ID   MTB3_ANEAE              Reviewed;         580 AA.
AC   P22772; Q44656;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   23-FEB-2022, sequence version 2.
DT   27-MAR-2024, entry version 81.
DE   RecName: Full=Type II methyltransferase M.BanIII {ECO:0000303|PubMed:12654995};
DE            Short=M.BanIII {ECO:0000303|PubMed:12654995};
DE            EC=2.1.1.72;
DE   AltName: Full=Adenine-specific methyltransferase BanIII;
DE   AltName: Full=Modification methylase BanIII;
GN   Name=banIIIM;
OS   Aneurinibacillus aneurinilyticus (Bacillus aneurinolyticus).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae;
OC   Aneurinibacillus group; Aneurinibacillus.
OX   NCBI_TaxID=1391;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-6.
RC   STRAIN=ATCC 12856 / DSM 5562 / JCM 9024 / NBRC 15521 / IAM 1077 / NRS
RC   1589;
RX   PubMed=1368640; DOI=10.1271/bbb1961.54.3227;
RA   Kawakami B., Sasaki A., Oka M., Maekawa Y.;
RT   "Nucleotide sequence of the gene coding for the BanIII DNA
RT   methyltransferase in Bacillus aneurinolyticus.";
RL   Agric. Biol. Chem. 54:3227-3233(1990).
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 gamma subtype methylase, recognizes the double-stranded
CC       sequence 5'-ATCGAT-3', methylates A-5 on both strands, and protects the
CC       DNA from cleavage by the BanIII endonuclease.
CC       {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   -!- MISCELLANEOUS: The protein sequnce was determined following expression
CC       in E.coli. {ECO:0000269|PubMed:1368640}.
CC   -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA58443.1; Type=Miscellaneous discrepancy; Note=Substitute stop codon at 506 with Tyr.; Evidence={ECO:0000305};
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DR   EMBL; X83417; CAA58443.1; ALT_SEQ; Genomic_DNA.
DR   PIR; JH0224; JH0224.
DR   AlphaFoldDB; P22772; -.
DR   SMR; P22772; -.
DR   REBASE; 3296; M.BanIII.
DR   PRO; PR:P22772; -.
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   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR003356; DNA_methylase_A-5.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR025931; TaqI_C.
DR   PANTHER; PTHR33841; DNA METHYLTRANSFERASE YEEA-RELATED; 1.
DR   PANTHER; PTHR33841:SF5; TYPE II METHYLTRANSFERASE M.HINDII; 1.
DR   Pfam; PF02384; N6_Mtase; 1.
DR   Pfam; PF12950; TaqI_C; 1.
DR   PRINTS; PR00507; N12N6MTFRASE.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; DNA-binding; Methyltransferase;
KW   Restriction system; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..580
FT                   /note="Type II methyltransferase M.BanIII"
FT                   /id="PRO_0000087943"
SQ   SEQUENCE   580 AA;  66276 MW;  8C5D2418DA00C48E CRC64;
     MELTIEEMLI KQKETGAHYT PTDLGDIIAK RLINELKKSG ISGTKKIRGL DPSCGDGELL
     LSLNRMGKFN NIDNIELIGI DEDKEAIKEA DFRLNEMGIN DAKLSGGDFL DMVDLEGNLS
     LFDDDLSKIE PVDLIIANPP YVRTQVLGAD RAQKLAKLFN LKGRVDLYHA FLVAMTLQLK
     PGGLIGVITS NKYLANTTGE SIRQFLAENY DIIEIMDLGD TKLFSGAVLQ AIFFGTKKLN
     KGIRQTAPAN FYKIYEETDP SKTEVSIKFE TLFGLLESSN TGVFNVDEKF YSVSCGKLIV
     PDSFKEPWVM ATDEEYNWIT NINNNSYCTI QDLCDLKVGI KTTADKVFIK STWEELPDEI
     KPEVEVLKLL ISTDHASKWR PLERIGNQKI LYTHENLNGK KKAIHFTQYP HALAYLETHR
     ETLEGRKYVI KAKRNWYQIW LPQNPDHWAL PKILFPDISP EPKFFYEDEG CCIDGNCYWI
     IPKEENNNDI LFLILGISNT KYMTNYHDIA FNNKLYPGRT RYLTQYVSNY PLPNPEANYS
     QEIIDVLREL LFQNPNDERK IEIENQIENL TALAFGVERL
//