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RNA-binding protein
This RNA binding Pelota domain [1] is at the C-terminus of a PRTase family [2]. These PRTase+Pelota genes are found in the biosynthetic operon associated with the Ter stress-response operon and are predicted to be involved in the biosynthesis of a ribo-nucleoside involved in stress response [2]. [1]. 11917006. Comparative genomics and evolution of proteins involved in RNA metabolism. Anantharaman V, Koonin EV, Aravind L;. Nucleic Acids Res. 2002;30:1427-1464. [2]. 23044854. Ter-dependent stress response systems: novel pathways related to metal sensing, production of a nucleoside-like metabolite, and DNA-processing. Anantharaman V, Iyer LM, Aravind L;. Mol Biosyst. 2012;8:3142-3165. (from Pfam)
cysteine protease StiP domain-containing protein
StiP (long term Stationary Phase-Induced Protein) is a cysteine proteinase, often found fused to a phosporibosyltransferase domain, in gene neighborhoods associated with tellurite resistance, that is, with resistance to stresses caused by common (but not yet well-understood) physiological conditions that can be induced experimentally with the normally extremely rare compound tellurite.
cysteine protease StiP family protein
cysteine protease StiP family protein similar to Acinetobacter baylyi StiP, a cysteine protease that may play a role in regulating cell morphology in response to stressful conditions which likely cause oxidative damage
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