Thoeris is a bacterial antiphage defense system, which consists of two genes, thsA and thsB, via NAD+ degradation [[cite:PUB00097806],[cite:PUB00101117],[cite:PUB00101118],[cite:PUB00160037]]. ThsA has robust NAD+ cleavage activity and a two-domain architecture containing an N-terminal NAD-binding domain (denoted as sirtuin-like or Macro) and C-terminal SLOG-like domain. In some instances, such as in B. amyloliquefaciens ThsA has an N-terminal transmembrane domain [[cite:PUB00097806]]. ThsB (also referred to as TIR1 and TIR2) is structurally similar to TIR domain proteins but without enzymatic activity. This domain is found at the C-terminal of ThsA proteins which adopts a Rossmann-like fold that binds NAD+/NAD+derivatives. It has been characterised as the SLOG-like domain which binds NAD+ derivatives such as ADPR molecules produced by ThsB, which drives an oligomeric state change in ThsA and activates the NADase activity (represented in [pfam:PF18185]) [[cite:PUB00097806],[cite:PUB00101118]]. This entry represents the NAD+-binding Macro domain from B. amyloliquefaciens [[cite:PUB00097806],[cite:PUB00101117]].
","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00101117":{"PMID":32499527,"ISBN":null,"volume":"11","issue":"1","year":2020,"title":"Structural and functional evidence of bacterial antiphage protection by Thoeris defense system via NAD+ degradation.","URL":null,"raw_pages":"2816","medline_journal":"Nat Commun","ISO_journal":"Nat Commun","authors":["Ka D","Oh H","Park E","Kim JH","Bae E."],"DOI_URL":null},"PUB00101118":{"PMID":34853457,"ISBN":null,"volume":"600","issue":"7887","year":2021,"title":"Antiviral activity of bacterial TIR domains via immune signalling molecules.","URL":null,"raw_pages":"116-120","medline_journal":"Nature","ISO_journal":"Nature","authors":["Ofir G","Herbst E","Baroz M","Cohen D","Millman A","Doron S","Tal N","Malheiro DBA","Malitsky S","Amitai G","Sorek R."],"DOI_URL":null},"PUB00097806":{"PMID":29371424,"ISBN":null,"volume":"359","issue":"6379","year":2018,"title":"Systematic discovery of antiphage defense systems in the microbial pangenome.","URL":null,"raw_pages":null,"medline_journal":"Science","ISO_journal":"Science","authors":["Doron S","Melamed S","Ofir G","Leavitt A","Lopatina A","Keren M","Amitai G","Sorek R."],"DOI_URL":null},"PUB00160037":{"PMID":38924412,"ISBN":null,"volume":"10","issue":"26","year":2024,"title":"Structural characterization of macro domain-containing Thoeris antiphage defense systems.","URL":null,"raw_pages":"eadn3310","medline_journal":"Sci Adv","ISO_journal":"Sci Adv","authors":["Shi Y","Masic V","Mosaiab T","Rajaratman P","Hartley-Tassell L","Sorbello M","Goulart CC","Vasquez E","Mishra BP","Holt S","Gu W","Kobe B","Ve T."],"DOI_URL":"https://doi.org/10.1126/sciadv.adn3310"}},"set_info":{"accession":"CL0223","name":"MACRO"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":9,"interactions":0,"matches":534,"pathways":0,"proteins":534,"proteomes":453,"sets":1,"structural_models":{"alphafold":310},"structures":5,"taxa":1034},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":57,"alignment:full":275},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":{"accession":"8v6s","name":"Crystal structure of PcThsA in complex with Imidazole Adenine Dinucleotide"}}}