The domain within your query sequence starts at position 4 and ends at position 443; the E-value for the Gasdermin domain shown below is 1.7e-148.

SFDRASKDVVKKLQGRDLRPVECLSDATKFRLFHILQETPRSGWETEDIPVGFTLLDLLE
PNFPVPEPEVSAPKPFIHVQSTDLEANLNVADIARGGVGYVGYGGYNIEVQSTSIPNPKL
EILQNRKLLDNLPTFMKFCRMERKNLYVVTEAYEVSKDTMLTGLSSVNLSVKGFFKQLFK
VRGKAGRSEKYSIPIPKGSVLAYKKQQLVIENNTCVILPSATKKKMTFPGTPKYASASEP
TEIYRTELQGLWINDIVPIGRIQEPAHLDFMCLQNEVYKQTEQLAELSKGVQEVVLSSIL
SMLYEGDRKVLYDLMNMLELNQLGHMDGPGGKILDELRKDSSNPCVDLKDLILYLLQALM
VLSDSQLNLLAQSVEMGILPHQVELVKSILQPNFKYPWNIPFTLQPQLLAPLQGEGLAIT
YELLEECGLKMELNNPRSTW

Gasdermin

Gasdermin
PFAM accession number:PF04598
Interpro abstract (IPR007677):

The precise function of this protein is unknown. However, it is thought that this entry represents the gasdermin family which plays a role as a secretory or metabolic product involved in the secretory pathway and includes gasdermin, non-syndromic hearing impairment protein 5 (DFNA5) and pejvakin. A N-terminal fragment released by proteolysis of gasmerdin A binds to lipids and homo-oligomerizes in the membrane forming pores, which may have a bacteriocidal function [(PUBMED:27281216)].

It may also play a role in achieving and maintaining the final differentiation state of epithelial cells [(PUBMED:15010812), (PUBMED:18038310)]. A deletion/insertion mutation is associated with an autosomal dominant non-syndromic hearing impairment form [(PUBMED:9771715)].

Gasmedin E is cleaved by caspase-3 and the N-terminal fragment released forms pores in the cell membrane, switching from cell death by apoptosis to pyroptosis [(PUBMED:28459430)].

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