BYKdb: the Bacterial protein tYrosine Kinase database

Bacterial tyrosine-kinases share no resemblance with their eukaryotic counterparts and they have been unified in a new protein family named BY-kinases. These enzymes have been shown to control several biological functions in the bacterial cells. In recent years biochemical studies, sequence analyses and structure resolutions allowed the deciphering of a common signature. However, BY-kinase sequence annotations in primary databases remain incomplete. This prompted us to develop a specialized database of computer-annotated BY-kinase sequences: the Bacterial protein tyrosine-kinase database (BYKdb). BY-kinase sequences are first identified, thanks to a workflow developed in a previous work. A second workflow annotates the UniProtKB entries in order to provide the BYKdb entries. The database can be accessed through a web interface that allows static and dynamic queries and offers integrated sequence analysis tools. BYKdb can be found at http://bykdb.ibcp.fr.

• Publication year

  2011

• Venue

  Nucleic Acids Res.

• Publication date

  2011-11-12

• Fields of study

  Biology, Medicine, Computer Science

• Identifiers
  DOI 10.1093/nar/gkr915PMID 22080550PMCID 3245071
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• Ongoing and future developments at the Universal Protein Resource

  2010cited by this paper
• Tyrosine phosphorylation: an emerging regulatory device of bacterial physiology.

  2007cited by this paper
• Pfam: clans, web tools and services

  2005cited by this paper
• NPS@: network protein sequence analysis.

  2000cited by this paper
• No longer an exclusive club: eukaryotic signalling domains in bacteria.

  2000cited by this paper
• Profile hidden Markov models

  1998cited by this paper
• Protein phosphorylation in chemotaxis and two-component regulatory systems of bacteria.

  1989cited by this paper
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  1988cited by this paper
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