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PASS2 database for the structure-based sequence alignment of distantly related SCOP domain superfamilies: update to version 5 and added features
Structure-based sequence alignment is an essential step in assessing and analysing the relationship of distantly related proteins. PASS2 is a database that records such alignments for protein domain superfamilies and has been constantly updated periodically. This update of the PASS2 version, named a...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4702857/ https://www.ncbi.nlm.nih.gov/pubmed/26553811 http://dx.doi.org/10.1093/nar/gkv1205 |
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author | Gandhimathi, Arumugam Ghosh, Pritha Hariharaputran, Sridhar Mathew, Oommen K. Sowdhamini, R. |
author_facet | Gandhimathi, Arumugam Ghosh, Pritha Hariharaputran, Sridhar Mathew, Oommen K. Sowdhamini, R. |
author_sort | Gandhimathi, Arumugam |
collection | PubMed |
description | Structure-based sequence alignment is an essential step in assessing and analysing the relationship of distantly related proteins. PASS2 is a database that records such alignments for protein domain superfamilies and has been constantly updated periodically. This update of the PASS2 version, named as PASS2.5, directly corresponds to the SCOPe 2.04 release. All SCOPe structural domains that share less than 40% sequence identity, as defined by the ASTRAL compendium of protein structures, are included. The current version includes 1977 superfamilies and has been assembled utilizing the structure-based sequence alignment protocol. Such an alignment is obtained initially through MATT, followed by a refinement through the COMPARER program. The JOY program has been used for structural annotations of such alignments. In this update, we have automated the protocol and focused on inclusion of new features such as mapping of GO terms, absolutely conserved residues among the domains in a superfamily and inclusion of PDBs, that are absent in SCOPe 2.04, using the HMM profiles from the alignments of the superfamily members and are provided as a separate list. We have also implemented a more user-friendly manner of data presentation and options for downloading more features. PASS2.5 version is available at http://caps.ncbs.res.in/pass2/. |
format | Online Article Text |
id | pubmed-4702857 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-47028572016-01-07 PASS2 database for the structure-based sequence alignment of distantly related SCOP domain superfamilies: update to version 5 and added features Gandhimathi, Arumugam Ghosh, Pritha Hariharaputran, Sridhar Mathew, Oommen K. Sowdhamini, R. Nucleic Acids Res Database Issue Structure-based sequence alignment is an essential step in assessing and analysing the relationship of distantly related proteins. PASS2 is a database that records such alignments for protein domain superfamilies and has been constantly updated periodically. This update of the PASS2 version, named as PASS2.5, directly corresponds to the SCOPe 2.04 release. All SCOPe structural domains that share less than 40% sequence identity, as defined by the ASTRAL compendium of protein structures, are included. The current version includes 1977 superfamilies and has been assembled utilizing the structure-based sequence alignment protocol. Such an alignment is obtained initially through MATT, followed by a refinement through the COMPARER program. The JOY program has been used for structural annotations of such alignments. In this update, we have automated the protocol and focused on inclusion of new features such as mapping of GO terms, absolutely conserved residues among the domains in a superfamily and inclusion of PDBs, that are absent in SCOPe 2.04, using the HMM profiles from the alignments of the superfamily members and are provided as a separate list. We have also implemented a more user-friendly manner of data presentation and options for downloading more features. PASS2.5 version is available at http://caps.ncbs.res.in/pass2/. Oxford University Press 2016-01-04 2015-11-08 /pmc/articles/PMC4702857/ /pubmed/26553811 http://dx.doi.org/10.1093/nar/gkv1205 Text en © The Author(s) 2015. Published by Oxford University Press on behalf of Nucleic Acids Research. http://creativecommons.org/licenses/by/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Database Issue Gandhimathi, Arumugam Ghosh, Pritha Hariharaputran, Sridhar Mathew, Oommen K. Sowdhamini, R. PASS2 database for the structure-based sequence alignment of distantly related SCOP domain superfamilies: update to version 5 and added features |
title | PASS2 database for the structure-based sequence alignment of distantly related SCOP domain superfamilies: update to version 5 and added features |
title_full | PASS2 database for the structure-based sequence alignment of distantly related SCOP domain superfamilies: update to version 5 and added features |
title_fullStr | PASS2 database for the structure-based sequence alignment of distantly related SCOP domain superfamilies: update to version 5 and added features |
title_full_unstemmed | PASS2 database for the structure-based sequence alignment of distantly related SCOP domain superfamilies: update to version 5 and added features |
title_short | PASS2 database for the structure-based sequence alignment of distantly related SCOP domain superfamilies: update to version 5 and added features |
title_sort | pass2 database for the structure-based sequence alignment of distantly related scop domain superfamilies: update to version 5 and added features |
topic | Database Issue |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4702857/ https://www.ncbi.nlm.nih.gov/pubmed/26553811 http://dx.doi.org/10.1093/nar/gkv1205 |
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