| Analysis | rpsblast_cdd | Start | 83 |
| End | 179 | Strand | + |
| Length | 97 | Note | Gaps:46 |
| Hit Coverage | 80.61 | Hit Length | 165 |
| Hit Pident | 30.08 | E Val | 7e-09 |
| Hit Description | cd02908 Macro_Appr_pase_like Macro domain Appr-1"-pase_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 displaying 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. This family is composed of uncharacterized proteins that show similarity to Appr-1"-pase containing conserved putative active site residues. Appr-1"-pase is a phosphatase specific for ADP-ribose-1"-monophosphate.. | Hit Pcons | 9.02 |
| Name | Qrob_P0002670.2 |
| Protein Identifier |
Organism . Name |
Score | Score Type | Protein Description | Alias (in v1) | Code Enzyme | Gene Prediction Quality |
|---|---|---|---|---|---|---|---|
| Qrob_P0002670.2 | Quercus robur | 100.0 | egn | (M=1) PTHR11106//PTHR11106:SF27 - GANGLIOSIDE INDUCED DIFFERENTIATION ASSOCIATED PROTEIN 2-RELATED // SUBFAMILY NOT NAMED | validated |
Powered by
