The domain within your query sequence starts at position 368 and ends at position 558; the E-value for the RGS-like domain shown below is 8.6e-87.

QCSCFQSIELLKSRPAHLAVFLHHVVSQFDPATLLCYLYSDLYKQTNSKETRRVFLEFHQ
FFLDRSAHLKVPVPEEISVDLEKRRPELIPEDLHRLYIQTMQERVHPEVQRHLEDFRQKR
SMGLTLAESELTKLDAERDKDRGTLEKERACAEQIVTKIEEVLMTAQAVEEERSSTMQYV
ILMYMKYLGVK

RGS-like

RGS-like
PFAM accession number:PF09128
Interpro abstract (IPR015212):

This entry represents a domain consisting of twelve helices that fold into a compact structure that contains the overall structural scaffold observed in other regulator of G protein signalling (RGS) proteins and three additional helical elements that pack closely to it. Helices 1-9 comprise the RGS fold, in which helices 4-7 form a classic antiparallel bundle adjacent to the other helices. Like other RGS structures, helices 7 and 8 span the length of the folded domain and form essentially one continuous helix with a kink in the middle. Helices 10-12 form an apparently stable C-terminal extension of the structural domain, and although other RGS proteins lack this structure, these elements are intimately associated with the rest of the structural framework by hydrophobic interactions. This domain binds to active G-alpha proteins, promoting GTP hydrolysis by the alpha subunit of heterotrimeric G proteins, thereby inactivating the G protein and rapidly switching off G protein-coupled receptor signalling pathways [(PUBMED:11470431)].

This RGS-like domain is found in Rho guanine nucleotide exchange factors (RhoGEF) such as Pdz-RhoGEF [(PUBMED:11470431)] and p115RhoGEF [(PUBMED:11524686)].

GO component:cytoplasm (GO:0005737)
GO function:Rho guanyl-nucleotide exchange factor activity (GO:0005089)

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