dual specificity phosphatase domain of slingshot homolog 1
Dual specificity protein phosphatase slingshot homolog 1 (SSH1), also called SSH-like protein 1, is part of the slingshot (SSH) family, whose members specifically dephosphorylate and reactivate Ser-3-phosphorylated cofilin (P-cofilin), an actin-binding protein that plays an essential role in actin filament dynamics. SSH1 links NOD1 signaling to actin remodeling, facilitating the changes that leads to NF-kappaB activation and innate immune responses. There are at least two human SSH1 isoforms reported: hSSH-1L (long) and hSSH-1S (short). As SSH family phosphatases, they contain an N-terminal, SSH family-specific non-catalytic (SSH-N) domain, followed by a short domain with similarity to the C-terminal domain of the chromatin-associated protein DEK, and a dual specificity phosphatase catalytic domain. They also contain C-terminal tails, differing in the lengths of the tail.
Feature 1: catalytic site [active site], 2 residue positions
Conserved feature residue pattern:C R
Evidence:
Comment:the catalytic cysteine initiates a nucleophilic attack on the phosphate group of the substrate, forming a transient phosphoenzyme intermediate and releasing the substrate dephosphorylated; the transition state is stabilized by the arginine present in the catalytic pocket