(data stored in ACNUC7421 zone)

SWISSPROT: D8NK18_RALSL

ID   D8NK18_RALSL            Unreviewed;       438 AA.
AC   D8NK18;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   08-MAY-2019, entry version 52.
DE   RecName: Full=Cytosine-specific methyltransferase {ECO:0000256|RuleBase:RU000417};
DE            EC=2.1.1.37 {ECO:0000256|RuleBase:RU000417};
GN   ORFNames=RCFBP_10010 {ECO:0000313|EMBL:CBJ41330.1};
OS   Ralstonia solanacearum CFBP2957.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=859656 {ECO:0000313|EMBL:CBJ41330.1, ECO:0000313|Proteomes:UP000008677};
RN   [1] {ECO:0000313|EMBL:CBJ41330.1, ECO:0000313|Proteomes:UP000008677}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFBP2957 {ECO:0000313|EMBL:CBJ41330.1};
RX   PubMed=20550686; DOI=10.1186/1471-2164-11-379;
RA   Remenant B., Coupat-Goutaland B., Guidot A., Cellier G., Wicker E.,
RA   Allen C., Fegan M., Pruvost O., Elbaz M., Calteau A., Salvignol G.,
RA   Mornico D., Mangenot S., Barbe V., Medigue C., Prior P.;
RT   "Genomes of three tomato pathogens within the Ralstonia solanacearum
RT   species complex reveal significant evolutionary divergence.";
RL   BMC Genomics 11:379-379(2010).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a
CC         5-methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:13681, Rhea:RHEA-COMP:11369,
CC         Rhea:RHEA-COMP:11370, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:85452, ChEBI:CHEBI:85454;
CC         EC=2.1.1.37; Evidence={ECO:0000256|RuleBase:RU000417};
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding
CC       methyltransferase superfamily. C5-methyltransferase family.
CC       {ECO:0000256|PROSITE-ProRule:PRU01016,
CC       ECO:0000256|RuleBase:RU000416}.
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DR   EMBL; FP885897; CBJ41330.1; -; Genomic_DNA.
DR   REBASE; 26794; M.RsoCFORF10010P.
DR   EnsemblBacteria; CBJ41330; CBJ41330; RCFBP_10010.
DR   KEGG; rsc:RCFBP_10010; -.
DR   HOGENOM; HOG000225505; -.
DR   KO; K00558; -.
DR   BioCyc; RSOL859656:G13C7-10-MONOMER; -.
DR   Proteomes; UP000008677; Chromosome.
DR   GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IEA:UniProtKB-EC.
DR   InterPro; IPR018117; C5_DNA_meth_AS.
DR   InterPro; IPR001525; C5_MeTfrase.
DR   InterPro; IPR031303; C5_meth_CS.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   Pfam; PF00145; DNA_methylase; 1.
DR   PRINTS; PR00105; C5METTRFRASE.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR00675; dcm; 1.
DR   PROSITE; PS00094; C5_MTASE_1; 1.
DR   PROSITE; PS00095; C5_MTASE_2; 1.
DR   PROSITE; PS51679; SAM_MT_C5; 1.
PE   3: Inferred from homology;
DR   PRODOM; D8NK18.
DR   SWISS-2DPAGE; D8NK18.
KW   Complete proteome {ECO:0000313|Proteomes:UP000008677};
KW   Methyltransferase {ECO:0000256|PROSITE-ProRule:PRU01016,
KW   ECO:0000256|RuleBase:RU000417, ECO:0000313|EMBL:CBJ41330.1};
KW   S-adenosyl-L-methionine {ECO:0000256|PROSITE-ProRule:PRU01016};
KW   Transferase {ECO:0000256|PROSITE-ProRule:PRU01016,
KW   ECO:0000256|RuleBase:RU000417, ECO:0000313|EMBL:CBJ41330.1}.
FT   ACT_SITE     96     96       {ECO:0000256|PROSITE-ProRule:PRU01016}.
SQ   SEQUENCE   438 AA;  49147 MW;  090CF388C82F9742 CRC64;
     MDNTKPLRFA DVFAGCGGLS LGLLEAGCQG VFAIERSPLA FETLRHNLID GKQHKFDWPN
     WLPKEAMTCE DLLFRHGAQL DGIKGAIDLI VGGPPCQGFS TAGRRDPADP RNQMTEQYLV
     LVEKLQPRFL VIENVAGFNM RFDDEENLDK LLKDPKHDSY ADYVAGRLED LGYSVFRGLV
     NCSDFGVPQN RLRYLVLCEL RGKSEGPMPD LFQELLKGRK AFLTSKDLPV KRKTTVKEAI
     ADLLVAGKPR VENEDSEVKG FKEAVYDAPR NPKGYLKLMR AYSPGEAPNS RRLPNHKKTT
     IEYFKKVQKV CRPGYSLTVK QRAKIGTKKH STTVLHADLP APTVTTLPDD ILHYSEPRIL
     TVRENARLQS FPDWFEFRGK YTTGGKQRKQ ECPRYTQVGN AVPPLLAEAI GRLVSSRSQA
     VTVEPDERTC LTTADIIV
//

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