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CyanoLyase: a database of phycobilin lyase sequences, motifs and functions.
Nucleic Acids Res ; 41(Database issue): D396-401, 2013 Jan.
Article em En | MEDLINE | ID: mdl-23175607
ABSTRACT
CyanoLyase (http//cyanolyase.genouest.org/) is a manually curated sequence and motif database of phycobilin lyases and related proteins. These enzymes catalyze the covalent ligation of chromophores (phycobilins) to specific binding sites of phycobiliproteins (PBPs). The latter constitute the building bricks of phycobilisomes, the major light-harvesting systems of cyanobacteria and red algae. Phycobilin lyases sequences are poorly annotated in public databases. Sequences included in CyanoLyase were retrieved from all available genomes of these organisms and a few others by similarity searches using biochemically characterized enzyme sequences and then classified into 3 clans and 32 families. Amino acid motifs were computed for each family using Protomata learner. CyanoLyase also includes BLAST and a novel pattern matching tool (Protomatch) that allow users to rapidly retrieve and annotate lyases from any new genome. In addition, it provides phylogenetic analyses of all phycobilin lyases families, describes their function, their presence/absence in all genomes of the database (phyletic profiles) and predicts the chromophorylation of PBPs in each strain. The site also includes a thorough bibliography about phycobilin lyases and genomes included in the database. This resource should be useful to scientists and companies interested in natural or artificial PBPs, which have a number of biotechnological applications, notably as fluorescent markers.
Assuntos

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Bases de Dados de Proteínas / Ficobilinas / Ficobiliproteínas / Liases Idioma: En Revista: Nucleic Acids Res Ano de publicação: 2013 Tipo de documento: Article País de afiliação: França

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Bases de Dados de Proteínas / Ficobilinas / Ficobiliproteínas / Liases Idioma: En Revista: Nucleic Acids Res Ano de publicação: 2013 Tipo de documento: Article País de afiliação: França