MRM2_DROME
ID MRM2_DROME Reviewed; 250 AA.
AC Q9VDT6;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 131.
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=CG11447;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
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 1579 (Um1579) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE014297; AAF55704.1; -; Genomic_DNA.
DR EMBL; AY071418; AAL49040.1; -; mRNA.
DR RefSeq; NP_650835.1; NM_142578.4.
DR AlphaFoldDB; Q9VDT6; -.
DR SMR; Q9VDT6; -.
DR IntAct; Q9VDT6; 5.
DR STRING; 7227.FBpp0083225; -.
DR PaxDb; Q9VDT6; -.
DR PRIDE; Q9VDT6; -.
DR DNASU; 42359; -.
DR EnsemblMetazoa; FBtr0083815; FBpp0083225; FBgn0038737.
DR GeneID; 42359; -.
DR KEGG; dme:Dmel_CG11447; -.
DR UCSC; CG11447-RA; d. melanogaster.
DR FlyBase; FBgn0038737; CG11447.
DR VEuPathDB; VectorBase:FBgn0038737; -.
DR eggNOG; KOG4589; Eukaryota.
DR GeneTree; ENSGT00730000111241; -.
DR HOGENOM; CLU_009422_4_2_1; -.
DR InParanoid; Q9VDT6; -.
DR OMA; HRQTDHL; -.
DR OrthoDB; 1039414at2759; -.
DR PhylomeDB; Q9VDT6; -.
DR BioGRID-ORCS; 42359; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 42359; -.
DR PRO; PR:Q9VDT6; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0038737; Expressed in adult hindgut (Drosophila) and 19 other tissues.
DR Genevisible; Q9VDT6; DM.
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; ISS:FlyBase.
DR GO; GO:1902775; P:mitochondrial large ribosomal subunit assembly; IMP:FlyBase.
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 2: Evidence at transcript level;
KW Methyltransferase; Mitochondrion; Reference proteome; rRNA processing;
KW S-adenosyl-L-methionine; Transferase; Transit peptide.
FT TRANSIT 1..35
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 36..250
FT /note="rRNA methyltransferase 2, mitochondrial"
FT /id="PRO_0000155584"
FT ACT_SITE 201
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P0C0R7"
FT BINDING 90..93
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9UI43"
FT BINDING 119
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9UI43"
FT BINDING 136..137
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9UI43"
FT BINDING 161
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9UI43"
SQ SEQUENCE 250 AA; 28137 MW; 76F3D2891D1BED4E CRC64;
MRLVFTGNCV FKRLLHTEIG GKYAKQQPRN LKGRSKSSQE WLTRQLADPY VEKARMMNYR
CRSAFKLLEI DDKYGILRPG DTVLECGAAP GSWTQVAVER TNANGKQERA PQGAVFSIDL
LHFHAVPGAT IFGGMDFTSS LAQKRLREAL QDRKVNCVLS DMAPNATGVR MLDQESITNL
CYEVLRFALA MSAPQAHLVV KVWDNGDVPK LERDMLRFYE KVKRVKPRAS RGDSAEHFLV
ARNFKGATDS
