Department of Biochemistry, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390, USA.
Bioinformatics. 2010 Jun 15;26(12):1564-5. doi: 10.1093/bioinformatics/btq208. Epub 2010 Apr 22.
Profile-based similarity search is an essential step in structure-function studies of proteins. However, inclusion of non-homologous sequence segments into a profile causes its corruption and results in false positives. Profile corruption is common in multidomain proteins, and single domains with long insertions are a significant source of errors. We developed a procedure (HangOut) that, for a single domain with specified insertion position, cleans erroneously extended PSI-BLAST alignments to generate better profiles.
HangOut is implemented in Python 2.3 and runs on all Unix-compatible platforms. The source code is available under the GNU GPL license at http://prodata.swmed.edu/HangOut/.
Supplementary data are available at Bioinformatics online.
基于轮廓的相似性搜索是蛋白质结构-功能研究的重要步骤。然而,将非同源序列段包含到轮廓中会导致其损坏,并导致假阳性。轮廓损坏在多域蛋白中很常见,具有长插入片段的单个域是错误的重要来源。我们开发了一种程序(HangOut),对于具有指定插入位置的单个域,它可以清理错误扩展的 PSI-BLAST 比对,以生成更好的轮廓。
HangOut 是用 Python 2.3 实现的,可在所有与 Unix 兼容的平台上运行。源代码可在 GNU GPL 许可证下从 http://prodata.swmed.edu/HangOut/ 获取。
补充数据可在 Bioinformatics 在线获取。