TRM7_YEAST
ID TRM7_YEAST Reviewed; 310 AA.
AC P38238; D6VQ61;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=tRNA (cytidine(32)/guanosine(34)-2'-O)-methyltransferase;
DE EC=2.1.1.205 {ECO:0000255|HAMAP-Rule:MF_03162};
DE AltName: Full=2'-O-ribose RNA methyltransferase TRM7;
DE AltName: Full=tRNA methylase 7;
GN Name=TRM7 {ECO:0000255|HAMAP-Rule:MF_03162}; OrderedLocusNames=YBR061C;
GN ORFNames=YBR0527;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP FUNCTION.
RX PubMed=11927565; DOI=10.1093/emboj/21.7.1811;
RA Pintard L., Lecointe F., Bujnicki J.M., Bonnerot C., Grosjean H.,
RA Lapeyre B.;
RT "Trm7p catalyses the formation of two 2'-O-methylriboses in yeast tRNA
RT anticodon loop.";
RL EMBO J. 21:1811-1820(2002).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [7]
RP FUNCTION, INTERACTION WITH TRM732 AND TRM734, AND DISRUPTION PHENOTYPE.
RX PubMed=22912484; DOI=10.1261/rna.035287.112;
RA Guy M.P., Podyma B.M., Preston M.A., Shaheen H.H., Krivos K.L.,
RA Limbach P.A., Hopper A.K., Phizicky E.M.;
RT "Yeast Trm7 interacts with distinct proteins for critical modifications of
RT the tRNAPhe anticodon loop.";
RL RNA 18:1921-1933(2012).
CC -!- FUNCTION: Methylates the 2'-O-ribose of nucleotides at positions 32 and
CC 34 of the tRNA anticodon loop of tRNA(Phe), tRNA(Trp) and
CC tRNA(Leu(UAA)). Requires TRM732 for methylation of the cytidine at
CC position 32 and RTT10/TRM734 for methylation of the nucleotides at
CC position 34 in substrate tRNAs. Lack of either of these modifications
CC in tRNA(Phe) reduces formation of wybutosine from 1-methylguanosine at
CC position 37. {ECO:0000269|PubMed:11927565,
CC ECO:0000269|PubMed:22912484}.
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 -!- SUBUNIT: Interacts with TRM732; for 2'-O-methylation of cytidine 32 in
CC substrate tRNAs. Interacts with RTT10/TRM734; for 2'-O-methylation of
CC position 34 in substrate tRNAs. {ECO:0000269|PubMed:22912484}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03162,
CC ECO:0000269|PubMed:14562095}.
CC -!- DISRUPTION PHENOTYPE: Causes severe growth and translation defects,
CC which is due to reduced decoding of Phe codons by hypomodified
CC tRNA(Phe). {ECO:0000269|PubMed:22912484}.
CC -!- MISCELLANEOUS: Present with 4110 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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; Z35930; CAA85004.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07181.1; -; Genomic_DNA.
DR PIR; S45919; S45919.
DR RefSeq; NP_009617.3; NM_001178409.3.
DR PDB; 6JP6; X-ray; 2.70 A; B/D=1-310.
DR PDB; 6JPL; X-ray; 2.32 A; B/D=1-310.
DR PDBsum; 6JP6; -.
DR PDBsum; 6JPL; -.
DR AlphaFoldDB; P38238; -.
DR SASBDB; P38238; -.
DR SMR; P38238; -.
DR BioGRID; 32765; 75.
DR DIP; DIP-4899N; -.
DR IntAct; P38238; 20.
DR MINT; P38238; -.
DR STRING; 4932.YBR061C; -.
DR MaxQB; P38238; -.
DR PaxDb; P38238; -.
DR PRIDE; P38238; -.
DR EnsemblFungi; YBR061C_mRNA; YBR061C; YBR061C.
DR GeneID; 852353; -.
DR KEGG; sce:YBR061C; -.
DR SGD; S000000265; TRM7.
DR VEuPathDB; FungiDB:YBR061C; -.
DR eggNOG; KOG1099; Eukaryota.
DR GeneTree; ENSGT00730000111146; -.
DR HOGENOM; CLU_009422_1_2_1; -.
DR OMA; GLHDMDI; -.
DR BioCyc; MetaCyc:YBR061C-MON; -.
DR BioCyc; YEAST:YBR061C-MON; -.
DR BRENDA; 2.1.1.205; 984.
DR PRO; PR:P38238; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38238; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0008173; F:RNA methyltransferase activity; IBA:GO_Central.
DR GO; GO:0106050; F:tRNA 2'-O-methyltransferase activity; IDA:SGD.
DR GO; GO:0008175; F:tRNA methyltransferase activity; IBA:GO_Central.
DR GO; GO:0002181; P:cytoplasmic translation; IMP:SGD.
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; IDA:SGD.
DR GO; GO:0002130; P:wobble position ribose methylation; IDA:SGD.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase; tRNA processing.
FT CHAIN 1..310
FT /note="tRNA (cytidine(32)/guanosine(34)-2'-O)-
FT methyltransferase"
FT /id="PRO_0000155587"
FT REGION 276..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 164
FT /note="Proton acceptor"
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 57
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03162"
FT BINDING 83
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03162"
FT BINDING 99
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"
FT HELIX 11..18
FT /evidence="ECO:0007829|PDB:6JPL"
FT HELIX 26..33
FT /evidence="ECO:0007829|PDB:6JPL"
FT TURN 34..36
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 46..50
FT /evidence="ECO:0007829|PDB:6JPL"
FT HELIX 56..65
FT /evidence="ECO:0007829|PDB:6JPL"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:6JPL"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 78..85
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 93..97
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:6JP6"
FT HELIX 104..112
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 118..123
FT /evidence="ECO:0007829|PDB:6JPL"
FT HELIX 133..154
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 155..166
FT /evidence="ECO:0007829|PDB:6JPL"
FT HELIX 171..177
FT /evidence="ECO:0007829|PDB:6JPL"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 182..188
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 199..207
FT /evidence="ECO:0007829|PDB:6JPL"
FT HELIX 237..245
FT /evidence="ECO:0007829|PDB:6JPL"
SQ SEQUENCE 310 AA; 34701 MW; 3C7F2583F2012CCB CRC64;
MGKSSKDKRD LYYRKAKEQG YRARSAFKLL QLNDQFHFLD DPNLKRVVDL CAAPGSWSQV
LSRKLFDESP SSDKEDRKIV SVDLQPMSPI PHVTTLQADI THPKTLARIL KLFGNEKADF
VCSDGAPDVT GLHDLDEYVQ QQLIMSALQL TACILKKGGT FVAKIFRGRD IDMLYSQLGY
LFDKIVCAKP RSSRGTSLEA FIVCLGYNPP SNWTPKLDVN TSVDEFFQGC FLNKLCISDK
LSHWNEEERN IAEFMACGSL QSFDSDATYH DLPSSVAGTS SSLDPVQSPT NPPYKKALEL
KRSGKLTRSV
