A1CLD2 · BUD32_ASPCL

Function

function

Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t6A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. BUD32 has ATPase activity in the context of the EKC/KEOPS complex and likely plays a supporting role to the catalytic subunit KAE1. The EKC/KEOPS complex also promotes both telomere uncapping and telomere elongation. The complex is required for efficient recruitment of transcriptional coactivators.

Catalytic activity

Features

Showing features for binding site, active site.

Type
IDPosition(s)Description
Binding site26-34ATP (UniProtKB | ChEBI)
Binding site49ATP (UniProtKB | ChEBI)
Active site172Proton acceptor

GO annotations

AspectTerm
Cellular Componentchromosome, telomeric region
Cellular Componentcytosol
Cellular ComponentEKC/KEOPS complex
Cellular Componentnucleus
Molecular FunctionATP binding
Molecular Functionhistone H2AS1 kinase activity
Molecular Functionhydrolase activity
Molecular Functionprotein serine kinase activity
Biological Processprotein phosphorylation
Biological ProcesstRNA processing
Biological ProcesstRNA threonylcarbamoyladenosine metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    EKC/KEOPS complex subunit bud32
  • EC number
  • Alternative names
    • Atypical serine/threonine protein kinase bud32 (EC:2.7.11.1
      ) . EC:2.7.11.1 (UniProtKB | ENZYME | Rhea)

Gene names

    • Name
      bud32
    • ORF names
      ACLA_041780

Organism names

Accessions

  • Primary accession
    A1CLD2

Proteomes

Organism-specific databases

Subcellular Location

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00002789051-277EKC/KEOPS complex subunit bud32

Keywords

Interaction

Subunit

Component of the EKC/KEOPS complex composed of at least Bud32, cgi121, gon7, kae1 and pcc1; the whole complex dimerizes.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for compositional bias, region, domain.

Type
IDPosition(s)Description
Compositional bias1-20Pro residues
Region1-23Disordered
Domain20-277Protein kinase

Domain

This protein is considered an atypical serine/threonine kinase, because it lacks the conventional structural elements necessary for the substrate recognition as well as a lysine residue that in all other serine/threonine kinases participates in the catalytic event (By similarity).
BUD32 has protein kinase activity in vitro, but in the context of the EKC/KEOPS complex, the catalytic subunit KAE1 switches the activity of BUD32 from kinase into ATPase (By similarity).

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    277
  • Mass (Da)
    31,061
  • Last updated
    2007-01-23 v1
  • Checksum
    C334D54533C62B09
MSSAEPYTPPPLPSPFTNTTPPPQLLTQGAEAHLYKTVFLSPSTPAALKVRPSKPYRHPILDRRLTRQRILQEARCLVKLVREGVNVPAVLALDWEGQNTEKGFGGAWLMMEWVEGLVVRVVLERWERWMKRNQGSSGAEELKEEENWVRDLLRRIGRAVGALHKAGVIHGDLTTSNLILRPPGHVGEQADTGESSPSMEGDVVLIDFGLASQSLQDEDRAVDLYVLERAFGSTHPRTEPFFEEVLNGYRESYKGASSALKRLEDVRMRGRKRSMIG

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias1-20Pro residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DS027056
EMBL· GenBank· DDBJ
EAW09956.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
Help