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Database: UniProt
Entry: A0A073CLU8_PLAAG
LinkDB: A0A073CLU8_PLAAG
Original site: A0A073CLU8_PLAAG 
ID   A0A073CLU8_PLAAG        Unreviewed;       505 AA.
AC   A0A073CLU8;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 29.
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=A19Y_4636 {ECO:0000313|EMBL:KEI69264.1};
OS   Planktothrix agardhii NIVA-CYA 126/8.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Oscillatoriales; Microcoleaceae; Planktothrix.
OX   NCBI_TaxID=388467 {ECO:0000313|EMBL:KEI69264.1, ECO:0000313|Proteomes:UP000027395};
RN   [1] {ECO:0000313|EMBL:KEI69264.1, ECO:0000313|Proteomes:UP000027395}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIVA-CYA 126/8 {ECO:0000313|EMBL:KEI69264.1,
RC   ECO:0000313|Proteomes:UP000027395};
RX   PubMed=24907328; DOI=10.1128/AEM.01188-14;
RA   Christiansen G., Goesmann A., Kurmayer R.;
RT   "Elucidation of insertion elements encoded on plasmids and in vitro
RT   construction of shuttle vectors from the toxic cyanobacterium
RT   Planktothrix.";
RL   Appl. Environ. Microbiol. 80:4887-4897(2014).
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};
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DR   EMBL; CM002803; KEI69264.1; -; Genomic_DNA.
DR   RefSeq; WP_042158029.1; NZ_CM002803.1.
DR   AlphaFoldDB; A0A073CLU8; -.
DR   STRING; 388467.A19Y_4636; -.
DR   PATRIC; fig|388467.6.peg.4577; -.
DR   eggNOG; COG0827; Bacteria.
DR   HOGENOM; CLU_043528_0_0_3; -.
DR   Proteomes; UP000027395; Chromosome.
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   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR003356; DNA_methylase_A-5.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR33841; DNA METHYLTRANSFERASE YEEA-RELATED; 1.
DR   PANTHER; PTHR33841:SF5; TYPE II METHYLTRANSFERASE M.HINDII; 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   4: Predicted;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:KEI69264.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027395};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KEI69264.1}.
FT   DOMAIN          14..193
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
SQ   SEQUENCE   505 AA;  58144 MW;  A9EA72403592E674 CRC64;
     MVAPTNRKQD KFQSYYTNCD HITSYMVGLL ECDNNMSVLE PCAGEGVFID ELLKQELTPE
     ITAYELNIDA VNQLNIKYNN LKNIEIIHQD FILANTNKKF DRVIANPPYG AYQSPEKRKQ
     LKKAYPHIYA KETYGLFLIR TMELLKQDGR LVFIIPDTYL SLHHHQGLRK EIISNYKIES
     ITLFPSDFFP GVNFGYAGLS IISIVKEKPN IDYNFPVYKG LHSPPELTEL LTKTKKNYEV
     CRLSYHQLIN NPSQAFFLSS KDWISQILSS DNMTVGDICF VVTGFYSGND GKYLRRSPSV
     TRGTKKYAIV ENNKICRDNL SINPPLNGIK NDCYWVPIVK GGNQRFYKQS EWFMDWGEKA
     VHDYKVTNKQ KARFQNSQFY FRQGIAVPMI SSSSITGSLL DGRLFDQSIV GIFPRQDYQD
     LIYYLLGFFN SKACNDLIRT INISTNNSAN YIKKIPLIIP QKQLLETILK EVGRLVILSK
     SNIINDQDLQ KLNEYFYDVY GAKIS
//
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