Q08960 · TYW1_YEAST
- ProteinS-adenosyl-L-methionine-dependent tRNA 4-demethylwyosine synthase
- GeneTYW1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids810 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryotic phenylalanine tRNA. Catalyzes the condensation of N-methylguanine with 2 carbon atoms from pyruvate to form the tricyclic 4-demethylwyosine, an intermediate in wybutosine biosynthesis (By similarity).
Miscellaneous
Present with 5410 molecules/cell in log phase SD medium.
Catalytic activity
- N1-methylguanosine37 in tRNA(Phe) + pyruvate + S-adenosyl-L-methionine = 4-demethylwyosine37 in tRNA(Phe) + 5'-deoxyadenosine + CO2 + H2O + L-methionine
RHEA-COMP:10165 CHEBI:73542 Position: 37+ CHEBI:15361 + CHEBI:59789 = RHEA-COMP:10164 CHEBI:64315 Position: 37+ CHEBI:17319 + CHEBI:16526 + CHEBI:15377 + CHEBI:57844
Cofactor
Note: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Pathway
tRNA modification; wybutosine-tRNA(Phe) biosynthesis.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 211-215 | FMN (UniProtKB | ChEBI) | ||||
Sequence: SLQGA | ||||||
Binding site | 304-337 | FMN (UniProtKB | ChEBI) | ||||
Sequence: VLGLGDSESWPEKFCYQAKRADHWISRLGGRRIF | ||||||
Binding site | 479 | [4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 483 | [4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 486 | [4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | endoplasmic reticulum | |
Molecular Function | 4 iron, 4 sulfur cluster binding | |
Molecular Function | FMN binding | |
Molecular Function | metal ion binding | |
Molecular Function | S-adenosyl-L-methionine binding | |
Molecular Function | tRNA-4-demethylwyosine synthase activity | |
Biological Process | wybutosine biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameS-adenosyl-L-methionine-dependent tRNA 4-demethylwyosine synthase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionQ08960
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 479 | Loss of function. | ||||
Sequence: C → A | ||||||
Mutagenesis | 483 | Loss of function. | ||||
Sequence: C → A | ||||||
Mutagenesis | 486 | Loss of function. | ||||
Sequence: C → A | ||||||
Mutagenesis | 532 | No effect. | ||||
Sequence: E → A | ||||||
Mutagenesis | 550 | Loss of function. | ||||
Sequence: E → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 12 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000217861 | 1-810 | S-adenosyl-L-methionine-dependent tRNA 4-demethylwyosine synthase | |||
Sequence: MDGFRVAGALVVGALTAAYLYFGGRFSIALVIIVGYGIYCNEASGGSQDSQEKLDLNKQQKKPCCSDKKIADGGKKTGGCCSDKKNGGGKGGGCCSSKGGKKGGCCSSKGGKKGGCCSSKKNIGDNENTATEVEKAVNYPVTVDFTEVFRKPTKKRSSTPKVFSKNSSSNSRVGKKLSVSKKIGPDGLIKSALTISNETLLSSQIYVLYSSLQGAASKAAKSVYDKLKELDELTNEPKLLNLDDLSDFDDYFINVPVENALYVLVLPSYDIDCPLDYFLQTLEENANDFRVDSFPLRKLVGYTVLGLGDSESWPEKFCYQAKRADHWISRLGGRRIFPLGKVCMKTGGSAKIDEWTSLLAETLKDDEPIIYEYDENADSEEDEEEGNGSDELGDVEDIGGKGSNGKFSGADEIKQMVAKDSPTYKNLTKQGYKVIGSHSGVKICRWTKNELRGKGSCYKKSLFNIASSRCMELTPSLACSSKCVFCWRHGTNPVSKNWRWEVDEPEYILENALKGHYSMIKQMRGVPGVIAERFAKAFEVRHCALSLVGEPILYPHINKFIQLLHQKGITSFLVCNAQHPEALRNIVKVTQLYVSIDAPTKTELKKVDRPLYKDFWERMVECLEILKTVQNHQRTVFRLTLVKGFNMGDVSAYADLVQRGLPGFIEVKGATFSGSSDGNGNPLTMQNIPFYEECVKFVKAFTTELQRRGLHYDLAAEHAHSNCLLIADTKFKINGEWHTHIDFDKFFVLLNSGKDFTYMDYLEKTPEWALFGNGGFAPGNTRVYRKDKKKQNKENQETTTRETPLPPIPA | ||||||
Cross-link | 496 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K |
Keywords
- PTM
Proteomic databases
PTM databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 86-116 | Disordered | ||||
Sequence: NGGGKGGGCCSSKGGKKGGCCSSKGGKKGGC | ||||||
Region | 156-176 | Disordered | ||||
Sequence: RSSTPKVFSKNSSSNSRVGKK | ||||||
Compositional bias | 159-176 | Polar residues | ||||
Sequence: TPKVFSKNSSSNSRVGKK | ||||||
Domain | 205-360 | Flavodoxin-like | ||||
Sequence: IYVLYSSLQGAASKAAKSVYDKLKELDELTNEPKLLNLDDLSDFDDYFINVPVENALYVLVLPSYDIDCPLDYFLQTLEENANDFRVDSFPLRKLVGYTVLGLGDSESWPEKFCYQAKRADHWISRLGGRRIFPLGKVCMKTGGSAKIDEWTSLLA | ||||||
Compositional bias | 374-392 | Acidic residues | ||||
Sequence: DENADSEEDEEEGNGSDEL | ||||||
Region | 374-407 | Disordered | ||||
Sequence: DENADSEEDEEEGNGSDELGDVEDIGGKGSNGKF | ||||||
Domain | 463-713 | Radical SAM core | ||||
Sequence: FNIASSRCMELTPSLACSSKCVFCWRHGTNPVSKNWRWEVDEPEYILENALKGHYSMIKQMRGVPGVIAERFAKAFEVRHCALSLVGEPILYPHINKFIQLLHQKGITSFLVCNAQHPEALRNIVKVTQLYVSIDAPTKTELKKVDRPLYKDFWERMVECLEILKTVQNHQRTVFRLTLVKGFNMGDVSAYADLVQRGLPGFIEVKGATFSGSSDGNGNPLTMQNIPFYEECVKFVKAFTTELQRRGLHYD | ||||||
Compositional bias | 782-797 | Basic and acidic residues | ||||
Sequence: RVYRKDKKKQNKENQE | ||||||
Region | 782-810 | Disordered | ||||
Sequence: RVYRKDKKKQNKENQETTTRETPLPPIPA |
Sequence similarities
Belongs to the TYW1 family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length810
- Mass (Da)89,805
- Last updated1996-11-01 v1
- ChecksumC6A18C949B6E5F8B
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 159-176 | Polar residues | ||||
Sequence: TPKVFSKNSSSNSRVGKK | ||||||
Compositional bias | 374-392 | Acidic residues | ||||
Sequence: DENADSEEDEEEGNGSDEL | ||||||
Compositional bias | 782-797 | Basic and acidic residues | ||||
Sequence: RVYRKDKKKQNKENQE |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Z73563 EMBL· GenBank· DDBJ | CAA97922.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z73562 EMBL· GenBank· DDBJ | CAA97921.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006949 EMBL· GenBank· DDBJ | DAA11229.1 EMBL· GenBank· DDBJ | Genomic DNA |