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Database: UniProt
Entry: A0A098RY56_9BACT
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ID   A0A098RY56_9BACT        Unreviewed;       292 AA.
AC   A0A098RY56;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
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   ORFNames=IX84_31645 {ECO:0000313|EMBL:KGE84815.1};
OS   Phaeodactylibacter xiamenensis.
OC   Bacteria; Bacteroidota; Saprospiria; Saprospirales; Haliscomenobacteraceae;
OC   Phaeodactylibacter.
OX   NCBI_TaxID=1524460 {ECO:0000313|EMBL:KGE84815.1, ECO:0000313|Proteomes:UP000029736};
RN   [1] {ECO:0000313|EMBL:KGE84815.1, ECO:0000313|Proteomes:UP000029736}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KD52 {ECO:0000313|EMBL:KGE84815.1,
RC   ECO:0000313|Proteomes:UP000029736};
RX   PubMed=25052393; DOI=10.1099/ijs.0.063909-0;
RA   Chen Z.Jr., Lei X., Lai Q., Li Y., Zhang B., Zhang J., Zhang H., Yang L.,
RA   Zheng W., Tian Y., Yu Z., Xu H.Jr., Zheng T.;
RT   "Phaeodactylibacter xiamenensis gen. nov., sp. nov., a member of the family
RT   Saprospiraceae isolated from the marine alga Phaeodactylum tricornutum.";
RL   Int. J. Syst. Evol. Microbiol. 64:3496-3502(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,
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}.
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:KGE84815.1}.
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DR   EMBL; JPOS01000126; KGE84815.1; -; Genomic_DNA.
DR   RefSeq; WP_044230294.1; NZ_JPOS01000126.1.
DR   AlphaFoldDB; A0A098RY56; -.
DR   STRING; 1524460.IX84_31645; -.
DR   REBASE; 100136; M.PxiKD52ORF31645P.
DR   OrthoDB; 9805629at2; -.
DR   Proteomes; UP000029736; Unassembled WGS sequence.
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:UP000029736};
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         22
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000398-1"
FT   BINDING         26
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000398-1"
FT   BINDING         67
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000398-1"
FT   BINDING         195
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000398-1"
SQ   SEQUENCE   292 AA;  33458 MW;  C60DDCF490A36D37 CRC64;
     MQLSLDNKFA TYIPPKSQLL KWVGNKQRFA GEIAKFFPVK FNTFYEPFIG SGAVIATVSP
     RNGVGSDAFK PLMDIWKKLQ SNPNELIEWY AVRRNRLEKE DKKTVYEDIK ASFNANHNGA
     DFLYLTRSCY GGIIRFRKSD GYMSTPCGVH TPISVKTFSK RVKEWNLRLR NVAFLNIDYK
     DAFDMAKEGD LIYCDPPYSH SQSILYGAQD FKLSELFEKI KEAKNKGVKV ALSIDGKKKS
     GNYLCDLPIP ENVFEEEIFV SVGRSMLRRF QMEGQSLESE LVSDRLLLNY SV
//
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