A0A1G6L984 · A0A1G6L984_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.

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 site118Fe cation (UniProtKB | ChEBI)
Binding site122Fe cation (UniProtKB | ChEBI)
Binding site139-143L-threonylcarbamoyladenylate (UniProtKB | ChEBI)
Binding site171L-threonylcarbamoyladenylate (UniProtKB | ChEBI)
Binding site184L-threonylcarbamoyladenylate (UniProtKB | ChEBI)
Binding site188L-threonylcarbamoyladenylate (UniProtKB | ChEBI)
Binding site267L-threonylcarbamoyladenylate (UniProtKB | ChEBI)
Binding site295Fe cation (UniProtKB | ChEBI)
Binding site375-383ATP (UniProtKB | ChEBI)
Binding site394ATP (UniProtKB | ChEBI)
Active site483Proton acceptor; for kinase activity

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular ComponentEKC/KEOPS complex
Molecular FunctionATP binding
Molecular Functionhistone H2AS1 kinase activity
Molecular Functioniron ion binding
Molecular Functionmetalloendopeptidase activity
Molecular FunctionN(6)-L-threonylcarbamoyladenine synthase 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
      SAMN04488694_10369
      , SAMN05192552_1003238

Organism names

  • Taxonomic identifier
  • Organism
  • Strains
    • CDM_1
    • CDM_6
  • Taxonomic lineage
    Archaea > Euryarchaeota > Stenosarchaea group > Halobacteria > Halobacteriales > Natrialbaceae > Natrinema

Accessions

  • Primary accession
    A0A1G6L984

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

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

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain, compositional bias.

Type
IDPosition(s)Description
Region1-334Kae1
Domain29-301Gcp-like
Region320-373Disordered
Compositional bias333-362Basic 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 status
    Complete
  • Length
    567
  • Mass (Da)
    61,884
  • Last updated
    2017-01-18 v1
  • Checksum
    AA7959E1735C3078
MSNSIRILGIEGTAWAASAALFDAETDDVVIETDAYQPESGGIHPREASEHMHDAIPDVVGRILEHARETHDGPVSEPPVDAVAFSRGPGLGPCLRVVGTAARALSQVLEVPLVGVNHMVAHLEIGRHTSGFDSPVCLNASGANAHLLAYRNGRYRVLGETMDTGVGNSIDKFTRHVGWSHPGGPKVEQAAKDGEYVDLPYVVKGMDFSFSGIMSAAKQRYDEGVPVEDVCYSLQENIFSMLTEVSERALSLTGSDELVLGGGVGHNARLREMLAEMCAQRGAEFHAPEPRFLGDNAGMIAVLGAKMYAAGDTLALEESHVDPNFRPDQVPVTWRGRSERSEDLDNASGDARNRERAAEPELAAGRGVDAADDSQVRGAEALVDLEPTGGRVTKRRRAKTYRHPALDERLRKERTTLEARLTSLARREGVPTPVLSDVDQTEARLELEYVGERDLQAALSSDRVRDVGRHLARLHQAGFVHGDPTTRNVRVDGEKAYLIDFGLGYHTDHVEDYAMDLHVFDQSLVGTADDPEPLREAARDGYRDVGDERVLERLHDVEGRGRYQSDT

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias333-362Basic and acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
FMZP01000003
EMBL· GenBank· DDBJ
SDC39718.1
EMBL· GenBank· DDBJ
Genomic DNA
FOIC01000003
EMBL· GenBank· DDBJ
SET00481.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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