MATAALLRSIRRREVVSSPFSAYRCLSSSGKASLNSSYLGQNFRSFSRAFSSKPAGNDVIGIDLGTTNSCVAVMEGKNPKVIENAEGARTTPSVVAFNTKGELLVGTPAKRQAVTNPTNTVSGTKRLIGRKFDDPQTQKEMKMVPYKIVRAPNGDAWVEANGQQYSPSQIGAFILTKMKETAEAYLGKSVTKAVVTVPAYFNDAQRQATKDAGRIAGLDVERIINEPTAAALSYGMTNKEGLIAVFDLGGGTFDVSVLEISNGVFEVKATNGDTFLGGEDFDNALLDFLVNEFKTTEGIDLAKDRLALQRLREAAEKAKIELSSTSQTEINLPFITADASGAKHFNITLTRSRFETLVNHLIERTRDPCKNCLKDAGISAKEVDEVLLVGGMTRVPKVQSIVAEIFGKSPSKGVNPDEAVAMGAALQGGILRGDVKELLLLDVTPLSLGIETLGGVFTRLITRNTTIPTKKSQVFSTAADNQTQVGIRVLQGEREMATDNKLLGEFDLVGIPPSPRGVPQIEVTFDIDANGIVTVSAKDKTTGKVQQITIRSSGGLSEDDIQKMVREAELHAQKDKERKELIDTKNTADTTIYSIEKSLGEYREKIPSEIAKEIEDAVADLRSASSGDDLNEIKAKIEAANKAVSKIGEHMSGGSGGGSAPGGGSEGGSDQAPEAEYEEVKK HSP70-10 F17I14_220 Mitochondrial heat shock protein 70-2 Heat shock 70 kDa protein 10, mitochondrial At5g09590 682 HSP7J_ARATH In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage (By similarity). MTHSC70-2 Heat shock protein 70-10 HSC70-5