AT1G07920.1 :

DomainDescriptionEvalueBitsGAStartEnd
GTP_EFTUElongation factor Tu GTP binding domain018020.207222
MMR_HSR1GTPase of unknown function1.2E-061824.509124
SRPRBSignal recognition particle receptor beta subunit0.22020.50928
AAA_22AAA domain0.000121127.0010117
SRPRBSignal recognition particle receptor beta subunit9.6E-051120.5083175
GTP_EFTU_D2Elongation factor Tu domain 26E-175121.20248313
GTP_EFTU_D4Elongation factor Tu domain 41E-051458.00252304
GTP_EFTU_D3Elongation factor Tu C-terminal domain7.6E-3410521.30322429

 449

GTP_EFTU
MMR_HSR1
SRPRB
AAA_22
SRPRB
GTP_EFTU_D2
GTP_EFTU_D4
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.

GTP_EFTU_D4

SRPRB
7844142 The beta subunit of the signal recognition particle receptor is a transmembrane GTPase that anchors the alpha subunit, a peripheral membrane GTPase, to the endoplasmic reticulum membrane. J Cell Biol. 1995;128:273-282.

AAA_22