| Primary Identifier | IPR015039 | Type | Domain |
| Short Name | NCF1_C |
| description | NCF1 (also known as NADPH oxidase subunit p47Phox) is one of the cytosolic regulatory components of NADPH oxidase and consists of a PX domain at the N-terminal, two tandem SH3 domains, a polybasic or autoinhibitory region (PBR/AIR, an arginine/lysine rich region) and a proline-rich region at the C-terminal. In the resting state, the SH3 domains of NCF1 are masked by an intramolecular interaction with the PBR/AIR, which maintains the enzyme in an inactive form []. This entry represents the C-terminal domain which contains conserved PxxP motifs that allow binding to SH3 domains, with subsequent activation of the NADPH oxidase, and generation of superoxide, which plays a crucial role in host defence against microbial infection []. |
