Protein Family Models for Protein (Select 496082539) - Protein Family Models

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Select item 4142721.

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Select item 4141802.

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Select item 4110743.

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Family Accession:

Select item 3925154.

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)

GO Terms:

Molecular Function:: GTP binding (GO:0005525)

Date:: 2024-07-10

Family Accession:: NF015126.4
Method:: HMM

Select item 3904425.

Elongation factor Tu C-terminal domain

Elongation factor Tu consists of three structural domains, this is the third domain. This domain adopts a beta barrel structure. This the third domain is involved in binding to both charged tRNA [1] and binding to EF-Ts Pfam:PF00889 [2]. [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.. [2]. 9253415. Crystal structure of the EF-Tu.EF-Ts complex from Thermus. thermophilus.. Wang Y, Jiang Y, Meyering-Voss M, Sprinzl M, Sigler PB;. Nat Struct Biol 1997;4:650-656. (from Pfam)

Date:: 2024-07-10

Family Accession:: NF015125.4
Method:: HMM

Select item 3886026.

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)

GO Terms:

Molecular Function:: GTPase activity (GO:0003924)

Molecular Function:: GTP binding (GO:0005525)

Date:: 2024-07-09

Family Accession:: NF012239.4
Method:: HMM

Select item 3504127.

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Select item 3494968.

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Family Accession:

Select item 3481609.

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Family Accession:

Select item 31830610.

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Select item 31821511.

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Select item 31580012.

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Select item 15039813.

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Select item 15039714.

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Select item 15009815.

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Family Accession:

Select item 15009716.

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Select item 14120417.

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Family Accession:

Select item 14098118.

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Family Accession:

Select item 5946019.

elongation factor Tu

elongation factor Tu promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis

Date:: 2023-03-08

Family Accession:: 11477830
Method:: Sparcle

Select item 3031020.

elongation factor Tu

EF-Tu; promotes GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis; when the tRNA anticodon matches the mRNA codon, GTP hydrolysis results; the inactive EF-Tu-GDP leaves the ribosome and release of GDP is promoted by elongation factor Ts

Date:: 2020-10-26

Family Accession:: NF009373.0
Method:: HMM

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