The domain within your query sequence starts at position 181 and ends at position 619; the E-value for the PRMT5 domain shown below is 4.5e-184.

GEEKTWMWWHNFRTLCDYSKRIAVALEIGADLPSNHVIDRWLGEPIKAAILPTSIFLTNK
KGFPVLSKVQQRLIFRLLKLEVQFIITGTNHHSEKEFCSYLQYLEYLSQNRPPPNAYELF
AKGYEDYLQSPLQPLMDNLESQTYEVFEKDPIKYSQYQQAIYKCLLDRVPEEEKETNVQV
LMVLGAGRGPLVNASLRAAKQAERRIRLYAVEKNPNAVVTLENWQFEEWGSQVTVVSSDM
REWVAPEKADIIVSELLGSFADNELSPECLDGAQHFLKDDGVSIPGEYTSFLAPISSSKL
YNEVRACREKDRDPEAQFEMPYVVRLHNFHQLSAPKPCFTFSHPNRDPMIDNNRYCTLEF
PVEVNTVLHGFAGYFETVLYRDITLSIRPETHSPGMFSWFPIFFPIKQPITVHEGQNICV
RFWRCSNSKKVWYEWAVTA

PRMT5

PRMT5
PFAM accession number:PF05185
Interpro abstract (IPR035075):

This entry represents a domain found in arginine-N-methyltransferase PRMT5. Proteins containing this domain include Skb1 from S. pombe [(PUBMED:11278267)], Hsl7 from S. cerevisiae [(PUBMED:10903903)] and their homologues PRMT5 from animals [(PUBMED:10531356), (PUBMED:11152681), (PUBMED:17709427)] and plants [(PUBMED:17363895)].

Skb1 is a mediator of hyperosmotic stress response in Schizosaccharomyces pombe [(PUBMED:11278267)]. Plant PMRT15 is involved in the post-transcriptional regulation of the circadian clock [(PUBMED:20962777)]. Human PRMT5 is a component of multiple protein complexes and contributes to essential cellular processes, such as RNA transport and splicing, cell cycle regulation, tumour growth, and chromatin remodelling, leading to either gene silencing or activation [(PUBMED:22269951)].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry PRMT5