A0A830E218 · A0A830E218_9EURY

  • Protein
    Probable bifunctional tRNA threonylcarbamoyladenosine biosynthesis protein
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

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.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

Fe2+ (UniProtKB | Rhea| CHEBI:29033 )

Note: Binds 1 Fe2+ ion per subunit.

Features

Showing features for binding site, active site.

Type
IDPosition(s)Description
Binding site128Fe cation (UniProtKB | ChEBI)
Binding site132Fe cation (UniProtKB | ChEBI)
Binding site149-153L-threonylcarbamoyladenylate (UniProtKB | ChEBI)
Binding site181L-threonylcarbamoyladenylate (UniProtKB | ChEBI)
Binding site194L-threonylcarbamoyladenylate (UniProtKB | ChEBI)
Binding site198L-threonylcarbamoyladenylate (UniProtKB | ChEBI)
Binding site277L-threonylcarbamoyladenylate (UniProtKB | ChEBI)
Binding site305Fe cation (UniProtKB | ChEBI)
Binding site360-368ATP (UniProtKB | ChEBI)
Binding site377ATP (UniProtKB | ChEBI)
Active site466Proton acceptor; for kinase activity

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular ComponentEKC/KEOPS complex
Molecular Functionacyltransferase activity, transferring groups other than amino-acyl groups
Molecular FunctionATP binding
Molecular Functioniron ion binding
Molecular Functionmetalloendopeptidase activity
Molecular Functionprotein serine/threonine kinase activity
Molecular Functionprotein serine/threonine/tyrosine kinase activity
Molecular Functionzinc ion binding
Biological Processphosphorylation
Biological ProcesstRNA threonylcarbamoyladenosine modification

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Probable bifunctional tRNA threonylcarbamoyladenosine biosynthesis protein

Including 2 domains:

  • Recommended name
    tRNA N6-adenosine threonylcarbamoyltransferase
  • EC number
  • Alternative names
    • tRNA threonylcarbamoyladenosine biosynthesis protein Kae1
    • t(6)A37 threonylcarbamoyladenosine biosynthesis protein Kae1
  • Recommended name
    Serine/threonine-protein kinase Bud32
  • EC number

Gene names

    • ORF names
      GCM10007209_34530

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • CCM 7217
  • Taxonomic lineage
    Archaea > Euryarchaeota > Stenosarchaea group > Halobacteria > Halobacteriales > Haloferacaceae > Haloferax

Accessions

  • Primary accession
    A0A830E218

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Component of the KEOPS complex that consists of Kae1, Bud32, Cgi121 and Pcc1; the whole complex dimerizes.

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-344Kae1
Domain41-311Gcp-like

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 status
    Complete
  • Length
    552
  • Mass (Da)
    59,061
  • Last updated
    2021-09-29 v1
  • MD5 Checksum
    1B445149E1CAF1B724179BF3BEFE008F
MRILGIEGTAWAASAAVFETDDPDALRSETGRAPDPAADHVFIESDPYQPDSGGIHPRESAEHMGNAIPEVVETALAHAAARHDGDGPVVDGVAFSRGPGLGPCLRIVGTAARSVAQTLDVPLLGVNHMVAHLEIGRYQSGFDSPVCLNASGANAHLLGYHNGRYRVLGETMDTGVGNALDKFTRHVGWTHPGGPKVEKAAEDGDYVELPYVVKGMDFSFSGIMSAAKDEADAGTPVPDICAGLQETVFAMLAEVAERALSLTGTDELVLGGGVGQNARLREMLAEMCDQRGAEFYAPDPRFLRDNAGMIAALGARMLAAGDTLAVEESTVDPNFRPDQVAVTWRGADESVARAHTDDGAIRGAEATVDIDSEEVVKRRVPKTYRHPELDERLRRERTKAEARLTSDARRAGVRTPVVRDVDPVDGVIAFQRVGDADLAERLDPEAVRVVGEYLARLHEAGIVHGDPTTRNVRVGTGPDGDPRVYLIDFGLGFHTGHVEDHAMDLHVFAQSVEGTAADADPLLDALEAGYEAVGSEEVIARLREVESRGRYR

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BMCI01000007
EMBL· GenBank· DDBJ
GGC69586.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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