The domain within your query sequence starts at position 23 and ends at position 160; the E-value for the Secretogranin_V domain shown below is 4e-13.

PAFAYSPRTPDRVSETDIQRLLHGVMEQLGIARPRVEYPAHQAMNLVGPQSIEGGAHEGL
QHLGPFGNIPNIVAELTGDNIPKDFSEDQGYPDPPNPCPLGKTADDGCLENAPDTAEFSR
EFQLDQHLFDPEHDYPGL

Secretogranin_V

 Secretogranin_V
PFAM accession number:PF05281
Interpro abstract (IPR007945):

Prohormone convertases (PCs) 1 and 2 are a family of eukaryotic subtilisins thought to mediate the proteolytic cleavage of many peptide precursors [ (PUBMED:10701998) ]. Protein 7B2 (secretogranin V) functions as a molecular chaperone for PC2, preventing its premature activation in the regulated secretory pathway [ (PUBMED:7913882) ]. 7B2 represents a potent inhibitor of PC2, and it is also required for the activation of PC2, which is synthesised as a zymogen. Protein 7B2 has an N-terminal activation domain and a C-terminal (CT) inhibitory domain (MEROPS inhibitor family I21), separated by a furin cleavage site [ (PUBMED:10506829) ]. 7B2 is synthesised as a precursor protein that is cleaved into the N-terminal fragment and the C-terminal peptide [ (PUBMED:11439082) ].

7B2 has been linked to neurodegenerative diseases. It may act as an anti-aggregation chaperone [ (PUBMED:23172224) ]. However, in an APP model mouse 7B2 knockout has been shown to reduce rather than enhance plaque burden [ (PUBMED:29955078) ].

GO process:neuropeptide signaling pathway (GO:0007218)
GO component:secretory granule (GO:0030141)

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