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Links from Protein

Items: 1 to 20 of 29

1.

Elongation factor Tu domain 4

Elongation factor Tu consists of several structural domains, and this is usually the fourth. (from Pfam)

Date:
2023-12-12
Family Accession:
NF025929.4
Method:
HMM
2.

Translation-initiation factor 2

IF-2 is a translation initiator in each of the three main phylogenetic domains (Eukaryotes [1], Bacteria [2] and Archaea [3]). IF2 interacts with formylmethionine-tRNA, GTP, IF1, IF3 and both ribosomal subunits [2]. Through these interactions, IF2 promotes the binding of the initiator tRNA to the A site in the smaller ribosomal subunit and catalyses the hydrolysis of GTP following initiation-complex formation [2]. [1]. 17086204. Global trends of whole-genome duplications revealed by the. ciliate Paramecium tetraurelia.. Aury JM, Jaillon O, Duret L, Noel B, Jubin C, Porcel BM,. Segurens B, Daubin V, Anthouard V, Aiach N, Arnaiz O, Billaut A,. Beisson J, Blanc I, Bouhouche K, Camara F, Duharcourt S, Guigo. R, Gogendeau D, Katinka M, Keller AM, Kissmehl R, Klotz C, Koll. F, Le. Nature. 2006;444:171-178.. [2]. 10878130. Investigation of the translation-initiation factor IF2 gene,. infB, as a tool to study the population structure of. Streptococcus agalactiae.. Hedegaard J, Hauge M, Fage-Larsen J, Mortensen KK, Kilian M,. Sperling-Petersen HU, Poulsen K;. Microbiology. 2000;146:1661-1670.. [3]. 16169924. Living with two extremes: conclusions from the genome sequence. of Natronomonas pharaonis.. Falb M, Pfeiffer F, Palm P, Rodewald K, Hickmann V, Tittor J,. Oesterhelt D;. Genome Res. 2005;15:1336-1343. (from Pfam)

Date:
2024-04-03
Family Accession:
NF023413.4
Method:
HMM
3.

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:
2024-04-03
Family Accession:
NF015126.4
Method:
HMM
4.

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).

GO Terms:
Molecular Function:
GTP binding (GO:0005525)
Date:
2024-04-03
Family Accession:
NF014036.4
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:
2024-04-03
Family Accession:
NF012239.4
Method:
HMM
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.
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.

translation initiation factor IF-2 family protein

translation initiation factor IF-2 family protein similar to Aeropyrum pernix translation initiation factor 5B (IF5B), a universally conserved translational GTPase that catalyzes ribosomal subunit joining

Date:
2018-10-02
Family Accession:
11480101
Method:
Sparcle
17.
new record, indexing in progress
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18.
new record, indexing in progress
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19.
new record, indexing in progress
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20.
new record, indexing in progress
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