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CATH Superfamily 3.40.525.10

CRAL-TRIO lipid binding domain

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:

"
CRAL-TRIO lipid binding 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 3454: SEC14-like 3 (S. cerevisiae)

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
Peptide-aspartate beta-dioxygenase. [EC: 1.14.11.16]
Peptide L-aspartate + 2-oxoglutarate + O(2) = peptide 3-hydroxy-L- aspartate + succinate + CO(2).
  • Some vitamin K-dependent coagulation factors, as well as synthetic peptides based on the structure of the first epidermal growth factor domain of human coagulation factor IX or X, can act as acceptors.
 13 A0A0B2PYP1 A0A0B2QHG0 A0A0B2QIJ4 A0A0B2QQ40 A0A0B2QZH3 A0A0B2RAD3 A0A0B2RNK6 A0A0B2RZC3 A0A0B2S3H6 A0A0B2SNQ2
(3 more...)
4-nitrophenylphosphatase. [EC: 3.1.3.41]
4-nitrophenyl phosphate + H(2)O = 4-nitrophenol + phosphate.
  • A number of other substances, including phenyl phosphate, 4-nitrophenyl sulfate, acetyl phosphate and glycerol phosphate, are not substrates.
 6 A0A0B2NZ06 A0A0B2QFK2 A0A0B2R487 A0A0B2RN77 A0A0B2RW94 A0A0B2SCF1
Peroxidase. [EC: 1.11.1.7]
2 phenolic donor + H(2)O(2) = 2 phenoxyl radical of the donor + 2 H(2)O.
    		 1 M4D5C6
    Glutaminyl-tRNA synthase (glutamine-hydrolyzing). [EC: 6.3.5.7]
    ATP + L-glutamyl-tRNA(Gln) + L-glutamine = ADP + phosphate + L-glutaminyl-tRNA(Gln) + L-glutamate.
    • In systems lacking discernible EC 6.1.1.18, glutaminyl-tRNA(Gln) is formed by a two-enzyme system.
    • In the first step, a nondiscriminating ligase (EC 6.1.1.24) mischarges tRNA(Gln) with glutamate, forming glutamyl-tRNA(Gln).
    • The glutamyl-tRNA(Gln) is not used in protein synthesis until the present enzyme converts it into glutaminyl-tRNA(Gln) (glutamyl- tRNA(Glu) is not a substrate for this reaction).
    • Ammonia or asparagine can substitute for the preferred substrate glutamine.
    		 1 A0A087SCL2