Summary: Elongation factor Tu C-terminal domain
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This is the Wikipedia entry entitled "EF-Tu". More...
EF-Tu Edit Wikipedia article
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This is the Wikipedia entry entitled "GTP-binding elongation factor family, EF-Tu/EF-1A subfamily". More...
GTP-binding elongation factor family, EF-Tu/EF-1A subfamily Edit Wikipedia article
Elongation factor Tu GTP binding domain | |||||||||
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![]() eif2gamma apo | |||||||||
Identifiers | |||||||||
Symbol | GTP_EFTU | ||||||||
Pfam | PF00009 | ||||||||
Pfam clan | CL0023 | ||||||||
InterPro | IPR000795 | ||||||||
PROSITE | PDOC00273 | ||||||||
SCOP2 | 1etu / SCOPe / SUPFAM | ||||||||
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Elongation factor Tu domain 2 | |||||||||
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![]() eif2gamma apo | |||||||||
Identifiers | |||||||||
Symbol | GTP_EFTU_D2 | ||||||||
Pfam | PF03144 | ||||||||
InterPro | IPR004161 | ||||||||
PROSITE | PDOC00273 | ||||||||
SCOP2 | 1etu / SCOPe / SUPFAM | ||||||||
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Elongation factor Tu C-terminal domain | |||||||||
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![]() whole, unmodified, ef-tu(elongation factor tu). | |||||||||
Identifiers | |||||||||
Symbol | GTP_EFTU_D3 | ||||||||
Pfam | PF03143 | ||||||||
InterPro | IPR004160 | ||||||||
SCOP2 | 1etu / SCOPe / SUPFAM | ||||||||
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In molecular biology, the GTP-binding elongation factor family, EF-Tu/EF-1A subfamily is a family of elongation factors, which includes the eukaryotic eEF-1 and the prokaryotic EF-Tu.
These proteins consist of three structural domains, the GTP-binding domain, domain 2 and domain 3.
The GTP-binding domain has been shown [1] to be involved in a conformational change mediated by the hydrolysis of GTP to GDP. This region is conserved in both EF-1alpha/EF-Tu and also in EF-2/EF-G and thus seems typical for GTP-dependent proteins which bind non-initiator tRNAs to the ribosome. The GTP-binding protein synthesis factor family also includes the eukaryotic peptide chain release factor GTP-binding subunits [2] and prokaryotic peptide chain release factor 3 (RF-3) [3]; the prokaryotic GTP-binding protein lepA and its homologue in yeast (GUF1) and Caenorhabditis elegans (ZK1236.1); yeast HBS1 [4]; rat statin S1 [5]; and the prokaryotic selenocysteine-specific elongation factor selB.[6]
Domain 2 adopts a beta-barrel structure, and is involved in binding to charged tRNA.[7] This domain is structurally related to the C-terminal domain of EF2, to which it displays weak sequence similarity. This domain is also found in other proteins such as translation initiation factor IF-2 and tetracycline-resistance proteins.
Domain 3 represents the C-terminal domain, which adopts a beta-barrel structure, and is involved in binding to both charged tRNA and to EF1B (or EF-Ts).[8]
References
- ^ Moller W, Schipper A, Amons R (1987). "A conserved amino acid sequence around Arg-68 of Artemia elongation factor 1 alpha is involved in the binding of guanine nucleotides and aminoacyl transfer RNAs". Biochimie. 69 (9): 983–9. PMID 3126836.
{{cite journal}}
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ignored (help)CS1 maint: multiple names: authors list (link) - ^ Stansfield I, Jones KM, Kushnirov VV, Dagkesamanskaya AR, Poznyakovski AI, Paushkin SV, Nierras CR, Cox BS, Ter-Avanesyan MD, Tuite MF (1995). "The products of the SUP45 (eRF1) and SUP35 genes interact to mediate translation termination in Saccharomyces cerevisiae". EMBO J. 14 (17): 4365–73. PMC 394521. PMID 7556078.
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ignored (help)CS1 maint: multiple names: authors list (link) - ^ Grentzmann G, Brechemier-Baey D, Heurgué-Hamard V, Buckingham RH (1995). "Function of polypeptide chain release factor RF-3 in Escherichia coli. RF-3 action in termination is predominantly at UGA-containing stop signals". J. Biol. Chem. 270 (18): 10595–600. PMID 7737996.
{{cite journal}}
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ignored (help)CS1 maint: multiple names: authors list (link) - ^ Nelson RJ, Ziegelhoffer T, Nicolet C, Werner-Washburne M, Craig EA (1992). "The translation machinery and 70 kd heat shock protein cooperate in protein synthesis". Cell. 71 (1): 97–105. PMID 1394434.
