(data stored in ACNUC7421 zone)

SWISSPROT: RLME_EDWI9

ID   RLME_EDWI9              Reviewed;         208 AA.
AC   C5BFB0;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 54.
DE   RecName: Full=Ribosomal RNA large subunit methyltransferase E {ECO:0000255|HAMAP-Rule:MF_01547};
DE            EC=2.1.1.166 {ECO:0000255|HAMAP-Rule:MF_01547};
DE   AltName: Full=23S rRNA Um2552 methyltransferase {ECO:0000255|HAMAP-Rule:MF_01547};
DE   AltName: Full=rRNA (uridine-2'-O-)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01547};
GN   Name=rlmE {ECO:0000255|HAMAP-Rule:MF_01547};
GN   Synonyms=ftsJ {ECO:0000255|HAMAP-Rule:MF_01547},
GN   rrmJ {ECO:0000255|HAMAP-Rule:MF_01547}; OrderedLocusNames=NT01EI_0458;
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146;
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Specifically methylates the uridine in position 2552 of
CC       23S rRNA at the 2'-O position of the ribose in the fully assembled
CC       50S ribosomal subunit. {ECO:0000255|HAMAP-Rule:MF_01547}.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + uridine(2552) in 23S
CC       rRNA = S-adenosyl-L-homocysteine + 2'-O-methyluridine(2552) in 23S
CC       rRNA. {ECO:0000255|HAMAP-Rule:MF_01547}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01547}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding
CC       methyltransferase superfamily. RNA methyltransferase RlmE family.
CC       {ECO:0000255|HAMAP-Rule:MF_01547}.
DR   EMBL; CP001600; ACR67696.1; -; Genomic_DNA.
DR   RefSeq; WP_015869898.1; NC_012779.2.
DR   ProteinModelPortal; C5BFB0; -.
DR   SMR; C5BFB0; -.
DR   STRING; 634503.NT01EI_0458; -.
DR   EnsemblBacteria; ACR67696; ACR67696; NT01EI_0458.
DR   GeneID; 7961283; -.
DR   KEGG; eic:NT01EI_0458; -.
DR   PATRIC; fig|634503.3.peg.417; -.
DR   eggNOG; ENOG4105F7M; Bacteria.
DR   eggNOG; COG0293; LUCA.
DR   HOGENOM; HOG000162367; -.
DR   KO; K02427; -.
DR   OMA; HRQTDHL; -.
DR   OrthoDB; POG091H05ST; -.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016436; F:rRNA (uridine) methyltransferase activity; IEA:InterPro.
DR   HAMAP; MF_01547; RNA_methyltr_E; 1.
DR   InterPro; IPR015507; rRNA-MeTfrase_E.
DR   InterPro; IPR002877; rRNA_MeTrfase_FtsJ_dom.
DR   InterPro; IPR004512; rRNA_MeTrfase_gammaproteobac.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   PANTHER; PTHR10920; PTHR10920; 1.
DR   Pfam; PF01728; FtsJ; 1.
DR   PIRSF; PIRSF005461; 23S_rRNA_mtase; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR00438; rrmJ; 1.
PE   3: Inferred from homology;
DR   PRODOM; C5BFB0.
DR   SWISS-2DPAGE; C5BFB0.
KW   Complete proteome; Cytoplasm; Methyltransferase; Reference proteome;
KW   rRNA processing; S-adenosyl-L-methionine; Transferase.
FT   CHAIN         1    208       Ribosomal RNA large subunit
FT                                methyltransferase E.
FT                                /FTId=PRO_1000215453.
FT   ACT_SITE    163    163       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01547}.
FT   BINDING      62     62       S-adenosyl-L-methionine; via amide
FT                                nitrogen. {ECO:0000255|HAMAP-
FT                                Rule:MF_01547}.
FT   BINDING      64     64       S-adenosyl-L-methionine; via amide
FT                                nitrogen. {ECO:0000255|HAMAP-
FT                                Rule:MF_01547}.
FT   BINDING      82     82       S-adenosyl-L-methionine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01547}.
FT   BINDING      98     98       S-adenosyl-L-methionine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01547}.
FT   BINDING     123    123       S-adenosyl-L-methionine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01547}.
SQ   SEQUENCE   208 AA;  23094 MW;  C43123521F0E8CAF CRC64;
     MGKKRSASSS RWLQEHFSDK YVQQAQKKGL RSRAWFKLDE IQGTDKIFRP GMTVVDLGAA
     PGGWSQYVVT QIGDKGRVIA CDLLPMDPIV GVDFLQGDFR DELVLAALME RVGDAKVQVV
     MSDMAPNMSG TPSVDIPRAM YLVELAFEMA KDVLAPGGSF VVKVFQGEGF DEYLGQIRSL
     FTKVKIRKPE ASRARSREVY IVATGRKL
//

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