(data stored in ACNUC7421 zone)

SWISSPROT: C6B2F9_RHILS

ID   C6B2F9_RHILS            Unreviewed;       239 AA.
AC   C6B2F9;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   07-JUN-2017, entry version 58.
DE   RecName: Full=Ribosomal RNA large subunit methyltransferase E {ECO:0000256|HAMAP-Rule:MF_01547};
DE            EC=2.1.1.166 {ECO:0000256|HAMAP-Rule:MF_01547};
DE   AltName: Full=23S rRNA Um2552 methyltransferase {ECO:0000256|HAMAP-Rule:MF_01547};
DE   AltName: Full=rRNA (uridine-2'-O-)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01547};
GN   Name=rlmE {ECO:0000256|HAMAP-Rule:MF_01547};
GN   Synonyms=ftsJ {ECO:0000256|HAMAP-Rule:MF_01547}, rrmJ
GN   {ECO:0000256|HAMAP-Rule:MF_01547};
GN   OrderedLocusNames=Rleg_0473 {ECO:0000313|EMBL:ACS54779.1};
OS   Rhizobium leguminosarum bv. trifolii (strain WSM1325).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=395491 {ECO:0000313|EMBL:ACS54779.1, ECO:0000313|Proteomes:UP000002256};
RN   [1] {ECO:0000313|EMBL:ACS54779.1, ECO:0000313|Proteomes:UP000002256}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM1325 {ECO:0000313|EMBL:ACS54779.1,
RC   ECO:0000313|Proteomes:UP000002256};
RX   PubMed=21304718;
RA   Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K.,
RA   Tiwari R., Copeland A., Nolan M., Han C., Brettin T., Land M.,
RA   Ovchinikova G., Ivanova N., Mavromatis K., Markowitz V., Kyrpides N.,
RA   Melino V., Denton M., Yates R., Howieson J.;
RT   "Complete genome sequence of Rhizobium leguminosarum bv. trifolii
RT   strain WSM1325, an effective microsymbiont of annual Mediterranean
RT   clovers.";
RL   Stand. Genomic Sci. 2:347-356(2010).
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:0000256|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:0000256|HAMAP-Rule:MF_01547}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01547}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding
CC       methyltransferase superfamily. RNA methyltransferase RlmE family.
CC       {ECO:0000256|HAMAP-Rule:MF_01547}.
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DR   EMBL; CP001622; ACS54779.1; -; Genomic_DNA.
DR   RefSeq; WP_012756166.1; NC_012850.1.
DR   ProteinModelPortal; C6B2F9; -.
DR   EnsemblBacteria; ACS54779; ACS54779; Rleg_0473.
DR   KEGG; rlg:Rleg_0473; -.
DR   HOGENOM; HOG000162366; -.
DR   KO; K02427; -.
DR   OMA; HRQTDHL; -.
DR   OrthoDB; POG091H05ST; -.
DR   Proteomes; UP000002256; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008650; F:rRNA (uridine-2'-O-)-methyltransferase activity; IEA:UniProtKB-HAMAP.
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; C6B2F9.
DR   SWISS-2DPAGE; C6B2F9.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002256};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01547};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_01547,
KW   ECO:0000313|EMBL:ACS54779.1};
KW   rRNA processing {ECO:0000256|HAMAP-Rule:MF_01547,
KW   ECO:0000256|SAAS:SAAS00676306};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01547,
KW   ECO:0000256|PIRSR:PIRSR005461-1};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01547,
KW   ECO:0000313|EMBL:ACS54779.1}.
FT   DOMAIN       49    227       FtsJ. {ECO:0000259|Pfam:PF01728}.
FT   ACT_SITE    184    184       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01547, ECO:0000256|PIRSR:PIRSR005461-
FT                                1}.
FT   BINDING      81     81       S-adenosyl-L-methionine; via amide
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_01547}.
FT   BINDING      83     83       S-adenosyl-L-methionine; via amide
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_01547}.
FT   BINDING     104    104       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01547}.
FT   BINDING     120    120       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01547}.
FT   BINDING     144    144       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01547}.
SQ   SEQUENCE   239 AA;  26448 MW;  C1D7DA6EC989ECA9 CRC64;
     MTKAPIAGNR TGRKLGQRVK NKKMKASSRQ WLERHINDPY VQRAQLEGYR ARAAFKLLEI
     DEKHHILRGA RRIIDLGAAP GSWSQIAAKV TGSTDDDIRV AAIDFLEMTQ LPGVKILQLD
     FLDPTAPEKL LEAVGGTPDL VISDMAAPTT GHHRTDHLRT MHLCEVAAHF AVEVLGEGGH
     FLTKTFQGGT ERELLAMLKQ NFRQVVHVKP NSSRAESVEM FLLAKGFKGR KAEGNAEEA
//

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