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The Universal Protein Resource (UniProt) is a comprehensive resource for protein sequence and annotation data. The UniProt databases are the UniProt Knowledgebase (UniProtKB), the UniProt Reference Clusters (UniRef), and the UniProt Archive (UniParc).
The Protein Data Bank (PDB) archive is the single worldwide repository of information about the 3D structures of large biological molecules, including proteins and nucleic acids. These are the molecules of life that are found in all organisms including bacteria, yeast, plants, flies, other animals, and humans. Understanding the shape of a molecule helps to understand how it works. This knowledge can be used to help deduce a structure's role in human health and disease, and in drug development. The structures in the archive range from tiny proteins and bits of DNA to complex molecular machines like the ribosome.
>>>!!!Bacterial (BCSDB) and Plant&Fungal (PFCSDB) carbohydrate structure databases have been merged into a single database, CSDB!!!<<< BCSDB database is aimed at provision of structural, bibliographic, taxonomic and related information on bacterial carbohydrate structures. Two key points of this service are: covering - is above 90% in the scope of bacterial carbohydrates. This means the negative search answer remains valuable scientific information. And consistence - we manually check the data, and aim at hight quality error-free content. The main source of data is a retrospective literature analysis. About 25% of data were imported from CCSD (Carbbank, ceased in 1997, University of Georgia, Athens; structures published before 1995) with subsequent manual curation and approval. Current coverage is displayed in red on the top of the left menu. The time lag between publication of new data and their deposition ~ 1 year. The scope is "bacterial carbohydrates" and covers nearly all structures of this class published up to 2016. Bacterial means that a structure has been found in bacteria or obtained by modification of those found in bacteria. Carohydrate means a structure composed of any residues linked by glycosidic, ester, amidic, ketal, phospho- or sulpho-diester bonds, in which at least one residue is a sugar or its derivative.
The repository is no longer available. <<<!!!<<< CCRIS information is migrated to PubChem (https://www.ncbi.nlm.nih.gov/pcsubstance?term=%22Chemical%20Carcinogenesis%20Research%20Information%20System%20(CCRIS)%22%5BSourceName%5D%20AND%20hasnohold%5Bfilt%5D) Help for CCRIS Users in PubChem: https://www.nlm.nih.gov/toxnet/Accessing_CCRIS_Content_from_PubChem.html or PDF: https://www.nlm.nih.gov/toxnet/Accessing_CCRIS_Content_from_PubChem.pdf. >>>!!!>>>
The RESID Database of Protein Modifications is a comprehensive collection of annotations and structures for protein modifications including amino-terminal, carboxyl-terminal and peptide chain cross-link post-translational modifications.
The World Register of Marine Species (WoRMS) integrates approximately 100 marine datbases to provide an authoritative and comprehensive list of marine organisms. WoRMS has an editorial system where taxonomic groups are managed by experts responsible for the quality of the information. WorMS register of marine species emerged from the European Register of Marine Species (ERMS) and the Flanders Marine Institute (VLIZ). WoRMS is a contribution to Lifewatch, Catalogue of Life, Encyclopedia of Life, Global Biodiversity Information Facility and the Census of Marine Life.
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APID Interactomes is a database that provides a comprehensive collection of protein interactomes for more than 400 organisms based in the integration of known experimentally validated protein-protein physical interactions (PPIs). Construction of the interactomes is done with a methodological approach to report quality levels and coverage over the proteomes for each organism included. In this way, APID provides interactomes from specific organisms that in 25 cases have more than 500 proteins. As a whole APID includes a comprehensive compendium of 90,379 distinct proteins and 678,441 singular interactions. The analytical and integrative effort done in APID unifies PPIs from primary databases of molecular interactions (BIND, BioGRID, DIP, HPRD, IntAct, MINT) and also from experimentally resolved 3D structures (PDB) where more than two distinct proteins have been identified. In this way, 8,388 structures have been analyzed to find specific protein-protein interactions reported with details of their molecular interfaces. APID also includes a new data visualization web-tool that allows the construction of sub-interactomes using query lists of proteins of interest and the visual exploration of the corresponding networks, including an interactive selection of the properties of the interactions (i.e. the reliability of the "edges" in the network) and an interactive mapping of the functional environment of the proteins (i.e. the functional annotations of the "nodes" in the network).
The Protein database is a collection of sequences from several sources, including translations from annotated coding regions in GenBank, RefSeq and TPA, as well as records from SwissProt, PIR, PRF, and PDB. Protein sequences are the fundamental determinants of biological structure and function.
GenBase is a genetic sequence database that accepts user submissions (mRNA, genomic DNAs, ncRNA, or small genomes such as organelles, viruses, plasmids, phages from any organism) and integrates data from INSDC.