DBC1/CCAR2 and CCAR1 Are Largely Disordered Proteins that Have Evolved from One Common Ancestor

Table 1

The domain structure and function of human DBC1 and CCAR1. The domains for hDBC1 and hCCAR1 are depicted along with the amino acid boundaries for each domain. The known or predicted function of each of the conserved domains is listed.

	Domain Function
	Homology to an RNA-binding domain.
	Nuclear localization signal. Acetylation of the NLS in DBC1 regulates nuclear localization.
	Likely non-functional in CCAR1. Regulation of a diverse set of cellular pathways in DBC1.
	Catalytically inactive hydrolase domain in DBC1 and CCAR1. Predicted to function as a sensor in DBC1 that may bind to NAD metabolites and regulate SIRT1.
	Homology to a putative DNA-binding motif predicted to be involved in chromosomal organization.
	Inactive variant of a calcium dependent regulator of multiple cellular processes.
	Predicted protein-protein interaction motif.

Domain Boundary References: a: [8], b: [9], c: [14], d: [15].