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208  structures 8926  species 0  interactions 21771  sequences 186  architectures

Family: EFG_IV (PF03764)

Summary: Elongation factor G, domain IV

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This is the Wikipedia entry entitled "EF-G". More...

EF-G Edit Wikipedia article

Protein-synthesizing GTPase
EF-G Post State PDB 4V5F.jpg
EC no.
Alt. namesElongation factor G, EF-G
IntEnzIntEnz view
ExPASyNiceZyme view
MetaCycmetabolic pathway
PDB structuresRCSB PDB PDBe PDBsum
Translation elongation factor EFG/EF2
EFG/EF2, domain IV
Pfam clanCL0329

EF-G (elongation factor G, historically known as translocase) is a prokaryotic elongation factor involved in protein translation. As a GTPase, EF-G catalyzes the movement (translocation) of transfer RNA (tRNA) and messenger RNA (mRNA) through the ribosome.[1]


Encoded by the fusA gene on the str operon,[2] EF-G is made up of 704 amino acids that form 5 domains, labeled Domain I through Domain V. Domain I may be referred to as the G-domain or as Domain I(G), since it binds to and hydrolyzes guanosine triphosphate (GTP). Domain I also helps EF-G bind to the ribosome, and contains the N-terminal of the polypeptide chain.[3][4] Domain IV is important for translocation, as it undergoes a significant conformational change and enters the A site on the 30S ribosomal subunit, pushing the mRNA and tRNA molecules from the A site to the P site.[5]

The five domains may be also separated into two super-domains. Super-domain I consists of Domains I and II, and super-domain II consists of Domains III - IV. Throughout translocation, super-domain I will remain relatively unchanged, as it is responsible for binding tightly to the ribosome. However, super-domain II will undergo a large rotational motion from the pre-translocational (PRE) state to the post-translocational (POST) state. Super-domain I is similar to the corresponding sections of EF-Tu.[6][7][8] Super-domain II in the POST state mimics the tRNA molecule of the EF-Tu • GTP • aa-tRNA ternary complex.[9]

Crystal structure of EF-G in the POST state with Domains I - V labeled. PDB ID: 4V5F

EF-G on the ribosome

Binding to L7/L12

L7/L12 is only a multicopy protein on the large ribosomal subunit of the bacterial ribosome that binds to certain GTPases, like Initiation Factor 2, Elongation factor-Tu, Release Factor 3, and EF-G.[10] Specifically, the C-terminal of L7/L12 will bind to EF-G and is necessary for GTP hydrolysis.[4]

Interaction with the GTPase Associated Center

The GTPase Associated Center (GAC) is a region on the large ribosomal subunit that consists of two smaller regions of 23S ribosomal RNA called the L11 stalk and the sarcin-ricin loop (SRL).[11] As a highly conserved rRNA loop in evolution, the SRL is critical in helping GTPases bind to the ribosome, but is not essential for GTP hydrolysis. There is some evidence to support that a phosphate oxygen in the A2662 residue of the SRL may help hydrolyze GTP.[12]

Animation of the 70S ribosome with the P site tRNA (orange), E site tRNA (green), mRNA (yellow), and elongation factor G (red) in the POST state. PDB ID: 4W29

Function in protein elongation

EF-G catalyzes the translocation of the tRNA and mRNA down the ribosome at the end of each round of polypeptide elongation.[1] In this process, the peptidyl transferase center (PTC) has catalyzed the formation of a peptide bond between amino acids, moving the polypeptide chain from the P site tRNA to the A site tRNA. The 50S and 30S ribosomal subunits are now allowed to rotate relative to each other by approximately 7°.[13][14] The subunit rotation is coupled with the movement of the 3' ends of both tRNA molecules on the large subunit from the A and P sites to the P and E sites, respectively, while the anticodon loops remain unshifted. This rotated ribosomal intermediate, in which the first tRNA occupies a hybrid A/P position and the second tRNA occupies a hybrid P/E position is a substrate for EF-G-GTP.[1][13]

