Your browser is unable to support new features implemented in HTML5 and CSS3 to render this site as intended. Your experience may suffer from functionality degradation but the site should remain usable. We strongly recommend the latest version of Google Chrome, OS X Safari or Mozilla Firefox. As Safari is bundled with OS X, if you are unable to upgrade to a newer version of OS X, we recommend using an open source browser. Dismiss message

IPR030389

Description

IPR030389 is a FeoB-type guanine nucleotide-binding (G) domain.

<p>The P-loop guanosine triphosphatases (GTPases) control a multitude of biological processes, ranging from cell division, cell cycling, and signal transduction, to ribosome assembly and protein synthesis. GTPases exert their control by interchanging between an inactive GDP-bound state and an active GTP-bound state, thereby acting as molecular switches. The common denominator of GTPases is the highly conserved guanine nucleotide-binding (G) domain that is responsible for binding and hydrolysis of guanine nucleotides.</p> <p>The FeoB family of GTPases is widespread, although not ubiquitous, in Bacteria and Archaea, but missing from Eukaryota. FeoB is involved in the uptake of ferrous iron (Fe(2+)), an important cofactor in biological electron transfer and catalysis. Most of the FeoB proteins contain an N-terminal G-domain, connected by an entirely α-helical linker peptide to the membrane domain with 8 to 12 predicted membrane-spanning α-helices, while in some organisms the G-domain is expressed separately as a soluble protein. The FeoB- type G domain belongs to the TrmE-Era-EngA-EngB-Septin-like (TEES) superfamily of the TRAFAC class GTPases.</p> <p>The structure of the FeoB-type G domain follows the typical fold of small GTP- binding proteins, consisting of a seven-stranded β-sheet surrounded by five α-helices. The ~170-residue FeoB-type G domain harbours five short amino-acid motifs (G1-G5) that are critical in the binding of both a magnesium (Mg(2+)) ion and the guanine nucleotide. The G1 motif (GxxxxGKS/T) (P-loop) is in position to stabilise the beta- and gamma-phosphates of GTP by hydrogen bonds donated by main-chain amides. The threonine of the G2 motif (P/AGxT) coordinates the Mg(2+). The G3 motif (DxxG) interacts with the Mg(2+) and an oxygen of the gamma-phosphate. The G4 motif (NxxD) is involved in recognition of the guanine nucleotide by forming hydrogen bonds to the guanine base. The G5 motif (S/VSTV]) is, despite low sequence conservation, attributed to critical guanine base coordination [[cite:PUB00013952], [cite:PUB00052758], [cite:PUB00053086], [cite:PUB00058539], [cite:PUB00054426], [cite:PUB00054907]].</p>

This description is obtained from EB-eye REST.

Associated GO terms

GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on , while the GO metadata was last updated on .

GO term Namespace Name Definition Relationships
Molecular function GTP binding Interacting selectively and non-covalently with GTP, guanosine triphosphate.

Associated Lotus transcripts 3

Transcript Name Description Predicted domains Domain count
PREDICTED: nucleolar GTP-binding protein 1-like [Glycine max] gi|356527250|ref|XP_003532225.1| 13
PREDICTED: nucleolar GTP-binding protein 1-like [Glycine max] gi|356527250|ref|XP_003532225.1| 14
Nucleolar GTP-binding protein 1; TAIR: AT1G80770.1 P-loop containing nucleoside triphosphate hydrolases superfamily protein; Swiss-Prot: sp|Q6FRV0|NOG1_CANGA Nucleolar GTP-binding protein 1; TrEMBL-Plants: tr|K7LAJ8|K7LAJ8_SOYBN Uncharacterized protein; Found in the gene: LotjaGi1g1v0597800 17

Co-occuring domains 1

A list of co-occurring predicted domains within the L. japonicus gene space:

Predicted domain Source Observations Saturation (%)
cd01897 CDD 1 33.33