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Initially identified as a transcriptional coactivator, SND1 was later established as a component of the RNA\u2011induced silencing complex, where it contributes to RNA turnover and microRNA regulation. SND1\u2019s diverse activities stem from its modular architecture, comprising four staphylococcal nuclease\u2011like domains, capable of direct RNA binding, and an extended Tudor domain that together form an integrated RNA\u2011binding and catalytic platform. This versatility also underlies its role in viral infection: SND1 acts as an m\u2076A reader and is exploited by RNA viruses, such as SARS\u2011CoV\u20112. Recent work showed that SND1 depletion, particularly loss of its third structured domain (SN3), reduces recruitment of the viral protein Nsp9 to the 3\u2032 untranslated region of the SARS\u2011CoV\u20112 genome, impairing viral RNA synthesis through a direct SN3\u2013Nsp9 interaction. Here, we report expression, purification, and near\u2011complete backbone NMR assignments of the SN3 domain of SND1. Secondary structure elements calculated by TALOS-N based on these assignments are in good agreement with the existing crystal structure of SN3. Our data provide an excellent foundation for future structural studies of SND1\u2013RNA complexes and their roles in viral RNA priming in SARS-CoV-2.<\/jats:p>","DOI":"10.1007\/s12104-026-10267-4","type":"journal-article","created":{"date-parts":[[2026,5,16]],"date-time":"2026-05-16T05:53:36Z","timestamp":1778910816000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Backbone resonance assignment of the third domain of the human staphylococcal nuclease domain-containing protein 1 (SND1)"],"prefix":"10.1007","volume":"20","author":[{"given":"Shradha","family":"Ajith","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5534-8328","authenticated-orcid":false,"given":"Liza","family":"Cubeddu","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1095-2569","authenticated-orcid":false,"given":"Roland","family":"Gamsjaeger","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"297","published-online":{"date-parts":[[2026,5,16]]},"reference":[{"key":"10267_CR1","doi-asserted-by":"publisher","unstructured":"Baquero-Perez B, Antanaviciute A, Yonchev ID, Carr IM, Wilson SA, Whitehouse A (2019) The Tudor SND1 protein is an m(6)A RNA reader essential for replication of Kaposi\u2019s sarcoma-associated herpesvirus. 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