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29  structures 7411  species 0  interactions 9275  sequences 23  architectures

Family: EFP_N (PF08207)

Summary: Elongation factor P (EF-P) KOW-like domain

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Elongation factor P Edit Wikipedia article

Elongation factor P (EF-P) KOW-like domain
PDB 1iz6 EBI.jpg
crystal structure of translation initiation factor 5a from pyrococcus horikoshii
Pfam clanCL0107
Elongation factor P (EF-P) OB domain
PDB 1ueb EBI.jpg
crystal structure of translation elongation factor p from thermus thermophilus hb8
Pfam clanCL0021
Elongation factor P, C-terminal
PDB 1ueb EBI.jpg
crystal structure of translation elongation factor p from thermus thermophilus hb8

EF-P (elongation factor P) is a prokaryotic protein translation factor required for efficient peptide bond synthesis on 70S ribosomes from fMet-tRNAfMet.[1] It probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase.

EF-P consists of three domains:

  • An N-terminal KOW-like domain
  • A central OB domain, which forms an oligonucleotide-binding fold. It is not clear if this region is involved in binding nucleic acids[2]
  • A C-terminal domain which adopts an OB-fold, with five beta-strands forming a beta-barrel in a Greek-key topology[2]

eIF5A is the eukaryotic homolog of EF-P.


It has been suggested that after binding of the initiator tRNA to the P/I site, it is correctly positioned to the P site by binding of EF-P to the E site.[3] Additionally, EF-P has been shown to assist in efficient translation of three or more consecutive proline residues.[4]

See also


  1. ^ Aoki H, Adams SL, Turner MA, Ganoza MC (1997). "Molecular characterization of the prokaryotic efp gene product involved in a peptidyltransferase reaction". Biochimie. 79 (1): 7–11. doi:10.1016/S0300-9084(97)87619-5. PMID 9195040.
  2. ^ a b Hanawa-Suetsugu K, Sekine S, Sakai H, Hori-Takemoto C, Terada T, Unzai S, Tame JR, Kuramitsu S, Shirouzu M, Yokoyama S (June 2004). "Crystal structure of elongation factor P from Thermus thermophilus HB8". Proc. Natl. Acad. Sci. U.S.A. 101 (26): 9595–600. Bibcode:2004PNAS..101.9595H. doi:10.1073/pnas.0308667101. PMC 470720. PMID 15210970.
  3. ^ Leaps in Translational Elongation Science (2009) 326, 677.
  4. ^ Ude, Susanne; Lassak, Jürgen; Starosta, Agata L.; Kraxenberger, Tobias; Wilson, Daniel N.; Jung, Kirsten (2013-01-04). "Translation Elongation Factor EF-P Alleviates Ribosome Stalling at Polyproline Stretches". Science. 339 (6115): 82–85. Bibcode:2013Sci...339...82U. doi:10.1126/science.1228985. ISSN 0036-8075. PMID 23239623.
This article incorporates text from the public domain Pfam and InterPro: IPR001059
This article incorporates text from the public domain Pfam and InterPro: IPR015365

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

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Elongation factor P (EF-P) KOW-like domain Provide feedback

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External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR013185

This entry represents the N-terminal domain of homologues of elongation factor P, which probably are translation initiation factors.

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Pfam Clan

This family is a member of clan KOW (CL0107), which has the following description:

This superfamily includes proteins involved in translation that have a KOW like SH3-fold.

The clan contains the following 7 members:

EFP_N KOW Ribosomal_L14e Ribosomal_L19 Ribosomal_L21e Ribosomal_L26 Ribosomal_L2_C


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Curation and family details

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Seed source: Prosite
Previous IDs: none
Type: Domain
Sequence Ontology: SO:0000417
Author: Finn RD , Bateman A
Number in seed: 153
Number in full: 9275
Average length of the domain: 57.70 aa
Average identity of full alignment: 35 %
Average coverage of the sequence by the domain: 30.43 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 57096847 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 20.6 20.6
Trusted cut-off 20.6 20.6
Noise cut-off 20.5 20.5
Model length: 58
Family (HMM) version: 14
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Species distribution

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Archea Archea Eukaryota Eukaryota
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Viroids Viroids Unclassified sequence Unclassified sequence


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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 EFP_N domain has been found. There are 29 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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