As a GTPase, EF-G binds to the rotated ribosome near the A site in its GTP-bound state, and hydrolyzes GTP, releasing GDP and inorganic phosphate:

The hydrolysis of GTP allows for a large conformational change within EF-G, forcing the A/P tRNA to fully occupy the P site, the P/E tRNA to fully occupy the E site (and exit the ribosome complex), and the mRNA to shift three nucleotides down relative to the ribosome. The GDP-bound EF-G molecule then dissociates from the complex, leaving another free A-site where the elongation cycle can start again.[1][15]

Crystal structure of the ribosome with two tRNAs (orange and green) and EF-G (in cyan) after translocation. PDB ID: 4W29.

Function in protein termination

Protein elongation continues until a stop codon appears on the mRNA. A Class I release factor (RF1 or RF2) binds to the stop codon, which induces hydrolysis of the tRNA-peptide bond in the P site, allowing the newly-formed protein to exit the ribosome. The nascent peptide continues to fold and leaves the 70S ribosome, the mRNA, the deacylated tRNA (P site), and the Class I release factor (A site).[16][17]

In a GTP-dependent manner, the subsequent recycling is catalyzed by a Class II release factor named RF3/prfC, Ribosome recycling factor (RRF), Initiation Factor 3 (IF3) and EF-G. The protein RF3 releases the Class I release factor so that it may occupy the ribosomal A site. EF-G hydrolyzes GTP and undergoes a large conformational change to push RF3 down the ribosome, which occurs alongside tRNA dissociation and promotes the ribosomal subunit rotation. This motion actively splits the B2a/B2b bridge, which connects the 30S and the 50S subunits, so that the ribosome can split.[16] IF3 then isolates the 30S subunit to prevent re-association of the large and small subunits.[18]

Clinical significance

EF-G in pathogenic bacteria can be inhibited by antibiotics that prevent EF-G from binding to the ribosome,[19] carrying out translocation[20] or dissociating from the ribosome.[21]

For example, the antibiotic thiostrepton prevents EF-G from binding stably to the ribosome,[19] while the antibiotics dityromycin and GE82832 inhibit the activity of EF-G by preventing the translocation of the A site tRNA. Dityromycin and GE82832 do not affect the binding of EF-G to the ribosome, however.[20]

The antibiotic fusidic acid is known to inhibit Staphylococcus aureus and other bacteria by binding to EF-G after one translocation event on the ribosome, preventing EF-G from dissociating.[21][22] However, some bacterial strains have developed resistance to fusidic acid due to point mutations in the fusA gene, which prevents fusidic acid from binding to EF-G.[23][24]


EF-G has a complex evolutionary history, with numerous paralogous versions of the factor present in bacteria, suggesting subfunctionalization of different EF-G variants.[25]

Elongation factors exist in all three domains of life with similar function on the ribosome. The eukaryotic and archeal homologs of EF-G are eEF2 and aEF2, respectively. In bacteria (and some archaea), the fusA gene that encodes EF-G is found within the conserved str gene with the sequence 5′ - rpsL - rpsG - fusA - tufA - 3′.[2] However, two other major forms of EF-G exist in some species of Spirochetes, Planctomycetes, and δ-Proteobacteria, which form the spd group of bacteria that have elongation factors spdEFG1 and spdEFG2.[25][26]

From spdEFG1 and spdEFG2 evolved the mitochondrial elongation factors mtEFG1 (GFM1) and mtEFG2 (GFM2), respectively.[25][26] The two roles of EF-G in elongation and termination of protein translation are split amongst the mitochondrial elongation factors, with mtEFG1 responsible for translocation and mtEFG2 responsible for termination and ribosomal recycling with mitochondrial RRF.

