(data stored in ACNUC7421 zone)

SWISSPROT: RLME_DESOH

ID   RLME_DESOH              Reviewed;         207 AA.
AC   A8ZT18;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   11-DEC-2019, entry version 67.
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=Dole_0372;
OS   Desulfococcus oleovorans (strain DSM 6200 / Hxd3).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC   Desulfobacteraceae; Desulfococcus.
OX   NCBI_TaxID=96561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6200 / Hxd3;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Wawrik B.,
RA   Richardson P.;
RT   "Complete sequence of Desulfococcus oleovorans Hxd3.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Specifically methylates the uridine in position 2552 of 23S
CC       rRNA at the 2'-O position of the ribose in the fully assembled 50S
CC       ribosomal subunit. {ECO:0000255|HAMAP-Rule:MF_01547}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-adenosyl-L-methionine + uridine(2552) in 23S rRNA = 2'-O-
CC         methyluridine(2552) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:42720, Rhea:RHEA-COMP:10202, Rhea:RHEA-COMP:10203,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:65315, ChEBI:CHEBI:74478; EC=2.1.1.166;
CC         Evidence={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 methyltransferase
CC       superfamily. RNA methyltransferase RlmE family. {ECO:0000255|HAMAP-
CC       Rule:MF_01547}.
DR   EMBL; CP000859; ABW66182.1; -; Genomic_DNA.
DR   RefSeq; WP_012173801.1; NC_009943.1.
DR   SMR; A8ZT18; -.
DR   STRING; 96561.Dole_0372; -.
DR   EnsemblBacteria; ABW66182; ABW66182; Dole_0372.
DR   KEGG; dol:Dole_0372; -.
DR   eggNOG; ENOG4105F7M; Bacteria.
DR   eggNOG; COG0293; LUCA.
DR   HOGENOM; HOG000162366; -.
DR   KO; K02427; -.
DR   OMA; HRQTDHL; -.
DR   OrthoDB; 1798571at2; -.
DR   BioCyc; DOLE96561:G1GAC-381-MONOMER; -.
DR   Proteomes; UP000008561; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008650; F:rRNA (uridine-2'-O-)-methyltransferase activity; IEA:UniProtKB-UniRule.
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   Pfam; PF01728; FtsJ; 1.
DR   PIRSF; PIRSF005461; 23S_rRNA_mtase; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   3: Inferred from homology;
DR   PRODOM; A8ZT18.
DR   SWISS-2DPAGE; A8ZT18.
KW   Cytoplasm; Methyltransferase; Reference proteome; rRNA processing;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..207
FT                   /note="Ribosomal RNA large subunit methyltransferase E"
FT                   /id="PRO_1000185293"
FT   ACT_SITE        156
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01547"
FT   BINDING         56
FT                   /note="S-adenosyl-L-methionine; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01547"
FT   BINDING         58
FT                   /note="S-adenosyl-L-methionine; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01547"
FT   BINDING         76
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01547"
FT   BINDING         94
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01547"
FT   BINDING         116
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01547"
SQ   SEQUENCE   207 AA;  22988 MW;  489085790FA06487 CRC64;
     MKRDPTKGRK TPDHYARKAK TEHYPARSVY KLQEIQKKHN VLKPGNAVLD LGCFPGSWMM
     FAAETVGRGG KVTGIDLKKV ATHMPAQATS LQEDIYEIDR EALAGTLGPL DVVLSDMAPD
     TMGNKFTDAA RSFHLAAAAL DLALFLLKPG GHFVCKVFQG EDFQNFVNMV KAEFERHKVF
     KPETCRKDSK ETYVIGFSKK ESTHVGS
//

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