Modomics - A Database of RNA Modifications

ID Card:

Full name: KEOPS complex subunit Pcc1
Synonym: PF2011
GI: 18978383
COG: COG2892
UniProt: Q8TZI1
Structures: | 3ENC | 3ENO | 5JMV |
Complex: EKC/KEOPS
Enzyme type: methyltransferase
Position of modification - modification: t:37 - t6A

PDB Structures:


Structure Description:


Abstract of the PDB Structure's related Publication:

Kae1 is a universally conserved ATPase and part of the essential gene set in bacteria. In archaea and eukaryotes, Kae1 is embedded within the protein kinase-containing KEOPS complex. Mutation of KEOPS subunits in yeast leads to striking telomere and transcription defects, but the exact biochemical function of KEOPS is not known. As a first step to elucidating its function, we solved the atomic structure of archaea-derived KEOPS complexes involving Kae1, Bud32, Pcc1, and Cgi121 subunits. Our studies suggest that Kae1 is regulated at two levels by the primordial protein kinase Bud32, which is itself regulated by Cgi121. Moreover, Pcc1 appears to function as a dimerization module, perhaps suggesting that KEOPS may be a processive molecular machine. Lastly, as Bud32 lacks the conventional substrate-recognition infrastructure of eukaryotic protein kinases including an activation segment, Bud32 may provide a glimpse of the evolutionary history of the protein kinase family.

Download RCSB-PDB Structures:

Pdb Files   3ENC.pdb   3ENO.pdb  
Pdbx/mmCIF Files   3ENC.cif   3ENO.cif  

Protein sequence:



Absent in Bacteria. Works with other proteins of the EKC/KEOPS complex (Bud32, Cgi121 and possibly Gon7).


Title Authors Journal Details PubMed Id DOI
Atomic structure of the KEOPS complex: an ancient protein kinase-containing molecular machine. Mao DY, Neculai D, Downey M, Orlicky S, Haffani YZ, Ceccarelli DF, Ho JS, Szilard RK, Zhang W, Ho CS, Wan L, Fares C, Rumpel S, Kurinov I, Arrowsmith CH, Durocher D, Sicheri F Mol Cell [details] 18951093 -