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Database: UniProt
Entry: A0A159YZC5_9RHOB
LinkDB: A0A159YZC5_9RHOB
Original site: A0A159YZC5_9RHOB 
ID   A0A159YZC5_9RHOB        Unreviewed;       503 AA.
AC   A0A159YZC5;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
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=AKL17_0517 {ECO:0000313|EMBL:AMY67777.1};
OS   Frigidibacter mobilis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Frigidibacter.
OX   NCBI_TaxID=1335048 {ECO:0000313|EMBL:AMY67777.1, ECO:0000313|Proteomes:UP000076128};
RN   [1] {ECO:0000313|EMBL:AMY67777.1, ECO:0000313|Proteomes:UP000076128}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cai42 {ECO:0000313|Proteomes:UP000076128};
RA   Geng S., Pan X., Wu X.;
RT   "Complete genome sequence of Defluviimonas alba cai42t isolated from an
RT   oilfield in Xinjiang.";
RL   Submitted (SEP-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};
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DR   EMBL; CP012661; AMY67777.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A159YZC5; -.
DR   STRING; 1335048.AKL17_0517; -.
DR   REBASE; 144415; M.Dal42ORF516P.
DR   KEGG; daa:AKL17_0517; -.
DR   PATRIC; fig|1335048.3.peg.537; -.
DR   Proteomes; UP000076128; 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; 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:AMY67777.1};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          52..164
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
SQ   SEQUENCE   503 AA;  55916 MW;  E9432BC84A32315E CRC64;
     MGVTPAKIPH HLTGVEIVTA EARAATERLR PDLGKAADKI VCNSDFFGWW QGTDQPAFDV
     IVGNPPFIRY QSFPEPHRAR AMAIMGDQGL KPNRLTNIWV PFVVAATASL KPGGRLALVL
     PAEILQVTYA AQLRSYLTDH FERIDVIACN ELFFENAEQE VVLLLADGAL AAATEDNTCR
     VALTAAETVA DITDIRPALL LDRAEPKIIC HDSEKWLKYF LDNRQISFMR ELRDAEITSS
     MSTHASIDVG VVTGKNEFFV LSTDQVKDFG LEGYTTPLVS RSVQLKGSQL GKADWISLAA
     DGNRVHLLNI SAAQASELSA KLRQYIEDGE RKEFHKGYKC SIRKPWYLVP SVWVPDGFAF
     RQIYDFPRMV LNASGATSTD TIHRMRSHGA KPERVIANTY TWLTAASAEI EGRSYGGGVL
     ELEPTEAERL LMPAKLNGAM PLKDVDQLVR AGRLDAVLEE NAKIILREHM GLSAADCDLL
     KSVWTQMRDR RNSRRRGTRK QAI
//
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