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The annotation and conditions in this rule are derived from the following entries: P9WNU7 (PAFA_MYCTU), A0QZ42 (PAFA_MYCS2), Q8NQE1 (PAFA_CORGL)

If a protein meets these conditions... i

Common conditions

Special conditions

    • Subsequence at position 16 - 16 aligns to "E" in entry Q8NQE1 (individually applies "Magnesium")
    • Subsequence at position 60 - 60 aligns to "R" in entry Q8NQE1 (individually applies "ATP")
    • Subsequence at position 62 - 62 aligns to "Y" in entry Q8NQE1 (individually applies "Magnesium")
    • Subsequence at position 64 - 64 aligns to "D" in entry Q8NQE1 (individually applies "Proton acceptor")
    • Subsequence at position 70 - 70 aligns to "E" in entry Q8NQE1 (individually applies "Magnesium")
    • Subsequence at position 73 - 73 aligns to "[TS]" in entry Q8NQE1 (individually applies "ATP; via carbonyl oxygen")
    • Subsequence at position 440 - 440 aligns to "W" in entry Q8NQE1 (individually applies "ATP")

... then these annotations are applied i

Protein namei

  • Recommended name:
    Pup--protein ligase (EC:6.3.1.19)
    Alternative name(s):
    Proteasome accessory factor A
    Pup-conjugating enzyme

Gene namei

  • Name:pafA

Pathwayi

  • Pathwayi: proteasomal Pup-dependent pathway

    This protein is involved in the pathway proteasomal Pup-dependent pathway, which is part of Protein degradation.
    View all proteins of this organism that are known to be involved in the pathway proteasomal Pup-dependent pathway and in Protein degradation.
  • Pathwayi: protein pupylation

    This protein is involved in the pathway protein pupylation, which is part of Protein modification.
    View all proteins of this organism that are known to be involved in the pathway protein pupylation and in Protein modification.

Functioni

  • Catalyzes the covalent attachment of the prokaryotic ubiquitin-like protein modifier Pup to the proteasomal substrate proteins, thereby targeting them for proteasomal degradation. This tagging system is termed pupylation. The ligation reaction involves the side-chain carboxylate of the C-terminal glutamate of Pup and the side-chain amino group of a substrate lysine.

Miscellaneousi

  • The reaction mechanism probably proceeds via the activation of Pup by phosphorylation of its C-terminal glutamate, which is then subject to nucleophilic attack by the substrate lysine, resulting in an isopeptide bond and the release of phosphate as a good leaving group.

Catalytic activityi

  • ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine = ADP + phosphate + N6-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine.

Sequence similaritiesi

Metal bindingi

  • Magnesium (to residues corresponding to position 16)
  • Magnesium (to residues corresponding to position 62)
  • Magnesium (to residues corresponding to position 70)

Active sitei

  • Proton acceptor (to residues corresponding to position 64)

Binding sitei

  • ATP (to residues corresponding to position 60)
  • ATP; via carbonyl oxygen (to residues corresponding to position 73)
  • ATP (to residues corresponding to position 440)

Keywordsi

GO (Gene Ontology) termsi