double-
CC       stranded sequence 5'-GATC-3', methylates A-2 on both strands, and
CC       protects the DNA from cleavage by the MboI endonuclease
CC       (PubMed:12654995) (Probable). This seems to be a stronger methylase
CC       than M2.MboI (Probable). {ECO:0000303|PubMed:12654995,
CC       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; BAA03071.1; -; Genomic_DNA.
DR   PIR; S35646; S35646.
DR   AlphaFoldDB; P34720; -.
DR   SMR; P34720; -.
DR   STRING; 476.B0182_10400; -.
DR   REBASE; 3667; M1.MboI.
DR   PRO; PR:P34720; -.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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; 1.10.1020.10; Adenine-specific Methyltransferase, Domain 2; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR023095; Ade_MeTrfase_dom_2.
DR   InterPro; IPR012263; M_m6A_EcoRV.
DR   InterPro; IPR012327; MeTrfase_D12.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   NCBIfam; TIGR00571; dam; 1.
DR   PANTHER; PTHR30481; DNA ADENINE METHYLASE; 1.
DR   PANTHER; PTHR30481:SF3; DNA ADENINE METHYLASE; 1.
DR   Pfam; PF02086; MethyltransfD12; 1.
DR   PIRSF; PIRSF000398; M_m6A_EcoRV; 1.
DR   PRINTS; PR00505; D12N6MTFRASE.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Methyltransferase; Restriction system;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..294
FT                   /note="Type II methyltransferase M1.MboI"
FT                   /id="PRO_0000087955"
FT   BINDING         7
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         11
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         61
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         198
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   294 AA;  33767 MW;  E042441B46C6BB04 CRC64;
     MKPFIKWAGG KNSLLDEIQK RLPDFVHSQD FCLVEPFVGG GAVSLWALSD LPHLKQLVIN
     DCNADLINVY QVIKNNPDDL IGYIENLQSH YDKLTDLESK KPYFYHKRDV FNQRTSNDIE
     QAGLFIFLNK SAFNGLYRVN KNNQFNVPIG NYKKPTFVDK ENILNISKKL QNTKILSGDF
     ELVLAHLPNN FPCLFYLDPP YRPISDTASF TSYSDNGFDD NEQKRLANFC KKIDKLGHYF
     LLSNSDPKNT NSSDEFFDEL YQDFKIERIQ ANRTISANSN GRKKVNEIIV SNGV
//