ID G5IZ30_CROWT Unreviewed; 282 AA.
AC G5IZ30;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
GN ORFNames=CWATWH0003_0527 {ECO:0000313|EMBL:EHJ14808.1};
OS Crocosphaera watsonii WH 0003.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Aphanothecaceae; Crocosphaera.
OX NCBI_TaxID=423471 {ECO:0000313|EMBL:EHJ14808.1, ECO:0000313|Proteomes:UP000003477};
RN [1] {ECO:0000313|EMBL:EHJ14808.1, ECO:0000313|Proteomes:UP000003477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH 0003 {ECO:0000313|EMBL:EHJ14808.1,
RC ECO:0000313|Proteomes:UP000003477};
RX PubMed=22232617;
RA Bench S.R., Ilikchyan I.N., Tripp H.J., Zehr J.P.;
RT "Two Strains of Crocosphaera watsonii with Highly Conserved Genomes are
RT Distinguished by Strain-Specific Features.";
RL Front. Microbiol. 2:261-261(2011).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHJ14808.1}.
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DR EMBL; AESD01000085; EHJ14808.1; -; Genomic_DNA.
DR RefSeq; WP_007309136.1; NZ_AESD01000085.1.
DR AlphaFoldDB; G5IZ30; -.
DR PATRIC; fig|423471.3.peg.484; -.
DR Proteomes; UP000003477; Unassembled WGS sequence.
DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC.
DR Gene3D; 1.10.1020.10; Adenine-specific Methyltransferase, Domain 2; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR023095; Ade_MeTrfase_dom_2.
DR InterPro; IPR012263; M_m6A_EcoRV.
DR InterPro; IPR012327; MeTrfase_D12.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR NCBIfam; TIGR00571; dam; 1.
DR PANTHER; PTHR30481; DNA ADENINE METHYLASE; 1.
DR PANTHER; PTHR30481:SF2; MODIFICATION METHYLASE; 1.
DR Pfam; PF02086; MethyltransfD12; 1.
DR PIRSF; PIRSF000398; M_m6A_EcoRV; 1.
DR PRINTS; PR00505; D12N6MTFRASE.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:EHJ14808.1};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EHJ14808.1}.
SQ SEQUENCE 282 AA; 33319 MW; DFAFCF85BC9D7503 CRC64;
MIKSPLRYPG GKSRAIKQIQ EQFPRRFTFS EYREPFVGGG SVFIYLKQIY PNIDIWINDL
NPELYLFWKI AQSDLKALVT ELRQIKKNRK DGRELFQELR ELDVGKISDF ERAVRFFILN
RITFSGTIES GGYSEKSFQT RFTESSIDRL EKLGQILPGI RITNLDYREV VKQKGENTFI
FLDPPYLTAT KSRLYGKDGD LHTSFNHQDF ANTMKKCDHQ WLMTYDDSQE IRNYFQDFNI
IPWQLQYGMN NYKQGKAEKG QEIFIRNYDI GVTQLSLNLN IY
//
