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Database: UniProt
Entry: I0KD50_9BACT
LinkDB: I0KD50_9BACT
Original site: I0KD50_9BACT 
ID   I0KD50_9BACT            Unreviewed;       280 AA.
AC   I0KD50;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 42.
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=FAES_4053 {ECO:0000313|EMBL:CCH02053.1};
OS   Fibrella aestuarina BUZ 2.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC   Fibrella.
OX   NCBI_TaxID=1166018 {ECO:0000313|EMBL:CCH02053.1, ECO:0000313|Proteomes:UP000011058};
RN   [1] {ECO:0000313|EMBL:CCH02053.1, ECO:0000313|Proteomes:UP000011058}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BUZ 2T {ECO:0000313|Proteomes:UP000011058};
RX   PubMed=22689241; DOI=10.1128/JB.00550-12;
RA   Filippini M., Qi W., Blom J., Goesmann A., Smits T.H., Bagheri H.C.;
RT   "Genome Sequence of Fibrella aestuarina BUZ 2T, a Filamentous Marine
RT   Bacterium.";
RL   J. Bacteriol. 194:3555-3555(2012).
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; HE796683; CCH02053.1; -; Genomic_DNA.
DR   RefSeq; WP_015333152.1; NC_020054.1.
DR   AlphaFoldDB; I0KD50; -.
DR   STRING; 1166018.FAES_4053; -.
DR   KEGG; fae:FAES_4053; -.
DR   eggNOG; COG0286; Bacteria.
DR   HOGENOM; CLU_993055_0_0_10; -.
DR   OrthoDB; 9814572at2; -.
DR   Proteomes; UP000011058; 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   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR003356; DNA_methylase_A-5.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR42933; SLR6095 PROTEIN; 1.
DR   PANTHER; PTHR42933:SF4; TYPE I RESTRICTION ENZYME ECOKI METHYLASE SUBUNIT; 1.
DR   Pfam; PF02384; N6_Mtase; 1.
DR   PRINTS; PR00507; N12N6MTFRASE.
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:CCH02053.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011058};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CCH02053.1}.
FT   DOMAIN          88..194
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
FT   REGION          235..280
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   280 AA;  31068 MW;  2E3FAA5773F0B183 CRC64;
     MPKSTDVPPE LRSLNKVFSQ LDYKWDYADS FRDFVDFLTE SFMPVRQGEY ERLQKKHGSL
     NWFVDMTREW VLVQDKMIAV DGTGGWYDAL GTFYETLASR GKKSSLGQFF TPPEVCEVMV
     RINGFTTDMT GKGLSIQDPA SGSGRMLLAA HVTAPGNYQY AADLDPICTK MAAANMCLHG
     CVGQAVCMDS LNPDDWRFGY AINRSLAWTG VPTIEPIQKE QCRAWNLAQQ QKADEAARQA
     APTTAPVPAP AVPKTARIDT PVRPQPEPTN AGKFGQLKLF
//
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