InterPro : IPR011063

Name  tRNA(Ile)-lysidine/2-thiocytidine synthase Short Name  tRNA-lysidine/thiocyt_synth
Type  Domain Description  This entry represents the PP-loop motif superfamily [,]. The PP-loop motif appears to be a modified version of the P-loop of nucleotide binding domain that is involved in phosphate binding []. Named PP-motif, since it appears to be a part of a previously uncharacterised ATP pyrophophatase domain. ATP sulfurylases, Escherichia coliNtrL, and Bacillus subtilisOutB consist of this domain alone. In other proteins, the pyrophosphatase domain is associated with amidotransferase domains (type I or type II), a putative citrulline-aspartate ligase domain or a nitrilase/amidase domain.
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Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

1 Child Features

Id Name Short Name Type
IPR012795 Lysidine-tRNA(Ile) synthetase, N-terminal Lysidine-tRNA-synth_N Domain

0 Contains

1 Found In

Id Name Short Name Type
IPR012089 2-thiocytidine tRNA biosynthesis protein, TtcA 2-thiocytidine_tRNA_synth_TtcA Family

1 Parent Features

Id Name Short Name Type
IPR014729 Rossmann-like alpha/beta/alpha sandwich fold Rossmann-like_a/b/a_fold Domain

2 Publications

First Author Title Year Journal Volume Pages
Bork P A P-loop-like motif in a widespread ATP pyrophosphatase domain: implications for the evolution of sequence motifs and enzyme activity. 1994 Proteins 20 347-55
Deyrup AT Chemical modification and site-directed mutagenesis of conserved HXXH and PP-loop motif arginines and histidines in the murine bifunctional ATP sulfurylase/adenosine 5'-phosphosulfate kinase. 1999 J Biol Chem 274 28929-36



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)