AT1G04170.1 :

DomainDescriptionEvalueBitsGAStartEnd
G-alphaG-protein alpha subunit0.0025620.103068
GTP_EFTUElongation factor Tu GTP binding domain4.5E-278420.2033237
Dynamin_NDynamin family0.000191121.003665
MMR_HSR1GTPase of unknown function1.5E-061724.5036183
RsgA_GTPaseRsgA GTPase0.16130.003960
RsgA_GTPaseRsgA GTPase2.5E-051330.00142222
G-alphaG-protein alpha subunit0.024320.10174235
MMR_HSR1_XtnC-terminal region of MMR_HSR1 domain3.9E-051335.20177236
GTP_EFTU_D2Elongation factor Tu domain 27.5E-144121.20269351
eIF2_CInitiation factor eIF2 gamma, C terminal3.9E-3510922.00363452

 465

G-alpha
GTP_EFTU
Dynamin_N
MMR_HSR1
RsgA_GTPase
RsgA_GTPase
G-alpha
MMR_HSR1_Xtn
GTP_EFTU_D2
eIF2_C


References:

MMR_HSR1
8180467 Structure and evolution of a member of a new subfamily of GTP-binding proteins mapping to the human MHC class I region. Mamm Genome 1994;5:100-105.

Dynamin_N
8939066 Dynamin GTPase, a force-generating molecular switch. Bioessays 1996;18:885-893.
2144893 Molecular cloning of the microtubule-associated mechanochemical enzyme dynamin reveals homology with a new family of GTP-binding proteins. Nature 1990;347:256-261.

GTP_EFTU_D2
7491491 Crystal structure of the ternary complex of Phe-tRNAPhe, EF-Tu, and a GTP analog. Science 1995;270:1464-1472.

GTP_EFTU
9311785 Visualization of elongation factor Tu on the Escherichia coli ribosome. Nature 1997;389:403-406.

G-alpha
8073283 Structures of active conformations of Gi alpha 1 and the mechanism of GTP hydrolysis. Science 1994;265:1405-1412.
8851656 How G proteins work: a continuing story. Trends Biochem Sci 1996;21:41-44.

RsgA_GTPase

eIF2_C
11927566 The large subunit of initiation factor aIF2 is a close structural homologue of elongation factors. EMBO J. 2002;21:1821-1832.

MMR_HSR1_Xtn