Unknown

Dataset Information

0

Gene3D: modelling protein structure, function and evolution.


ABSTRACT: The Gene3D release 4 database and web portal (http://cathwww.biochem.ucl.ac.uk:8080/Gene3D) provide a combined structural, functional and evolutionary view of the protein world. It is focussed on providing structural annotation for protein sequences without structural representatives--including the complete proteome sets of over 240 different species. The protein sequences have also been clustered into whole-chain families so as to aid functional prediction. The structural annotation is generated using HMM models based on the CATH domain families; CATH is a repository for manually deduced protein domains. Amongst the changes from the last publication are: the addition of over 100 genomes and the UniProt sequence database, domain data from Pfam, metabolic pathway and functional data from COGs, KEGG and GO, and protein-protein interaction data from MINT and BIND. The website has been rebuilt to allow more sophisticated querying and the data returned is presented in a clearer format with greater functionality. Furthermore, all data can be downloaded in a simple XML format, allowing users to carry out complex investigations at their own computers.

SUBMITTER: Yeats C 

PROVIDER: S-EPMC1347420 | biostudies-literature | 2006 Jan

REPOSITORIES: biostudies-literature

altmetric image

Publications

Gene3D: modelling protein structure, function and evolution.

Yeats Corin C   Maibaum Michael M   Marsden Russell R   Dibley Mark M   Lee David D   Addou Sarah S   Orengo Christine A CA  

Nucleic acids research 20060101 Database issue


The Gene3D release 4 database and web portal (http://cathwww.biochem.ucl.ac.uk:8080/Gene3D) provide a combined structural, functional and evolutionary view of the protein world. It is focussed on providing structural annotation for protein sequences without structural representatives--including the complete proteome sets of over 240 different species. The protein sequences have also been clustered into whole-chain families so as to aid functional prediction. The structural annotation is generate  ...[more]

Similar Datasets

| S-EPMC4948869 | biostudies-literature
| S-EPMC1182425 | biostudies-literature
| S-EPMC5054710 | biostudies-literature
| S-EPMC2921592 | biostudies-literature
| S-EPMC5798203 | biostudies-literature
| S-EPMC2691936 | biostudies-literature
| S-EPMC6563846 | biostudies-literature
| S-EPMC2098864 | biostudies-other
| S-EPMC5302727 | biostudies-literature
| S-EPMC2094735 | biostudies-literature