Protein Family Models

This family locates between the N-terminal domain and MMR_HSR1 50S ribosome-binding GTPase of GTP-binding HflX-like proteins. The full-length members bind and interact with the 50S ribosome and are GTPases, hydrolysing GTP/GDP/ATP/ADP. This region is unknown for its function. (from Pfam)

Date:

2024-08-14

This is the N-terminal region of GTP-binding HflX-like proteins. The full-length members bind and interact with the 50S ribosome and are GTPases, hydrolysing GTP/GDP/ATP/ADP. This N-terminal region is necessary for stability of the whole protein. [1]. 19109926. E. coli HflX interacts with 50S ribosomal subunits in presence of nucleotides. Jain N, Dhimole N, Khan AR, De D, Tomar SK, Sajish M, Dutta D, Parrack P, Prakash B;. Biochem Biophys Res Commun. 2009;379:201-205. [2]. 19181811. Properties of HflX, an enigmatic protein from Escherichia coli. Dutta D, Bandyopadhyay K, Datta AB, Sardesai AA, Parrack P;. J Bacteriol. 2009;191:2307-2314. [3]. 19824612. Toward understanding the function of the universally conserved GTPase HflX from Escherichia coli: a kinetic approach. Shields MJ, Fischer JJ, Wieden HJ;. Biochemistry. 2009;48:10793-10802. (from Pfam)

Date:

2024-10-16

GTR1 was first identified in S. cerevisiae as a suppressor of a mutation in RCC1. Biochemical analysis revealed that Gtr1 is in fact a G protein of the Ras family. The RagA/B proteins are the human homologues of Gtr1. Included in this family is the human Rag C, a novel protein that has been shown to interact with RagA/B [1,2,3,4]. [1]. 1620108. Putative GTP-binding protein, Gtr1, associated with the function of the Pho84 inorganic phosphate transporter in Saccharomyces cerevisiae. Bun-Ya M, Harashima S, Oshima Y;. Mol Cell Biol 1992;12:2958-2966. [2]. 7499430. Cloning of a novel family of mammalian GTP-binding proteins (RagA, RagBs, RagB1) with remote similarity to the Ras-related GTPases. Schurmann A, Brauers A, Massmann S, Becker W, Joost HG;. J Biol Chem 1995;270:28982-28988. [3]. 10388807. Saccharomyces cerevisiae putative G protein, Gtr1p, which forms complexes with itself and a novel protein designated as Gtr2p, negatively regulates the Ran/Gsp1p G protein cycle through Gtr2p. Nakashima N, Noguchi E, Nishimoto T;. Genetics 1999;152:853-867. [4]. 11073942. Novel G proteins, Rag C and Rag D, interact with GTP-binding proteins, Rag A and Rag B. Sekiguchi T, Hirose E, Nakashima N, Ii M, Nishimoto T;. J Biol Chem 2001;276:7246-7257. (from Pfam)

Date:

2024-10-16

This HMM identifies the P-loop-containing domain of large numbers of GTPases with ribosome-associated functions, including many involved in ribosome maturation (Der, Era, etc), ribosome rescue (HflX), and protein translation (InfB, Tuf, PrfC).

Date:

2024-10-16

HflX GTPase family protein similar to GTPase HflX, which is a GTP-binding protein with a GTP hydrolysis activity that is stimulated by binding to the 50S ribosome subunit, and it may play a role during protein synthesis or ribosome biogenesis

Date:

2024-04-29

This protein family is one of a number of homologous small, well-conserved GTP-binding proteins with pleiotropic effects. Bacterial members are designated HflX, following the naming convention in Escherichia coli where HflX is encoded immediately downstream of the RNA chaperone Hfq, and immediately upstream of HflKC, a membrane-associated protease pair with an important housekeeping function. Over large numbers of other bacterial genomes, the pairing with hfq is more significant than with hflK and hlfC. The gene from Homo sapiens in this family has been named PGPL (pseudoautosomal GTP-binding protein-like).

Gene:

hflX

Date:

2024-07-08