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Protein

tRNA (guanine-N(7)-)-methyltransferase

Gene

TRM8

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

Methyltransferase that catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA, a modification required to maintain stability of tRNAs; its absence resulting in tRNA decay. Both the D-stem and T-stem structures of tRNAs are required for efficient methyltransferase activity.UniRule annotation2 Publications

Catalytic activityi

S-adenosyl-L-methionine + guanine(46) in tRNA = S-adenosyl-L-homocysteine + N(7)-methylguanine(46) in tRNA.UniRule annotation1 Publication

Pathwayi: N(7)-methylguanine-tRNA biosynthesis

This protein is involved in the pathway N(7)-methylguanine-tRNA biosynthesis, which is part of tRNA modification.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway N(7)-methylguanine-tRNA biosynthesis and in tRNA modification.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei103S-adenosyl-L-methionine; via carbonyl oxygenUniRule annotation1 Publication1
Binding sitei181S-adenosyl-L-methionine; via carbonyl oxygenUniRule annotation1 Publication1
Active sitei184Curated1

GO - Molecular functioni

GO - Biological processi

  • tRNA methylation Source: SGD
  • tRNA modification Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

RNA-binding, S-adenosyl-L-methionine, tRNA-binding

Enzyme and pathway databases

BioCyciYEAST:YDL201W-MONOMER.
BRENDAi2.1.1.33. 984.
ReactomeiR-SCE-6782315. tRNA modification in the nucleus and cytosol.
UniPathwayiUPA00989.

Names & Taxonomyi

Protein namesi
Recommended name:
tRNA (guanine-N(7)-)-methyltransferaseUniRule annotation (EC:2.1.1.33UniRule annotation)
Alternative name(s):
Transfer RNA methyltransferase 8UniRule annotation
tRNA (guanine(46)-N(7))-methyltransferaseUniRule annotation
tRNA(m7G46)-methyltransferaseUniRule annotation
Gene namesi
Name:TRM8UniRule annotation
Ordered Locus Names:YDL201W
ORF Names:D1075
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDL201W.
SGDiS000002360. TRM8.

Subcellular locationi

GO - Cellular componenti

  • nucleoplasm Source: Reactome
  • tRNA methyltransferase complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001714371 – 286tRNA (guanine-N(7)-)-methyltransferaseAdd BLAST286

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei7Phosphoserine; by ATM or ATRCombined sources1
Modified residuei59PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ12009.
PRIDEiQ12009.

PTM databases

iPTMnetiQ12009.

Interactioni

Subunit structurei

Forms a complex with TRM82.UniRule annotation1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
TRM82Q037745EBI-19552,EBI-19486

Protein-protein interaction databases

BioGridi31845. 49 interactors.
DIPiDIP-8614N.
IntActiQ12009. 1 interactor.
MINTiMINT-2782058.

Structurei

Secondary structure

1286
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi63 – 65Combined sources3
Helixi73 – 75Combined sources3
Helixi78 – 80Combined sources3
Helixi83 – 85Combined sources3
Turni88 – 91Combined sources4
Beta strandi92 – 94Combined sources3
Beta strandi97 – 102Combined sources6
Helixi108 – 116Combined sources9
Beta strandi120 – 127Combined sources8
Helixi129 – 144Combined sources16
Beta strandi147 – 150Combined sources4
Turni151 – 154Combined sources4
Beta strandi155 – 159Combined sources5
Helixi166 – 168Combined sources3
Beta strandi175 – 182Combined sources8
Helixi199 – 208Combined sources10
Beta strandi209 – 220Combined sources12
Helixi222 – 234Combined sources13
Beta strandi238 – 240Combined sources3
Helixi243 – 247Combined sources5
Helixi250 – 257Combined sources8
Helixi260 – 267Combined sources8
Beta strandi273 – 279Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2VDUX-ray2.40E/F39-286[»]
2VDVX-ray2.30E/F47-286[»]
ProteinModelPortaliQ12009.
SMRiQ12009.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ12009.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni126 – 127S-adenosyl-L-methionine binding2
Regioni161 – 162S-adenosyl-L-methionine binding2
Regioni259 – 261S-adenosyl-L-methionine binding3

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. TrmB family.UniRule annotation

