(data stored in SCRATCH zone)

SWISSPROT: D3VG57_XENNA

ID   D3VG57_XENNA            Unreviewed;       272 AA.
AC   D3VG57;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   16-JAN-2019, entry version 46.
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:CBJ88147.1};
GN   OrderedLocusNames=XNC1_0059 {ECO:0000313|EMBL:CBJ88147.1};
OS   Xenorhabdus nematophila (strain ATCC 19061 / DSM 3370 / LMG 1036 /
OS   NCIB 9965 / AN6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406817 {ECO:0000313|EMBL:CBJ88147.1, ECO:0000313|Proteomes:UP000008075};
RN   [1] {ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RA   Goodrich-Blair H., Barbazuk B., Bode H.B., Darby C., Du Z., Forst S.,
RA   Gaudriault S., Goldman B.S., Goodner B., Henkhaus J., Latreille P.,
RA   Medigue C., Miller N., Norton S., Ogier J.C., Rouy Z., Slater S.,
RA   Suen G.;
RT   "Complete genome sequence of Xenorhabdus nematophila (strain ATCC
RT   19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6).";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBJ88147.1, ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
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; FN667742; CBJ88147.1; -; Genomic_DNA.
DR   RefSeq; WP_010847520.1; NC_014228.1.
DR   STRING; 406817.XNC1_0059; -.
DR   REBASE; 26667; M.XnePDam.
DR   EnsemblBacteria; CBJ88147; CBJ88147; XNC1_0059.
DR   KEGG; xne:XNC1_0059; -.
DR   eggNOG; ENOG4105DFE; Bacteria.
DR   eggNOG; COG0338; LUCA.
DR   HOGENOM; HOG000281348; -.
DR   KO; K06223; -.
DR   OMA; MNRHGFN; -.
DR   Proteomes; UP000008075; 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; D3VG57.
DR   SWISS-2DPAGE; D3VG57.
KW   Complete proteome {ECO:0000313|Proteomes:UP000008075};
KW   Methyltransferase {ECO:0000256|RuleBase:RU361257,
KW   ECO:0000313|EMBL:CBJ88147.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008075};
KW   S-adenosyl-L-methionine {ECO:0000256|RuleBase:RU361257};
KW   Transferase {ECO:0000256|RuleBase:RU361257,
KW   ECO:0000313|EMBL:CBJ88147.1}.
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;  31802 MW;  6CBBCA3AC7D6DAC0 CRC64;
     MKKKRAFLKW AGGKYPLVDD IKRHLPEGDC LIEPFVGAGS VFLNTDYDSY ILSDINSDLI
     NLYNTVKSRA DEFINHARPL FFPEFNTSEN FYRMREEFNK SSDPFYRSIL FLYLNRHCYN
     GLCRYNSRGQ FNVPFGRYKK PYFPENELYW FAEKSQKATF ICQHYEIALN NAPKGAVVYC
     DPPYAPLSAT ANFTAYHTNN FNLLDQENLA QIAYHLSSQR GIPVLISNHD TPMTREWYHQ
     ASLYIVKARR TISRNILARS KVDELLALYC QK
//

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