scholarly journals Hydrophobic-cluster analysis of plant protein sequences. A domain homology between storage and lipid-transfer proteins

1988 ◽  
Vol 255 (3) ◽  
pp. 901-905 ◽  
Author(s):  
B Henrissat ◽  
Y Popineau ◽  
J C Kader

Hydrophobic-cluster analysis was used to characterize a conserved domain located near the C-terminal amino acid sequence of wheat (Triticum aestivum) storage proteins. This domain was transformed into a linear template for a global search for similarities in over 5200 protein sequences. In addition to proteins that had already been found to exhibit homology to wheat storage proteins, a previously unreported homology was found with non-specific lipid-transfer proteins from castor bean (Ricinus communis) and from spinach (Spinacia oleracea) leaf. Hydrophobic-cluster analysis of various members of the present protein group clearly shows a typical domain structure where (i) variable and conserved domains are located along the sequence at precise positions, (ii) the conserved domains probably reflect a common ancestor, and (iii) the unique properties of a given protein (chain cut into subunits, repetitive domains, trypsin-inhibitor active site) are associated with the variable domains.

Biochimie ◽  
1990 ◽  
Vol 72 (8) ◽  
pp. 555-574 ◽  
Author(s):  
L. Lemesle-Varloot ◽  
B. Henrissat ◽  
C. Gaboriaud ◽  
V. Bissery ◽  
A. Morgat ◽  
...  

PROTEOMICS ◽  
2018 ◽  
Vol 18 (21-22) ◽  
pp. 1800054 ◽  
Author(s):  
Tristan Bitard-Feildel ◽  
Alexis Lamiable ◽  
Jean-Paul Mornon ◽  
Isabelle Callebaut

1995 ◽  
pp. 129-144
Author(s):  
Michel T. Semertzidis ◽  
Etienne Thoreau ◽  
Anne Tasso ◽  
Bernard Henrissat ◽  
Isabelle Callebaut ◽  
...  

2018 ◽  
Author(s):  
Tristan Bitard-Feildel ◽  
Isabelle Callebaut

AbstractMotivation: Detecting protein domains sharing no similarity to known domains, as stored in domain databases, is a challenging problem, particularly for unannotated proteomes, domains emerged recently, fast diverging proteins or domains with intrinsically disordered regions.Results: We developed pyHCA and HCAtk, a python API and standalone tool gathering together improved versions of previously developed methodologies, with new functionalities. The developed tools can be either used from command line or from a python API.Availability: HCAtk and pyHCA are available at https://github.com/T-B-F/pyHCA under the CeCILL-C license.


1993 ◽  
Vol 9 (1) ◽  
pp. 37-44 ◽  
Author(s):  
L. Lemesle-Varloot ◽  
C. Gaboriaud ◽  
A. Morgat ◽  
G. Pantel ◽  
J. P. Mornon ◽  
...  

2000 ◽  
Vol 347 (3) ◽  
pp. 741-747 ◽  
Author(s):  
Isabelle MOUYNA ◽  
Michel MONOD ◽  
Thierry FONTAINE ◽  
Bernard HENRISSAT ◽  
Barbara LÉCHENNE ◽  
...  

A new family of glycosylphosphatidylinositol-anchored β(1-3)glucanosyltransferases (Gelp), recently identified and characterized in the filamentous fungus Aspergillus fumigatus, showed functional similarity to the Gas/Phr/Epd protein families, which are involved in yeast morphogenesis. Sequence comparisons and hydrophobic cluster analysis (HCA) showed that all the Gas/Phr/Epd/Gel proteins belong to a new family of glycosylhydrolases, family 72. We confirmed by site-directed mutagenesis and biochemical analysis that the two conserved glutamate residues (the putative catalytic residues of this family, as determined by HCA) are involved in the active site of this family of glycosylhydrolases.


1997 ◽  
Vol 235 (1) ◽  
pp. 103-107 ◽  
Author(s):  
Isabelle Callebaut ◽  
Jean-Claude Courvalin ◽  
Howard J. Worman ◽  
Jean-Paul Mornon

Sign in / Sign up

Export Citation Format

Share Document