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InterPro (The Integrated Resource of Protein Domains and Functional Sites)

The family and motif databases, PROSITE, PRINTS, Pfam and ProDom, have been integrated into a powerful resource for protein secondary annotation. As of June 2000, InterPro had processed 384 572 proteins in SWISS-PROT and TrEMBL. Because the contributing databases have different clustering principles...

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Detalles Bibliográficos
Autor principal: Southan, Christopher
Formato: Texto
Lenguaje:English
Publicado: Hindawi Publishing Corporation 2000
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2448387/
https://www.ncbi.nlm.nih.gov/pubmed/11119311
http://dx.doi.org/10.1002/1097-0061(200012)17:4<327::AID-YEA45>3.0.CO;2-K
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author Southan, Christopher
author_facet Southan, Christopher
author_sort Southan, Christopher
collection PubMed
description The family and motif databases, PROSITE, PRINTS, Pfam and ProDom, have been integrated into a powerful resource for protein secondary annotation. As of June 2000, InterPro had processed 384 572 proteins in SWISS-PROT and TrEMBL. Because the contributing databases have different clustering principles and scoring sensitivities, the combined assignments compliment each other for grouping protein families and delineating domains. The graphic displays of all matches above the scoring thresholds enables judgements to be made on the concordances or differences between the assignments. The website links can be used to analyse novel sequences and for queries across the proteomes of 32 organisms, including the partial human set, by domain and/or protein family. An analysis of selected HtrA/DegQ proteases demonstrates the utility of this website for detailed comparative genomics. Further information on the project can be found at the European Bioinformatics Institute at http://www.ebi.ac.uk/interpro/.
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spelling pubmed-24483872008-07-14 InterPro (The Integrated Resource of Protein Domains and Functional Sites) Southan, Christopher Yeast Research Article The family and motif databases, PROSITE, PRINTS, Pfam and ProDom, have been integrated into a powerful resource for protein secondary annotation. As of June 2000, InterPro had processed 384 572 proteins in SWISS-PROT and TrEMBL. Because the contributing databases have different clustering principles and scoring sensitivities, the combined assignments compliment each other for grouping protein families and delineating domains. The graphic displays of all matches above the scoring thresholds enables judgements to be made on the concordances or differences between the assignments. The website links can be used to analyse novel sequences and for queries across the proteomes of 32 organisms, including the partial human set, by domain and/or protein family. An analysis of selected HtrA/DegQ proteases demonstrates the utility of this website for detailed comparative genomics. Further information on the project can be found at the European Bioinformatics Institute at http://www.ebi.ac.uk/interpro/. Hindawi Publishing Corporation 2000 /pmc/articles/PMC2448387/ /pubmed/11119311 http://dx.doi.org/10.1002/1097-0061(200012)17:4<327::AID-YEA45>3.0.CO;2-K Text en Copyright © 2000 Hindawi Publishing Corporation. http://creativecommons.org/licenses/by/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Southan, Christopher
InterPro (The Integrated Resource of Protein Domains and Functional Sites)
title InterPro (The Integrated Resource of Protein Domains and Functional Sites)
title_full InterPro (The Integrated Resource of Protein Domains and Functional Sites)
title_fullStr InterPro (The Integrated Resource of Protein Domains and Functional Sites)
title_full_unstemmed InterPro (The Integrated Resource of Protein Domains and Functional Sites)
title_short InterPro (The Integrated Resource of Protein Domains and Functional Sites)
title_sort interpro (the integrated resource of protein domains and functional sites)
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2448387/
https://www.ncbi.nlm.nih.gov/pubmed/11119311
http://dx.doi.org/10.1002/1097-0061(200012)17:4<327::AID-YEA45>3.0.CO;2-K
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