577
Views
5
CrossRef citations to date
0
Altmetric
Perspective

Novel aspects of Cell Division Cycle and Apoptosis Regulator 1 (CCAR1) protein in Morus notabilis: an in silico approach

ORCID Icon & ORCID Icon
Article: 1795396 | Received 26 Jun 2020, Accepted 09 Jul 2020, Published online: 21 Jul 2020

Figures & data

Figure 1. (a) iTOL server has been used to construct the phylogenetic tree of CCAR1 protein sequences. (b) Identification of conserved motifs of CCAR1 protein family. (c) The positions of the motifs are denoted by P1, P2, P3, P4, and P5. Conserved domain structure of M. notabilis CCAR1 protein along with predicted fold/unfold property. Despite Nudix/DBC1 homology domain, MAEBL and calmodulin (CaM) domains are also found in C-terminal of CCAR1 protein. Deleted in breast cancer domain and it homologs from diverse eukaryotes are a catalytically inactive version of the Nudix hydrolase (MutT) domain. It is predicted to bind NAD metabolites and regulate the activity of SIRT1 or related deacetylases by sensing the soluble products or substrates of the NAD-dependent deacetylation reaction.

Figure 1. (a) iTOL server has been used to construct the phylogenetic tree of CCAR1 protein sequences. (b) Identification of conserved motifs of CCAR1 protein family. (c) The positions of the motifs are denoted by P1, P2, P3, P4, and P5. Conserved domain structure of M. notabilis CCAR1 protein along with predicted fold/unfold property. Despite Nudix/DBC1 homology domain, MAEBL and calmodulin (CaM) domains are also found in C-terminal of CCAR1 protein. Deleted in breast cancer domain and it homologs from diverse eukaryotes are a catalytically inactive version of the Nudix hydrolase (MutT) domain. It is predicted to bind NAD metabolites and regulate the activity of SIRT1 or related deacetylases by sensing the soluble products or substrates of the NAD-dependent deacetylation reaction.
Supplemental material

Supplemental Material

Download MS Word (25.9 KB)

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.