The name of this superfamily has been modified since the most recent official CATH+ release (v4_2_0). At the point of the last release, this superfamily was named:

"
Translation factors
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 37319: Translation elongation factor LepA

There are 3 EC terms in this cluster

Please note: EC annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

Note: The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.

EC Term Annotations Evidence
Elongation factor 4. [EC: 3.6.5.n1]
GTP + H(2)O = GDP + phosphate.
  • The enzyme is required for accurate and efficient protein synthesis under certain stress conditions.
  • May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes.
  • Back-translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly.
  • Binds to ribosomes in a GTP-dependent manner.
7340 A0A009ESC7 A0A009ESC7 A0A009G4V0 A0A009G4V0 A0A009HA15 A0A009HA15 A0A009I9X8 A0A009I9X8 A0A009INH8 A0A009INH8
(7330 more...)
Protein-synthesizing GTPase. [EC: 3.6.5.3]
GTP + H(2)O = GDP + phosphate.
  • This enzyme comprises a family of proteins involved in prokaryotic as well as eukaryotic protein synthesis.
  • In the initiation factor complex, it is IF-2b (98 kDa) that binds GTP and subsequently hydrolyzes it in prokaryotes.
  • In eukaryotes, it is eIF-2 (150 kDa) that binds GTP.
  • In the elongation phase, the GTP-hydrolyzing proteins are the EF-Tu polypeptide of the prokaryotic transfer factor (43 kDa), the eukaryotic elongation factor EF-1-alpha (53 kDa), the prokaryotic EF-G (77 kDa), the eukaryotic EF-2 (70-110 kDa) and the signal recognition particle that play a role in endoplasmic reticulum protein synthesis (325 kDa).
  • EF-Tu and EF-1-alpha catalyze binding of aminoacyl-tRNA to the ribosomal A-site, while EF-G and EF-2 catalyze the translocation of peptidyl-tRNA from the A-site to the P-site.
  • GTPase activity is also involved in polypeptide release from the ribosome with the aid of the pRFs and eRFs.
  • Formerly EC 3.6.1.48.
22 U5N266 U5N266 U5N273 U5N273 U5N2N5 U5N2N5 U5N2N8 U5N2N8 U5N2S6 U5N2S6
(12 more...)
Sulfate adenylyltransferase. [EC: 2.7.7.4]
ATP + sulfate = diphosphate + adenylyl sulfate.
  • The human phosphoadenosine-phosphosulfate synthase (PAPS) system is a bifunctional enzyme: ATP sulfurylase, which catalyzes the formation of adenosine 5'-phosphosulfate (APS) from ATP and inorganic sulfate and the second step is catalyzed by the APS kinase portion of 3'-phosphoadenosine 5'-phosphosulfate (PAPS) synthase, which involves the formation of PAPS from enzyme bound APS and ATP.
  • This is in contrast to what is found in bacteria, yeasts, fungi and plants, where the formation of PAPS is carried out by two individual polypeptides, EC 2.7.7.4 and EC 2.7.1.25.
4 E6PL46 E6PL46 E6QV71 E6QV71
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