Macro domain, Af1521- and BAL-like family. The macro domain is a high-affinity ADP-ribose binding module found in a variety of proteins as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Some macro domains recognize poly ADP-ribose as a ligand. Previously identified as an Appr-1"-p (ADP-ribose-1"-monophosphate) processing activity, the macro domain may play roles in distinct ADP-ribose pathways, such as the ADP-ribosylation of proteins, an important post-translational modification which occurs in DNA repair, transcription, chromatin biology, and long-term memory formation, among other processes. The macro domains in this family show similarity to Af1521, a protein from Archaeoglobus fulgidus containing a stand-alone macro domain. Af1521 binds ADP-ribose and exhibits phosphatase activity toward Appr-1"-p. Also included in this family are the N-terminal (or first) macro domains of BAL (B-aggressive lymphoma) proteins which contain multiple macro domains. Most BAL proteins also contain a C-terminal PARP active site and are also named as PARPs. Human BAL1 (or PARP-9) was originally identified as a risk-related gene in diffuse large B-cell lymphoma that promotes malignant B-cell migration. Some BAL family proteins exhibit PARP activity. Poly (ADP-ribosyl)ation is an immediate DNA-damage-dependent post-translational modification of histones and other nuclear proteins. BAL proteins may also function as transcription repressors.
cd02907 is part of a hierarchy of related CD models. Use the graphical representation to navigate this hierarchy. cd02907 is a member of the superfamily cl00019.
cd02907 Sequence Cluster
Sub-family Hierarchy
Citing CDD
Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res. 37(D)205-10.
Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res. 37(D)205-10.
