Q18KI0 · KAE1B_HALWD
- ProteinProbable bifunctional tRNA threonylcarbamoyladenosine biosynthesis protein
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids533 (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
- ATP + L-seryl-[protein] = ADP + H+ + O-phospho-L-seryl-[protein]
Cofactor
Note: Binds 1 Fe2+ ion per subunit.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 112 | Fe cation (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 116 | Fe cation (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 133-137 | L-threonylcarbamoyladenylate (UniProtKB | ChEBI) | ||||
Sequence: NASGA | ||||||
Binding site | 165 | L-threonylcarbamoyladenylate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 178 | L-threonylcarbamoyladenylate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 182 | L-threonylcarbamoyladenylate (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 261 | L-threonylcarbamoyladenylate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 289 | Fe cation (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 347-354 | ATP (UniProtKB | ChEBI) | ||||
Sequence: VRGAEAIV | ||||||
Binding site | 363 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Active site | 452 | Proton acceptor; for kinase activity | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | EKC/KEOPS complex | |
Molecular Function | ATP binding | |
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 kinase activity | |
Molecular Function | protein serine/threonine/tyrosine kinase activity | |
Molecular Function | zinc ion binding | |
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 > Haloferacaceae > Haloquadratum
Accessions
- Primary accessionQ18KI0
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000303649 | 1-533 | Probable bifunctional tRNA threonylcarbamoyladenosine biosynthesis protein | |||
Sequence: MRILGIEGTAWAASAALYNTHDETIVIESDPYQPDSGGLHPREAAEHMSTALPEVISTILERAVSSGNTDAIGIDAIAFSRGPGLGPCLRVVGTAARTLTQALSVPLIGVNHMIAHLEIGRHQSGFTTPVCLNASGANAHLLGYHRRQYQVLGETMDTGVGNAIDKFTRHLGWNHPGGPKVEAAATDGSYHDLPYVVKGMDFSFSGIMSAAKDAVDNEVPVVDVCTGLQETIFAMLTEVAERALSLTGSNELVLGGGVGQNDRLREMLSTMCTARGASFYAPESRFLRDNAGMIAVLGAAMYEAGQTISVNDSAVDPTFRPDAVTVTWRDDETSVTRTPATLDKTPVRGAEAIVRRINDHVVKRRVEKSYRHPKLDRRLRAERTRAEARLTSAARRLGVPTPLIFDADPETGTLVFEYVGETDLAADLTVSRCHAVGQHLGRIHNAGFVHGDPTTRNVRVDSAQNYLIDFGLGYHTDHVEDHAMDLHVFIQSVTGTASDPAPLITAFESGYAETGISTVQSRLRDIESRGRYH |
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-328 | Kae1 | ||||
Sequence: MRILGIEGTAWAASAALYNTHDETIVIESDPYQPDSGGLHPREAAEHMSTALPEVISTILERAVSSGNTDAIGIDAIAFSRGPGLGPCLRVVGTAARTLTQALSVPLIGVNHMIAHLEIGRHQSGFTTPVCLNASGANAHLLGYHRRQYQVLGETMDTGVGNAIDKFTRHLGWNHPGGPKVEAAATDGSYHDLPYVVKGMDFSFSGIMSAAKDAVDNEVPVVDVCTGLQETIFAMLTEVAERALSLTGSNELVLGGGVGQNDRLREMLSTMCTARGASFYAPESRFLRDNAGMIAVLGAAMYEAGQTISVNDSAVDPTFRPDAVTVTW | ||||||
Domain | 339-533 | Protein kinase | ||||
Sequence: PATLDKTPVRGAEAIVRRINDHVVKRRVEKSYRHPKLDRRLRAERTRAEARLTSAARRLGVPTPLIFDADPETGTLVFEYVGETDLAADLTVSRCHAVGQHLGRIHNAGFVHGDPTTRNVRVDSAQNYLIDFGLGYHTDHVEDHAMDLHVFIQSVTGTASDPAPLITAFESGYAETGISTVQSRLRDIESRGRYH |
Sequence similarities
In the N-terminal section; belongs to the KAE1 / TsaD family.
In the C-terminal section; belongs to the protein kinase superfamily. Tyr protein kinase family. BUD32 subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length533
- Mass (Da)57,542
- Last updated2006-07-25 v1
- ChecksumA504147E944A27A2
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AM180088 EMBL· GenBank· DDBJ | CAJ51469.1 EMBL· GenBank· DDBJ | Genomic DNA |