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The unique evolution of the carbohydrate‐binding module CBM 20 in laforin
Author(s) -
Kuchtová Andrea,
Gentry Matthew S.,
Janeček Štefan
Publication year - 2018
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12994
Subject(s) - lafora disease , biology , progressive myoclonus epilepsy , in silico , phosphatase , biochemistry , genetics , gene , phosphorylation
Laforin catalyses glycogen dephosphorylation. Mutations in its gene result in Lafora disease, a fatal progressive myoclonus epilepsy, the hallmark being water‐insoluble, hyperphosphorylated carbohydrate inclusions called Lafora bodies. Human laforin consists of an N‐terminal carbohydrate‐binding module ( CBM ) from family CBM 20 and a C‐terminal dual‐specificity phosphatase domain. Laforin is conserved in all vertebrates, some basal metazoans and a small group of protozoans. The present in silico study defines the evolutionary relationships among the CBM 20s of laforin with an emphasis on newly identified laforin orthologues. The study reveals putative laforin orthologues in Trichinella , a parasitic nematode, and identifies two sequence inserts in the CBM 20 of laforin from parasitic coccidia. Finally, we identify that the putative laforin orthologues from some protozoa and algae possess more than one CBM 20.