Phylogenomic databases

GeneTreeiENSGT00390000017840.
HOGENOMiHOG000260965.
InParanoidiQ12009.
KOiK03439.
OMAiPNFFYKG.
OrthoDBiEOG092C0GMH.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
HAMAPiMF_03055. tRNA_methyltr_TrmB_euk. 1 hit.
InterProiIPR029063. SAM-dependent_MTases.
IPR025763. Trm8_euk.
IPR003358. tRNA_(Gua-N-7)_MeTrfase_Trmb.
[Graphical view]
PfamiPF02390. Methyltransf_4. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
TIGRFAMsiTIGR00091. TIGR00091. 1 hit.
PROSITEiPS51625. SAM_MT_TRMB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q12009-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKAKPLSQDP GSKRYAYRIN KEENRKELKH VKINESSLVQ EGQKIDLPKK
60 70 80 90 100
RYYRQRAHSN PFSDHQLEYP VSPQDMDWSK LYPYYKNAEN GQMTKKVTIA
110 120 130 140 150
DIGCGFGGLM IDLSPAFPED LILGMEIRVQ VTNYVEDRII ALRNNTASKH
160 170 180 190 200
GFQNINVLRG NAMKFLPNFF EKGQLSKMFF CFPDPHFKQR KHKARIITNT
210 220 230 240 250
LLSEYAYVLK EGGVVYTITD VKDLHEWMVK HLEEHPLFER LSKEWEENDE
260 270 280
CVKIMRNATE EGKKVERKKG DKFVACFTRL PTPAIL
Length:286
Mass (Da):33,391
Last modified:November 1, 1996 - v1
Checksum:i0280B9A7B02C85B7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X99000 Genomic DNA. Translation: CAA67468.1.
Z74249 Genomic DNA. Translation: CAA98779.1.
BK006938 Genomic DNA. Translation: DAA11663.1.
PIRiS67760.
RefSeqiNP_010080.1. NM_001180261.1.

Genome annotation databases

EnsemblFungiiYDL201W; YDL201W; YDL201W.
GeneIDi851326.
KEGGisce:YDL201W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X99000 Genomic DNA. Translation: CAA67468.1.
Z74249 Genomic DNA. Translation: CAA98779.1.
BK006938 Genomic DNA. Translation: DAA11663.1.
PIRiS67760.
RefSeqiNP_010080.1. NM_001180261.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2VDUX-ray2.40E/F39-286[»]
2VDVX-ray2.30E/F47-286[»]
ProteinModelPortaliQ12009.
SMRiQ12009.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31845. 49 interactors.
DIPiDIP-8614N.
IntActiQ12009. 1 interactor.
MINTiMINT-2782058.

PTM databases

iPTMnetiQ12009.

Proteomic databases

MaxQBiQ12009.
PRIDEiQ12009.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDL201W; YDL201W; YDL201W.
GeneIDi851326.
KEGGisce:YDL201W.

Organism-specific databases

EuPathDBiFungiDB:YDL201W.
SGDiS000002360. TRM8.

Phylogenomic databases

GeneTreeiENSGT00390000017840.
HOGENOMiHOG000260965.
InParanoidiQ12009.
KOiK03439.
OMAiPNFFYKG.
OrthoDBiEOG092C0GMH.

Enzyme and pathway databases

UniPathwayiUPA00989.
BioCyciYEAST:YDL201W-MONOMER.
BRENDAi2.1.1.33. 984.
ReactomeiR-SCE-6782315. tRNA modification in the nucleus and cytosol.

Miscellaneous databases

EvolutionaryTraceiQ12009.
PROiQ12009.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
HAMAPiMF_03055. tRNA_methyltr_TrmB_euk. 1 hit.
InterProiIPR029063. SAM-dependent_MTases.
IPR025763. Trm8_euk.
IPR003358. tRNA_(Gua-N-7)_MeTrfase_Trmb.
[Graphical view]
PfamiPF02390. Methyltransf_4. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
TIGRFAMsiTIGR00091. TIGR00091. 1 hit.
PROSITEiPS51625. SAM_MT_TRMB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTRMB_YEAST
AccessioniPrimary (citable) accession number: Q12009
Secondary accession number(s): D6VRF3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2003
Last sequence update: November 1, 1996
Last modified: November 30, 2016
This is version 133 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 2630 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: 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.