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RNMT_MYCBP
ID   RNMT_MYCBP              Reviewed;         245 AA.
AC   A1KMV3;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Rhamnosyl O-methyltransferase;
DE            EC=2.1.1.-;
DE   Flags: Precursor;
GN   OrderedLocusNames=BCG_2980c;
OS   Mycobacterium bovis (strain BCG / Pasteur 1173P2).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=410289;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCG / Pasteur 1173P2;
RX   PubMed=17372194; DOI=10.1073/pnas.0700869104;
RA   Brosch R., Gordon S.V., Garnier T., Eiglmeier K., Frigui W., Valenti P.,
RA   Dos Santos S., Duthoy S., Lacroix C., Garcia-Pelayo C., Inwald J.K.,
RA   Golby P., Garcia J.N., Hewinson R.G., Behr M.A., Quail M.A., Churcher C.,
RA   Barrell B.G., Parkhill J., Cole S.T.;
RT   "Genome plasticity of BCG and impact on vaccine efficacy.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:5596-5601(2007).
CC   -!- FUNCTION: Catalyzes the O-methylation of the hydroxyl group located on
CC       C-2 of the first rhamnosyl residue linked to the phenolic group of
CC       glycosylated phenolphthiocerol dimycocerosates (PGL) and p-
CC       hydroxybenzoic acid derivatives (p-HBAD). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the rhamnosyl O-methyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AM408590; CAL72969.1; -; Genomic_DNA.
DR   RefSeq; WP_003414919.1; NC_008769.1.
DR   AlphaFoldDB; A1KMV3; -.
DR   SMR; A1KMV3; -.
DR   GeneID; 45426947; -.
DR   KEGG; mbb:BCG_2980c; -.
DR   HOGENOM; CLU_063868_0_0_11; -.
DR   OMA; MIQGSSI; -.
DR   Proteomes; UP000001472; Chromosome.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008610; P:lipid biosynthetic process; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR007072; Rhamnosyl_O-MeTrfase_CmcI.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF04989; CmcI; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   3: Inferred from homology;
KW   Lipid biosynthesis; Lipid metabolism; Methyltransferase; Signal;
KW   Transferase.
FT   SIGNAL          1..38
FT                   /evidence="ECO:0000255"
FT   CHAIN           39..245
FT                   /note="Rhamnosyl O-methyltransferase"
FT                   /id="PRO_0000305179"
SQ   SEQUENCE   245 AA;  27845 MW;  0B2540CBB532E3A6 CRC64;
     MGLVWRSRTS LVGQLIGLVR LVASFAAQLF YRPSDAVAEE YHKWYYGNLV WTKTTYMGIN
     CWKSVSDMWN YQEILSELQP SLVIEFGTRY GGSAVYFANI MRQIGQPFKV LTVDNSHKAL
     DPRARREPDV LFVESSSTDP AIAEQIQRLK NEYPGKIFAI LDSDHSMNHV LAEMKLLRPL
     LSAGDYLVVE DSNINGHPVL PGFGPGPYEA IEAYEDEFPN DYKHDAEREN KFGWTSAPNG
     FLIRN
 
 
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