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B3LH81 (TRMB_YEAS1) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 27. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
tRNA (guanine-N(7)-)-methyltransferase

EC=2.1.1.33
Alternative name(s):
Transfer RNA methyltransferase 8
tRNA (guanine(46)-N(7))-methyltransferase
tRNA(m7G46)-methyltransferase
Gene names
Name:TRM8
ORF Names:SCRG_00691
OrganismSaccharomyces cerevisiae (strain RM11-1a) (Baker's yeast) [Complete proteome]
Taxonomic identifier285006 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length286 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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 By similarity. HAMAP-Rule MF_03055

Catalytic activity

S-adenosyl-L-methionine + guanine46 in tRNA = S-adenosyl-L-homocysteine + N(7)-methylguanine46 in tRNA. HAMAP-Rule MF_03055

Pathway

tRNA modification; N(7)-methylguanine-tRNA biosynthesis. HAMAP-Rule MF_03055

Subunit structure

Forms a complex with TRM82 By similarity. HAMAP-Rule MF_03055

Subcellular location

Nucleus By similarity HAMAP-Rule MF_03055.

Sequence similarities

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

Ontologies

Keywords
   Biological processtRNA processing
   Cellular componentNucleus
   LigandRNA-binding
S-adenosyl-L-methionine
tRNA-binding
   Molecular functionMethyltransferase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Cellular_componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functiontRNA (guanine-N7-)-methyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

tRNA binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 286286tRNA (guanine-N(7)-)-methyltransferase HAMAP-Rule MF_03055
PRO_0000370607

Regions

Region126 – 1272S-adenosyl-L-methionine binding By similarity
Region161 – 1622S-adenosyl-L-methionine binding By similarity
Region259 – 2613S-adenosyl-L-methionine binding By similarity

Sites

Active site1841 By similarity
Binding site1031S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site1811S-adenosyl-L-methionine; via carbonyl oxygen By similarity

Amino acid modifications

Modified residue71Phosphoserine By similarity
Modified residue591Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
B3LH81 [UniParc].

Last modified September 2, 2008. Version 1.
Checksum: 0280B9A7B02C85B7

FASTA28633,391
        10         20         30         40         50         60 
MKAKPLSQDP GSKRYAYRIN KEENRKELKH VKINESSLVQ EGQKIDLPKK RYYRQRAHSN 

        70         80         90        100        110        120 
PFSDHQLEYP VSPQDMDWSK LYPYYKNAEN GQMTKKVTIA DIGCGFGGLM IDLSPAFPED 

       130        140        150        160        170        180 
LILGMEIRVQ VTNYVEDRII ALRNNTASKH GFQNINVLRG NAMKFLPNFF EKGQLSKMFF 

       190        200        210        220        230        240 
CFPDPHFKQR KHKARIITNT LLSEYAYVLK EGGVVYTITD VKDLHEWMVK HLEEHPLFER 

       250        260        270        280 
LSKEWEENDE CVKIMRNATE EGKKVERKKG DKFVACFTRL PTPAIL 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CH408043 Genomic DNA. Translation: EDV08460.1.

3D structure databases

ProteinModelPortalB3LH81.
SMRB3LH81. Positions 60-286.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

OrthoDBEOG708W9T.

Enzyme and pathway databases

UniPathwayUPA00989.

Family and domain databases

HAMAPMF_03055. tRNA_methyltr_TrmB_euk.
InterProIPR025763. Trm8_euk.
IPR003358. tRNA_(Gua-N-7)_MeTrfase.
[Graphical view]
PfamPF02390. Methyltransf_4. 1 hit.
[Graphical view]
TIGRFAMsTIGR00091. TIGR00091. 1 hit.
PROSITEPS51625. SAM_MT_TRMB. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTRMB_YEAS1
AccessionPrimary (citable) accession number: B3LH81
Entry history
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: September 2, 2008
Last modified: April 16, 2014
This is version 27 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways