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11  structures 487  species 3  interactions 874  sequences 17  architectures

Family: EF1_GNE (PF00736)

Summary: EF-1 guanine nucleotide exchange domain

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This is the Wikipedia entry entitled "EF1 guanine nucleotide exchange domain". More...

EF1 guanine nucleotide exchange domain Edit Wikipedia article

EF1_GNE
PDB 2b7c EBI.jpg
yeast guanine nucleotide exchange factor eef1balpha k205a mutant in complex with eef1a
Identifiers
Symbol EF1_GNE
Pfam PF00736
InterPro IPR014038
PROSITE PDOC00648
SCOP 1b64
SUPERFAMILY 1b64

In molecular biology, the EF1 guanine nucleotide exchange domain is a protein domain found in the beta and delta chains of elongation factors from eukaryotes and archaea.

Elongation factor EF1B (also known as EF-Ts or EF-1beta/gamma/delta) is a nucleotide exchange factor that is required to regenerate EF1A from its inactive form (EF1A-GDP) to its active form (EF1A-GTP). EF1A is then ready to interact with a new aminoacyl-tRNA to begin the cycle again. EF1B is more complex in eukaryotes than in bacteria, and can consist of three subunits: EF1B-alpha (or EF-1beta), EF1B-gamma (or EF-1gamma) and EF1B-beta (or EF-1delta).[1]

The EF1 guanine nucleotide exchange domain is found in the beta (EF-1beta, also known as EF1B-alpha) and delta (EF-1delta, also known as EF1B-beta) chains of EF1B proteins from eukaryotes and archaea. The beta and delta chains have exchange activity, which mainly resides in their homologous guanine nucleotide exchange domains, found in the C-terminal region of the peptides. Their N-terminal regions may be involved in interactions with the gamma chain (EF-1gamma).[2]

[edit] References

  1. ^ Andersen GR, Nyborg J (2001). "Structural studies of eukaryotic elongation factors". Cold Spring Harb. Symp. Quant. Biol. 66: 425–37. PMID 12762045.
  2. ^ Pérez, J. M.; Siegal, G.; Kriek, J.; Hård, K.; Dijk, J.; Canters, G. W.; Möller, W. (1999). "The solution structure of the guanine nucleotide exchange domain of human elongation factor 1beta reveals a striking resemblance to that of EF-Ts from Escherichia coli". Structure (London, England : 1993) 7 (2): 217–226. doi:10.1016/S0969-2126(99)80027-6. PMID 10368288. edit

This article incorporates text from the public domain Pfam and InterPro IPR014038

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

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EF-1 guanine nucleotide exchange domain Provide feedback

This family is the guanine nucleotide exchange domain of EF-1 beta and EF-1 delta chains.

Literature references

  1. Perez JM, Siegal G, Kriek J, H rd K, Dijk J, Canters GW, Moller W; , Structure Fold Des 1999;7:217-226.: The solution structure of the guanine nucleotide exchange domain of human elongation factor 1beta reveals a striking resemblance to that of EF-Ts from Escherichia coli. PUBMED:10368288 EPMC:10368288


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR014038

Translation elongation factors are responsible for two main processes during protein synthesis on the ribosome [PUBMED:12762045, PUBMED:15922593, PUBMED:12932732]. EF1A (or EF-Tu) is responsible for the selection and binding of the cognate aminoacyl-tRNA to the A-site (acceptor site) of the ribosome. EF2 (or EF-G) is responsible for the translocation of the peptidyl-tRNA from the A-site to the P-site (peptidyl-tRNA site) of the ribosome, thereby freeing the A-site for the next aminoacyl-tRNA to bind. Elongation factors are responsible for achieving accuracy of translation and both EF1A and EF2 are remarkably conserved throughout evolution.

Elongation factor EF1B (also known as EF-Ts or EF-1beta/gamma/delta) is a nucleotide exchange factor that is required to regenerate EF1A from its inactive form (EF1A-GDP) to its active form (EF1A-GTP). EF1A is then ready to interact with a new aminoacyl-tRNA to begin the cycle again. EF1B is more complex in eukaryotes than in bacteria, and can consist of three subunits: EF1B-alpha (or EF-1beta), EF1B-gamma (or EF-1gamma) and EF1B-beta (or EF-1delta) [PUBMED:12762045].

This entry represents the guanine nucleotide exchange domain of the beta (EF-1beta, also known as EF1B-alpha) and delta (EF-1delta, also known as EF1B-beta) chains of EF1B proteins from eukaryotes and archaea. The beta and delta chains have exchange activity, which mainly resides in their homologous guanine nucleotide exchange domains, found in the C-terminal region of the peptides. Their N-terminal regions may be involved in interactions with the gamma chain (EF-1gamma).

More information about these proteins can be found at Protein of the Month: Elongation Factors [PUBMED:].

Gene Ontology

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Domain organisation

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Alignments

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(87)
Full
(874)
Representative proteomes NCBI
(872)
Meta
(67)
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(149)
RP35
(255)
RP55
(374)
RP75
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  Seed
(87)
Full
(874)
Representative proteomes NCBI
(872)
Meta
(67)
RP15
(149)
RP35
(255)
RP55
(374)
RP75
(461)
Alignment:
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  Seed
(87)
Full
(874)
Representative proteomes NCBI
(872)
Meta
(67)
RP15
(149)
RP35
(255)
RP55
(374)
RP75
(461)
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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

External links

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Pfam alignments:

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Curation and family details

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Curation View help on the curation process

Seed source: Pfam-B_488 (release 2.1)
Previous IDs: EF1BD;
Type: Domain
Author: Bateman A
Number in seed: 87
Number in full: 874
Average length of the domain: 86.40 aa
Average identity of full alignment: 48 %
Average coverage of the sequence by the domain: 37.56 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 20.8 20.8
Trusted cut-off 21.4 21.0
Noise cut-off 20.5 18.1
Model length: 89
Family (HMM) version: 14
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Species distribution

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Interactions

There are 3 interactions for this family. More...

GTP_EFTU GTP_EFTU_D2 GTP_EFTU_D3

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 EF1_GNE domain has been found. There are 11 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 seqence.

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