Protein Family Models

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 [1]; Serine/threonine-protein kinases, tyrosine-protein kinases, and dual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins). This entry represents the catalytic domain found in a number of serine/threonine- and tyrosine-protein kinases. It does not include the catalytic domain of dual specificity kinases. [1]. 3291115. The protein kinase family: conserved features and deduced phylogeny of the catalytic domains. Hanks SK, Quinn AM, Hunter T;. Science. 1988;241:42-52. [2]. 1956325. Protein kinase catalytic domain sequence database: identification of conserved features of primary structure and classification of family members. Hanks SK, Quinn AM;. Methods Enzymol 1991;200:38-62. [3]. 7768349. Protein kinases 6. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification. Hanks SK, Hunter T;. FASEB J 1995;9:576-596. [4]. 9020587. The protein kinases of budding yeast: six score and more. Hunter T, Plowman GD;. Trends Biochem Sci 1997;22:18-22. (from Pfam)

Date:

2024-10-16

This HMM describes a region found in AarF/ABC1/UbiB family proteins. We do not use the term ABC1 (activator of bc1 complex) in protein product names assigned because of the risk of confusion with ABC (ATP-binding cassette) transporter proteins.

Date:

2024-10-16

The universal stress protein UspA Swiss:P28242 [1] is a small cytoplasmic bacterial protein whose expression is enhanced when the cell is exposed to stress agents. UspA enhances the rate of cell survival during prolonged exposure to such conditions, and may provide a general "stress endurance" activity. The crystal structure of Haemophilus influenzae UspA [3] reveals an alpha/beta fold similar to that of the Methanococcus jannaschii MJ0577 protein, which binds ATP [2], though UspA lacks ATP-binding activity. [1]. 8152377. Expression and role of the universal stress protein, UspA, of Escherichia coli during growth arrest. Nystrom T, Neidhardt FC;. Mol Microbiol 1994;11:537-544. [2]. 9860944. Structure-based assignment of the biochemical function of a hypothetical protein: a test case of structural genomics. Zarembinski TI, Hung LW, Mueller-Dieckmann HJ, Kim KK, Yokota H, Kim R, Kim SH;. Proc Natl Acad Sci U S A 1998;95:15189-15193. [3]. 11738040. Structure of the universal stress protein of Haemophilus influenzae. Sousa MC, McKay DB;. Structure (Camb) 2001;9:1135-1141. (from Pfam)

Date:

2024-10-16

Date:

2024-11-05

serine/threonine protein kinase catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates; similar to Bacillus subtilis serine/threonine-protein kinase YbdM

Date:

2024-05-17