See also


  1. ^ a b c d Shoji, S; Walker, SE; Fredrick, K (2009). "Ribosomal translocation: one step closer to the molecular mechanism". ACS Chem Biol. 4 (2): 93–107. doi:10.1021/cb8002946. PMC 3010847. PMID 19173642.
  2. ^ a b Post, L. E.; Nomura, M. (1980-05-25). "DNA sequences from the str operon of Escherichia coli". The Journal of Biological Chemistry. 255 (10): 4660–4666. doi:10.1016/S0021-9258(19)85545-X. ISSN 0021-9258. PMID 6989816.
  3. ^ Liu, Kaixian; Rehfus, Joseph E.; Mattson, Elliot; Kaiser, Christian M. (2017-07-01). "The ribosome destabilizes native and non-native structures in a nascent multidomain protein". Protein Science. 26 (7): 1439–1451. doi:10.1002/pro.3189. ISSN 1469-896X. PMC 5477528. PMID 28474852.
  4. ^ a b Carlson, Markus A.; Haddad, Bassam G.; Weis, Amanda J.; Blackwood, Colby S.; Shelton, Catherine D.; Wuerth, Michelle E.; Walter, Justin D.; Spiegel, Paul Clint (2017-06-01). "Ribosomal protein L7/L12 is required for GTPase translation factors EF-G, RF3, and IF2 to bind in their GTP state to 70S ribosomes". The FEBS Journal. 284 (11): 1631–1643. doi:10.1111/febs.14067. ISSN 1742-4658. PMC 5568246. PMID 28342293.
  5. ^ Salsi, Enea; Farah, Elie; Dann, Jillian; Ermolenko, Dmitri N. (2014). "Following movement of domain IV of elongation factor G during ribosomal translocation". Proceedings of the National Academy of Sciences. 111 (42): 15060–15065. Bibcode:2014PNAS..11115060S. doi:10.1073/pnas.1410873111. PMC 4210333. PMID 25288752.
  6. ^ Lin, Jinzhong; Gagnon, Matthieu G.; Bulkley, David; Steitz, Thomas A. (2015). "Conformational Changes of Elongation Factor G on the Ribosome during tRNA Translocation". Cell. 160 (1–2): 219–227. doi:10.1016/j.cell.2014.11.049. PMC 4297320. PMID 25594181.
  7. ^ Li, Wen; Trabuco, Leonardo G.; Schulten, Klaus; Frank, Joachim (2011-05-01). "Molecular dynamics of EF-G during translocation". Proteins: Structure, Function, and Bioinformatics. 79 (5): 1478–1486. doi:10.1002/prot.22976. ISSN 1097-0134. PMC 3132869. PMID 21365677.
  8. ^ Zhang, Dejiu; Yan, Kaige; Zhang, Yiwei; Liu, Guangqiao; Cao, Xintao; Song, Guangtao; Xie, Qiang; Gao, Ning; Qin, Yan (2015). "New insights into the enzymatic role of EF-G in ribosome recycling". Nucleic Acids Research. 43 (21): 10525–33. doi:10.1093/nar/gkv995. PMC 4666400. PMID 26432831.
  9. ^ Nyborg, J.; Nissen, P.; Kjeldgaard, M.; Thirup, S.; Polekhina, G.; Clark, B. F. (March 1996). "Structure of the ternary complex of EF-Tu: macromolecular mimicry in translation". Trends in Biochemical Sciences. 21 (3): 81–82. doi:10.1016/S0968-0004(96)30008-X. ISSN 0968-0004. PMID 8882578.
