AT1G18070.1 :

DomainDescriptionEvalueBitsGAStartEnd
G-alphaG-protein alpha subunit1.2E-051320.1090135
GTP_EFTUElongation factor Tu GTP binding domain014820.2099312
MMR_HSR1GTPase of unknown function1.3E-061724.50103248
G-alphaG-protein alpha subunit0.11020.10164191
GTP_EFTU_D4Elongation factor Tu domain 40.68-158.00187211
GTP_EFTU_D4Elongation factor Tu domain 40.000261058.00340397
GTP_EFTU_D2Elongation factor Tu domain 23.3E-123621.20343409
GTP_EFTU_D3Elongation factor Tu C-terminal domain9.1E-309221.30416525

 532

G-alpha
GTP_EFTU
MMR_HSR1
G-alpha
GTP_EFTU_D4
GTP_EFTU_D4
GTP_EFTU_D2
GTP_EFTU_D3


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.

GTP_EFTU_D3
7491491 Crystal structure of the ternary complex of Phe-tRNAPhe, EF-Tu, and a GTP analog. Science 1995;270:1464-1472.
9253415 Crystal structure of the EF-Tu.EF-Ts complex from Thermus thermophilus. Nat Struct Biol 1997;4:650-656.

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.

GTP_EFTU_D4