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Database: UniProt
Entry: A0A0F3MLI6_9RICK
LinkDB: A0A0F3MLI6_9RICK
Original site: A0A0F3MLI6_9RICK 
ID   A0A0F3MLI6_9RICK        Unreviewed;       274 AA.
AC   A0A0F3MLI6;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-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   ORFNames=OCHUTO_0441 {ECO:0000313|EMBL:KJV56536.1};
OS   Orientia chuto str. Dubai.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Orientia.
OX   NCBI_TaxID=1359168 {ECO:0000313|EMBL:KJV56536.1, ECO:0000313|Proteomes:UP000033616};
RN   [1] {ECO:0000313|EMBL:KJV56536.1, ECO:0000313|Proteomes:UP000033616}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fuller {ECO:0000313|EMBL:KJV56536.1,
RC   ECO:0000313|Proteomes:UP000033616};
RA   Daugherty S.C., Su Q., Abolude K., Beier-Sexton M., Carlyon J.A.,
RA   Carter R., Day N.P., Dumler S.J., Dyachenko V., Godinez A., Kurtti T.J.,
RA   Lichay M., Mullins K.E., Ott S., Pappas-Brown V., Paris D.H., Patel P.,
RA   Richards A.L., Sadzewicz L., Sears K., Seidman D., Sengamalay N.,
RA   Stenos J., Tallon L.J., Vincent G., Fraser C.M., Munderloh U.,
RA   Dunning-Hotopp J.C.;
RT   "Genome Sequencing of Rickettsiales.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
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:KJV56536.1}.
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DR   EMBL; LANP01000008; KJV56536.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F3MLI6; -.
DR   STRING; 1359168.OCHUTO_0441; -.
DR   PATRIC; fig|1359168.3.peg.1208; -.
DR   Proteomes; UP000033616; 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:UP000033616};
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         13
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000398-1"
FT   BINDING         17
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000398-1"
FT   BINDING         57
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000398-1"
FT   BINDING         178
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000398-1"
SQ   SEQUENCE   274 AA;  32383 MW;  FFF8292C4A742A0A CRC64;
     MSVATANKPF LHWVGGKRRI INKLLEHLPS GPYYNYYEPG RGAFQVKHIF KQCFLSDINL
     DLITSYHAVK KNPEEVNRLL NLYHENHSEN YYYRINYYSN DPNYITAKFI YLNKYSFRGI
     YRLNRDGTSA QTFSDKQYLK LHIGSRIYKC SKLLTGVSIY GMDFSFIEPK QGDFVYLDPP
     YHKSGERFYT RIPFNEKEQI RLRNFVHELT DKGVKIMLSN TAFIKDLYKT FTSRLLELHT
     LSMNNVIMLI KYMLNPLLDL RCSITAGIKF PIKR
//
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