The domain within your query sequence starts at position 8 and ends at position 181; the E-value for the Gtr1_RagA domain shown below is 2.1e-7.

KVLVLGDSGVGKSSLVHLLCHNQVLGNPSWTVGCSVDIRVHDYKEGTPEEKTYYIELWDV
GGSVGSASSVKSTRAVFYNSVNGIILVHDLTNKKSSQNLYRWSLEVLNRDAVPTGVLVTN
GDYDREQFADNQIPLLVIGTKLDQIHETKRHEVLIRTAFLAEDFNAEEINLDCT

Gtr1_RagA

Gtr1_RagA
PFAM accession number:PF04670
Interpro abstract (IPR006762):

GTR1 was first identified in Saccharomyces cerevisiae (Baker's yeast) as a suppressor of a mutation in RCC1. RCC1 catalyzes guanine nucleotide exchange on Ran, a well characterised nuclear Ras-like small G protein that plays an essential role in the import and export of proteins and RNAs across the nuclear membrane through the nuclear pore complex. RCC1 is located inside the nucleus, bound to chromatin. The concentration of GTP within the cell is ~30 times higher than the concentration of GDP, thus resulting in the preferential production of the GTP form of Ran by RCC1 within the nucleus.

Gtr1p is located within both the cytoplasm and the nucleus and has been reported to play a role in cell growth. 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 and Rag A and Gtr1p belong to the sixth subfamily of the Ras-like small GTPase superfamily [(PUBMED:11073942)].

GO function:GTP binding (GO:0005525)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Gtr1_RagA