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.
« Back to all FunFams

FunFam 88701: Probable glutamate--tRNA ligase, cytoplasmic

There are 5 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
Glutamine--tRNA ligase. [EC: 6.1.1.18]
ATP + L-glutamine + tRNA(Gln) = AMP + diphosphate + L-glutaminyl- tRNA(Gln).
    12328 A0A009FMX8 A0A009FMX8 A0A009GJU2 A0A009GJU2 A0A009H9I9 A0A009H9I9 A0A009HIB0 A0A009HIB0 A0A009HRF2 A0A009HRF2
    (12318 more...)
    Glutamate--tRNA ligase. [EC: 6.1.1.17]
    ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu).
      688 A0A023B965 A0A023B965 A0A031LMQ5 A0A031LMQ5 A0A060HN78 A0A060HN78 A0A060S2Q8 A0A060S2Q8 A0A060S360 A0A060S360
      (678 more...)
      Proline--tRNA ligase. [EC: 6.1.1.15]
      ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro).
        8 B3M314 B3M314 B4N9E6 B4N9E6 P28668 P28668 Q298M5 Q298M5
        Glutamate--tRNA(Gln) ligase. [EC: 6.1.1.24]
        ATP + L-glutamate + tRNA(Glx) = AMP + diphosphate + L-glutamyl-tRNA(Glx).
        • When this enzyme acts on tRNA(Glu), it catalyzes the same reaction as EC 6.1.1.17.
        • It has, however, diminished discrimination, so that it can also form glutamate-tRNA(Gln).
        • This relaxation of specificity has been found to result from the absence of a loop in the tRNA that specifically recognizes the third position of the anticodon.
        • This accounts for the ability of this enzyme in, for example, Bacillus subtilis, to recognize both tRNA(1)(Gln) (UUG anticodon) and tRNA(Glu) (UUC anticodon) but not tRNA(2)(Gln) (CUG anticodon).
        • The ability of this enzyme to recognize both tRNA(Glu) and one of the tRNA(Gln) isoacceptors derives from their sharing a major identity element, a hypermodified derivative of U34 (5-methylaminomethyl-2- thiouridine).
        • The glutamyl-tRNA(Gln) is not used in protein synthesis until it is converted by EC 6.3.5.7 into glutaminyl-tRNA(Gln).
        6 A0A0W8F4F0 A0A0W8F4F0 A0A0W8FFP8 A0A0W8FFP8 D7FN57 D7FN57
        Phosphatidate cytidylyltransferase. [EC: 2.7.7.41]
        CTP + phosphatidate = diphosphate + CDP-diacylglycerol.
          2 F0YCB2 F0YCB2