Lon proteuse betongs to the Al'Pase associated with diverse ce]lular activities (AAA+) superfainily and is mainly responsibae for eliminuting n]isfplded or damaged pTotcins as wcll as for centrolling the cellular activiLies of shurt-lived regulatory proteins. It censists of threc distinct functional demains, and the small a demain. a subdomaiii of thc central AI]Pase domain, is suggesred as the substraterecognitien and
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