ID   MTA1_ACICA              Reviewed;         540 AA.
AC   P25201;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 2.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Type II methyltransferase M.AccI {ECO:0000303|PubMed:12654995};
DE            Short=M.AccI {ECO:0000303|PubMed:12654995};
DE            EC=2.1.1.72;
DE   AltName: Full=Adenine-specific methyltransferase AccI;
DE   AltName: Full=Modification methylase AccI;
GN   Name=accIM;
OS   Acinetobacter calcoaceticus.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=471;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 49823;
RX   PubMed=1368703; DOI=10.1271/bbb1961.55.1553;
RA   Kawakami B., Hilzheber C., Nagatomo M., Oka M.;
RT   "Cloning and nucleotide sequences of the AccI restriction-modification
RT   genes in Acinetobacter calcoaceticus.";
RL   Agric. Biol. Chem. 55:1553-1559(1991).
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'-GTMKAC-3', methylates A-5 on both strands, and protects the
CC       DNA from cleavage by the AccI 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   -!- SUBUNIT: Monomer.
CC   -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; D10671; BAA01523.1; -; Genomic_DNA.
DR   PIR; JU0470; JU0470.
DR   AlphaFoldDB; P25201; -.
DR   SMR; P25201; -.
DR   REBASE; 3271; M.AccI.
DR   PRO; PR:P25201; -.
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; IPR011639; RM_methylase_Eco57I-like.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF07669; Eco57I; 1.
DR   SUPFAM; SSF53335; SSF53335; 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..540
FT                   /note="Type II methyltransferase M.AccI"
FT                   /id="PRO_0000087941"
SQ   SEQUENCE   540 AA;  63093 MW;  A2569693712E0F59 CRC64;
     MIKTTEHIVN NSIERDYSKS ISLEHRKKFA QFFTPFPIAY AMAKWILGNK QLKTVLEPAF
     GLGVFSRAIL SQQKEINIKA FEVDETIFEN AKEYFDDFEN VNILLQDYMY NDWKNKYDGI
     ICNPPYFKFH DYDNKNILKE IETNLKCKLN GFTNLYTLFL LKSIHQLSQN GRCAYIIPSE
     FLNSDYGKLV KTYLIKSKTL RHIIVIDFEE NVFDDALTTA SIILCANDNI TDKVQFNNIQ
     SLQDLSKIDE IINKYPNFLE TEQTYNFSDL NPEIKWKAYY QKQNSIKFKN LVPFSTYAKV
     VRGIATGSNE YFTFNLSKAK EFNIDEQYLL PCICSAKDAK TSFFTKQDFE ELKKSDKSVF
     LFNAQNSTDK NISSYIQKGE SEEINKRFLT ASRTPWYSLE NRKPAPIWVS VFNRSGLRFI
     RNEANISNLT SYHCIIQNKQ VVSEIDIDLL FAYLLTDTAK QIFEDNSRQY GNGLQKFEPN
     DLNKGMMLDL GLLDKQTSDE ILNLYKEYKY LILDNKNGDE IINKIDKILT DKYSEKKHWA