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CATH Superfamily 3.90.1170.10

Ribosomal protein L16/L10

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:

"
Ribosomal protein L10e/L16
".

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 1938: 60S ribosomal protein L10

There are 4 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-S-isoprenylcysteine O-methyltransferase. [EC: 2.1.1.100]
S-adenosyl-L-methionine + protein C-terminal S-farnesyl-L-cysteine = S-adenosyl-L-homocysteine + protein C-terminal S-farnesyl-L-cysteine methyl ester.
  • C-terminal S-geranylgeranylcysteine and S-geranylcysteine residues are also methylated, more slowly.
  • Formerly EC 2.1.1.24.
 1 A0A1I7RRM0
Phospholipid-translocating ATPase. [EC: 3.6.3.1]
ATP + H(2)O + phospholipid(Side 1) = ADP + phosphate + phospholipid(Side 2).
  • P-type ATPase that undergoes covalent phosphorylation during the transport cycle.
  • The enzyme apparently has several activities, one of them being the movement of phospholipids from one membrane face to the other.
  • Formerly EC 3.6.3.13.
 1 A0A1I8JBR7
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.
 1 Q90YV9
Protein-serine/threonine phosphatase. [EC: 3.1.3.16]
[a protein]-serine/threonine phosphate + H(2)O = [a protein]- serine/threonine + phosphate.
  • A group of enzymes removing the serine- or threonine-bound phosphate group from a wide range of phosphoproteins, including a number of enzymes which have been phosphorylated under the action of a kinase (cf. EC 3.1.3.48).
  • The spleen enzyme also acts on phenolic phosphates and phosphamides (cf. EC 3.9.1.1).
 1 A0A024VKF9
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