ID   MTAA_SYNP2              Reviewed;         248 AA.
AC   P34882; B1XKE1;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Type II methyltransferase M.AquIA {ECO:0000303|PubMed:12654995};
DE            Short=M.AquiA {ECO:0000303|PubMed:12654995};
DE            EC=2.1.1.37;
DE   AltName: Full=Cytosine-specific methyltransferase AquI subunit alpha;
DE   AltName: Full=Modification methylase AquI subunit alpha {ECO:0000303|PubMed:2104605};
DE            Short=M.AquI subunit alpha {ECO:0000303|PubMed:2104605};
GN   Name=aquIMA; Synonyms=dcm; OrderedLocusNames=SYNPCC7002_A1188;
OS   Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum
OS   quadruplicatum).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=32049;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PROBABLE SUBUNIT.
RC   STRAIN=ATCC 27264 / PCC 7002 / PR-6;
RX   PubMed=2104605; DOI=10.1128/jb.172.1.266-272.1990;
RA   Karreman C., de Waard A.;
RT   "Agmenellum quadruplicatum M.AquI, a novel modification methylase.";
RL   J. Bacteriol. 172:266-272(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27264 / PCC 7002 / PR-6;
RA   Li T., Zhao J., Zhao C., Liu Z., Zhao F., Marquardt J., Nomura C.T.,
RA   Persson S., Detter J.C., Richardson P.M., Lanz C., Schuster S.C., Wang J.,
RA   Li S., Huang X., Cai T., Yu Z., Luo J., Zhao J., Bryant D.A.;
RT   "Complete sequence of Synechococcus sp. PCC 7002.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN   [3]
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, recognizes the double-stranded sequence 5'-
CC       CYCGRG-3', methylates C-1 on both strands, and protects the DNA from
CC       cleavage by the AquI endonuclease. {ECO:0000269|PubMed:2104605,
CC       ECO:0000303|PubMed:12654995}.
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         Evidence={ECO:0000255|PROSITE-ProRule:PRU10018};
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit.
CC       {ECO:0000305|PubMed:2104605}.
CC   -!- DOMAIN: Corresponds to the N-terminal half of the enzymatic domain.
CC       {ECO:0000305|PubMed:2104605}.
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; M28051; AAA22067.1; -; Genomic_DNA.
DR   EMBL; CP000951; ACA99187.1; -; Genomic_DNA.
DR   RefSeq; WP_012306810.1; NC_010475.1.
DR   AlphaFoldDB; P34882; -.
DR   SMR; P34882; -.
DR   STRING; 32049.SYNPCC7002_A1188; -.
DR   REBASE; 3283; M.AquI.
DR   EnsemblBacteria; ACA99187; ACA99187; SYNPCC7002_A1188.
DR   KEGG; syp:SYNPCC7002_A1188; -.
DR   eggNOG; COG0270; Bacteria.
DR   HOGENOM; CLU_006958_7_0_3; -.
DR   OMA; LWPEMFR; -.
DR   PRO; PR:P34882; -.
DR   Proteomes; UP000001688; Chromosome.
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; 3.40.50.150; -; 1.
DR   InterPro; IPR018117; C5_DNA_meth_AS.
DR   InterPro; IPR001525; C5_MeTfrase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF00145; DNA_methylase; 1.
DR   PRINTS; PR00105; C5METTRFRASE.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR00675; dcm; 1.
DR   PROSITE; PS00094; C5_MTASE_1; 1.
DR   PROSITE; PS51679; SAM_MT_C5; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Methyltransferase; Reference proteome; Restriction system;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..248
FT                   /note="Type II methyltransferase M.AquIA"
FT                   /id="PRO_0000087854"
FT   DOMAIN          3..248
FT                   /note="SAM-dependent MTase C5-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
FT   ACT_SITE        82
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016,
FT                   ECO:0000255|PROSITE-ProRule:PRU10018"
SQ   SEQUENCE   248 AA;  27161 MW;  FFF6B42B0997D82F CRC64;
     MEKKLISLFS GAGGMDIGFH AAGFSTAVAV EQDPSCCNTL RLNMPDTPVI EGDITSITTQ
     VILEAAKVNP LEIDLVIGGP PCQSFSLAGK RMGMDDPRGM LVLEFLRVVR EALPKCFVME
     NVKGMINWSK GKALEAIMTE ASQPIKYAGK EYKYAVSYHV LNAADFGVPQ FRERVFIVGN
     RLGKTFQFPE PTHGPSNQAR QIDLFGKQLK PYKTVQDAIS TLPPATPPSA MALRVSQTIK
     DRIKNHGY