A0A5E4E5B2 · A0A5E4E5B2_PRUDU
- ProteintRNA (guanine(37)-N1)-methyltransferase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids468 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Specifically methylates the N1 position of guanosine-37 in various cytoplasmic and mitochondrial tRNAs. Methylation is not dependent on the nature of the nucleoside 5' of the target nucleoside. This is the first step in the biosynthesis of wybutosine (yW), a modified base adjacent to the anticodon of tRNAs and required for accurate decoding.
Catalytic activity
- guanosine37 in tRNA + S-adenosyl-L-methionine = H+ + N1-methylguanosine37 in tRNA + S-adenosyl-L-homocysteine
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 186 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 224-225 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: DL | ||||||
Binding site | 252-253 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: DA | ||||||
Binding site | 383 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: N |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrial matrix | |
Cellular Component | nucleus | |
Molecular Function | tRNA (guanine(37)-N1)-methyltransferase activity | |
Biological Process | tRNA N1-guanine methylation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nametRNA (guanine(37)-N1)-methyltransferase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > fabids > Rosales > Rosaceae > Amygdaloideae > Amygdaleae > Prunus
Accessions
- Primary accessionA0A5E4E5B2
Proteomes
Genome annotation databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Predominantly in the mitochondria and in the nucleus.
Keywords
- Cellular component
Interaction
Subunit
Monomer.
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 96-464 | SAM-dependent methyltransferase TRM5/TYW2-type | ||||
Sequence: YWGAGHVAHLNIHDELLPYKDVIAKVIYDKNYPRIKTIVNKVGTIENEFRVPKFEVLAGEDDMVTEVKQYGATFKLDYSLVYWNSRLEHEHVRLVSQFRAGEIICDMFAGIGPFAIPAAQKGCMVYANDLNPDSIRYLKINAETNKVDNRVRAYNIDARKFISQLMTVPNSDEKSDSDISMLKTGEKCDIQGNQEPKSENGRLGVEVKEVPDTVISNPDALQASSRNADSSVPPVKRPSDSCQSENESVDGTSAFVAGRRKGSKTKRMRGPEISNVKTWEHVDHVIMNLPASALQFLDAFRGLIQRKYWTGSLPWIHCYCFIRAIETQEYIISVAESGLNAHIKDPIFHRVRDVAPNKAMFCLSFRLPE | ||||||
Region | 311-364 | Disordered | ||||
Sequence: SNPDALQASSRNADSSVPPVKRPSDSCQSENESVDGTSAFVAGRRKGSKTKRMR | ||||||
Compositional bias | 312-346 | Polar residues | ||||
Sequence: NPDALQASSRNADSSVPPVKRPSDSCQSENESVDG |
Sequence similarities
Belongs to the TRM5 / TYW2 family.
Belongs to the class I-like SAM-binding methyltransferase superfamily. TRM5/TYW2 family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length468
- Mass (Da)53,060
- Last updated2019-11-13 v1
- ChecksumBF9FD3597D797DCA
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 312-346 | Polar residues | ||||
Sequence: NPDALQASSRNADSSVPPVKRPSDSCQSENESVDG |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CABIKO010000002 EMBL· GenBank· DDBJ | VVA10556.1 EMBL· GenBank· DDBJ | Genomic DNA |