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AGODB: a comprehensive domain annotation database of argonaute proteins

Argonaute (Ago) proteins are widely expressed in almost all organisms. Eukaryotic Ago (eAgo) proteins bind small RNA guides forming RNA-induced silencing complex that silence gene expression, and prokaryotic Ago (pAgo) proteins defend against invading nucleic acids via binding small RNAs or DNAs. pA...

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Autores principales: Li, Bowen, Yang, Shanshan, Long, Jinjin, Chen, Xue, Zhang, Qianyue, Ning, Lin, He, Bifang, Chen, Heng, Huang, Jian
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9448894/
https://www.ncbi.nlm.nih.gov/pubmed/36068786
http://dx.doi.org/10.1093/database/baac078
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author Li, Bowen
Yang, Shanshan
Long, Jinjin
Chen, Xue
Zhang, Qianyue
Ning, Lin
He, Bifang
Chen, Heng
Huang, Jian
author_facet Li, Bowen
Yang, Shanshan
Long, Jinjin
Chen, Xue
Zhang, Qianyue
Ning, Lin
He, Bifang
Chen, Heng
Huang, Jian
author_sort Li, Bowen
collection PubMed
description Argonaute (Ago) proteins are widely expressed in almost all organisms. Eukaryotic Ago (eAgo) proteins bind small RNA guides forming RNA-induced silencing complex that silence gene expression, and prokaryotic Ago (pAgo) proteins defend against invading nucleic acids via binding small RNAs or DNAs. pAgo proteins have shown great potential as a candidate ‘scissors’ for gene editing. Protein domains are fundamental units of protein structure, function and evolution; however, the domains of Ago proteins are not well annotated/curated currently. Therefore, full functional domain annotation of Ago proteins is urgently needed for researchers to understand the function and mechanism of Ago proteins. Herein, we constructed the first comprehensive domain annotation database of Ago proteins (AGODB). The database curates detailed information of 1902 Ago proteins, including 1095 eAgos and 807 pAgos. Especially for long pAgo proteins, all six domains are annotated and curated. Gene Ontology (GO) enrichment analysis revealed that Ago genes in different species were enriched in the following GO terms: biological processes (BPs), molecular function and cellular compartment. GO enrichment analysis results were integrated into AGODB, which provided insights into the BP that Ago genes may participate in. AGODB also allows users to search the database with a variety of options and download the search results. We believe that the AGODB will be a useful resource for understanding the function and domain components of Ago proteins. This database is expected to cater to the needs of scientific community dedicated to the research of Ago proteins. DATABASE URL: http://i.uestc.edu.cn/agodb/
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spelling pubmed-94488942022-09-08 AGODB: a comprehensive domain annotation database of argonaute proteins Li, Bowen Yang, Shanshan Long, Jinjin Chen, Xue Zhang, Qianyue Ning, Lin He, Bifang Chen, Heng Huang, Jian Database (Oxford) Original Article Argonaute (Ago) proteins are widely expressed in almost all organisms. Eukaryotic Ago (eAgo) proteins bind small RNA guides forming RNA-induced silencing complex that silence gene expression, and prokaryotic Ago (pAgo) proteins defend against invading nucleic acids via binding small RNAs or DNAs. pAgo proteins have shown great potential as a candidate ‘scissors’ for gene editing. Protein domains are fundamental units of protein structure, function and evolution; however, the domains of Ago proteins are not well annotated/curated currently. Therefore, full functional domain annotation of Ago proteins is urgently needed for researchers to understand the function and mechanism of Ago proteins. Herein, we constructed the first comprehensive domain annotation database of Ago proteins (AGODB). The database curates detailed information of 1902 Ago proteins, including 1095 eAgos and 807 pAgos. Especially for long pAgo proteins, all six domains are annotated and curated. Gene Ontology (GO) enrichment analysis revealed that Ago genes in different species were enriched in the following GO terms: biological processes (BPs), molecular function and cellular compartment. GO enrichment analysis results were integrated into AGODB, which provided insights into the BP that Ago genes may participate in. AGODB also allows users to search the database with a variety of options and download the search results. We believe that the AGODB will be a useful resource for understanding the function and domain components of Ago proteins. This database is expected to cater to the needs of scientific community dedicated to the research of Ago proteins. DATABASE URL: http://i.uestc.edu.cn/agodb/ Oxford University Press 2022-09-07 /pmc/articles/PMC9448894/ /pubmed/36068786 http://dx.doi.org/10.1093/database/baac078 Text en © The Author(s) 2022. Published by Oxford University Press. https://creativecommons.org/licenses/by-nc/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial License (https://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com
spellingShingle Original Article
Li, Bowen
Yang, Shanshan
Long, Jinjin
Chen, Xue
Zhang, Qianyue
Ning, Lin
He, Bifang
Chen, Heng
Huang, Jian
AGODB: a comprehensive domain annotation database of argonaute proteins
title AGODB: a comprehensive domain annotation database of argonaute proteins
title_full AGODB: a comprehensive domain annotation database of argonaute proteins
title_fullStr AGODB: a comprehensive domain annotation database of argonaute proteins
title_full_unstemmed AGODB: a comprehensive domain annotation database of argonaute proteins
title_short AGODB: a comprehensive domain annotation database of argonaute proteins
title_sort agodb: a comprehensive domain annotation database of argonaute proteins
topic Original Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9448894/
https://www.ncbi.nlm.nih.gov/pubmed/36068786
http://dx.doi.org/10.1093/database/baac078
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