Pipeline for transferring annotations between proteins beyond globular domains

Background DisProt is the primary repository of Intrinsically Disordered Proteins (IDPs). This database is manually curated and the annotations there have strong experimental support. Currently, DisProt contains a relatively small number of proteins highlighting the importance of transferring annota...

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Detalles Bibliográficos
Autores: Martinez Perez, Elizabeth, Pajkos, Mátyás, Tosatto, Silvio C. E., Gibson, Toby James, Dosztanyi, Zsuzsanna, Marino, Cristina Ester
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2023
País:Argentina
Institución:Consejo Nacional de Investigaciones Científicas y Técnicas
Repositorio:CONICET Digital (CONICET)
Idioma:inglés
OAI Identifier:oai:ri.conicet.gov.ar:11336/228717
Acceso en línea:http://hdl.handle.net/11336/228717
Access Level:acceso abierto
Palabra clave:ANNOTATION
DISPROT
HOMOLOGY TRANSFER
INTRINSICALLY DISORDERED PROTEINS
MULTIPLE SEQUENCE ALIGNMENT
ONTOLOGY TERMS
ORTHOLOGOUS PROTEINS
https://purl.org/becyt/ford/1.7
https://purl.org/becyt/ford/1
Descripción
Sumario:Background DisProt is the primary repository of Intrinsically Disordered Proteins (IDPs). This database is manually curated and the annotations there have strong experimental support. Currently, DisProt contains a relatively small number of proteins highlighting the importance of transferring annotations regarding verified disorder state and corresponding functions to homologous proteins in other species. In such a way, providing them with highly valuable information to better understand their biological roles. While the principles and practicalities of homology transfer are well-established for globular proteins, these are largely lacking for disordered proteins. Methods We used DisProt to evaluate the transferability of the annotation terms to orthologous proteins. For each protein, we looked for their orthologs, with the assumption that they will have a similar function. Then, for each protein and their orthologs we made multiple sequence alignments (MSAs). Disordered sequences are fast evolving and can be hard to align: Therefore we implemented alignment quality control steps ensuring robust alignments before mapping the annotations. Results We have designed a pipeline to obtain good quality MSAs and to transfer annotations from any protein to their orthologs. Applying the pipeline to DisProt proteins, from the 1,731 entries with 5,623 annotations we can reach 97,555 orthologs and transfer a total of 301,190 terms by homology. We also provide a web server for consulting the results of DisProt proteins and execute the pipeline for any other protein. The server Homology Transfer IDP (HoTIDP) is accessible at http://hotidp.leloir.org.ar.