ID MTAB_SYNP2 Reviewed; 139 AA.
AC P34883;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 02-NOV-2016, entry version 72.
DE RecName: Full=Modification methylase AquI subunit beta;
DE Short=M.AquI subunit beta;
DE Short=M.AquIB;
DE EC=2.1.1.37;
DE AltName: Full=Cytosine-specific methyltransferase AquI subunit beta;
GN Name=aquIMB; OrderedLocusNames=SYNPCC7002_A1188.1;
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 -!- SUBUNIT: Heterodimer of an alpha and a beta subunit.
CC -!- DOMAIN: Corresponds to the C-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; AAA22068.1; -; Genomic_DNA.
DR EMBL; CP000951; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; WP_012308460.1; NC_010475.1.
DR ProteinModelPortal; P34883; -.
DR STRING; 32049.SYNPCC7002_A2880; -.
DR REBASE; 3283; M.AquI.
DR eggNOG; COG0270; LUCA.
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 InterPro; IPR001525; C5_MeTfrase.
DR InterPro; IPR031303; C5_meth_CS.
DR InterPro; IPR029063; SAM-dependent_MTases.
DR Pfam; PF00145; DNA_methylase; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS00095; C5_MTASE_2; 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 1 139 Modification methylase AquI subunit beta.
FT /FTId=PRO_0000087855.
FT DOMAIN 1 135 SAM-dependent MTase C5-type.
FT {ECO:0000255|PROSITE-ProRule:PRU01016}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 110 128 ipat:C5_MTASE_2 [T]
FT MYHIT 19 129 ipfam:DNA_methylase [T]
FT MYHIT 1 135 iprf:SAM_MT_C5 [T]
SQ SEQUENCE 139 AA; 15760 MW; 8550B7E0194CE006 CRC64;
MDIKNVHIKN HEQTAHAPST LEKIRKVKQG GKLSEQTKTF GSTYRRLDPN QPSPTVTRSG
YRDFIHPFED RMLTVRELAC LQTFPLDWEF TGTRLDSYSS KRKVTMTQFG QVGNAVPPLL
AEAVAKAVSE QLLDVIDEK
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