Diversity in domain architectures of Ser/Thr kinases and their homologues in prokaryotes.

ABSTRACT:

Background

Ser/Thr/Tyr kinases (STYKs) commonly found in eukaryotes have been recently reported in many bacterial species. Recent studies elucidating their cellular functions have established their roles in bacterial growth and development. However functions of a large number of bacterial STYKs still remain elusive. The organisation of domains in a large dataset of bacterial STYKs has been investigated here in order to recognise variety in domain combinations which determine functions of bacterial STYKs.

Results

Using sensitive sequence and profile search methods, domain organisation of over 600 STYKs from 125 prokaryotic genomes have been examined. Kinase catalytic domains of STYKs tethered to a wide range of enzymatic domains such as phosphatases, HSP70, peptidyl prolyl is

SUBMITTER: Krupa A 

PROVIDER: S-EPMC1262709 | biostudies-literature | 2005 Sep

REPOSITORIES: biostudies-literature