  10. ^ Mandava, C. S.; Peisker, K.; Ederth, J.; Kumar, R.; Ge, X.; Szaflarski, W.; Sanyal, S. (2011-11-18). "Bacterial ribosome requires multiple L12 dimers for efficient initiation and elongation of protein synthesis involving IF2 and EF-G". Nucleic Acids Research. 40 (5): 2054–2064. doi:10.1093/nar/gkr1031. ISSN 0305-1048. PMC 3299993. PMID 22102582.
  11. ^ Maklan, E. J. (2012). Genetic and Biochemical Analysis of the GTPase Associated Center of the Ribosome. UC Santa Cruz. Merritt ID: ark:/13030/m5js9t4d. Retrieved from
  12. ^ Shi, Xinying; Khade, Prashant K.; Sanbonmatsu, Karissa Y.; Joseph, Simpson (2012). "Functional Role of the Sarcin–Ricin Loop of the 23S rRNA in the Elongation Cycle of Protein Synthesis". Journal of Molecular Biology. 419 (3–4): 125–138. doi:10.1016/j.jmb.2012.03.016. PMC 3348345. PMID 22459262.
  13. ^ a b Choi, Junhong; Puglisi, Joseph D. (2017). "Three tRNAs on the ribosome slow translation elongation". Proceedings of the National Academy of Sciences. 114 (52): 13691–13696. doi:10.1073/pnas.1719592115. PMC 5748233. PMID 29229848.
  14. ^ Guo, Z.; Noller, H. F. (2012). "Rotation of the head of the 30S ribosomal subunit during mRNA translocation". Proceedings of the National Academy of Sciences. 109 (50): 20391–20394. Bibcode:2012PNAS..10920391G. doi:10.1073/pnas.1218999109. PMC 3528506. PMID 23188795.
  15. ^ da Cunha, CE; Belardinelli, R; Peske, F; Holtkamp, W; Wintermeyer, W; Rodnina, MV (2013). "Dual use of GTP hydrolysis by elongation factor G on the ribosome". Translation. 1 (1): e24315. doi:10.4161/trla.24315. PMC 4718068. PMID 26824016.
  16. ^ a b Das, Debasis; Samanta, Dibyendu; Bhattacharya, Arpita; Basu, Arunima; Das, Anindita; Ghosh, Jaydip; Chakrabarti, Abhijit; Gupta, Chanchal Das (2017-01-18). "A Possible Role of the Full-Length Nascent Protein in Post-Translational Ribosome Recycling". PLOS ONE. 12 (1): e0170333. Bibcode:2017PLoSO..1270333D. doi:10.1371/journal.pone.0170333. ISSN 1932-6203. PMC 5242463. PMID 28099529.
  17. ^ Zavialov AV, Hauryliuk VV, Ehrenberg M (2005). "Splitting of the posttermination ribosome into subunits by the concerted action of RRF and EF-G". Molecular Cell. 18 (6): 675–686. doi:10.1016/j.molcel.2005.05.016. PMID 15949442.
  18. ^ Hirokawa, Go; Nijman, Romana M.; Raj, V. Samuel; Kaji, Hideko; Igarashi, Kazuei; Kaji, Akira (2005-08-01). "The role of ribosome recycling factor in dissociation of 70S ribosomes into subunits". RNA. 11 (8): 1317–1328. doi:10.1261/rna.2520405. ISSN 1355-8382. PMC 1370814. PMID 16043510.
