LIS - Legume Information System
Information about legume traits for crop improvement
GlycineMine
v5.1.0.3
Glycine data from LIS
v5.1.0.3
Glycine data from LIS
| Type | Homologous_superfamily |
| Description | Protein kinases ( ) modify other proteins by chemically adding phosphate groups to them. This process is fundamental to most signalling and regulatory processes in the eukaryotic cell [ ]. The protein kinases contain a catalytic core that is common to both serine/threonine and tyrosine protein kinases. The catalytic domain contains the nucleotide-binding site and the catalytic apparatus in an inter-lobe cleft. Structurally it shares functional and structural similarities with the ATP-grasp fold, which is found in enzymes that catalyse the formation of an amide bond. The three-dimensional fold of the protein kinase catalytic domain is similar to domains found in several other proteins. These include:the catalytic domain of phosphoinositide-3-kinase (PI3K), which phosphorylates phosphoinositides and, as such, is involved in a number of fundamental cellular processes such as apoptosis, proliferation, motility and adhesion [ ] choline kinase, which catalyses the ATP-dependent phosphorylation of choline during the biosynthesis of phosphatidylcholine [ ] 3',5'-aminoglycoside phosphotransferase type IIIa, a bacterial enzyme that confers resistance to a range of aminoglycoside antibiotics [ ] This superfamily represents the protein-kinase domain and other related domains that share a similar structure. |
| Short Name | Kinase-like_dom_sf |
