(data stored in SCRATCH zone)

SWISSPROT: D3UY28_XENBS

ID   D3UY28_XENBS            Unreviewed;       272 AA.
AC   D3UY28;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   16-JAN-2019, entry version 48.
DE   RecName: Full=Site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|RuleBase:RU361257};
DE            EC=2.1.1.72 {ECO:0000256|RuleBase:RU361257};
GN   Name=dam {ECO:0000313|EMBL:CBJ79206.1};
GN   OrderedLocusNames=XBJ1_0055 {ECO:0000313|EMBL:CBJ79206.1};
OS   Xenorhabdus bovienii (strain SS-2004).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406818 {ECO:0000313|EMBL:CBJ79206.1, ECO:0000313|Proteomes:UP000002045};
RN   [1] {ECO:0000313|EMBL:CBJ79206.1, ECO:0000313|Proteomes:UP000002045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS-2004 {ECO:0000313|EMBL:CBJ79206.1,
RC   ECO:0000313|Proteomes:UP000002045};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
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,
CC         Rhea:RHEA-COMP:12419, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:90615, ChEBI:CHEBI:90616;
CC         EC=2.1.1.72; Evidence={ECO:0000256|RuleBase:RU361257};
CC   -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC       {ECO:0000256|RuleBase:RU361257}.
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DR   EMBL; FN667741; CBJ79206.1; -; Genomic_DNA.
DR   RefSeq; WP_012986679.1; NC_013892.1.
DR   STRING; 406818.XBJ1_0055; -.
DR   REBASE; 24504; M.XboSSDamP.
DR   EnsemblBacteria; CBJ79206; CBJ79206; XBJ1_0055.
DR   GeneID; 8829683; -.
DR   KEGG; xbo:XBJ1_0055; -.
DR   PATRIC; fig|406818.4.peg.48; -.
DR   eggNOG; ENOG4105DFE; Bacteria.
DR   eggNOG; COG0338; LUCA.
DR   HOGENOM; HOG000281348; -.
DR   KO; K06223; -.
DR   OMA; MNRHGFN; -.
DR   BioCyc; XBOV406818:XBJ1_RS00255-MONOMER; -.
DR   Proteomes; UP000002045; 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; -; 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.
DR   PANTHER; PTHR30481; PTHR30481; 1.
DR   Pfam; PF02086; MethyltransfD12; 1.
DR   PIRSF; PIRSF000398; M_m6A_EcoRV; 1.
DR   PRINTS; PR00505; D12N6MTFRASE.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR00571; dam; 1.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; D3UY28.
DR   SWISS-2DPAGE; D3UY28.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002045};
KW   Methyltransferase {ECO:0000256|RuleBase:RU361257,
KW   ECO:0000313|EMBL:CBJ79206.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002045};
KW   S-adenosyl-L-methionine {ECO:0000256|RuleBase:RU361257};
KW   Transferase {ECO:0000256|RuleBase:RU361257,
KW   ECO:0000313|EMBL:CBJ79206.1}.
FT   BINDING      10     10       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PIRSR:PIRSR000398-1}.
FT   BINDING      14     14       S-adenosyl-L-methionine; via amide
FT                                nitrogen. {ECO:0000256|PIRSR:PIRSR000398-
FT                                1}.
FT   BINDING      54     54       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PIRSR:PIRSR000398-1}.
FT   BINDING     181    181       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PIRSR:PIRSR000398-1}.
SQ   SEQUENCE   272 AA;  31938 MW;  6E879113613D9EAD CRC64;
     MKKKRAFLKW AGGKYPLVDD IRRHLPEGER LIEPFVGAGS VFLNTDYDSY ILSDINSDLI
     NLYDTVKSRP EEFINHARPL FSQEFNTAED FYRLREEFNK SQEPLYRSLL FLYLNRHCYN
     GLCRYNSRGE FNVPFGRYKK PYFPEDELYW FAEKAQKASF VCQHYQITLD NAPQGSVIYC
     DPPYAPLSAT ANFTAYHTNS FNLLDQENLA RMAYHLSSQQ GIPVLISNHD TLMTREWYHQ
     ATLHIVKARR TISRNILARS KVDELLALYC RK
//

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