A0A2R6D1S9 · A0A2R6D1S9_9EURY
- ProteinProbable bifunctional tRNA threonylcarbamoyladenosine biosynthesis protein
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids587 (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 | 136 | Fe cation (UniProtKB | ChEBI) | |||
Binding site | 140 | Fe cation (UniProtKB | ChEBI) | |||
Binding site | 157-161 | L-threonylcarbamoyladenylate (UniProtKB | ChEBI) | |||
Binding site | 189 | L-threonylcarbamoyladenylate (UniProtKB | ChEBI) | |||
Binding site | 202 | L-threonylcarbamoyladenylate (UniProtKB | ChEBI) | |||
Binding site | 206 | L-threonylcarbamoyladenylate (UniProtKB | ChEBI) | |||
Binding site | 301 | L-threonylcarbamoyladenylate (UniProtKB | ChEBI) | |||
Binding site | 329 | Fe cation (UniProtKB | ChEBI) | |||
Binding site | 393-401 | ATP (UniProtKB | ChEBI) | |||
Binding site | 410 | ATP (UniProtKB | ChEBI) | |||
Active site | 499 | 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 kinase 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
- Strain
- Taxonomic lineageArchaea > Euryarchaeota > Stenosarchaea group > Halobacteria > Halobacteriales
Accessions
- Primary accessionA0A2R6D1S9
Proteomes
Subcellular Location
Interaction
Subunit
Component of the KEOPS complex that consists of Kae1, Bud32, Cgi121 and Pcc1; the whole complex dimerizes.
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 1-368 | Kae1 | |||
Compositional bias | 71-85 | Basic and acidic residues | |||
Region | 71-96 | Disordered | |||
Domain | 92-335 | Gcp-like | |||
Region | 242-261 | Disordered | |||
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.
Family and domain databases
Sequence
- Sequence statusComplete
- Length587
- Mass (Da)62,716
- Last updated2018-06-20 v1
- Checksum91F3DD4B8D626905
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 71-85 | Basic and acidic residues | |||
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
PXQP01000204 EMBL· GenBank· DDBJ | PSP36877.1 EMBL· GenBank· DDBJ | Genomic DNA |