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CATH Superfamily 3.40.250.10

Rhodanese-like 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:

"
Rhodanese-like 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 16151: tRNA s(4)U8 sulfurtransferase

There are 2 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
TRNA sulfurtransferase. [EC: 2.8.1.4]
L-cysteine + 'activated' tRNA = L-serine + tRNA containing a thionucleotide.
  • A group of enzymes transferring sulfur to various nucleotides in a tRNA chain, producing residues such as 4-thiouridylate.
  • With some enzymes mercaptopyruvate can act as sulfur donor.
 1973 A0A010SVT8 A0A011P4T2 A0A014NC82 A0A017ILI9 A0A022PP82 A0A023CFI6 A0A023E7Q5 A0A023RIB7 A0A023V832 A0A023WXU3
(1963 more...)
CCA tRNA nucleotidyltransferase. [EC: 2.7.7.72]
A tRNA precursor + 2 CTP + ATP = a tRNA with a 3' CCA end + 3 diphosphate.
  • The acylation of all tRNAs with an amino acid occurs at the terminal ribose of a 3' CCA sequence.
  • The CCA sequence is added to the tRNA precursor by stepwise nucleotide addition performed by a single enzyme that is ubiquitous in all living organisms.
  • Although the enzyme has the option of releasing the product after each addition, it prefers to stay bound to the product and proceed with the next addition.
  • Formerly EC 2.7.7.21 and EC 2.7.7.25.
 1 A0A1L9ESZ7
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