Modomics - A Database of RNA Modifications

ID Card:

Full name: Kinase-associated endopeptidase 1
Synonym: PYRAB17710
GI: 14521970
Orf: PAB1159
COG: COG0533
UniProt: Q9UXT7
Structures: | 2IVN | 2IVO | 2IVP |
Alpha Fold Predicted Structure: AF-Q9UXT7-F1
Complex: EKC/KEOPS
Enzyme type: endopeptidase predicted
Position of modification - modification: t:37 - t6A


PDB Structures:


2IVN

Structure Description:

Title:
Classification:
Technique:

Abstract of the PDB Structure's related Publication:

The Kae1 (Kinase-associated endopeptidase 1) protein is a member of the recently identified transcription complex EKC and telomeres maintenance complex KEOPS in yeast. Kae1 homologues are encoded by all sequenced genomes in the three domains of life. Although annotated as putative endopeptidases, the actual functions of these universal proteins are unknown. Here we show that the purified Kae1 protein (Pa-Kae1) from Pyrococcus abyssi is an iron-protein with a novel type of ATP-binding site. Surprisingly, this protein did not exhibit endopeptidase activity in vitro but binds cooperatively to single and double-stranded DNA and induces unusual DNA conformational change. Furthermore, Pa-Kae1 exhibits a class I apurinic (AP)-endonuclease activity (AP-lyase). Both DNA binding and AP-endonuclease activity are inhibited by ATP. Kae1 is thus a novel and atypical universal DNA interacting protein whose importance could rival those of RecA (RadA/Rad51) in the maintenance of genome integrity in all living cells.

Download RCSB-PDB Structures:

Pdb Files   2IVN.pdb   2IVO.pdb   2IVP.pdb   2KEM.pdb  
Pdbx/mmCIF Files   2IVN.cif   2IVO.cif   2IVP.cif   2KEM.cif  


Protein sequence:

MLALGIEGTAHTLGIGIVSEDKVLANVFDTLTTEKGGIHPKEAAEHHARLMKPLLRKALSEAGVSLDDIDVIAFSQGPGLGPALRVVATAARALAVKYRKPIVGVNHCIAHVEITKMFGVKDPVGLYVSGGNTQVLALEGGRYRVFGETLDIGIGNAIDVFARELGLGFPGGPKVEKLAEKGEKYIELPYAVKGMDLSFSGLLTEAIRKYRSGKYRVEDLAYSFQETAFAALVEVTERAVAHTEKDEVVLVGGVAANNRLREMLRIMTEDRGIKFFVPPYDLCRDNGAMIAYTGLRMYKAGISFRLEETIVKQKFRTDEVEIVW

Comments:

Archaeal Kae1 (Kinase-Associated Endopeptidase 1) is a ortholog of bacterial TsaD (YgjD) and mitochondrial Qri7. As in most archaea, the P. abyssi Kae1 is fused to an atypical small RIO-type kinase homologous to the yeast protein Bud32 (PRPK for p53-related protein kinase). P. abyssi Kae1 is an iron metalloprotein that has a novel type of ATP-binding site. It works with other proteins of the KEOPS complex (Bud32, Pcc1 and Cgi121).





Alpha Fold Predicted Structure:






Clear Selection and Reset Camera

Protein sequence:

M L A L G I E G T A H T L G I G I V S E D K V L A N V F D T L T T E K G G I H P K E A A E H H A R L M K P L L R K A L S E A G V S L D D I D V I A F S Q G P G L G P A L R V V A T A A R A L A V K Y R K P I V G V N H C I A H V E I T K M F G V K D P V G L Y V S G G N T Q V L A L E G G R Y R V F G E T L D I G I G N A I D V F A R E L G L G F P G G P K V E K L A E K G E K Y I E L P Y A V K G M D L S F S G L L T E A I R K Y R S G K Y R V E D L A Y S F Q E T A F A A L V E V T E R A V A H T E K D E V V L V G G V A A N N R L R E M L R I M T E D R G I K F F V P P Y D L C R D N G A M I A Y T G L R M Y K A G I S F R L E E T I V K Q K F R T D E V E I V W

Secondary Structure Alphabet

  • G: 3-turn helix (310helix)
  • H: α-helix
  • I: 𝝅-helix (5 - turn helix)
  • T: Hydrogen Bonded Turn
  • B: β-sheet
  • S: Bend
  • C: Coil (residues not present in any of the above conformations)
  • N: Not assigned

Download PDB Structures & DSSP Secondary Structures:

Alpha Fold Pdb Files   AF-Q9UXT7-F1.pdb  
Alpha Fold Pdbx/mmCIF Files   AF-Q9UXT7-F1.cif  
DSSP Secondary Structures   Q9UXT7.dssp  





Publications:

Title Authors Journal Details PubMed Id DOI
An archaeal orthologue of the universal protein Kae1 is an iron metalloprotein which exhibits atypical DNA-binding properties and apurinic-endonuclease activity in vitro. Hecker A, Leulliot N, Gadelle D, Graille M, Justome A, Dorlet P, Brochier C, Quevillon-Cheruel S, Le Cam E, van Tilbeurgh H, Forterre P Nucleic Acids Res [details] 17766251 -

Links:

_PubMed_