View in Gene3D

CATH Superfamily 2.40.30.10

Translation factors

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.
« Back to all FunFams

FunFam 19802: Translation elongation factor Tu

There are 5 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
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.
 75 A0A017H1K9 A0A017H253 A0A017H2I8 A0A087F5B5 A0A094IQR5 A0A098T3Q1 A0A099DWC8 A0A099VRW4 A0A0A2YH90 A0A0A2YJK3
(65 more...)
Heterotrimeric G-protein GTPase. [EC: 3.6.5.1]
GTP + H(2)O = GDP + phosphate.
  • This group comprises GTP-hydrolyzing systems, where GTP and GDP alternate in binding.
  • This group includes stimulatory and inhibitory G-proteins such as G(s), G(i), G(o) and G(olf), targeting adenylate cyclase and/or K(+) and Ca(2+) channels; G(q) stimulating phospholipase C; transducin activating cGMP phosphodiesterase; gustducin activating cAMP phosphodiesterase.
  • G(olf) is instrumental in odor perception, transducin in vision and gustducin in taste recognition.
  • At least 16 different alpha subunits (39-52 kDa), 5 beta subunits (36 kDa) and 12 gamma subunits (6-9 kDa) are known.
  • Formerly EC 3.6.1.46.
 24 A0A0A0V1J3 A0A0A0V1K0 A0A0A0V1L8 A0A0A0V1N1 A0A0A0V1N5 A0A0A0V2C0 A0A0A0V2C8 A0A0A0V2G8 A0A0A0V2H3 A0A0A0V3C1
(14 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.
 1 A0A139XHW1
Adenylosuccinate synthase. [EC: 6.3.4.4]
GTP + IMP + L-aspartate = GDP + phosphate + N(6)-(1,2-dicarboxyethyl)- AMP.
    		 1 A0A0J9W6L4
    Nucleoside-triphosphate phosphatase. [EC: 3.6.1.15]
    NTP + H(2)O = NDP + phosphate.
    • The enzyme is found in eukaryotes and thermophilic bacteria, but appears to be absent from mesophilic bacteria.
    • Also hydrolyzes nucleoside diphosphates, thiamine diphosphate and FAD.
    • The enzyme from the plant Pisum sativum (garden pea) is regulated by calmodulin.
    		 1 A0A161TEH6
    CATH-Gene3D is a Global Biodata Core Resource Learn more...