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MEROPS: the peptidase database

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TLDR
The MEROPS database has added an analysis tool to the relevant species pages to show significant gains and losses of peptidase genes relative to related species, and has collected over 39 000 known cleavage sites in proteins, peptides and synthetic substrates.
Abstract
Peptidases (proteolytic enzymes) are of great relevance to biology, medicine and biotechnology. This practical importance creates a need for an integrated source of information about them, and also about their natural inhibitors. The MEROPS database (http://merops.sanger.ac.uk) aims to fill this need. The organizational principle of the database is a hierarchical classification in which homologous sets of the proteins of interest are grouped in families and the homologous families are grouped in clans. Each peptidase, family and clan has a unique identifier. The database has recently been expanded to include the protein inhibitors of peptidases, and these are classified in much the same way as the peptidases. Forms of information recently added include new links to other databases, summary alignments for peptidase clans, displays to show the distribution of peptidases and inhibitors among organisms, substrate cleavage sites and indexes for expressed sequence tag libraries containing peptidases. A new way of making hyperlinks to the database has been devised and a BlastP search of our library of peptidase and inhibitor sequences has been added.

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MEROPS: the database of proteolytic enzymes, their substrates and inhibitors

TL;DR: The MEROPS database has been expanded to include proteolytic enzymes other than peptidases, and the inclusion of small-molecule inhibitors in the tables of peptidase–inhibitor interactions is included.
References
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Journal ArticleDOI

MUSCLE: a multiple sequence alignment method with reduced time and space complexity

TL;DR: MUSCLE offers a range of options that provide improved speed and / or alignment accuracy compared with currently available programs, and a new option, MUSCLE-fast, designed for high-throughput applications.
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UniProt: the Universal Protein knowledgebase

TL;DR: The Swiss-Prot, TrEMBL and PIR protein database activities have united to form the Universal Protein Knowledgebase (UniProt), which is to provide a comprehensive, fully classified, richly and accurately annotated protein sequence knowledgebase, with extensive cross-references and query interfaces.
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SCOP: a structural classification of proteins database for the investigation of sequences and structures.

TL;DR: This database provides a detailed and comprehensive description of the structural and evolutionary relationships of the proteins of known structure and provides for each entry links to co-ordinates, images of the structure, interactive viewers, sequence data and literature references.
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Rapid and sensitive protein similarity searches

TL;DR: An algorithm was developed which facilitates the search for similarities between newly determined amino acid sequences and sequences already available in databases and increases sensitivity by giving high scores to those amino acid replacements which occur frequently in evolution.
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