M0ERN8 · M0ERN8_9EURY
- ProteinProbable bifunctional tRNA threonylcarbamoyladenosine biosynthesis protein
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids571 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
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 | 110 | Fe cation (UniProtKB | ChEBI) | |||
Binding site | 114 | Fe cation (UniProtKB | ChEBI) | |||
Binding site | 131-135 | L-threonylcarbamoyladenylate (UniProtKB | ChEBI) | |||
Binding site | 163 | L-threonylcarbamoyladenylate (UniProtKB | ChEBI) | |||
Binding site | 176 | L-threonylcarbamoyladenylate (UniProtKB | ChEBI) | |||
Binding site | 180 | L-threonylcarbamoyladenylate (UniProtKB | ChEBI) | |||
Binding site | 273 | L-threonylcarbamoyladenylate (UniProtKB | ChEBI) | |||
Binding site | 301 | Fe cation (UniProtKB | ChEBI) | |||
Binding site | 365-373 | ATP (UniProtKB | ChEBI) | |||
Binding site | 386 | ATP (UniProtKB | ChEBI) | |||
Active site | 475 | Proton acceptor; for kinase activity | |||
GO annotations
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
- Strain
- Taxonomic lineageArchaea > Methanobacteriati > Methanobacteriota > Stenosarchaea group > Halobacteria > Halobacteriales > Haloferacaceae > Halorubrum > Halorubrum distributum group
Accessions
- Primary accessionM0ERN8
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, domain, compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 1-340 | Kae1 | |||
Domain | 27-307 | Gcp-like | |||
Region | 345-371 | Disordered | |||
Compositional bias | 360-369 | Basic and acidic residues | |||
Region | 476-499 | 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
- Length571
- Mass (Da)60,123
- Last updated2013-04-03 v1
- MD5 Checksum38B26DCEF6ED1052C0A0415392D568DA
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 360-369 | Basic and acidic residues | |||
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AOJM01000046 EMBL· GenBank· DDBJ | ELZ49542.1 EMBL· GenBank· DDBJ | Genomic DNA |