RLME_THEVO
ID RLME_THEVO Reviewed; 197 AA.
AC Q97C13;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 109.
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=rrmJ {ECO:0000255|HAMAP-Rule:MF_01547}; OrderedLocusNames=TV0292;
GN ORFNames=TVG0303954;
OS Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC
OS 15438 / GSS1).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1;
RX PubMed=11121031; DOI=10.1073/pnas.97.26.14257;
RA Kawashima T., Amano N., Koike H., Makino S., Higuchi S., Kawashima-Ohya Y.,
RA Watanabe K., Yamazaki M., Kanehori K., Kawamoto T., Nunoshiba T.,
RA Yamamoto Y., Aramaki H., Makino K., Suzuki M.;
RT "Archaeal adaptation to higher temperatures revealed by genomic sequence of
RT Thermoplasma volcanium.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(2000).
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}.
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DR EMBL; BA000011; BAB59434.1; -; Genomic_DNA.
DR RefSeq; WP_010916547.1; NC_002689.2.
DR PDB; 3DOU; X-ray; 1.45 A; A=17-196.
DR PDBsum; 3DOU; -.
DR AlphaFoldDB; Q97C13; -.
DR SMR; Q97C13; -.
DR STRING; 273116.14324507; -.
DR PRIDE; Q97C13; -.
DR DNASU; 1440805; -.
DR EnsemblBacteria; BAB59434; BAB59434; BAB59434.
DR GeneID; 1440805; -.
DR KEGG; tvo:TVG0303954; -.
DR eggNOG; arCOG00079; Archaea.
DR HOGENOM; CLU_009422_4_4_2; -.
DR OMA; HRQTDHL; -.
DR OrthoDB; 105478at2157; -.
DR PhylomeDB; Q97C13; -.
DR EvolutionaryTrace; Q97C13; -.
DR Proteomes; UP000001017; 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 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Methyltransferase; rRNA processing;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..197
FT /note="Ribosomal RNA large subunit methyltransferase E"
FT /id="PRO_0000155574"
FT ACT_SITE 151
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01547"
FT BINDING 50
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01547"
FT BINDING 52
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01547"
FT BINDING 67
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01547"
FT BINDING 83
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01547"
FT BINDING 111
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01547"
FT HELIX 21..33
FT /evidence="ECO:0007829|PDB:3DOU"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:3DOU"
FT HELIX 51..56
FT /evidence="ECO:0007829|PDB:3DOU"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:3DOU"
FT STRAND 61..69
FT /evidence="ECO:0007829|PDB:3DOU"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:3DOU"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:3DOU"
FT HELIX 89..100
FT /evidence="ECO:0007829|PDB:3DOU"
FT STRAND 103..110
FT /evidence="ECO:0007829|PDB:3DOU"
FT HELIX 120..141
FT /evidence="ECO:0007829|PDB:3DOU"
FT STRAND 142..153
FT /evidence="ECO:0007829|PDB:3DOU"
FT HELIX 158..165
FT /evidence="ECO:0007829|PDB:3DOU"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:3DOU"
FT STRAND 169..175
FT /evidence="ECO:0007829|PDB:3DOU"
FT STRAND 186..194
FT /evidence="ECO:0007829|PDB:3DOU"
SQ SEQUENCE 197 AA; 22604 MW; DC1682A2E42D05E5 CRC64;
MTGDRRDEYY WKAKKEQLRS RAAFKLEFLL DRYRVVRKGD AVIEIGSSPG GWTQVLNSLA
RKIISIDLQE MEEIAGVRFI RCDIFKETIF DDIDRALREE GIEKVDDVVS DAMAKVSGIP
SRDHAVSYQI GQRVMEIAVR YLRNGGNVLL KQFQGDMTND FIAIWRKNFS SYKISKPPAS
RGSSSEIYIM FFGFKAP
