{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,2]],"date-time":"2026-04-02T00:46:44Z","timestamp":1775090804004,"version":"3.50.1"},"reference-count":24,"publisher":"Oxford University Press (OUP)","issue":"19","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2012,10,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>Summary: Gibberellic acids (GAs) are key plant hormones, regulating various aspects of growth and development, which have been at the center of the \u2018green revolution\u2019. GRAS family proteins, the primary players in GA signaling pathways, remain poorly understood. Using sequence-profile searches, structural comparisons and phylogenetic analysis, we establish that the GRAS family first emerged in bacteria and belongs to the Rossmann fold methyltransferase superfamily. All bacterial and a subset of plant GRAS proteins are likely to function as small-molecule methylases. The remaining plant versions have lost one or more AdoMet (SAM)-binding residues while preserving their substrate-binding residues. We predict that GRAS proteins might either modify or bind small molecules such as GAs or their derivatives.<\/jats:p>\n               <jats:p>Contact: \u00a0aravind@ncbi.nlm.nih.gov<\/jats:p>\n               <jats:p>Supplementary Information: \u00a0Supplementary Material for this article is available at Bioinformatics online.<\/jats:p>","DOI":"10.1093\/bioinformatics\/bts464","type":"journal-article","created":{"date-parts":[[2012,7,25]],"date-time":"2012-07-25T04:49:56Z","timestamp":1343191796000},"page":"2407-2411","source":"Crossref","is-referenced-by-count":93,"title":["Bacterial GRAS domain proteins throw new light on gibberellic acid response mechanisms"],"prefix":"10.1093","volume":"28","author":[{"given":"Dapeng","family":"Zhang","sequence":"first","affiliation":[{"name":"National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, MD 20894, USA"}]},{"given":"Lakshminarayan M.","family":"Iyer","sequence":"additional","affiliation":[{"name":"National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, MD 20894, USA"}]},{"given":"L.","family":"Aravind","sequence":"additional","affiliation":[{"name":"National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, MD 20894, USA"}]}],"member":"286","published-online":{"date-parts":[[2012,7,24]]},"reference":[{"key":"2023012513054925400_bts464-B1","doi-asserted-by":"crossref","first-page":"3389","DOI":"10.1093\/nar\/25.17.3389","article-title":"Gapped BLAST and PSI-BLAST: a new generation of protein database search programs","volume":"25","author":"Altschul","year":"1997","journal-title":"Nucleic Acids Res."},{"key":"2023012513054925400_bts464-B2","doi-asserted-by":"crossref","first-page":"D419","DOI":"10.1093\/nar\/gkm993","article-title":"Data growth and its impact on the SCOP database: new developments","volume":"36","author":"Andreeva","year":"2008","journal-title":"Nucleic Acids Res."},{"key":"2023012513054925400_bts464-B3","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1016\/B978-0-12-387685-0.00004-4","article-title":"Natural history of the eukaryotic chromatin protein methylation system","volume":"101","author":"Aravind","year":"2011","journal-title":"Prog. 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