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Links from Protein

Items: 10

1.

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:
2024-10-16

Family Accession:
NF015126.5
Method:
HMM

2.

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:
2024-10-16

Family Accession:
NF015125.5
Method:
HMM

3.

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:
2024-10-16

Family Accession:
NF012239.5
Method:
HMM

4.
new record, indexing in progress
Family Accession:
5.
new record, indexing in progress
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6.
new record, indexing in progress
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7.
new record, indexing in progress
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8.
new record, indexing in progress
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9.

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

GO Terms:
Molecular Function:
translation elongation factor activity (GO:0003746)
Molecular Function:
GTPase activity (GO:0003924)
Molecular Function:
GTP binding (GO:0005525)
Biological Process:
translational elongation (GO:0006414)
Date:
2022-01-26

Family Accession:
NF009372.0
Method:
HMM

10.

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:
NF000766.0
Method:
HMM

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