MRM3_DROME
ID MRM3_DROME Reviewed; 407 AA.
AC Q9VW14; Q8SZ70;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=rRNA methyltransferase 3, mitochondrial {ECO:0000250|UniProtKB:Q9HC36};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:Q9HC36};
DE AltName: Full=RNA methyltransferase-like protein 1 {ECO:0000250|UniProtKB:Q9HC36};
DE AltName: Full=rRNA (guanosine-2'-O)-methyltransferase {ECO:0000250|UniProtKB:Q9HC36};
DE Flags: Precursor;
GN ORFNames=CG14100;
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 METHYLGUANOSINE 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-methylguanosine
CC at position 1580 (Gm1580) in the mitochondrial large subunit ribosomal
CC RNA (mtLSU rRNA), a conserved modification in the peptidyl transferase
CC domain of the mtLSU rRNA. {ECO:0000250|UniProtKB:Q9HC36,
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:Q9HC36};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9HC36}.
CC -!- SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase
CC superfamily. RNA methyltransferase TrmH family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL48701.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AE014296; AAF49141.1; -; Genomic_DNA.
DR EMBL; AY071079; AAL48701.1; ALT_FRAME; mRNA.
DR RefSeq; NP_649130.2; NM_140873.4.
DR AlphaFoldDB; Q9VW14; -.
DR SMR; Q9VW14; -.
DR BioGRID; 65402; 1.
DR IntAct; Q9VW14; 7.
DR STRING; 7227.FBpp0074739; -.
DR PaxDb; Q9VW14; -.
DR PRIDE; Q9VW14; -.
DR EnsemblMetazoa; FBtr0074971; FBpp0074739; FBgn0036889.
DR GeneID; 40132; -.
DR KEGG; dme:Dmel_CG14100; -.
DR UCSC; CG14100-RA; d. melanogaster.
DR FlyBase; FBgn0036889; CG14100.
DR VEuPathDB; VectorBase:FBgn0036889; -.
DR eggNOG; KOG2506; Eukaryota.
DR GeneTree; ENSGT00940000166642; -.
DR HOGENOM; CLU_021322_1_1_1; -.
DR InParanoid; Q9VW14; -.
DR OMA; ERKRAPG; -.
DR OrthoDB; 1183644at2759; -.
DR PhylomeDB; Q9VW14; -.
DR BioGRID-ORCS; 40132; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 40132; -.
DR PRO; PR:Q9VW14; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0036889; Expressed in cleaving embryo and 20 other tissues.
DR ExpressionAtlas; Q9VW14; baseline and differential.
DR Genevisible; Q9VW14; DM.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1330.30; -; 1.
DR Gene3D; 3.40.1280.10; -; 1.
DR InterPro; IPR029028; Alpha/beta_knot_MTases.
DR InterPro; IPR029064; L30e-like.
DR InterPro; IPR001537; SpoU_MeTrfase.
DR InterPro; IPR013123; SpoU_subst-bd.
DR InterPro; IPR029026; tRNA_m1G_MTases_N.
DR Pfam; PF00588; SpoU_methylase; 1.
DR Pfam; PF08032; SpoU_sub_bind; 1.
DR SMART; SM00967; SpoU_sub_bind; 1.
DR SUPFAM; SSF55315; SSF55315; 1.
DR SUPFAM; SSF75217; SSF75217; 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..25
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 26..407
FT /note="rRNA methyltransferase 3, mitochondrial"
FT /id="PRO_0000311307"
FT BINDING 347
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 373
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 382
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
SQ SEQUENCE 407 AA; 45044 MW; CFD7041331D92C41 CRC64;
MLCNIFKRSL QANIRNVNNL NVLRLSSSSG PRGEIQDALD IEANLFGNSD LRHEPMNTRE
ALRKNRFAGR KPKVPFASVA SRNLSAPSNP APRVAPTPAP VIKDNELNLE FVRLTLQDPL
TSTLLTTVRS RKRRDKNRQI IVEGRRLIQE ALQCGLKMEV LLFSQKDQLA LVKEEVGVAQ
VETGTKIYKV PQHDLKTWSS LVTPPGLMAI FDRPSDKGLE KNLAEQQRLG SQPFPITVVC
DNIREPNNLG SIIRTCAALP CSQVVVTHGC CDPWESKALR GGCGGQFRVP IRDDVTWDEL
ALTIPPEAAD DCHVFIAETN QRKRENNQTI DYADIKGLGA HNLLIIGGES HGVSEEAYRF
LNLVGGKGKC IYIPLAAGID SLNVASALTL LLFELRRKLI HQASEKE
