ID   MTA1_ACEPA              Reviewed;         429 AA.
AC   O52702;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   13-SEP-2023, entry version 74.
DE   RecName: Full=Type II methyltransferase M.ApaLI {ECO:0000303|PubMed:12654995};
DE            Short=M.ApaLI {ECO:0000303|PubMed:9862476};
DE            EC=2.1.1.37;
DE   AltName: Full=Cytosine-specific methyltransferase ApaLI;
DE   AltName: Full=Modification methylase ApaLI;
GN   Name=apaLIM {ECO:0000303|PubMed:9862476};
OS   Acetobacter pasteurianus (Acetobacter turbidans).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Acetobacter.
OX   NCBI_TaxID=438;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROBABLE FUNCTION, AND PROBABLE
RP   METHYLATION SITE.
RC   STRAIN=ATCC 12875;
RX   PubMed=9862476; DOI=10.1007/s004380050890;
RA   Xu S.-Y., Xiao J.-P., Ettwiller L., Holden M., Aliotta J., Poh C.L.,
RA   Dalton M., Robinson D.P., Petronzio T.R., Moran L., Ganatra M., Ware J.,
RA   Slatko B., Benner J. II;
RT   "Cloning and expression of the ApaLI, NspI, NspHI, SacI, ScaI, and SapI
RT   restriction-modification systems in Escherichia coli.";
RL   Mol. Gen. Genet. 260:226-231(1998).
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 methylase that recognizes the double-stranded sequence
CC       5'-GTGCAC-3', probably methylates C-4 on both strands, and protects the
CC       DNA from cleavage by the ApaLI endonuclease.
CC       {ECO:0000303|PubMed:12654995, ECO:0000305|PubMed:9862476}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-
CC         methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:13681, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:11370,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:85452, ChEBI:CHEBI:85454; EC=2.1.1.37;
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. C5-methyltransferase family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01016}.
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DR   EMBL; AF044847; AAC97180.1; -; Genomic_DNA.
DR   AlphaFoldDB; O52702; -.
DR   SMR; O52702; -.
DR   REBASE; 159865; M.Bli1202ORF3247P.
DR   REBASE; 165448; M.Fba101ORF1712P.
DR   REBASE; 204038; M.Bli141ORF2448P.
DR   REBASE; 204039; M.Bli27ORF3140P.
DR   REBASE; 205332; M.Bso1395ORF1912P.
DR   REBASE; 205335; M.Bsu1392ORF209P.
DR   REBASE; 250814; M.BliADL4ORF1182P.
DR   REBASE; 3281; M.ApaLI.
DR   PRO; PR:O52702; -.
DR   GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.120.10; DNA Methylase, subunit A, domain 2; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR001525; C5_MeTfrase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   NCBIfam; TIGR00675; dcm; 1.
DR   PANTHER; PTHR10629; CYTOSINE-SPECIFIC METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR10629:SF52; DNA (CYTOSINE-5)-METHYLTRANSFERASE 1; 1.
DR   Pfam; PF00145; DNA_methylase; 1.
DR   PRINTS; PR00105; C5METTRFRASE.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51679; SAM_MT_C5; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Methyltransferase; Restriction system;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..429
FT                   /note="Type II methyltransferase M.ApaLI"
FT                   /id="PRO_0000087857"
FT   DOMAIN          5..383
FT                   /note="SAM-dependent MTase C5-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
FT   REGION          282..305
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        81
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
SQ   SEQUENCE   429 AA;  46547 MW;  E011C7D15B33F5F3 CRC64;
     MNKDEVVVSL FAGAGGFSSG FSQAGLKPLF GAEINADACQ TYQENVGSPC HQLDLSTVDP
     SHIEMLTGGK RPFVVIGGPP CQGFSTAGPR NFADPRNLLI FNYLNIVERL SPRWLIFENV
     EGLLTSGGGR DLARLVREFV DMGYSVRLQK VNLAAYGVPQ TRKRVLIIGN RLGIDFQFPE
     ELYSFDSGKA KKASGKPLAP SLAEAVAGLG PAASDKDALV PYASSEPVNA FDARMRAGNR
     VEVVTHHVRV EAAERMQVEL LKPGQTMKDL PPELWHESYR RRANRRVSDG TPTEKRGGAP
     SGIKRLHGNL QSLTITGPAA REFIHPTEHR PLTIRECARI QTFPDKYRWV GNNASVIQQI
     GNAVPPLAAE RLAKHLRDID GSFGADTRPA GAMSAKLLGF VLTEALGMSP ALKSTEALLA
     EMHQGGFVF
//