ArticlePLoS biology2009
Exploration of uncharted regions of the protein universe.
Article in PLoS biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 82 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
82 citing papers in PubMed.
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- Systematic discovery of enzyme promiscuity in Escherichia coli using in vitro metabolomics.Communications biology · 2026Article
- Identification and Analysis of DUF506 Gene Family in Peanut (Biomolecules · 2026Article
- AI-driven discovery of probiotic gene modules and their functional impact in food and health.Frontiers in microbiology · 2026Article
- Charting unknown metabolic reactions by mass spectrometry-resolved stable-isotope tracing metabolomics.Nature communications · 2025Article
- jdispatcher-viewers: interactive visualizations of sequence similarity search results and domain predictions.Bioinformatics advances · 2025Article
- Structure based functional identification of an uncharacterized protein from Coxiella burnetii involved in adipogenesis.Scientific reports · 2024Article
- Review
- Crystal structure of domain of unknown function 507 (DUF507) reveals a new protein fold.Scientific reports · 2023Article
- Beyond the limits of the unassigned protist microbiome: inferring large-scale spatio-temporal patterns of Syndiniales marine parasites.ISME communications · 2023Article
- Elucidating the functional roles of prokaryotic proteins using big data and artificial intelligence.FEMS microbiology reviews · 2023Review
- Sampling of structure and sequence space of small protein folds.Nature communications · 2022Article
- mebipred: identifying metal-binding potential in protein sequence.Bioinformatics (Oxford, England) · 2022Article
- A novel gene from the acidophilic bacterium Leptospirillum sp. CF-1 and its role in oxidative stress and chromate tolerance.Biological research · 2022Article
- Article
- Hypothetical protein predicted to be tumor suppressor: a protein functional analysis.Genomics & informatics · 2022Article
- In-silico characterization and structure-based functional annotation of a hypothetical protein from Campylobacter jejuni involved in propionate catabolism.Genomics & informatics · 2021Article
- A roadmap for metagenomic enzyme discovery.Natural product reports · 2021Review
- Life-history strategies of soil microbial communities in an arid ecosystem.The ISME journal · 2021Article
- TIM29 is required for enhanced stem cell activity during regeneration in the flatworm Macrostomum lignano.Scientific reports · 2021Article
22 more citing papers are in PubMed but not listed here.
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8 authors.
Funding
Abstract
The genome projects have unearthed an enormous diversity of genes of unknown function that are still awaiting biological and biochemical characterization. These genes, as most others, can be grouped into families based on sequence similarity. The PFAM database currently contains over 2,200 such families, referred to as domains of unknown function (DUF). In a coordinated effort, the four large-scale centers of the NIH Protein Structure Initiative have determined the first three-dimensional structures for more than 250 of these DUF families. Analysis of the first 248 reveals that about two thirds of the DUF families likely represent very divergent branches of already known and well-characterized families, which allows hypotheses to be formulated about their biological function. The remainder can be formally categorized as new folds, although about one third of these show significant substructure similarity to previously characterized folds. These results infer that, despite the enormous increase in the number and the diversity of new genes being uncovered, the fold space of the proteins they encode is gradually becoming saturated. The previously unexplored sectors of the protein universe appear to be primarily shaped by extreme diversification of known protein families, which then enables organisms to evolve new functions and adapt to particular niches and habitats. Notwithstanding, these DUF families still constitute the richest source for discovery of the remaining protein folds and topologies.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.