MRM2_CAEEL
ID MRM2_CAEEL Reviewed; 214 AA.
AC O62251;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=rRNA methyltransferase 2, mitochondrial {ECO:0000250|UniProtKB:Q9UI43};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:Q9UI43};
DE AltName: Full=rRNA (uridine-2'-O)-methyltransferase {ECO:0000250|UniProtKB:Q9UI43};
DE Flags: Precursor;
GN ORFNames=F45G2.9;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP POSITION OF MODIFIED METHYLURIDINE IN MTLSU RRNA.
RX PubMed=25009282; DOI=10.1091/mbc.e14-01-0014;
RA Rorbach J., Boesch P., Gammage P.A., Nicholls T.J., Pearce S.F., Patel D.,
RA Hauser A., Perocchi F., Minczuk M.;
RT "MRM2 and MRM3 are involved in biogenesis of the large subunit of the
RT mitochondrial ribosome.";
RL Mol. Biol. Cell 25:2542-2555(2014).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent 2'-O-ribose
CC methyltransferase that catalyzes the formation of 2'-O-methyluridine at
CC position 808 (Um808) in the mitochondrial large subunit ribosomal RNA
CC (mtLSU rRNA), a universally conserved modification in the peptidyl
CC transferase domain of the mtLSU rRNA. {ECO:0000250|UniProtKB:Q9UI43,
CC ECO:0000305|PubMed:25009282}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a uridine in rRNA + S-adenosyl-L-methionine = a 2'-O-
CC methyluridine in rRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:54152, Rhea:RHEA-COMP:13812, Rhea:RHEA-COMP:13814,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:65315, ChEBI:CHEBI:74478;
CC Evidence={ECO:0000250|UniProtKB:Q9UI43};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9UI43}.
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; BX284603; CAB07618.1; -; Genomic_DNA.
DR PIR; T22241; T22241.
DR RefSeq; NP_499776.1; NM_067375.4.
DR AlphaFoldDB; O62251; -.
DR SMR; O62251; -.
DR STRING; 6239.F45G2.9; -.
DR PaxDb; O62251; -.
DR EnsemblMetazoa; F45G2.9.1; F45G2.9.1; WBGene00009735.
DR GeneID; 185813; -.
DR KEGG; cel:CELE_F45G2.9; -.
DR UCSC; F45G2.9; c. elegans.
DR CTD; 185813; -.
DR WormBase; F45G2.9; CE16052; WBGene00009735; -.
DR eggNOG; KOG4589; Eukaryota.
DR GeneTree; ENSGT00730000111241; -.
DR HOGENOM; CLU_009422_4_2_1; -.
DR InParanoid; O62251; -.
DR OMA; HRQTDHL; -.
DR OrthoDB; 1039414at2759; -.
DR PhylomeDB; O62251; -.
DR PRO; PR:O62251; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00009735; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0008173; F:RNA methyltransferase activity; IBA:GO_Central.
DR GO; GO:0008650; F:rRNA (uridine-2'-O-)-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0001510; P:RNA methylation; IBA:GO_Central.
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 Methyltransferase; Mitochondrion; Reference proteome; rRNA processing;
KW S-adenosyl-L-methionine; Transferase; Transit peptide.
FT TRANSIT 1..18
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 19..214
FT /note="rRNA methyltransferase 2, mitochondrial"
FT /id="PRO_0000155585"
FT ACT_SITE 169
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P0C0R7"
FT BINDING 63..66
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9UI43"
FT BINDING 83
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9UI43"
FT BINDING 100..101
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9UI43"
FT BINDING 125
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9UI43"
SQ SEQUENCE 214 AA; 24297 MW; AD3F32F72663B0C7 CRC64;
MFSTKKSQGN LHKYIQRQST DEFAVKAREH NYRARSAFKL IEINEKFKFL KPESTVIDIG
CAPGSWLQVV VQKCPNGYAS GVDLQNVLPI RGADILSLSD ITDPAVKLKI REKLAHRQVD
VVLSDMAPNP TGDNATDHLR LIELCRSVFR LFSVENEIEL VKNGVYLCKI WDGSARAEFV
RELSDRFSTV KTVKPTACRD NSAELYLFCR NFKK
