TY - JOUR A1 - Sigrist, Christian J. A. A1 - Cerutti, Lorenzo A1 - de Castro, Edouard A1 - Langendijk-Genevaux, Petra S. A1 - Bulliard, Virginie A1 - Bairoch, Amos A1 - Hulo, Nicolas T1 - PROSITE, a protein domain database for functional characterization and annotation Y1 - 2010/01/01 JF - Nucleic Acids Research JO - Nucleic Acids Research SP - D161 EP - D166 N1 - 10.1093/nar/gkp885 VL - 38 IS - suppl 1 UR - http://nar.oxfordjournals.org/content/38/suppl_1/D161.abstract N2 - PROSITE consists of documentation entries describing protein domains, families and functional sites, as well as associated patterns and profiles to identify them. It is complemented by ProRule, a collection of rules based on profiles and patterns, which increases the discriminatory power of these profiles and patterns by providing additional information about functionally and/or structurally critical amino acids. PROSITE is largely used for the annotation of domain features of UniProtKB/Swiss-Prot entries. Among the 983 (DNA-binding) domains, repeats and zinc fingers present in Swiss-Prot (release 57.8 of 22 September 2009), 696 (∼70%) are annotated with PROSITE descriptors using information from ProRule. In order to allow better functional characterization of domains, PROSITE developments focus on subfamily specific profiles and a new profile building method giving more weight to functionally important residues. Here, we describe AMSA, an annotated multiple sequence alignment format used to build a new generation of generalized profiles, the migration of ScanProsite to Vital-IT, a cluster of 633 CPUs, and the adoption of the Distributed Annotation System (DAS) to facilitate PROSITE data integration and interchange with other sources. The latest version of PROSITE (release 20.54, of 22 September 2009) contains 1308 patterns, 863 profiles and 869 ProRules. PROSITE is accessible at: http://www.expasy.org/prosite/. ER -