AT1G22300.1 :

DomainDescriptionEvalueBitsGAStartEnd
DUF4710Domain of unknown function (DUF4710)0.12127.00564
Sec8_exocystSec8 exocyst complex component specific domain0.0075525.50834
TPR_8Tetratricopeptide repeat0.00053925.701135
14-3-314-3-3 protein034920.7011233
ProtoglobinProtoglobin0.0013720.301242
Sec8_exocystSec8 exocyst complex component specific domain0.014425.5071100
ProtoglobinProtoglobin0.0082520.3076162
Ca_bind_SSO6904Calcium binding protein SSO69045.8E-051225.0076124
TPR_8Tetratricopeptide repeat0.45025.70147158
Sec8_exocystSec8 exocyst complex component specific domain0.068225.50195224

 254

DUF4710
Sec8_exocyst
TPR_8
14-3-3
Protoglobin
Sec8_exocyst
Protoglobin
Ca_bind_SSO6904
TPR_8
Sec8_exocyst


References:

DUF4710

Sec8_exocyst
8978675 The Exocyst is a multiprotein complex required for exocytosis in Saccharomyces cerevisiae. EMBO J 1996;15:6483-6494.

Ca_bind_SSO6904

14-3-3
7603573 Structure of a 14-3-3 protein and implications for coordination of multiple signalling pathways. Nature 1995;376:188-191.
7603574 Crystal structure of the zeta isoform of the 14-3-3 protein. Nature 1995;376:191-194.
8601312 Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine. Cell 1996;84:889-897.
9280296 The 14-3-3 protein binds its target proteins with a common site located towards the C-terminus. FEBS Lett 1997;413:273-276.
8798343 Molecular evolution of the 14-3-3 protein family. J Mol Evol 1996;43:384-398.
8684458 Function of 14-3-3 proteins. Nature 1996;382:308-308.
12184815 The 14-3-3s. Genome Biol 2002;3:REVIEWS3010.

Protoglobin
18188182 Archaeal protoglobin structure indicates new ligand diffusion paths and modulation of haem-reactivity. EMBO Rep. 2008;9:157-163.

TPR_8