  19. ^ a b Walter, Justin D.; Hunter, Margaret; Cobb, Melanie; Traeger, Geoff; Spiegel, P. Clint (2012-01-01). "Thiostrepton inhibits stable 70S ribosome binding and ribosome-dependent GTPase activation of elongation factor G and elongation factor 4". Nucleic Acids Research. 40 (1): 360–370. doi:10.1093/nar/gkr623. ISSN 0305-1048. PMC 3245911. PMID 21908407.
  20. ^ a b Bulkley, David; Brandi, Letizia; Polikanov, Yury S.; Fabbretti, Attilio; O’Connor, Michael; Gualerzi, Claudio O.; Steitz, Thomas A. (2014). "The Antibiotics Dityromycin and GE82832 Bind Protein S12 and Block EF-G-Catalyzed Translocation". Cell Reports. 6 (2): 357–365. doi:10.1016/j.celrep.2013.12.024. PMC 5331365. PMID 24412368.
  21. ^ a b Belardinelli, Riccardo; Rodnina, Marina V. (2017-09-05). "Effect of Fusidic Acid on the Kinetics of Molecular Motions During EF-G-Induced Translocation on the Ribosome". Scientific Reports. 7 (1): 10536. Bibcode:2017NatSR...710536B. doi:10.1038/s41598-017-10916-8. ISSN 2045-2322. PMC 5585275. PMID 28874811.
  22. ^ Koripella, Ravi Kiran; Chen, Yang; Peisker, Kristin; Koh, Cha San; Selmer, Maria; Sanyal, Suparna (2012). "Mechanism of Elongation Factor-G-mediated Fusidic Acid Resistance and Fitness Compensation inStaphylococcus aureus". Journal of Biological Chemistry. 287 (36): 30257–30267. doi:10.1074/jbc.m112.378521. PMC 3436278. PMID 22767604.
  23. ^ Macvanin M, Hughes D (June 2005). "Hyper-susceptibility of a fusidic acid-resistant mutant of Salmonella to different classes of antibiotics". FEMS Microbiology Letters. 247 (2): 215–20. doi:10.1016/j.femsle.2005.05.007. PMID 15935566.
  24. ^ Macvanin M, Johanson U, Ehrenberg M, Hughes D (July 2000). "Fusidic acid-resistant EF-G perturbs the accumulation of ppGpp". Molecular Microbiology. 37 (1): 98–107. doi:10.1046/j.1365-2958.2000.01967.x. PMID 10931308. S2CID 10307058.
  25. ^ a b c G C Atkinson; S L Baldauf (2011). "Evolution of elongation factor G and the origins of mitochondrial and chloroplast forms". Molecular Biology and Evolution. 28 (3): 1281–92. doi:10.1093/molbev/msq316. PMID 21097998.
  26. ^ a b Margus, Tõnu; Remm, Maido; Tenson, Tanel (2011-08-04). "A Computational Study of Elongation Factor G (EFG) Duplicated Genes: Diverged Nature Underlying the Innovation on the Same Structural Template". PLOS ONE. 6 (8): e22789. Bibcode:2011PLoSO...622789M. doi:10.1371/journal.pone.0022789. ISSN 1932-6203. PMC 3150367. PMID 21829651.

