RLME_TREPR
ID RLME_TREPR Reviewed; 202 AA.
AC Q8KTR0;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Ribosomal RNA large subunit methyltransferase E;
DE EC=2.1.1.166;
DE AltName: Full=23S rRNA Um2552 methyltransferase;
DE AltName: Full=rRNA (uridine-2'-O-)-methyltransferase;
GN Name=rlmE; Synonyms=ftsJ, rrmJ;
OS Tremblaya princeps.
OC Bacteria; Proteobacteria; Betaproteobacteria; Candidatus Tremblaya.
OX NCBI_TaxID=189385;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12088995; DOI=10.1128/aem.68.7.3198-3205.2002;
RA Baumann L., Thao M.L., Hess J.M., Johnson M.W., Baumann P.;
RT "The genetic properties of the primary endosymbionts of mealybugs differ
RT from those of other endosymbionts of plant sap-sucking insects.";
RL Appl. Environ. Microbiol. 68:3198-3205(2002).
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:0000250}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RNA methyltransferase RlmE family. {ECO:0000305}.
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DR EMBL; AF481102; AAM75988.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8KTR0; -.
DR SMR; Q8KTR0; -.
DR STRING; 1053648.TCP_037; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008650; F:rRNA (uridine-2'-O-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_01547; RNA_methyltr_E; 1.
DR InterPro; IPR002877; RNA_MeTrfase_FtsJ_dom.
DR InterPro; IPR015507; rRNA-MeTfrase_E.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF01728; FtsJ; 1.
DR PIRSF; PIRSF005461; 23S_rRNA_mtase; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Methyltransferase; rRNA processing; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..202
FT /note="Ribosomal RNA large subunit methyltransferase E"
FT /id="PRO_0000155543"
FT ACT_SITE 160
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 57
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 59
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 80
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 96
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 120
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
SQ SEQUENCE 202 AA; 22594 MW; 8C0DB15077D882E1 CRC64;
MGRTSEWYAR HVGDSFVRTS KAWGYRARAA CKLKRLDAKY GLMSRQCDVL ELGSSPGVWS
QYISYERRVS GMAWRTVSVD TRAMVRVRGV SFIHGDITEA ETMAEVSSRL PSGVGLILSD
ICPHPSCERY LDSIATAKVA ETLLMVSRRF LLDGGALLHK TFVIRAEHIA SVMERHFSSV
EVYRDASSRS FNSEAYLLCV GD
