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A7TT36 (TRMB_VANPO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 41. 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:Kpol_269p6
OrganismVanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294) (Kluyveromyces polysporus) [Complete proteome]
Taxonomic identifier436907 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeVanderwaltozyma

Protein attributes

Sequence length286 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA 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
   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_0000370605

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

Sequences

Sequence LengthMass (Da)Tools
A7TT36 [UniParc].

Last modified October 2, 2007. Version 1.
Checksum: 2BBAED087EC7B1D7

FASTA28633,804
        10         20         30         40         50         60 
MDLRNPNRDP NSRRVLYRTN KEENRKELKH VKIDESTLAQ EGKKLDLPKK RFYRQRAHSN 

        70         80         90        100        110        120 
PFSDHQLDYP TSPDDMNWSK LFPHYYDSTT GKMTKDVTIA DIGCGFGGLL IDLSPAFPED 

       130        140        150        160        170        180 
LILGMEIRVQ VTNYVEDRII ALRTNHAKDY QYQNINVIRG NAMKFLPNFF QRAQLSKMFF 

       190        200        210        220        230        240 
CFPDPHFKQR KHKARIITNT LLSEYAYVLK DNGVIYTITD VEDLHNWMVK HLEEHPLFER 

       250        260        270        280 
YDKEWEDNDK CVQIMRNATE EGKKVERKKG DKFVACFRRL PNPAIV 

« Hide

References

[1]"Independent sorting-out of thousands of duplicated gene pairs in two yeast species descended from a whole-genome duplication."
Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.
Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 22028 / DSM 70294.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DS480540 Genomic DNA. Translation: EDO14572.1.
RefSeqXP_001642430.1. XM_001642380.1.

3D structure databases

ProteinModelPortalA7TT36.
SMRA7TT36. Positions 60-286.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING436907.A7TT36.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5542586.
KEGGvpo:Kpol_269p6.

Phylogenomic databases

eggNOGCOG0220.
KOK03439.
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_VANPO
AccessionPrimary (citable) accession number: A7TT36
Entry history
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: October 2, 2007
Last modified: April 16, 2014
This is version 41 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