(data stored in ACNUC7421 zone)

SWISSPROT: RLME_SINFN

ID   RLME_SINFN              Reviewed;         245 AA.
AC   C3MGQ4;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   07-JUN-2017, entry version 50.
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=NGR_c03730;
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234;
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of
RT   secretion systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
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; CP001389; ACP24169.1; -; Genomic_DNA.
DR   RefSeq; WP_012706954.1; NC_012587.1.
DR   RefSeq; YP_002824922.1; NC_012587.1.
DR   ProteinModelPortal; C3MGQ4; -.
DR   SMR; C3MGQ4; -.
DR   STRING; 394.NGR_c03730; -.
DR   EnsemblBacteria; ACP24169; ACP24169; NGR_c03730.
DR   GeneID; 7791599; -.
DR   KEGG; rhi:NGR_c03730; -.
DR   PATRIC; fig|394.7.peg.3178; -.
DR   eggNOG; ENOG4105F7M; Bacteria.
DR   eggNOG; COG0293; LUCA.
DR   HOGENOM; HOG000162366; -.
DR   KO; K02427; -.
DR   OMA; HRQTDHL; -.
DR   OrthoDB; POG091H05ST; -.
DR   Proteomes; UP000001054; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0001510; P:RNA methylation; IEA:InterPro.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR   HAMAP; MF_01547; RNA_methyltr_E; 1.
DR   InterPro; IPR015507; rRNA-MeTfrase_E.
DR   InterPro; IPR002877; rRNA_MeTrfase_FtsJ_dom.
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.
PE   3: Inferred from homology;
DR   PRODOM; C3MGQ4.
DR   SWISS-2DPAGE; C3MGQ4.
KW   Complete proteome; Cytoplasm; Methyltransferase; Reference proteome;
KW   rRNA processing; S-adenosyl-L-methionine; Transferase.
FT   CHAIN         1    245       Ribosomal RNA large subunit
FT                                methyltransferase E.
FT                                /FTId=PRO_1000185300.
FT   ACT_SITE    184    184       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01547}.
FT   BINDING      81     81       S-adenosyl-L-methionine; via amide
FT                                nitrogen. {ECO:0000255|HAMAP-
FT                                Rule:MF_01547}.
FT   BINDING      83     83       S-adenosyl-L-methionine; via amide
FT                                nitrogen. {ECO:0000255|HAMAP-
FT                                Rule:MF_01547}.
FT   BINDING     104    104       S-adenosyl-L-methionine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01547}.
FT   BINDING     120    120       S-adenosyl-L-methionine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01547}.
FT   BINDING     144    144       S-adenosyl-L-methionine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01547}.
SQ   SEQUENCE   245 AA;  26986 MW;  6AEDE3F8ACF919EA CRC64;
     MTKSPIGGNR SGRKLGQKVK KGKLKASSRR WLERHINDPY VQRAQLEGYR ARAAFKLLEI
     DEKHKILAGA RRIIDLGAAP GSWSQIAAKV TNSTDADPRV AAIDFLEMDP IPGVRFLQLD
     FLDPEAPEKL KEAIGGTPDL VLSDMAAPTT GHRQTDHLRT MHLCEVAAHF AVDVLAKGGH
     FLAKTFQGGT ERDLLNMLKQ NFSQVIHVKP ASSRTESVEM FLLAKGFKGR RKAETEEPAE
     DAAAE
//

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