{PDOC51466} {PS51466; PINIT} {BEGIN} ************************ * PINIT domain profile * ************************ The Siz/PIAS RING family of SUMO E3 ligases structure reveals a modular architecture that includes an N-terminal PINIT domain, a central SP-RING domain (see ), and a unique C-terminal domain (SP-CTD). The N- terminal PINIT domain is formed by two antiparallel beta sheets; one includes beta1, beta2, beta4, and beta9, and the other includes beta3, beta5, and beta8 (see ). The beta sheets are connected by protruding loops (L1, L2, and L3) that join strands beta2-3, beta4-5, and beta8-9 at one end of the molecule, while beta3-4 and beta5-8 are connected by alpha helix alpha1 and a loop, respectively, on the opposite surface [1]. Most E3 ligases achieve substrate specificity by recruiting the E2~Ub/Ubl thioester and substrate into a complex to promote conjugation. The PINIT domain serves as a scaffold to coordinate PCNA to promote SUMO conjugation to both consensus and nonconsensus lysine side chains [1]. The profile we developed covers the entire PINIT domain. -Sequences known to belong to this class detected by the profile: ALL. -Other sequence(s) detected in Swiss-Prot: NONE. -Last update: October 2009 / First entry. [ 1] Yunus A.A., Lima C.D. "Structure of the Siz/PIAS SUMO E3 ligase Siz1 and determinants required for SUMO modification of PCNA." Mol. Cell 35:669-682(2009). PubMed=19748360; DOI=10.1016/j.molcel.2009.07.013 -------------------------------------------------------------------------------- PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html -------------------------------------------------------------------------------- {END}