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Entry: A0A0F6QXQ0_9CORY
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ID   A0A0F6QXQ0_9CORY        Unreviewed;       276 AA.
AC   A0A0F6QXQ0;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900, ECO:0000256|RuleBase:RU361257};
DE            EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900, ECO:0000256|RuleBase:RU361257};
GN   Name=llaDCHIA {ECO:0000313|EMBL:AKE39690.1};
GN   ORFNames=UL81_08700 {ECO:0000313|EMBL:AKE39690.1};
OS   Corynebacterium camporealensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=161896 {ECO:0000313|EMBL:AKE39690.1, ECO:0000313|Proteomes:UP000033566};
RN   [1] {ECO:0000313|EMBL:AKE39690.1, ECO:0000313|Proteomes:UP000033566}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44610 {ECO:0000313|EMBL:AKE39690.1,
RC   ECO:0000313|Proteomes:UP000033566};
RX   PubMed=26021938;
RA   Ruckert C., Albersmeier A., Winkler A., Tauch A.;
RT   "Complete Genome Sequence of Corynebacterium camporealensis DSM 44610,
RT   Isolated from the Milk of a Manchega Sheep with Subclinical Mastitis.";
RL   Genome Announc. 3:e00572-15(2015).
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         ECO:0000256|RuleBase:RU361257};
CC   -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00006594, ECO:0000256|RuleBase:RU361257}.
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DR   EMBL; CP011311; AKE39690.1; -; Genomic_DNA.
DR   RefSeq; WP_046453488.1; NZ_CP011311.1.
DR   AlphaFoldDB; A0A0F6QXQ0; -.
DR   REBASE; 110097; M.Cca44610ORF8700P.
DR   KEGG; ccj:UL81_08700; -.
DR   PATRIC; fig|161896.4.peg.1704; -.
DR   HOGENOM; CLU_063430_0_0_11; -.
DR   OrthoDB; 9805629at2; -.
DR   Proteomes; UP000033566; Chromosome.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-UniRule.
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; IPR002052; DNA_methylase_N6_adenine_CS.
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:SF3; DNA ADENINE 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.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000256|RuleBase:RU361257};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033566};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|RuleBase:RU361257};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361257}.
FT   BINDING         10
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000398-1"
FT   BINDING         14
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000398-1"
FT   BINDING         56
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000398-1"
FT   BINDING         186
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000398-1"
SQ   SEQUENCE   276 AA;  31171 MW;  77DD0F52D24C7FC9 CRC64;
     MNELKPLVKW VGGKRQLLPQ IHAALPQDGF NRYFEPFLGG GAVLFSLAPE QATVNDLNSE
     LINLYRVVRD DVDELIALLR GYRNEEEFFY EMRGLDRAPE YAQLTAVERA ARTVYLNKTC
     YNGLYRVNNA GQFNAPFGRY SNPVICDEPT LRAVSEYLNN SDVQFHNGDY ATITEHATAG
     DLVYFDPPYD PVNPTSNFTG YQSGGFTRDD QIRLKEVCDD LDSRGVKFLL SNSATEFIRE
     LYADYNVSIV GAKRAINSVA SKRGKVDEVL VRNYDS
//
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