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HSP20-like domain found in ArsA
This domain is found at the C-terminus of ArsA like proteins. This domain is related to HSP20. (from Pfam)
AAA family ATPase
This family includes a wide variety of AAA domains including some that have lost essential nucleotide binding residues in the P-loop. (from Pfam)
P-loop NTPase
This family contains ATPases involved in plasmid partitioning [1]. It also contains the cytosolic Fe-S cluster assembling factor NBP35 which is required for biogenesis and export of both ribosomal subunits [2]. [1]. 2149583. A family of ATPases involved in active partitioning of diverse bacterial plasmids. Motallebi-Veshareh M, Rouch DA, Thomas CM;. Mol Microbiol 1990;4:1455-1463. [2]. 15728363. The eukaryotic P loop NTPase Nbp35: an essential component of the cytosolic and nuclear iron-sulfur protein assembly machinery. Hausmann A, Aguilar Netz DJ, Balk J, Pierik AJ, Muhlenhoff U, Lill R;. Proc Natl Acad Sci U S A. 2005;102:3266-3271. (from Pfam)
CobQ/CobB/MinD/ParA nucleotide binding domain
This family consists of various cobyrinic acid a,c-diamide synthases. These include CbiA Swiss:P29946 and CbiP Swiss:Q05597 from S.typhimurium [4], and CobQ Swiss:Q52686 from R. capsulatus [3]. These amidases catalyse amidations to various side chains of hydrogenobyrinic acid or cobyrinic acid a,c-diamide in the biosynthesis of cobalamin (vitamin B12) from uroporphyrinogen III. Vitamin B12 is an important cofactor and an essential nutrient for many plants and animals and is primarily produced by bacteria [4]. The family also contains dethiobiotin synthetases as well as the plasmid partitioning proteins of the MinD/ParA family [6]. [1]. 9742225. Cobalamin (vitamin B12) biosynthesis: identification and characterization of a Bacillus megaterium cobI operon. Raux E, Lanois A, Warren MJ, Rambach A, Thermes C;. Biochem J 1998;335:159-166. [2]. 9742226. Cobalamin (vitamin B12) biosynthesis: functional characterization of the Bacillus megaterium cbi genes required to convert uroporphyrinogen III into cobyrinic acid a,c-diamide. Raux E, Lanois A, Rambach A, Warren MJ, Thermes C;. Biochem J 1998;335:167-173. [3]. 7635831. Identification and sequence analysis of genes involved in late steps in cobalamin (vitamin B12) synthesis in Rhodobacter capsulatus. Pollich M, Klug G;. J Bacteriol 1995;177:4481-4487. [4]. 8501034. Characterization of the cobalamin (vitamin B12) biosynthetic genes of Salmonella typhimurium. Roth JR, Lawrence JG, Rubenfield M, Kieffer-Higgins S, Church GM;. J Bacteriol 1993;175:3303-3316. [5]. 10966576. The synthetase domains of cobalamin biosynthesis amidotransferases cobB and cobQ belong to a new family of AT. TRUNCATED at 1650 bytes (from Pfam)
ArsA-related P-loop ATPase
This Pfam family represents a conserved domain, which is sometimes repeated, in an anion-transporting ATPase. The ATPase is involved in the removal of arsenate, antimonite, and arsenate from the cell. [1]. 1704144. The plasmid-encoded arsenical resistance pump: an anion-translocating ATPase. Rosen BP;. Res Microbiol 1990;141:336-341. (from Pfam)
ArsA family ATPase
ArsA family ATPase with similarity to Escherichia coli arsenical pump-driving ATPase, an anion-transporting ATPase that catalyzes the extrusion of the oxyanions arsenite, antimonite, and arsenate
TRC40/GET3/ArsA family transport-energizing ATPase
Members of this family are ATPases that energize transport, although with different partner proteins for different functions. Recent findings show that TRC40 (GET3 in yeast) in involved in the insertion of tail-anchored membrane proteins in eukaryotes. A similar function is expected for members of this family in archaea. However, the earliest discovery of a function for this protein family is ArsA, an arsenic resistance protein that partners with ArsB (see PF02040) for As(III) efflux.
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