v5.1.0.3
Cicer data from the Legume Information System
| Type | Family |
| Description | The PP-loop motif appears to be a modified version of the P-loop of nucleotide binding domain that is involved in phosphate binding [ ]. Named PP-motif, since it appears to be a part of a previously uncharacterised ATP pyrophophatase domain. ATP sulfurylases, Escherichia coli NtrL, and Bacillus subtilis OutB consist of this domain alone. In other proteins, the pyrophosphatase domain is associated with amidotransferase domains (type I or type II), a putative citrulline-aspartate ligase domain or a nitrilase/amidase domain.PP-loop ATPases are part of the HUP domain class (after HIGH-signature proteins, UspA, and PP-ATPase), along with the nucleotide-binding domains of class I aminoacyl-tRNA synthetases, UspA protein (USPA domains), photolyases, and electron transport flavoproteins (ETFP). The HUP domain is a distinct class of alpha/beta domain [ ].This group represents MJ1638-type predicted PP-loop ATPases. |
| Short Name | ATPase_PP-loop_MJ1638 |