InterPro : IPR004516

Name  Histidine-tRNA ligase/ATP phosphoribosyltransferase regulatory subunit Short Name  HisRS/HisZ
Type  Family Description  This entry represents histidine-tRNA ligase (HisS or HisRS) and its paralogue, ATP phosphoribosyltransferase regulatory subunit (HisZ). Despite the significant sequential and structural similarity, HisRS and HisZ have different functions []. HisRS is a class IIa aminoacyl-tRNA synthetase (ligase), while HisZ is a regulatory subunit of the hetero-octameric ATP phosphoribosyl transferase that regulate reactions initiating histidine biosynthesis [, ]. From the phylogenetic analysis, HisZ proteins form a monophyletic group that attaches outside the predominant bacterial HisRS clade []. HisZ are represented in a highly divergent set of bacteria (including an aquificale, cyanobacteria, firmicutes, and proteobacteria), but are missing from other bacteria, including mycrobacteria and certain proteobacteria []. It has been suggested that the absences of HisZ from bacteria are due to its loss during evolution [].
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Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

2 Child Features

Id Name Short Name Type
IPR015807 Histidine-tRNA ligase His-tRNA-ligase Family
IPR004517 ATP phosphoribosyltransferase regulatory subunit HisZ Family

3 Contains

Id Name Short Name Type
IPR004154 Anticodon-binding Anticodon-bd Domain
IPR002314 Aminoacyl-tRNA synthetase, class II (G/ H/ P/ S), conserved domain aa-tRNA-synt_IIb_cons-dom Domain
IPR006195 Aminoacyl-tRNA synthetase, class II aa-tRNA-synth_II Domain

0 Found In

0 Parent Features

4 Publications

First Author Title Year Journal Volume Pages
Vega MC Regulation of the hetero-octameric ATP phosphoribosyl transferase complex from Thermotoga maritima by a tRNA synthetase-like subunit. 2005 Mol Microbiol 55 675-86
Champagne KS Activation of the hetero-octameric ATP phosphoribosyl transferase through subunit interface rearrangement by a tRNA synthetase paralog. 2005 J Biol Chem 280 34096-104
Merritt EA Crystal structures of trypanosomal histidyl-tRNA synthetase illuminate differences between eukaryotic and prokaryotic homologs. 2010 J Mol Biol 397 481-94
Bond JP Proteobacterial histidine-biosynthetic pathways are paraphyletic. 2000 J Mol Evol 50 339-47



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)