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CATH Superfamily 3.30.70.3550

Leucyl/phenylalanyl-tRNA-protein transferase, N-terminal domain

The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_0). At the point of the last release, this superfamily was named:

"
Leucyl/phenylalanyl-tRNA-protein transferase, N-terminal domain
".

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 2: Leucyl/phenylalanyl-tRNA--protein transferase

There are 1 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
Lysine/arginine leucyltransferase. [EC: 2.3.2.6]
(1) L-leucyl-tRNA(Leu) + N-terminal L-lysyl-[protein] = tRNA(Leu) + N-terminal L-leucyl-L-lysyl-[protein]. (2) L-leucyl-tRNA(Leu) + N-terminal L-arginyl-[protein] = tRNA(Leu) + N-terminal L-leucyl-L-arginyl-[protein].
  • Participates in the N-end rule protein degradation pathway in certain bacteria, by attaching the primary destabilizing residue L-leucine to the N-termini of proteins that have an N-terminal L-arginine or L-lysine residue.
  • Once modified, the proteins are recognized by EC 3.4.21.92.
  • The enzyme also transfers L-phenylalanine in vitro, but this has not been observed in vivo.
  • Cf. EC 2.3.2.8 and EC 2.3.2.29.
 54 A0A0M3GYV3 A0A0M3GYV3 A0A0M3GYV3 A0A0M3GYV3 A0A0M3GYV3 A0A0M3GYV3 A0A0Y6GCQ0 A0A0Y6GCQ0 A0A1D3ETR9 A0A1D3ETR9
(44 more...)
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