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CATH Superfamily 1.10.510.10

Transferase(Phosphotransferase) domain 1

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:

"
Transferase(Phosphotransferase) 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 79228: Related to Serine/threonine-protein kinase

There are 3 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
Non-specific serine/threonine protein kinase. [EC: 2.7.11.1]
ATP + a protein = ADP + a phosphoprotein.
  • This is a heterogeneous group of serine/threonine protein kinases that do not have an activating compound and are either non-specific or their specificity has not been analyzed to date.
  • Formerly EC 2.7.1.37 and EC 2.7.1.70.
 50 A0A061HZP8 A0A061HZP8 A0A061I237 A0A061I237 A0A0L8VQX9 A0A0L8VQX9 A0A0S2Z4D1 A0A0S2Z4D1 A0A178UN27 A0A178UN27
(40 more...)
Calcium/calmodulin-dependent protein kinase. [EC: 2.7.11.17]
ATP + a protein = ADP + a phosphoprotein.
  • Requires calmodulin.
  • A wide range of proteins can act as acceptor, including vimentin, synapsin, glycogen synthase, myosin light-chains and the microtubule- associated tau protein.
  • Not identical with EC EC 2.7.11.18 or EC 2.7.11.26.
  • Formerly EC 2.7.1.120 and EC 2.7.1.123.
 32 A0A024RBQ0 A0A024RBQ0 A0A0F8AXB5 A0A0F8AXB5 A2R9L6 A2R9L6 B6HGS2 B6HGS2 E0VY77 E0VY77
(22 more...)
Methionyl aminopeptidase. [EC: 3.4.11.18]
Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.
  • This membrane-bound enzyme, which is present in both prokaryotes and eukaryotes, releases the initiator methionine from nascent peptides.
  • The activity is dependent on the identity of the second, third and fourth amino acid residues of the target protein, but in general the enzyme acts only when the penultimate residue is small and uncharged (e.g. Gly, Ala, Cys, Ser, Thr, and Val).
  • Belongs to peptidase family M24A.
 2 F4PI41 F4PI41
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