The PROSITE database consists of a large collection of biologically meaningful signatures that are described as patterns or profiles. Each signature is linked to a documentation that provides useful biological information on the protein family, domain or functional site identified by the signature. The PROSITE database is now complemented by a series of rules that can give more precise information about specific residues. During the last 2 years, the documentation and the ScanProsite web pages were redesigned to add more functionalities. The latest version of PROSITE (release 19.11 of September 27, 2005) contains 1329 patterns and 552 profile entries. Over the past 2 years more than 200 domains have been added, and now 52% of UniProtKB/Swiss-Prot entries (release 48.1 of September 27, 2005) have a cross-reference to a PROSITE entry. The database is accessible at http://www.expasy.org/prosite/.
Download full-text PDF |
Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1347426 | PMC |
| http://dx.doi.org/10.1093/nar/gkj063 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Bioinformatics Analysis and Spatiotemporal Distribution of the fliC Gene and Its Protein Isolated from Escherichia coli-Infected Patients in Eastern Algeria.
Malays J Med Sci
October 2024
Department of Applied Biology, Faculty of Nature and Life Sciences, Laboratory of Microbiology Engineering and Applications, Frère Mentouri Constantine 1 University, Ain El-Bey, Algeria.
Background: The locus in primarily encodes flagellar (H) antigens. Exploring sequence diversity will shed light on the mechanisms of bacterial pathogenicity. This study examined the presence of mutant strains of in infected patients from different age groups, sexes and sample types in eastern Algerian provinces over a span of 2 years.
View Article and Find Full Text PDFCOLLAPSE: A representation learning framework for identification and characterization of protein structural sites.
Protein Sci
February 2023
Department of Biomedical Data Science, Stanford University, Stanford, California, USA.
The identification and characterization of the structural sites which contribute to protein function are crucial for understanding biological mechanisms, evaluating disease risk, and developing targeted therapies. However, the quantity of known protein structures is rapidly outpacing our ability to functionally annotate them. Existing methods for function prediction either do not operate on local sites, suffer from high false positive or false negative rates, or require large site-specific training datasets, necessitating the development of new computational methods for annotating functional sites at scale.
View Article and Find Full Text PDFThe limitations of the current protein classification tools in identifying lipolytic features in putative bacterial lipase sequences.
J Biotechnol
June 2022
School of Engineering, Newcastle University, Newcastle-upon-Tyne NE1 7RU, UK. Electronic address:
Metagenomics sequencing has generated millions of new protein sequences, most of them with unknown functions. A relatively quick first step for function assignment is to use the existing public protein databases and their scanning tools. However, to date these tools are not able to identify all sequence features like conserved motifs or patterns.
View Article and Find Full Text PDFIdentification of the most damaging nsSNPs in the human CFL1 gene and their functional and structural impacts on cofilin-1 protein.
Gene
April 2022
Department of Pharmacy, BGC Trust University Bangladesh, Chittagong 4381, Bangladesh. Electronic address:
The cofilin-1 protein, encoded by CFL1, is an actin-binding protein that regulates F-actin depolymerization and nucleation activity through phosphorylation and dephosphorylation. CFL1 has been implicated in the development of neurodegenerative diseases (Alzheimer's disease and Huntington's disease), neuronal migration disorders (lissencephaly, epilepsy, and schizophrenia), and neural tube closure defects. Mutations in CFL1 have been associated with impaired neural crest cell migration and neural tube closure defects.
View Article and Find Full Text PDFProNAB: database for binding affinities of protein-nucleic acid complexes and their mutants.
Nucleic Acids Res
January 2022
Department of Biotechnology, Bhupat and Jyoti Mehta School of Biosciences, Indian Institute of Technology Madras, Chennai 600036, India.
Protein-nucleic acid interactions are involved in various biological processes such as gene expression, replication, transcription, translation and packaging. The binding affinities of protein-DNA and protein-RNA complexes are important for elucidating the mechanism of protein-nucleic acid recognition. Although experimental data on binding affinity are reported abundantly in the literature, no well-curated database is currently available for protein-nucleic acid binding affinity.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!