Years of evolution have kept actin conserved throughout various clades of life. It is an essential protein starring in many cellular processes. In a primitive eukaryote named Entamoeba histolytica, actin directs the process of phagocytosis. A finely tuned coordination between various actin‐binding proteins (ABPs) choreographs this process and forms one of the virulence factors for this protist pathogen. The ever‐expanding world of ABPs always has space to accommodate new and varied types of proteins to the earlier existing repertoire. In this article, we report the identification of 390 ABPs from Entamoeba histolytica. These proteins are part of diverse families that have been known to regulate actin dynamics. Most of the proteins are primarily uncharacterized in this organism; however, this study aims to annotate the ABPs based on their domain arrangements. A unique characteristic about some of the ABPs found is the combination of domains present in them unlike any other reported till date. Calponin domain‐containing proteins formed the largest group among all types with 38 proteins, followed by 29 proteins with the infamous BAR domain in them, and 23 proteins belonging to actin‐related proteins. The other protein families had a lesser number of members. Presence of exclusive domain arrangements in these proteins could guide us to yet unknown actin regulatory mechanisms prevalent in nature. This article is the first step to unraveling them.

中文翻译：

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溶组织内阿米巴中的肌动蛋白细胞骨架乐团。


多年的进化使肌动蛋白在生命的各个分支中保持保守。它是许多细胞过程中的重要蛋白质。在一种名为溶组织内阿米巴的原始真核生物中，肌动蛋白指导吞噬过程。各种肌动蛋白结合蛋白（ABP）之间的精细协调精心设计了这一过程，并形成了这种原生病原体的毒力因子之一。不断扩大的 ABP 世界总是有空间容纳新的和不同类型的蛋白质到早期现有的库中。在本文中，我们报告了从溶组织内阿米巴中鉴定出 390 个 ABP。这些蛋白质属于已知调节肌动蛋白动力学的不同家族的一部分。大多数蛋白质在该生物体中基本上是未知的；然而，本研究旨在根据 ABP 的领域排列对其进行注释。所发现的一些 ABP 的一个独特特征是其中存在的域组合，这与迄今为止报道的任何其他 ABP 不同。含有钙调蛋白结构域的蛋白质是所有类型中最大的一组，共有 38 种蛋白质，其次是 29 种含有臭名昭著的 BAR 结构域的蛋白质，以及 23 种属于肌动蛋白相关蛋白质。其他蛋白质家族的成员数量较少。这些蛋白质中存在的专有结构域排列可以引导我们发现自然界中普遍存在的未知肌动蛋白调节机制。本文是解开它们的第一步。