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Protein

tRNA (cytidine(32)/guanosine(34)-2'-O)-methyltransferase

Gene

TRM7

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Methylates the 2'-O-ribose of nucleotides at positions 32 and 34 of the tRNA anticodon loop of tRNA(Phe), tRNA(Trp) and tRNA(Leu(UAA)). Requires TRM732 for methylation of the cytidine at position 32 and RTT10/TRM734 for methylation of the nucleotides at position 34 in substrate tRNAs. Lack of either of these modifications in tRNA(Phe) reduces formation of wybutosine from 1-methylguanosine at position 37.2 Publications

Catalytic activityi

S-adenosyl-L-methionine + cytidine(32)/guanosine(34) in tRNA = S-adenosyl-L-homocysteine + 2'-O-methylcytidine(32)/2'-O-methylguanosine(34) in tRNA.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei55 – 551S-adenosyl-L-methionine; via amide nitrogenUniRule annotation
Binding sitei57 – 571S-adenosyl-L-methionine; via amide nitrogenUniRule annotation
Binding sitei83 – 831S-adenosyl-L-methionineUniRule annotation
Binding sitei99 – 991S-adenosyl-L-methionineUniRule annotation
Binding sitei124 – 1241S-adenosyl-L-methionineUniRule annotation
Active sitei164 – 1641Proton acceptorUniRule annotation

GO - Molecular functioni

  • tRNA methyltransferase activity Source: SGD

GO - Biological processi

  • cytoplasmic translation Source: SGD
  • tRNA methylation Source: SGD
  • tRNA nucleoside ribose methylation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciMetaCyc:YBR061C-MONOMER.
YEAST:YBR061C-MONOMER.
BRENDAi2.1.1.205. 984.

Names & Taxonomyi

Protein namesi
Recommended name:
tRNA (cytidine(32)/guanosine(34)-2'-O)-methyltransferase (EC:2.1.1.205UniRule annotation)
Alternative name(s):
2'-O-ribose RNA methyltransferase TRM7
tRNA methylase 7
Gene namesi
Name:TRM7UniRule annotation
Ordered Locus Names:YBR061C
ORF Names:YBR0527
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:YBR061C.
SGDiS000000265. TRM7.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Causes severe growth and translation defects, which is due to reduced decoding of Phe codons by hypomodified tRNA(Phe).1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 310310tRNA (cytidine(32)/guanosine(34)-2'-O)-methyltransferasePRO_0000155587Add
BLAST

Proteomic databases

MaxQBiP38238.

Interactioni

Subunit structurei

Interacts with TRM732; for 2'-O-methylation of cytidine 32 in substrate tRNAs. Interacts with RTT10/TRM734; for 2'-O-methylation of position 34 in substrate tRNAs.1 Publication

Protein-protein interaction databases

BioGridi32765. 46 interactions.
DIPiDIP-4899N.
MINTiMINT-501454.

Structurei

3D structure databases

ProteinModelPortaliP38238.
SMRiP38238. Positions 21-190.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA methyltransferase RlmE family. TRM7 subfamily.UniRule annotation

Phylogenomic databases

GeneTreeiENSGT00730000111146.
HOGENOMiHOG000162368.
KOiK14864.
OMAiHFEGQPA.
OrthoDBiEOG7SXWDC.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
HAMAPiMF_01547. RNA_methyltr_E.
MF_03162. RNA_methyltr_E_TRM7.
InterProiIPR028590. RNA_methyltr_E_Trm7.
IPR015507. rRNA-MeTfrase_E.
IPR002877. rRNA_MeTrfase_FtsJ_dom.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR10920. PTHR10920. 1 hit.
PfamiPF01728. FtsJ. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.

Sequencei

Sequence statusi: Complete.

P38238-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKSSKDKRD LYYRKAKEQG YRARSAFKLL QLNDQFHFLD DPNLKRVVDL
60 70 80 90 100
CAAPGSWSQV LSRKLFDESP SSDKEDRKIV SVDLQPMSPI PHVTTLQADI
110 120 130 140 150
THPKTLARIL KLFGNEKADF VCSDGAPDVT GLHDLDEYVQ QQLIMSALQL
160 170 180 190 200
TACILKKGGT FVAKIFRGRD IDMLYSQLGY LFDKIVCAKP RSSRGTSLEA
210 220 230 240 250
FIVCLGYNPP SNWTPKLDVN TSVDEFFQGC FLNKLCISDK LSHWNEEERN
260 270 280 290 300
IAEFMACGSL QSFDSDATYH DLPSSVAGTS SSLDPVQSPT NPPYKKALEL
310
KRSGKLTRSV
Length:310
Mass (Da):34,701
Last modified:October 1, 1994 - v1
Checksum:i3C7F2583F2012CCB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z35930 Genomic DNA. Translation: CAA85004.1.
BK006936 Genomic DNA. Translation: DAA07181.1.
PIRiS45919.
RefSeqiNP_009617.3. NM_001178409.3.

Genome annotation databases

EnsemblFungiiYBR061C; YBR061C; YBR061C.
GeneIDi852353.
KEGGisce:YBR061C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z35930 Genomic DNA. Translation: CAA85004.1.
BK006936 Genomic DNA. Translation: DAA07181.1.
PIRiS45919.
RefSeqiNP_009617.3. NM_001178409.3.

3D structure databases

ProteinModelPortaliP38238.
SMRiP38238. Positions 21-190.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32765. 46 interactions.
DIPiDIP-4899N.
MINTiMINT-501454.

Proteomic databases

MaxQBiP38238.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYBR061C; YBR061C; YBR061C.
GeneIDi852353.
KEGGisce:YBR061C.

Organism-specific databases

EuPathDBiFungiDB:YBR061C.
SGDiS000000265. TRM7.

Phylogenomic databases

GeneTreeiENSGT00730000111146.
HOGENOMiHOG000162368.
KOiK14864.
OMAiHFEGQPA.
OrthoDBiEOG7SXWDC.

Enzyme and pathway databases

BioCyciMetaCyc:YBR061C-MONOMER.
YEAST:YBR061C-MONOMER.
BRENDAi2.1.1.205. 984.

Miscellaneous databases

PROiP38238.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
HAMAPiMF_01547. RNA_methyltr_E.
MF_03162. RNA_methyltr_E_TRM7.
InterProiIPR028590. RNA_methyltr_E_Trm7.
IPR015507. rRNA-MeTfrase_E.
IPR002877. rRNA_MeTrfase_FtsJ_dom.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR10920. PTHR10920. 1 hit.
PfamiPF01728. FtsJ. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete DNA sequence of yeast chromosome II."
    Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C.
    , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
    EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "Trm7p catalyses the formation of two 2'-O-methylriboses in yeast tRNA anticodon loop."
    Pintard L., Lecointe F., Bujnicki J.M., Bonnerot C., Grosjean H., Lapeyre B.
    EMBO J. 21:1811-1820(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  4. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "Yeast Trm7 interacts with distinct proteins for critical modifications of the tRNAPhe anticodon loop."
    Guy M.P., Podyma B.M., Preston M.A., Shaheen H.H., Krivos K.L., Limbach P.A., Hopper A.K., Phizicky E.M.
    RNA 18:1921-1933(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TRM732 AND TRM734, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiTRM7_YEAST
AccessioniPrimary (citable) accession number: P38238
Secondary accession number(s): D6VQ61
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: July 6, 2016
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 4110 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome II
    Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.