A0A1G6L984 · A0A1G6L984_9EURY
- ProteinProbable bifunctional tRNA threonylcarbamoyladenosine biosynthesis protein
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids567 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t6A37) in tRNAs that read codons beginning with adenine. Is a component of the KEOPS complex that is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. The Kae1 domain likely plays a direct catalytic role in this reaction. The Bud32 domain probably displays kinase activity that regulates Kae1 function.
Catalytic activity
- L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H+
Cofactor
Note: Binds 1 Fe2+ ion per subunit.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 118 | Fe cation (UniProtKB | ChEBI) | |||
Binding site | 122 | Fe cation (UniProtKB | ChEBI) | |||
Binding site | 139-143 | L-threonylcarbamoyladenylate (UniProtKB | ChEBI) | |||
Binding site | 171 | L-threonylcarbamoyladenylate (UniProtKB | ChEBI) | |||
Binding site | 184 | L-threonylcarbamoyladenylate (UniProtKB | ChEBI) | |||
Binding site | 188 | L-threonylcarbamoyladenylate (UniProtKB | ChEBI) | |||
Binding site | 267 | L-threonylcarbamoyladenylate (UniProtKB | ChEBI) | |||
Binding site | 295 | Fe cation (UniProtKB | ChEBI) | |||
Binding site | 375-383 | ATP (UniProtKB | ChEBI) | |||
Binding site | 394 | ATP (UniProtKB | ChEBI) | |||
Active site | 483 | Proton acceptor; for kinase activity | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | EKC/KEOPS complex | |
Molecular Function | ATP binding | |
Molecular Function | histone H2AS1 kinase activity | |
Molecular Function | iron ion binding | |
Molecular Function | metalloendopeptidase activity | |
Molecular Function | N(6)-L-threonylcarbamoyladenine synthase activity | |
Molecular Function | protein serine/threonine/tyrosine kinase activity | |
Molecular Function | zinc ion binding | |
Biological Process | phosphorylation | |
Biological Process | tRNA threonylcarbamoyladenosine modification |
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameProbable bifunctional tRNA threonylcarbamoyladenosine biosynthesis protein
Including 2 domains:
- Recommended nametRNA N6-adenosine threonylcarbamoyltransferase
- EC number
- Alternative names
- Recommended nameSerine/threonine-protein kinase Bud32
- EC number
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageArchaea > Euryarchaeota > Stenosarchaea group > Halobacteria > Halobacteriales > Natrialbaceae > Natrinema
Accessions
- Primary accessionA0A1G6L984
Proteomes
Subcellular Location
Interaction
Subunit
Component of the KEOPS complex that consists of Kae1, Bud32, Cgi121 and Pcc1; the whole complex dimerizes.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, domain, compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 1-334 | Kae1 | |||
Domain | 29-301 | Gcp-like | |||
Region | 320-373 | Disordered | |||
Compositional bias | 333-362 | Basic and acidic residues | |||
Sequence similarities
In the C-terminal section; belongs to the protein kinase superfamily. Tyr protein kinase family. BUD32 subfamily.
In the N-terminal section; belongs to the KAE1 / TsaD family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length567
- Mass (Da)61,884
- Last updated2017-01-18 v1
- ChecksumAA7959E1735C3078
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 333-362 | Basic and acidic residues | |||
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
FMZP01000003 EMBL· GenBank· DDBJ | SDC39718.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
FOIC01000003 EMBL· GenBank· DDBJ | SET00481.1 EMBL· GenBank· DDBJ | Genomic DNA |