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FunTree: a resource for exploring the functional evolution of structurally defined enzyme superfamilies.
Furnham, Nicholas; Sillitoe, Ian; Holliday, Gemma L; Cuff, Alison L; Rahman, Syed A; Laskowski, Roman A; Orengo, Christine A; Thornton, Janet M.
Afiliação
  • Furnham N; European Molecular Biology Laboratory, European Bioinformatics Institute, Wellcome Trust Genome Campus, Hinxton, Cambridge CB10 1SD, UK. nickf@ebi.ac.uk
Nucleic Acids Res ; 40(Database issue): D776-82, 2012 Jan.
Article em En | MEDLINE | ID: mdl-22006843
ABSTRACT
FunTree is a new resource that brings together sequence, structure, phylogenetic, chemical and mechanistic information for structurally defined enzyme superfamilies. Gathering together this range of data into a single resource allows the investigation of how novel enzyme functions have evolved within a structurally defined superfamily as well as providing a means to analyse trends across many superfamilies. This is done not only within the context of an enzyme's sequence and structure but also the relationships of their reactions. Developed in tandem with the CATH database, it currently comprises 276 superfamilies covering ~1800 (70%) of sequence assigned enzyme reactions. Central to the resource are phylogenetic trees generated from structurally informed multiple sequence alignments using both domain structural alignments supplemented with domain sequences and whole sequence alignments based on commonality of multi-domain architectures. These trees are decorated with functional annotations such as metabolite similarity as well as annotations from manually curated resources such the catalytic site atlas and MACiE for enzyme mechanisms. The resource is freely available through a web interface www.ebi.ac.uk/thorton-srv/databases/FunTree.
Assuntos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Bases de Dados de Proteínas / Enzimas Idioma: En Revista: Nucleic Acids Res Ano de publicação: 2012 Tipo de documento: Article País de afiliação: Reino Unido

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Bases de Dados de Proteínas / Enzimas Idioma: En Revista: Nucleic Acids Res Ano de publicação: 2012 Tipo de documento: Article País de afiliação: Reino Unido