Modomics - A Database of RNA Modifications

ID Card:

Full name: tRNA threonylcarbamoyladenosine biosynthesis protein SUA5
GI: 417826
Orf: G1660
COG: COG0009
UniProt: P32579
Alpha Fold Predicted Structure: AF-P32579-F1
Complex: EKC/KEOPS
Enzyme type: threonylcarbamoyladenosine synthetase
Position of modification - modification: t:37 - t6A



Protein sequence:

MYLGRHFLAMTSKALFDTKILKVNPLSIIFSPDAHIDGSLPTITDPETEAALVEAARIIRDTDETVAFPTETVYGLGGSALNDNSVLSIYRAKNRPSDNPLITHVSSIDQLNRKVFNQPHLSGTSLFDNIPSIYRPLISSLWPGPLTILLPVPSSEHSALSKLTTADQPTFAVRIPANPVARALIALSDTPIAAPSANASTRPSPTLASHVYHDLKDKIPIILDGGACKVGVESTVVDGLCNPPTLLRPGGFTYEEIVKLGGEAWSLCKVENKKTVEKGEKVRTPGMKYRHYSPSAKVVLLVPHCEGDGILKGVDRMERLKRLIETELKANSNIKKIAILTSLKLRDSDLQSKIFNEPDFSSKTFIIERLGQSGEEIQTNLFAALRKVDENDKVDLIFVEGINEEGEGLAVMNRLRKAAANNCIQF

Comments:

Sua5 is required for the formation of threonylcarbamoyl group on the adenosine at position 37(t6A37) in almost all tRNAs decoding ANN codons ( Pichard-Kostuch et al. 2018). It likely catalyzes the condensation of L-threonine bicarbonate (HCO-3) and ATP to give threonylcarbamoyl-AMP (TC-AMP). KEOPS/EKC complex is a tRNA modification complex involved in the biosynthesis of N6-threonylcarbamoyl adenosine (t6) ( Wan et al. 2017). In arachaea and eukaryotes, KEOPS/EKC is composed of OSGEP/Kae1, PRPK/Bud32, TPRKB/Cgi121, and LAGE3/PCC1.Fungi contains an additional subbunit, Gon7, whose orthologues in other species, if present, remain unidentified. Together with Sua5, they catalyze the in vivo formation of t6. Structurally,Sua5 displays a YrdC-like domain between A50 and G250. The yrdC-like domain is typically an ~185-residue module which can be found in stand-alone form ( YrdC-like) , or in association with other domains such as the acylphosphatase-like domain which catalyzes the hydrolysis of various acyl phosphate carboxyl-phosphate bonds such as carbamyl phosphate, succinyl phosphate, 1,3-diphosphoglycerate, etc ( YrdC-like).The yrdC-like domain features a large concave surface on one side that exhibits a positive electrostatic potential. The dimension of this depression, its curvature, and the fact that conserved basic amino acids are located at its floor suggest that it may be a nucleic acid binding domain.





Alpha Fold Predicted Structure:




Downloading... [229114/381746]


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Protein sequence:

M Y L G R H F L A M T S K A L F D T K I L K V N P L S I I F S P D A H I D G S L P T I T D P E T E A A L V E A A R I I R D T D E T V A F P T E T V Y G L G G S A L N D N S V L S I Y R A K N R P S D N P L I T H V S S I D Q L N R K V F N Q P H L S G T S L F D N I P S I Y R P L I S S L W P G P L T I L L P V P S S E H S A L S K L T T A D Q P T F A V R I P A N P V A R A L I A L S D T P I A A P S A N A S T R P S P T L A S H V Y H D L K D K I P I I L D G G A C K V G V E S T V V D G L C N P P T L L R P G G F T Y E E I V K L G G E A W S L C K V E N K K T V E K G E K V R T P G M K Y R H Y S P S A K V V L L V P H C E G D G I L K G V D R M E R L K R L I E T E L K A N S N I K K I A I L T S L K L R D S D L Q S K I F N E P D F S S K T F I I E R L G Q S G E E I Q T N L F A A L R K V D E N D K V D L I F V E G I N E E G E G L A V M N R L R K A A A N N C I Q F
50100150200250300350400SequenceGHITBSN

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-P32579-F1.pdb  
Alpha Fold Pdbx/mmCIF Files   AF-P32579-F1.cif  
DSSP Secondary Structures   P32579.dssp  





Publications: