InterPro domain: IPR037278

The ARFGAP domain was first identified in the cell cycle control GTPase activating protein (GAP) GCS1 [ 1 ]. GCS1 is important for the inactivation of the ADP ribosylation factor ARF a member of the Ras superfamily of GTP-binding proteins. GTP-bound form of ARF is essential for the maintenance of normal Golgi morphology, it participates in recruitment of coat proteins which are required for budding and fission of membranes. Before the fusion with an acceptor compartment the membrane must be uncoated. This step required the hydrolysis of GTP associated to ARF, a process dependent on the ARFGAP domain of GCS1 [ 2 ].

The ARFGAP domain contains a characteristic zinc finger motif (Cys-x2-Cys-x(16,17)-Cys-x2-Cys) which displays some similarity to the C4-type GATA zinc finger. The ARFGAP domain display no obvious similarity to other GAP proteins. However a C4-type zinc finger is also found in the ARD1 GAP domain [ 2 ].

This entry represents a structure domain containing the zinc finger motif that can also be found in bacterial protein RecO.

RecO is a DNA repair protein involved in damage avoidance-tolerance pathway(s) [ 3 ].

1. A member of a novel family of yeast 'zn-finger' proteins mediates the transition from stationary phase to cell proliferation. EMBO J. 13, 3812-21
2. Molecular characterization of the GTPase-activating domain of ADP-ribosylation factor domain protein 1 (ARD1). J. Biol. Chem. 273, 2553-60
3. Molecular analysis of the Escherichia coli recO gene. J. Bacteriol. 171, 3641-9