MT1A_MORBO
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 03-AUG-2022, entry version 87.
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; Proteobacteria; 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 / NCTC
RC 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; -; 1.
DR Gene3D; 3.40.50.150; -; 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 PANTHER; PTHR30481; PTHR30481; 1.
DR Pfam; PF02086; MethyltransfD12; 1.
DR PIRSF; PIRSF000398; M_m6A_EcoRV; 1.
DR PRINTS; PR00505; D12N6MTFRASE.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00571; dam; 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
