Protein Domain : IPR012582

Type:  Domain Name:  NUC194
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 [].This is domain B in the catalytic subunit of DNA-dependent protein kinases. Short Name:  NUC194

0 Child Features

0 Contains

1 Cross References

Identifier
PF08163

1 Found In

DB identifier Type Name
IPR016024 Domain Armadillo-type fold

5 GO Annotations

GO Term Gene Name
GO:0003677 IPR012582
GO:0004677 IPR012582
GO:0005524 IPR012582
GO:0006303 IPR012582
GO:0005634 IPR012582

5 Ontology Annotations

GO Term Gene Name
GO:0003677 IPR012582
GO:0004677 IPR012582
GO:0005524 IPR012582
GO:0006303 IPR012582
GO:0005634 IPR012582

0 Parent Features

25 Proteins

DB identifier UniProt Accession Secondary Identifier Organism Name Length
63567 I0YXU1 PAC:27392389 Coccomyxa subellipsoidea C-169 2536  
17614 PAC:27417165 Ostreococcus lucimarinus 3912  
Cre09.g397327.t1.1 A0A2K3DEN6 PAC:30781509 Chlamydomonas reinhardtii 6856  
Sphfalx0167s0024.1.p PAC:32617584 Sphagnum fallax 4146  
Pp3c9_15240V3.2.p A0A2K1K3A5 PAC:32914054 Physcomitrium patens 4098  
Pp3c9_15240V3.1.p A0A2K1K3A5 PAC:32914053 Physcomitrium patens 4098  
Pp3c9_15240V3.4.p A0A2K1K3A5 PAC:32914055 Physcomitrium patens 4098  
Pp3c9_15240V3.3.p PAC:32914056 Physcomitrium patens 4097  
Mapoly0069s0061.2.p A0A2R6WPH2 PAC:33018802 Marchantia polymorpha 4152  
Mapoly0069s0061.1.p A0A2R6WPH2 PAC:33018801 Marchantia polymorpha 4152  
Cz16g08300.t1 PAC:38239545 Chromochloris zofingiensis 3599  
Bobra.39_1s0001.1.p PAC:40704333 Botryococcus braunii 2932  
Sphmag06G108400.2.p PAC:41921526 Sphagnum magellanicum 3913  
Sphmag06G108400.1.p PAC:41921525 Sphagnum magellanicum 3922  
Sphmag06G108400.3.p PAC:41921528 Sphagnum magellanicum 3390  
Sphmag06G108400.4.p PAC:41921527 Sphagnum magellanicum 3399  
Sphfalx06G105000.2.p PAC:41973258 Sphagnum fallax 3985  
Sphfalx06G105000.1.p PAC:41973257 Sphagnum fallax 4146  
Sphfalx06G105000.3.p PAC:41973259 Sphagnum fallax 3406  
CepurR40.7G029300.1.p PAC:43027123 Ceratodon purpureus R40 4070  
CepurGG1.7G027900.1.p PAC:43047689 Ceratodon purpureus GG1 4070  
Ceric.1Z120700.3.p PAC:50630139 Ceratopteris richardii 2135  
Ceric.1Z120700.1.p PAC:50630137 Ceratopteris richardii 2993  
Ceric.1Z120700.2.p PAC:50630138 Ceratopteris richardii 2822  
Vocar.0009s0222.1.p PAC:32893448 Volvox carteri 4384  

5 Publications

First Author Title Year Journal Volume Pages PubMed ID
            3291115
            12368087
            12471243
            15078142
            15320712