CyanoLyase: a database of phycobilin lyase sequences, motifs and functions

被引:28
作者
Bretaudeau, Anthony [2 ]
Coste, Francois [3 ]
Humily, Florian [1 ,4 ]
Garczarek, Laurence [1 ,4 ]
Le Corguille, Gildas [1 ,5 ]
Six, Christophe [1 ,4 ]
Ratin, Morgane [1 ,4 ]
Collin, Olivier [2 ]
Schluchter, Wendy M. [6 ]
Partensky, Frederic [1 ,4 ]
机构
[1] Univ Paris 06, Biol Stn, F-29680 Roscoff, France
[2] INRIA Irisa, GenOuest Platform, F-35042 Rennes, France
[3] INRIA Irisa, Dyliss Team, F-35042 Rennes, France
[4] CNRS, Ocean Plankton Grp, UMR Adaptat & Divers Marine Environm 7144, F-29680 Roscoff, France
[5] CNRS, Anal & Bioinformat Marine Sci ABiMS FR2424, F-29680 Roscoff, France
[6] Univ New Orleans, Dept Biol Sci, New Orleans, LA 70148 USA
基金
美国国家科学基金会;
关键词
PHYCOCYANIN; PHYCOERYTHROCYANIN; PHYCOVIOLOBILIN; SYNECHOCOCCUS; CYANOBACTERIA; BILIPROTEINS; CHROMOPHORE; ATTACHMENT; EVOLUTION; ALIGNMENT;
D O I
10.1093/nar/gks1091
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:D396 / D401
页数:6
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