ID B1XQR7_SYNP2 Unreviewed; 482 AA.
AC B1XQR7;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 24-JAN-2024, entry version 88.
DE RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
GN OrderedLocusNames=SYNPCC7002_C0003 {ECO:0000313|EMBL:ACB00848.1};
OS Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum
OS quadruplicatum).
OG Plasmid pAQ3 {ECO:0000313|EMBL:ACB00848.1,
OG ECO:0000313|Proteomes:UP000001688}.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Geminocystaceae; Picosynechococcus.
OX NCBI_TaxID=32049 {ECO:0000313|EMBL:ACB00848.1, ECO:0000313|Proteomes:UP000001688};
RN [1] {ECO:0000313|Proteomes:UP000001688}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27264 / PCC 7002 / PR-6
RC {ECO:0000313|Proteomes:UP000001688};
RC PLASMID=pAQ3 {ECO:0000313|Proteomes:UP000001688};
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.
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 Evidence={ECO:0000256|ARBA:ARBA00001279};
CC -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC {ECO:0000256|ARBA:ARBA00006594}.
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DR EMBL; CP000953; ACB00848.1; -; Genomic_DNA.
DR RefSeq; WP_012308463.1; NZ_JAHHPU010000018.1.
DR AlphaFoldDB; B1XQR7; -.
DR REBASE; 17548; M.AquV.
DR KEGG; syp:SYNPCC7002_C0003; -.
DR HOGENOM; CLU_018284_4_0_3; -.
DR OMA; VWFYEHP; -.
DR Proteomes; UP000001688; Plasmid pAQ3.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro.
DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC.
DR Gene3D; 1.20.1260.30; -; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR022749; D12N6_MeTrfase_N.
DR InterPro; IPR003356; DNA_methylase_A-5.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR038333; T1MK-like_N_sf.
DR PANTHER; PTHR42933; SLR6095 PROTEIN; 1.
DR PANTHER; PTHR42933:SF4; TYPE I RESTRICTION ENZYME ECOKI M PROTEIN; 1.
DR Pfam; PF12161; HsdM_N; 1.
DR Pfam; PF02384; N6_Mtase; 1.
DR PRINTS; PR00507; N12N6MTFRASE.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000313|EMBL:ACB00848.1};
KW Plasmid {ECO:0000313|EMBL:ACB00848.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001688};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW Transferase {ECO:0000313|EMBL:ACB00848.1}.
FT DOMAIN 4..82
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 151..449
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 482 AA; 54336 MW; 6FAAF6C6D88F14E2 CRC64;
MFEQTFKNID DVLRKEAGCA TELDYAEQIS WILFLKYLDD LETDRESKAS LTGEKYEPLL
DEPYRWKSWA YPRDEKGELI KTAAVGDDLI AFVSGELFPY FRGFKDYVEP GTFGAKIGEI
FSGVSNKFQS GYNLREVLES IDALRFQTQQ EKHELSDLYE TRINNMGNAG RNGGEYYTPR
PLIRAMIRVI KPQLGETIYD GACGSAGFLC EAYEFLRPLV KSAAELERLQ TATLYGQEKK
GLAYIIGVMN LILHGVEAPN IIQMNTLTEN IQGFQEKDRH DVILANPPFG GKEREEIKQN
FTIATGETAF LFLQHFIKRL KVGGRAAVVI KNTFLSNADN ASRALRQELT SSCNLHTVLD
CPAKTFLGAG VKTVVLFFEK GTPTEKIWFY QLDPGRSLGK TNPLNDDDLK EFVEFQSTFR
ESERSWFLAL KDVDPASFDL SVKNPNAPED DPLREPEEIL AEIADLDQES AEILAAIGEM
LA
//