Further reading

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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 G, domain IV Provide feedback

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.

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External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR005517

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 EF2 (EF-G) is a G-protein. It brings about the translocation of peptidyl-tRNA and mRNA through a ratchet-like mechanism: the binding of GTP-EF2 to the ribosome causes a counter-clockwise rotation in the small ribosomal subunit; the hydrolysis of GTP to GDP by EF2 and the subsequent release of EF2 causes a clockwise rotation of the small subunit back to the starting position [ PUBMED:12762009 , PUBMED:12762047 ]. This twisting action destabilises tRNA-ribosome interactions, freeing the tRNA to translocate along the ribosome upon GTP-hydrolysis by EF2. EF2 binding also affects the entry and exit channel openings for the mRNA, widening it when bound to enable the mRNA to translocate along the ribosome.

EF2 has five domains. This entry represents domain IV found in EF2 (or EF-G) of both prokaryotes and eukaryotes. The EF2-GTP-ribosome complex undergoes extensive structural rearrangement for tRNA-mRNA movement to occur. Domain IV, which extends from the 'body' of the EF2 molecule much like a lever arm, facilitates the movement of peptidyl-tRNA from the A to the P site, being critical for the structural transition to take place [ PUBMED:25288752 ].

Included in this entry is a domain of mitochondrial Elongation factor G1 (mtEFG1) proteins that is homologous to domain IV of EF-G. Eukaryotic cells harbor 2 protein synthesis systems: one localized in the cytoplasm, the other in the mitochondria. Most factors regulating mitochondrial protein synthesis are encoded by nuclear genes, translated in the cytoplasm, and then transported to the mitochondria. The eukaryotic system of elongation factor (EF) components is more complex than that in prokaryotes, with both cytoplasmic and mitochondrial elongation factors and multiple isoforms being expressed in certain species. During the process of peptide synthesis and tRNA site changes, the ribosome is moved along the mRNA a distance equal to one codon with the addition of each amino acid. In bacteria this translocation step is catalyzed by EF-G_GTP, which is hydrolyzed to provide the required energy. Thus, this action releases the uncharged tRNA from the P site and transfers the newly formed peptidyl-tRNA from the A site to the P site. Eukaryotic mtEFG1 proteins show significant homology to bacterial EF-Gs. Mutants in yeast mtEFG1 have impaired mitochondrial protein synthesis, respiratory defects and a tendency to lose mitochondrial DNA [ PUBMED:11735030 , PUBMED:1935960 , PUBMED:15922593 , PUBMED:1602493 , PUBMED:8159735 , PUBMED:10837219 , PUBMED:12471894 , PUBMED:16213500 , PUBMED:12932345 ].

Gene Ontology

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Domain organisation

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Pfam Clan

This family is a member of clan S5 (CL0329), which has the following description:

This superfamily contains a wide range of families that possess a structure similar to the second domain of ribosomal S5 protein.

The clan contains the following 18 members:

ChlI DNA_gyraseB DNA_mis_repair EFG_IV Fae GalKase_gal_bdg GHMP_kinases_N IGPD Lon_C LpxC Morc6_S5 Ribonuclease_P Ribosomal_S5_C Ribosomal_S9 RNase_PH Topo-VIb_trans UPF0029 Xol-1_N


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Curation and family details

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Seed source: Pfam-B_40 (release 2.1)
Previous IDs: none
Type: Domain
Sequence Ontology: SO:0000417
Author: Bateman A , Griffiths-Jones SR
Number in seed: 64
Number in full: 21771
Average length of the domain: 118.70 aa
Average identity of full alignment: 32 %
Average coverage of the sequence by the domain: 16.22 %

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build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 24.0 24.0
Trusted cut-off 24.0 24.0
Noise cut-off 23.9 23.9
Model length: 121
Family (HMM) version: 21
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Species distribution

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Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
Viruses Viruses Unclassified Unclassified
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 EFG_IV domain has been found. There are 208 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.

Protein Predicted structure External Information
A0A096QR66 View 3D Structure Click here
A0A1D6E4M0 View 3D Structure Click here
A0A1D6I3L1 View 3D Structure Click here
A0A1D6LAW0 View 3D Structure Click here
A0A1D6P3B9 View 3D Structure Click here
A0A1D8PH71 View 3D Structure Click here
A0A286Y8X9 View 3D Structure Click here
A0B7D5 View 3D Structure Click here
A0JMI9 View 3D Structure Click here
A0KQ96 View 3D Structure Click here
A0L5X0 View 3D Structure Click here
A0LRL7 View 3D Structure Click here
A0PXU3 View 3D Structure Click here
A0RW30 View 3D Structure Click here
A0SXL6 View 3D Structure Click here
A1A0T0 View 3D Structure Click here
A1AVJ7 View 3D Structure Click here
A1B023 View 3D Structure Click here
A1BJ37 View 3D Structure Click here
A1CHC3 View 3D Structure Click here
A1CXG4 View 3D Structure Click here
A1KB30 View 3D Structure Click here
A1R8V0 View 3D Structure Click here
A1SNN6 View 3D Structure Click here
A1T4L5 View 3D Structure Click here
A1TJ04 View 3D Structure Click here
A1UBL0 View 3D Structure Click here
A1W2Q4 View 3D Structure Click here
A1WHC2 View 3D Structure Click here
A1WVC5 View 3D Structure Click here
A2CE51 View 3D Structure Click here
A2QI77 View 3D Structure Click here
A2SLG0 View 3D Structure Click here
A3CQM2 View 3D Structure Click here
A3DIZ9 View 3D Structure Click here
A3DMV6 View 3D Structure Click here
A3GHT9 View 3D Structure Click here
A3N247 View 3D Structure Click here
A3PEZ8 View 3D Structure Click here
A4FPM8 View 3D Structure Click here