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TypA/BipA C-terminal domain
Elongation factor G domain 2
EF-Tu/IF-2/RF-3 family GTPase
Elongation factor Tu consists of three structural domains, this is the second domain. This domain adopts a beta barrel structure. This the second domain is involved in binding to charged tRNA [1]. This domain is also found in other proteins such as elongation factor G and translation initiation factor IF-2. This domain is structurally related to Pfam:PF03143, and in fact has weak sequence matches to this domain. [1]. 7491491. Crystal structure of the ternary complex of Phe-tRNAPhe, EF-Tu,. and a GTP analog.. Nissen P, Kjeldgaard M, Thirup S, Polekhina G, Reshetnikova L,. Clark BF, Nyborg J;. Science 1995;270:1464-1472. (from Pfam)
GTPase
This HMM identifies the P-loop-containing domain of large numbers of GTPases with ribosome-associated functions, including many involved in ribosome maturation (Der, Era, etc), ribosome rescue (HflX), and protein translation (InfB, Tuf, PrfC).
GTP-binding protein
This domain contains a P-loop motif, also found in several other families such as Pfam:PF00071, Pfam:PF00025 and Pfam:PF00063. Elongation factor Tu consists of three structural domains, this plus two C-terminal beta barrel domains. Cryoelectron microscopy structure.. [1]. 9311785. Visualization of elongation factor Tu on the Escherichia coli. ribosome.. Stark H, Rodnina MV, Rinke-Appel J, Brimacombe R, Wintermeyer W,. van Heel M;. Nature 1997;389:403-406. (from Pfam)
Elongation factor G C-terminus
This domain includes the carboxyl terminal regions of Elongation factor G, elongation factor 2 and some tetracycline resistance proteins and adopt a ferredoxin-like fold. (from Pfam)
translational GTPase TypA
This bacterial (and Arabidopsis) protein, termed TypA or BipA, a GTP-binding protein, is phosphorylated on a tyrosine residue under some cellular conditions. Mutants show altered regulation of some pathways, but the precise function is unknown.
GTP-binding protein TypA/BipA
GTP-binding protein TypA/BipA such as the large ribosomal subunit assembly factor BipA, a 50S ribosomal subunit assembly protein with GTPase and nucleotide-independent chaperone activity, required for 50S subunit assembly at low temperatures, which may also play a role in translation
Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once. This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model.
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