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:

"
HUPs
".

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 87272: Probable arginine--tRNA ligase, cytoplasmic

There are 6 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
Arginine--tRNA ligase. [EC: 6.1.1.19]
ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg).
    16026 A0A009GEA3 A0A009GEA3 A0A009NFU1 A0A009NFU1 A0A010Q2H0 A0A010Q2H0 A0A010Q7J3 A0A010Q7J3 A0A010SQ67 A0A010SQ67
    (16016 more...)
    DTMP kinase. [EC: 2.7.4.9]
    ATP + dTMP = ADP + dTDP.
      2 A0A0G1TA74 A0A0G1TA74
      Calcium-transporting ATPase. [EC: 3.6.3.8]
      ATP + H(2)O + Ca(2+)(Side 1) = ADP + phosphate + Ca(2+)(Side 2).
      • P-type ATPase that undergoes covalent phosphorylation during the transport cycle.
      • This enzyme family comprises three types of Ca(2+)-transporting enzymes that are found in the plasma membrane, the sarcoplasmic reticulum and in Saccharomyces cerevisiae.
      • The first and third transport one ion per ATP hydrolyzed, whereas the second transports two ions.
      • Formerly EC 3.6.1.38.
      2 R9AIV1 R9AIV1
      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.
      2 A0A0G2GSN8 A0A0G2GSN8
      DNA helicase. [EC: 3.6.4.12]
      ATP + H(2)O = ADP + phosphate.
      • DNA helicases utilize the energy from ATP hydrolysis to unwind double-stranded DNA.
      • Some of them unwind duplex DNA with a 3' to 5' polarity (1,3,5,8), other show 5' to 3' polarity (10,11,12,13) or unwind DNA in both directions (14,15).
      • Some helicases unwind DNA as well as RNA (4,9).
      • May be identical with EC 3.6.4.13 (RNA helicase).
      2 A0A0B7MU10 A0A0B7MU10
      Protein S-acyltransferase. [EC: 2.3.1.225]
      Palmitoyl-CoA + [protein]-L-cysteine = [protein]-S-palmitoyl-L-cysteine + CoA.
      • The enzyme catalyzes the posttranslational protein palmitoylation that plays a role in protein-membrane interactions, protein trafficking, and enzyme activity.
      • Palmitoylation increases the hydrophobicity of proteins or protein domains and contributes to their membrane association.
      2 A0A0J7KNJ1 A0A0J7KNJ1