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von Willebrand factor type A domain
VWA domain-containing protein
Vault protein inter-alpha-trypsin domain
Inter-alpha-trypsin inhibitors (ITIs) consist of one light chain and a variable set of heavy chains. ITIs play a role in extracellular matrix (ECM) stabilisation and tumour metastasis as well as in plasma protease inhibition [1]. The vault protein inter-alpha-trypsin (VIT) domain described here is found to the N-terminus of a von Willebrand factor type A domain (Pfam:PF00092) in ITI heavy chains (ITIHs) and their precursors. [1]. 14744536. ITIH5, a novel member of the inter-alpha-trypsin inhibitor heavy chain family is downregulated in breast cancer. Himmelfarb M, Klopocki E, Grube S, Staub E, Klaman I, Hinzmann B, Kristiansen G, Rosenthal A, Durst M, Dahl E;. Cancer Lett 2004;204:69-77. [2]. 10830112. VIT-1: the second member of a new branch of the von Willebrand factor A domain superfamily. Mayne R, Ren ZX, Liu J, Cook T, Carson M, Narayana S;. Biochem Soc Trans. 1999;27:832-835. (from Pfam)
VIT domain-containing protein
protein kinase
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)
protein kinase domain-containing protein
4-Cys prefix domain-containing protein
Most proteins with this N-terminal domain are protein serine/threonine protein kinases that resemble eukaryotic ribosomal protein S6 kinase and the Mycobacterium tuberculosis serine/threonine protein kinases PknA and PknB, although those proteins lack this domain. Some, however, are protein serine/threonine phosphatases. Members of this domain family have an almost perfectly invariant CxxPxC and CxxCG motifs at the two ends of an N-terminal 22 to 25-amino region that begins the seed alignment for the HMM. AlphaFold predicted structure A0A3E0L7C2 shows this region to form a discrete N-terminal domain with very high pLDDT scores.
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