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Items: 1 to 20 of 21

1.

Elongation factor G domain 2

Date:
2024-08-14

Family Accession:
NF046178.1
Method:
HMM

2.

Elongation Factor G, domain III

This domain is found in Elongation Factor G. It shares a similar structure with domain V (Pfam:PF00679). Structural studies in drosophila indicate this is domain 3 [1]. [1]. 23636399. Structures of the human and Drosophila 80S ribosome.. Anger AM, Armache JP, Berninghausen O, Habeck M, Subklewe M,. Wilson DN, Beckmann R;. Nature. 2013;497:80-85. (from Pfam)

Date:
2024-08-14

Family Accession:
NF025845.5
Method:
HMM

3.

Elongation factor G, domain IV

This domain is found in elongation factor G, elongation factor 2 and some tetracycline resistance proteins and adopts a ribosomal protein S5 domain 2-like fold. (from Pfam)

GO Terms:
Molecular Function:
translation elongation factor activity (GO:0003746)
Molecular Function:
GTP binding (GO:0005525)
Date:
2024-08-14

Family Accession:
NF015706.5
Method:
HMM

4.

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:
2024-08-14

Family Accession:
NF015126.5
Method:
HMM

5.

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:
2024-08-14

Family Accession:
NF012239.5
Method:
HMM

6.

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)

Date:
2024-08-14

Family Accession:
NF012882.5
Method:
HMM

7.
new record, indexing in progress
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8.
new record, indexing in progress
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9.
new record, indexing in progress
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10.
new record, indexing in progress
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11.
new record, indexing in progress
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12.
new record, indexing in progress
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13.
new record, indexing in progress
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14.
new record, indexing in progress
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15.
new record, indexing in progress
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16.
new record, indexing in progress
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17.

elongation factor G

elongation factor G catalyzes the translocation step of protein synthesis in bacteria and mitochondria

Date:
2024-04-25

Family Accession:
11422284
Method:
Sparcle

18.

elongation factor G

Gene:
fusA
Date:
2021-05-06

Family Accession:
NF009381.0
Method:
HMM

19.

elongation factor G

GO Terms:
Molecular Function:
GTPase activity (GO:0003924)
Molecular Function:
GTP binding (GO:0005525)
Date:
2021-09-20

Family Accession:
NF009379.0
Method:
HMM

20.

elongation factor G

After peptide bond formation, this elongation factor of bacteria and organelles catalyzes the translocation of the tRNA-mRNA complex, with its attached nascent polypeptide chain, from the A-site to the P-site of the ribosome. Every completed bacterial genome has at least one copy, but some species have additional EF-G-like proteins.

Gene:
fusA
GO Terms:
Molecular Function:
translation elongation factor activity (GO:0003746)
Molecular Function:
GTP binding (GO:0005525)
Biological Process:
translational elongation (GO:0006414)
Date:
2024-05-30

Family Accession:
TIGR00484.1
Method:
HMM

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