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Updated: Jul 2, 2025
11:23
Characterization at the Molecular Level using Robust Biochemical Approaches of a New Kinase Protein
Published on: June 30, 2019
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KINtaro: protein kinase-like database
Bartosz Baranowski1, Marianna Krysińska2, Marcin Gradowski3
1Laboratory of Plant Pathogenesis, Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw, Poland.
BMC Research Notes
|February 16, 2024
Summary
The KINtaro database consolidates information on Protein Kinase-like (PKL) protein families, including novel ones. This resource aids researchers in understanding PKL proteins
Area of Science:
- Biochemistry
- Structural Biology
- Bioinformatics
Background:
- Protein Kinase-like (PKL) proteins share a common 3D fold and exhibit diverse enzymatic activities beyond phosphorylation.
- PKL proteins are crucial in biological processes, including pathogen survival and human diseases like cancer and neurological disorders.
- The expanding superfamily of PKL proteins necessitates continuous information gathering.
Purpose of the Study:
- To establish a centralized resource for collecting and disseminating information on PKL protein families.
- To provide comprehensive data on PKL families, including those not currently recognized in established databases.
Main Methods:
- Development of the KINtaro database (http://bioinfo.sggw.edu.pl/kintaro/).
- Integration of protein sequence data with extensive annotations for over 70 PKL families.
- Inclusion of 32 novel PKL families absent from existing domain databases.
Main Results:
- KINtaro offers a searchable platform for PKL protein information.
- The database provides access to family descriptions, sequences, alignments, HMM models, and 3D structures.
- Annotated experimental structures and sequence logos with catalytic residues are available.
Conclusions:
- KINtaro serves as a valuable resource for researchers studying the diverse PKL protein superfamily.
- The database facilitates the exploration of PKL protein functions and evolutionary relationships.
- KINtaro supports ongoing research into PKL proteins' roles in health and disease.
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