The domain within your query sequence starts at position 74 and ends at position 596; the E-value for the SRP68 domain shown below is 5.5e-156.

LRHGDFQRYRGYCSRRQRRLRKTLNFKMGNRHKFTGKKVTEELLTDNRYLLLVLMDAERA
WSYAMQLKQEANTEPRKRFHLLSRLRKAVKHAEELERLCESNRVDAKTKLEAQAYTAYLS
GMLRFEHQEWKSAIEAFNKCKTIYEKLASAFTEEQAVLYNQRVEEISPNIRYCAYNIGDQ
SAINELMQMRLRSGGTEGLLAEKLEALITQTRAKQAATMSEVEWRGRTVPVKIDKVRIFL
LGLADNEAAIVQAESEETKERLFESMLSECRDALQAVREELKPDQKQRDYALDGESGKVS
NLQYLHSYLTYIKLSTAIRRNENMAKGLHRALLQQQPEDDSKRSPRPQDLIRLYDIILQN
LVELLQLPGLEEDRTFQKEISLKTLVFKAYRCFFIAQSYVLVKKWSEALVLYDRVLKYAN
EVSSHGGASKNSLKDLPDVQELITQVRSEKCSLQAAAILDANDSHQTDTSSQVKDNTPLV
ERFESFCLDPSLVTKQANLVHFPPGFQPIPCKPLFFDLALNHV

SRP68

SRP68
PFAM accession number:PF16969
Interpro abstract (IPR026258):

The signal recognition particle (SRP) is a large ribonucleoprotein complex that targets secretory and membrane proteins to the endoplasmic reticulum membrane [ (PUBMED:17254600) ]. The mammalian SRP contains a 303-nucleotide SRP RNA and six proteins, named SRP9, SRP14, SRP19, SRP54, SRP68, and SRP72. Among them, the two largest, SRP68 and SRP72, form a stable SRP68/72 heterodimer of unknown structure, which is required for sorting secretory proteins [ (PUBMED:19693936) ]. SRP68 binds to SRP RNA directly, while SRP72 binds the SRP RNA largely via non-specific electrostatic interaction. The binding of SRP72 with SRP RNA enhances the affinity of SRP68 for the RNA.

GO process:SRP-dependent cotranslational protein targeting to membrane (GO:0006614)
GO component:signal recognition particle, endoplasmic reticulum targeting (GO:0005786)
GO function:endoplasmic reticulum signal peptide binding (GO:0030942), signal recognition particle binding (GO:0005047), 7S RNA binding (GO:0008312)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry SRP68