The Structure-Function Linkage Database
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Archivos
Fecha
2014-01-01
Profesor/a Guía
Facultad/escuela
Idioma
en
Título de la revista
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Título del volumen
Editor
Oxford University Press
Nombre de Curso
Licencia CC
CC BY-NC-ND 3.0
ATTRIBUTION-NONCOMMERCIAL-NODERIVS 3.0 UNPORTED
Deed
Licencia CC
https://creativecommons.org/licenses/by-nc-nd/3.0/
Resumen
The Structure-Function Linkage Database (SFLD, http://sfld.rbvi.ucsf.edu/) is a manually curated classification resource describing structure-function relationships for functionally diverse enzyme superfamilies. Members of such superfamilies are diverse in their overall reactions yet share a common ancestor and some conserved active site features associated with conserved functional attributes such as a partial reaction. Thus, despite their different functions, members of these superfamilies 'look alike', making them easy to misannotate. To address this complexity and enable rational transfer of functional features to unknowns only for those members for which we have sufficient functional information, we subdivide superfamily members into subgroups using sequence information, and lastly into families, sets of enzymes known to catalyze the same reaction using the same mechanistic strategy. Browsing and searching options in the SFLD provide access to all of these levels. The SFLD offers manually curated as well as automatically classified superfamily sets, both accompanied by search and download options for all hierarchical levels. Additional information includes multiple sequence alignments, tab-separated files of functional and other attributes, and sequence similarity networks. The latter provide a new and intuitively powerful way to visualize functional trends mapped to the context of sequence similarity. © 2013 The Author(s). Published by Oxford University Press.
Notas
INDEXACIÓN: SCOPUS.
Palabras clave
Databases, Protein, Enzymes, Internet, Molecular Sequence Annotation, Sequence Alignment, Structure-Activity Relationship
Citación
Nucleic Acids Research, Volume 42, Issue D1, Pages D521-D530, 1 January 2014
DOI
10.1093/nar/gkt1130