ID   MTMU_MYCSP              Reviewed;         233 AA.
AC   P43641;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Type II methyltransferase M.MunI {ECO:0000303|PubMed:12654995};
DE            Short=M.MunI {ECO:0000303|PubMed:8181741};
DE            EC=2.1.1.72;
DE   AltName: Full=Adenine-specific methyltransferase MunI;
DE   AltName: Full=Modification methylase MunI;
GN   Name=munIM {ECO:0000303|PubMed:8181741};
OS   Mycoplasma sp.
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma;
OC   unclassified Mycoplasma.
OX   NCBI_TaxID=2108;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX   PubMed=8181741; DOI=10.1016/0378-1119(94)90347-6;
RA   Siksnys V., Zareckaja N., Vaisvila R., Timinskas A., Stakenas P.,
RA   Butkus V., Janulaitis A.;
RT   "CAATTG-specific restriction-modification munI genes from Mycoplasma:
RT   sequence similarities between R.MunI and R.EcoRI.";
RL   Gene 142:1-8(1994).
RN   [2]
RP   NOMENCLATURE.
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 methylase that recognizes the double-stranded sequence 5'-
CC       CAATTG-3', methylates A-3 on both strands, and protects the DNA from
CC       cleavage by the MunI endonuclease. {ECO:0000303|PubMed:12654995,
CC       ECO:0000305|PubMed:8181741}.
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   -!- SIMILARITY: Belongs to the MT-A70-like family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00489}.
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DR   EMBL; X76192; CAA53786.1; -; Genomic_DNA.
DR   PIR; S38899; S38899.
DR   AlphaFoldDB; P43641; -.
DR   SMR; P43641; -.
DR   REBASE; 3449; M.MunI.
DR   PRO; PR:P43641; -.
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; 3.40.50.150; -; 1.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR007757; MT-A70-like.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF05063; MT-A70; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51143; MT_A70; 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..233
FT                   /note="Type II methyltransferase M.MunI"
FT                   /id="PRO_0000207637"
SQ   SEQUENCE   233 AA;  26933 MW;  0BE21A05BB2A3A2E CRC64;
     MENKVTAYSI YNKKAKKNTK VNPLDEVFPQ LPRKKYQVIY ADPPWDYGGK MQYDKSTIKS
     ENEGFKRDIF ISSASFKYPT LKLKELQQLD VPSITADDCI LFMWTTGPQM ANSILLGESW
     GFEYKTVAFV WDKMVHNPGR YTLSQTEFVL VFKKGKIPTP RGARNVRQLL QIHRGQHSEK
     PYAVIDGITK MFPALDKIEL FARNNFVGWD NWGLEIPDNK IEIPTQGEID ENK