TRM71_DROME
ID TRM71_DROME Reviewed; 302 AA.
AC Q9VEP1; Q53YH6;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Putative tRNA (cytidine(32)/guanosine(34)-2'-O)-methyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_03162};
DE EC=2.1.1.205 {ECO:0000255|HAMAP-Rule:MF_03162};
DE AltName: Full=2'-O-ribose RNA methyltransferase TRM7 homolog 1 {ECO:0000255|HAMAP-Rule:MF_03162};
GN ORFNames=CG5220;
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).
CC -!- FUNCTION: Methylates the 2'-O-ribose of nucleotides at positions 32 and
CC 34 of the tRNA anticodon loop of substrate tRNAs. {ECO:0000255|HAMAP-
CC Rule:MF_03162}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(32)/guanosine(34) in tRNA + 2 S-adenosyl-L-methionine
CC = 2'-O-methylcytidine(32)/2'-O-methylguanosine(34) in tRNA + 2 H(+) +
CC 2 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:42396, Rhea:RHEA-
CC COMP:10246, Rhea:RHEA-COMP:10247, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74269,
CC ChEBI:CHEBI:74445, ChEBI:CHEBI:74495, ChEBI:CHEBI:82748;
CC EC=2.1.1.205; Evidence={ECO:0000255|HAMAP-Rule:MF_03162};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03162}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RNA methyltransferase RlmE family. TRM7 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03162}.
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DR EMBL; AE014297; AAF55380.1; -; Genomic_DNA.
DR EMBL; BT001481; AAN71236.1; -; mRNA.
DR RefSeq; NP_650590.1; NM_142333.3.
DR AlphaFoldDB; Q9VEP1; -.
DR SMR; Q9VEP1; -.
DR BioGRID; 67096; 1.
DR DIP; DIP-23852N; -.
DR IntAct; Q9VEP1; 2.
DR STRING; 7227.FBpp0082832; -.
DR PaxDb; Q9VEP1; -.
DR PRIDE; Q9VEP1; -.
DR DNASU; 42056; -.
DR EnsemblMetazoa; FBtr0083391; FBpp0082832; FBgn0038471.
DR GeneID; 42056; -.
DR KEGG; dme:Dmel_CG5220; -.
DR UCSC; CG5220-RA; d. melanogaster.
DR FlyBase; FBgn0038471; CG5220.
DR VEuPathDB; VectorBase:FBgn0038471; -.
DR eggNOG; KOG1099; Eukaryota.
DR GeneTree; ENSGT00730000111146; -.
DR HOGENOM; CLU_009422_1_2_1; -.
DR InParanoid; Q9VEP1; -.
DR OMA; GLHDMDI; -.
DR OrthoDB; 1362679at2759; -.
DR PhylomeDB; Q9VEP1; -.
DR BioGRID-ORCS; 42056; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 42056; -.
DR PRO; PR:Q9VEP1; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0038471; Expressed in eye disc (Drosophila) and 47 other tissues.
DR Genevisible; Q9VEP1; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0008173; F:RNA methyltransferase activity; IBA:GO_Central.
DR GO; GO:0052666; F:tRNA (cytosine-2'-O-)-methyltransferase activity; IMP:FlyBase.
DR GO; GO:0008175; F:tRNA methyltransferase activity; IBA:GO_Central.
DR GO; GO:0002181; P:cytoplasmic translation; IBA:GO_Central.
DR GO; GO:0001510; P:RNA methylation; IBA:GO_Central.
DR GO; GO:0030488; P:tRNA methylation; IBA:GO_Central.
DR GO; GO:0002128; P:tRNA nucleoside ribose methylation; IMP:FlyBase.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_01547; RNA_methyltr_E; 1.
DR HAMAP; MF_03162; RNA_methyltr_E_TRM7; 1.
DR InterPro; IPR028590; RNA_methyltr_E_TRM7.
DR InterPro; IPR002877; RNA_MeTrfase_FtsJ_dom.
DR InterPro; IPR015507; rRNA-MeTfrase_E.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR10920:SF12; PTHR10920:SF12; 1.
DR Pfam; PF01728; FtsJ; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase; tRNA processing.
FT CHAIN 1..302
FT /note="Putative tRNA (cytidine(32)/guanosine(34)-2'-O)-
FT methyltransferase 1"
FT /id="PRO_0000155582"
FT ACT_SITE 164
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03162"
FT BINDING 53
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03162"
FT BINDING 55
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03162"
FT BINDING 82
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03162"
FT BINDING 98
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03162"
FT BINDING 124
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03162"
SQ SEQUENCE 302 AA; 33402 MW; EDFB3BAD445693DA CRC64;
MGKTSKDKRD IYYRQAKDEG WRARSAFKLL HVDEAYGILN GVQRAVDLCA APGSWSQVLS
RKLYDTCETD DEKSAVKIIA VDLQAMAPIR GILQLQGDIT KQSTAEAIIG HFGGNEKAQL
VVCDGAPDVT GVHEMDEYMQ HQLLVAALSI ATCVLETGGT FVAKIFKGNA TSLLSSQMQI
FFKKFDIYKP PSSRPSSIEA FVVCSDFCLP EGYIPQVINP ARDDIRLLAQ KTGSEVNRRL
VPFIACGDLN GLSDPEEGKT SSSDESKSNL EYVYDAVMDD ASYPLEFKEI LKQVYDEQRH
II
