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 02-NOV-2016, entry version 87.
DE RecName: Full=Modification methylase AquI subunit alpha;
DE Short=M.AquI subunit alpha;
DE Short=M.AquiA;
DE EC=2.1.1.37;
DE AltName: Full=Cytosine-specific methyltransferase AquI subunit alpha;
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;
OC Synechococcus.
OX NCBI_TaxID=32049;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2104605;
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.,
RA Wang J., 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.
CC -!- FUNCTION: This methylase recognizes the double-stranded sequence
CC CYCGRG, causes specific methylation on C-1 on both strands, and
CC protects the DNA from cleavage by the AquI endonuclease.
CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + DNA = S-adenosyl-L-
CC homocysteine + DNA containing 5-methylcytosine.
CC {ECO:0000255|PROSITE-ProRule:PRU10018}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit.
CC -!- DOMAIN: Corresponds to the N-terminal half of the enzymatic
CC domain.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding
CC methyltransferase superfamily. C5-methyltransferase family.
CC {ECO:0000255|PROSITE-ProRule:PRU01016}.
CC -!- SIMILARITY: Contains 1 SAM-dependent MTase C5-type domain.
CC {ECO:0000255|PROSITE-ProRule:PRU01016}.
DR EMBL; M28051; AAA22067.1; -; Genomic_DNA.
DR EMBL; CP000951; ACA99187.1; -; Genomic_DNA.
DR RefSeq; WP_012306810.1; NC_010475.1.
DR ProteinModelPortal; P34882; -.
DR STRING; 32049.SYNPCC7002_A1188; -.
DR REBASE; 3283; M.AquI.
DR EnsemblBacteria; ACA99187; ACA99187; SYNPCC7002_A1188.
DR KEGG; syp:SYNPCC7002_A1188; -.
DR PATRIC; 23816916; VBISynSp37135_1410.
DR eggNOG; ENOG4105NI8; Bacteria.
DR eggNOG; COG0270; LUCA.
DR KO; K00558; -.
DR OMA; KFILMEN; -.
DR OrthoDB; POG091H02EL; -.
DR Proteomes; UP000001688; Chromosome.
DR GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase 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; IPR018117; C5_DNA_meth_AS.
DR InterPro; IPR001525; C5_MeTfrase.
DR InterPro; IPR029063; SAM-dependent_MTases.
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 3: Inferred from homology;
KW Complete proteome; Methyltransferase; Reference proteome;
KW Restriction system; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1 248 Modification methylase AquI subunit
FT alpha.
FT /FTId=PRO_0000087854.
FT DOMAIN 3 248 SAM-dependent MTase C5-type.
FT {ECO:0000255|PROSITE-ProRule:PRU01016}.
FT ACT_SITE 82 82 {ECO:0000255|PROSITE-ProRule:PRU01016,
FT ECO:0000255|PROSITE-ProRule:PRU10018}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 3 248 iprf:SAM_MT_C5 [T]
FT MYHIT 4 192 ipfam:DNA_methylase [T]
FT MYHIT 74 86 ipat:C5_MTASE_1 [T]
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
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