SMART: Pfam domain GTP1

The domain within your query sequence starts at position 71 and ends at position 222; the E-value for the GTP1_OBG domain shown below is 1.5e-49.

FVDHRRVLVRGGSGGSGMSCFHSEPRKEFGGPDGGDGGNGGHIILRVDQQVKSLSSVLSQ
YQGFSGEDGGSKNCSGRGGATLYIQVPVGTLVKEGDKIVADLSNLGDEYVAALGGAGGKG
NRFFLANDNRAPVTCTPGQPGQERVLYLELKT

GTP1_OBG

PFAM accession number:	PF01018
Interpro abstract (IPR006169):	Several proteins have recently been shown to contain the 5 structural motifs characteristic of GTP-binding proteins [ (PUBMED:1449490) ]. These include murine DRG protein; GTP1 protein from Schizosaccharomyces pombe; OBG protein from Bacillus subtilis; and several others. Although the proteins contain GTP-binding motifs and are similar to each other, they do not share sequence similarity to other GTP-binding proteins, and have thus been classed as a novel group, the GTP1/OBG family. As yet, the functions of these proteins is uncertain, but they have been shown to be important in development and normal cell metabolism [ (PUBMED:8462872) (PUBMED:2537815) ]. The N-terminal domain of GTPase Obg has the OBG fold, which is formed by three glycine-rich regions inserted into a small 8-stranded beta-sandwich these regions form six left-handed collagen-like helices packed and H-bonded together.

PFAM accession number:

PF01018

Interpro abstract (IPR006169):

Several proteins have recently been shown to contain the 5 structural motifs characteristic of GTP-binding proteins [ (PUBMED:1449490) ]. These include murine DRG protein; GTP1 protein from Schizosaccharomyces pombe; OBG protein from Bacillus subtilis; and several others. Although the proteins contain GTP-binding motifs and are similar to each other, they do not share sequence similarity to other GTP-binding proteins, and have thus been classed as a novel group, the GTP1/OBG family. As yet, the functions of these proteins is uncertain, but they have been shown to be important in development and normal cell metabolism [ (PUBMED:8462872) (PUBMED:2537815) ].

The N-terminal domain of GTPase Obg has the OBG fold, which is formed by three glycine-rich regions inserted into a small 8-stranded beta-sandwich these regions form six left-handed collagen-like helices packed and H-bonded together.

This is a PFAM domain. For full annotation and more information, please see the PFAM entry GTP1_OBG