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:

"
Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
".

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 15796: Proteasome subunit alpha type

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
Proteasome endopeptidase complex. [EC: 3.4.25.1]
Cleavage of peptide bonds with very broad specificity.
  • A 20-S protein composed of 28 subunits arranged in four rings of seven.
  • The outer rings are composed of alpha subunits, but the beta subunits forming the inner rings are responsible for peptidase activity.
  • In eukaryotic organisms there are up to seven different types of beta subunits, three of which may carry the N-terminal threonine residues that are the nucleophiles in catalysis, and show different specificities.
  • The molecule is barrel-shaped, and the active sites are on the inner surfaces.
  • Terminal apertures restrict access of substrates to the active sites.
  • Inhibited by mercurial reagents and some inhibitors of serine endopeptidases.
  • Belongs to peptidase family T1.
  • Formerly EC 3.4.22.21, EC 3.4.24.5 and EC 3.4.99.46.
20134 A0A010R0B7 A0A010R0B7 A0A010R3P6 A0A010R3P6 A0A010R3Y3 A0A010R3Y3 A0A010RC07 A0A010RC07 A0A010RQJ3 A0A010RQJ3
(20124 more...)
Ribonuclease P. [EC: 3.1.26.5]
Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
  • Essential for tRNA processing; generates 5'-termini of mature tRNA molecules.
2 U1NEZ8 U1NEZ8
DNA ligase (ATP). [EC: 6.5.1.1]
ATP + (deoxyribonucleotide)(n)-3'-hydroxyl + 5'-phospho- (deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) + AMP + diphosphate.
  • The enzyme catalyzes the ligation of DNA strands with 3'-hydroxyl and 5'-phosphate termini, forming a phosphodiester and sealing certain types of single-strand breaks in duplex DNA.
  • Catalysis occurs by a three-step mechanism, starting with the activation of the enzyme by ATP, forming a phosphoramide bond between adenylate and a lysine residue.
  • The adenylate group is then transferred to the 5'-phosphate terminus of the substrate, forming the capped structure 5'-(5'-diphosphoadenosine)-(DNA).
  • Finally, the enzyme catalyzes a nucleophilic attack of the 3'-OH terminus on the capped terminus, which results in formation of the phosphodiester bond and release of the adenylate.
  • RNA can also act as substrate, to some extent.
  • Cf. EC 6.5.1.2, EC 6.5.1.6 and EC 6.5.1.7.
2 I4YE06 I4YE06
UMP/CMP kinase. [EC: 2.7.4.14]
(1) ATP + (d)CMP = ADP + (d)CDP. (2) ATP + UMP = ADP + UDP.
  • This eukaryotic enzyme is a bifunctional enzyme that catalyzes the phosphorylation of both CMP and UMP with similar efficiency.
  • dCMP can also act as acceptor.
  • Different from the monofunctional prokaryotic enzymes EC 2.7.4.25, CMP kinase and EC 2.7.4.22, UMP kinase.
  • This eukaryotic enzyme is a bifunctional enzyme that catalyzes the phosphorylation of both CMP and UMP with similar efficiency.
  • dCMP can also act as acceptor.
  • Different from the monofunctional prokaryotic enzymes EC 2.7.4.25 and EC 2.7.4.22.
  • Formerly EC 2.7.4.5.
2 A0A1J9QWI9 A0A1J9QWI9