Protein Domain : IPR000961

Type:  Domain Name:  AGC-kinase, C-terminal
Description:  Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyse the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyse the reverse process. Protein kinases fall into three broad classes, characterised with respect to substrate specificity []:Serine/threonine-protein kinasesTyrosine-protein kinasesDual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins)Protein kinase function is evolutionarily conserved from Escherichia coli to human []. Protein kinases play a role in a multitude of cellular processes, including division, proliferation, apoptosis, and differentiation []. Phosphorylation usually results in a functional change of the target protein by changing enzyme activity, cellular location, or association with other proteins. The catalytic subunits of protein kinases are highly conserved, and several structures have been solved [], leading to large screens to develop kinase-specific inhibitors for the treatments of a number of diseases [].The AGC (cAMP-dependent, cGMP-dependent and protein kinase C) protein kinase family embraces a collection of protein kinases that display a high degree of sequence similarity within their respective kinase domains. AGC kinase proteins are characterised by three conserved phosphorylation sites that critically regulate their function. The first one is located in an activation loop in the centre of the kinase domain. The two other phosphorylation sites are located outside the kinase domain in a conserved region on its C-terminal side, the AGC-kinase C-terminal domain. These sites serves as phosphorylation-regulated switches to control both intra- and inter-molecular interactions. Without these priming phosphorylations, the kinases are catalytically inactive [, , ].Several structures of the AGC-kinase C-terminal domain have been solved. The first phosphorylation site is located in a turn motif, the second one at the end of the domain in an hydrophobic pocket. In PKB the phosphorylated hydrophobic motif engages a hydrophobic groove within the N-lobe of the kinase domain which orders alpha helices close to the active site []. Short Name:  AGC-kinase_C

1 Child Features

DB identifier Type Name
IPR017892 Domain Protein kinase, C-terminal

0 Contains

2 Cross Referencess


3 Found Ins

DB identifier Type Name
IPR020684 Family Rho-associated protein kinase 1/2
IPR002374 Family cGMP-dependent kinase
IPR000239 Family GPCR kinase

3 GO Annotations

GO Term Gene Name Organism
GO:0004674 IPR000961
GO:0005524 IPR000961
GO:0006468 IPR000961

0 Parent Features

1185 Proteins

DB identifier UniProt Accession Secondary Identifier Organism Name Length
181752 D8SQ64 PAC:15418456 Selaginella moellendorffii 456  
83225 D8R2Q2 PAC:15412597 Selaginella moellendorffii 317  
112057 D8S980 PAC:15410338 Selaginella moellendorffii 972  
117203 D8SHG2 PAC:15403880 Selaginella moellendorffii 489  
179756 D8SHG4 PAC:15412360 Selaginella moellendorffii 527  
91298 D8REX3 PAC:15414173 Selaginella moellendorffii 530  
89070 D8RB45 PAC:15406334 Selaginella moellendorffii 756  
evm.model.supercontig_3.296 PAC:16416586 Carica papaya 1184  
evm.model.supercontig_3.372 PAC:16416671 Carica papaya 361  
evm.TU.contig_29663.1 PAC:16429720 Carica papaya 102  
evm.model.supercontig_165.21 PAC:16410361 Carica papaya 516  
evm.model.supercontig_28.121 PAC:16415862 Carica papaya 151  
evm.model.supercontig_49.23 PAC:16421090 Carica papaya 522  
evm.model.supercontig_64.71 PAC:16424307 Carica papaya 292  
evm.model.supercontig_678.1 PAC:16424802 Carica papaya 547  
evm.model.supercontig_7.126 PAC:16425027 Carica papaya 459  
evm.model.supercontig_84.83 PAC:16427369 Carica papaya 430  
evm.model.supercontig_86.71 PAC:16427627 Carica papaya 192  
evm.model.supercontig_1116.3 PAC:16405900 Carica papaya 155  
27651.m000097 B9T5A7 PAC:16798903 Ricinus communis 1289  
28492.m000480 B9SV26 PAC:16800960 Ricinus communis 575  
29739.m003581 B9RQT0 PAC:16807361 Ricinus communis 623  
29912.m005311 B9RK53 PAC:16813190 Ricinus communis 492  
29915.m000484 B9SRT9 PAC:16813499 Ricinus communis 481  
30147.m014030 B9R905 PAC:16820045 Ricinus communis 297  
30170.m013870 B9R7B8 PAC:16821714 Ricinus communis 522  
30170.m014013 B9R7R7 PAC:16821854 Ricinus communis 1106  
Cucsa.383560.1 A0A0A0LKM0 PAC:16982408 Cucumis sativus 551  
Cucsa.383560.2 A0A0A0LKM0 PAC:16982409 Cucumis sativus 551  
Cucsa.388210.1 A0A0A0K5D9 PAC:16982820 Cucumis sativus 557  

9 Publications

First Author Title Year Journal Volume Pages PubMed ID