{{cite journal}}
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ignored (help)CS1 maint: multiple names: authors list (link) - ^ Ann DK, Moutsatsos IK, Nakamura T, Lin HH, Mao PL, Lee MJ, Chin S, Liem RK, Wang E (1991). "Isolation and characterization of the rat chromosomal gene for a polypeptide (pS1) antigenically related to statin". J. Biol. Chem. 266 (16): 10429–37. PMID 1709933.
{{cite journal}}
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ignored (help)CS1 maint: multiple names: authors list (link) - ^ Forchhammer K, Leinfelder W, Bock A (1989). "Identification of a novel translation factor necessary for the incorporation of selenocysteine into protein". Nature. 342 (6248): 453–6. doi:10.1038/342453a0. PMID 2531290.
{{cite journal}}
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ignored (help)CS1 maint: multiple names: authors list (link) - ^ Nissen P, Kjeldgaard M, Thirup S, Polekhina G, Reshetnikova L, Clark BF, Nyborg J (1995). "Crystal structure of the ternary complex of Phe-tRNAPhe, EF-Tu, and a GTP analog". Science. 270 (5241): 1464–72. PMID 7491491.
{{cite journal}}
: Unknown parameter|month=
ignored (help)CS1 maint: multiple names: authors list (link) - ^ Wang Y, Jiang Y, Meyering-Voss M, Sprinzl M, Sigler PB (1997). "Crystal structure of the EF-Tu.EF-Ts complex from Thermus thermophilus". Nat. Struct. Biol. 4 (8): 650–6. PMID 9253415.
{{cite journal}}
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ignored (help)CS1 maint: multiple names: authors list (link)
This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.
This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.
Elongation factor Tu C-terminal domain Provide feedback
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 PF00889 [2].
Literature references
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Nissen P, Kjeldgaard M, Thirup S, Polekhina G, Reshetnikova L, Clark BF, Nyborg J; , Science 1995;270:1464-1472.: Crystal structure of the ternary complex of Phe-tRNAPhe, EF-Tu, and a GTP analog. PUBMED:7491491 EPMC:7491491
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Wang Y, Jiang Y, Meyering-Voss M, Sprinzl M, Sigler PB; , Nat Struct Biol 1997;4:650-656.: Crystal structure of the EF-Tu.EF-Ts complex from Thermus thermophilus. PUBMED:9253415 EPMC:9253415
Internal database links
SCOOP: | GTP_EFTU GTP_EFTU_D2 |
External database links
SCOP: | 1etu |
This tab holds annotation information from the InterPro database.
InterPro entry IPR004160
Elongation factor EF1A (also known as EF-1alpha or EF-Tu) promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. EF1A consists of three structural domains. Release factor eRF3, which governs translation termination, has a similar overall structure. RF3 has an N-terminal extension and a EF1A-like C-terminal region which comprises a GTP-binding domain (G domain) and two beta-barrel domains that are similar to the three respective domains of elongation factor EF-Tu/eEF1A [ PUBMED:10676813 ]. Archaeal EF1A is both involved in translational elongation and termination, as well as in mRNA surveillance, which explains the lack of an eRF3 orthologue in archaea [ PUBMED:20974926 ].
This entry represents the C-terminal domain of both EF1A and eRF3, which adopts a beta-barrel structure. In EF1A, this domain is involved in binding to both charged tRNA and to EF1B (or EF-Ts, INTERPRO ) [ PUBMED:9253415 ].
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Alignments
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Seed (50) |
Full (21227) |
Representative proteomes | UniProt (108713) |
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RP15 (3537) |
RP35 (9972) |
RP55 (19082) |
RP75 (29432) |
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Jalview | |||||||
HTML | |||||||
PP/heatmap | 1 |
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
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Seed (50) |
Full (21227) |
Representative proteomes | UniProt (108713) |
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RP15 (3537) |
RP35 (9972) |
RP55 (19082) |
RP75 (29432) |
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Raw Stockholm | |||||||
Gzipped |
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
HMM logo
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
Trees
This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.
Note: You can also download the data file for the tree.
Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
Seed source: | PF00009 |
Previous IDs: | none |
Type: | Domain |
Sequence Ontology: | SO:0000417 |
Author: |
Bateman A |
Number in seed: | 50 |
Number in full: | 21227 |
Average length of the domain: | 98.6 aa |
Average identity of full alignment: | 37 % |
Average coverage of the sequence by the domain: | 22.19 % |
HMM information
HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
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Model details: |
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Model length: | 108 | ||||||||||||
Family (HMM) version: | 20 | ||||||||||||
Download: | download the raw HMM for this family |
Species distribution
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Structures
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the GTP_EFTU_D3 domain has been found. There are 215 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.
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AlphaFold Structure Predictions
The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.