{"metadata":{"accession":"PF08845","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR014944","hierarchy":null,"name":{"name":"Toxin SymE, type I toxin-antitoxin system","short":"SymE_toxin"},"description":[{"text":"<p>SymE (SOS-induced yjiW gene with similarity to MazE ) is an SOS-induced toxin. It inhibits cell growth, decreases protein synthesis and increases RNA degradation. It may play a role in the recycling of RNAs damaged under SOS response-inducing conditions. It is predicted to have an AbrB fold, similar to that of the antitoxin MazE. Its translation is repressed by the antisense RNA SymR, which acts as an antitoxin [[cite:PUB00064452],[cite:PUB00053151]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":[{"title":"SymR_RNA","extract":"<p>The <b>SymE-SymR toxin-antitoxin system</b> consists of a small symbiotic endonuclease toxin, SymE, and a non-coding RNA symbiotic RNA antitoxin, SymR, which inhibits SymE translation. SymE-SymR is a type I toxin-antitoxin system, and is under regulation by the antitoxin, SymR. The SymE-SymR complex is believed to play an important role in recycling damaged RNA and DNA. The relationship and corresponding structures of SymE and SymR provide insight into the mechanism of toxicity and overall role in prokaryotic systems.</p>","thumbnail":null}],"literature":{"PUB00064452":{"PMID":17376733,"ISBN":null,"volume":"10","issue":"2","year":2007,"title":"RNA antitoxins.","URL":null,"raw_pages":"117-24","medline_journal":"Curr Opin Microbiol","ISO_journal":"Curr. Opin. Microbiol.","authors":["Gerdes K","Wagner EG."],"DOI_URL":"http://dx.doi.org/10.1016/j.mib.2007.03.003"},"PUB00053151":{"PMID":17462020,"ISBN":null,"volume":"64","issue":"3","year":2007,"title":"An antisense RNA controls synthesis of an SOS-induced toxin evolved from an antitoxin.","URL":null,"raw_pages":"738-54","medline_journal":"Mol Microbiol","ISO_journal":"Mol. Microbiol.","authors":["Kawano M","Aravind L","Storz G."],"DOI_URL":"http://dx.doi.org/10.1111/j.1365-2958.2007.05688.x"}},"set_info":null,"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":7,"interactions":0,"matches":2175,"pathways":0,"proteins":2175,"proteomes":892,"sets":0,"structural_models":{"alphafold":1246},"structures":0,"taxa":1422},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":22,"alignment:full":680},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}