The domain within your query sequence starts at position 16 and ends at position 183; the E-value for the Patatin domain shown below is 1.4e-14.

ISFSGSGFLSYYQAGAVDALRDLAPRMLDTAHRFAGTSAGAVIAALVVCGIEMEKYLRVL
NMGLAEVKKFFLGPLSPSCKMVQMMRQFLYDVLPEDSYKFATGKLHVSLTRVTDGENVVV
SEYRSKEELIEALYCSCFVPVYCGFIPPTYRGERYIDGGFTSMQPCSF

Patatin

Patatin
PFAM accession number:PF01734
Interpro abstract (IPR002641):

The patatin glycoprotein is a nonspecific lipid acyl hydrolase that is found in high concentrations in mature potato tubers. Patatin is reported to play a role in plant signaling, to cleave fatty acids from membrane lipids, and to act as defense against plant parasites. Proteins encoding a patatin-like phospholipase (PNPLA) domain are ubiquitously distributed across all life forms, including eukaryotes and prokaryotes, and are observed to participate in a miscellany of biological roles, including sepsis induction, host colonization, triglyceride metabolism, and membrane trafficking. PNPLA domain containing proteins display lipase and transacylase properties and appear to have major roles in lipid and energy homeostasis [(PUBMED:16799181), (PUBMED:19029121), (PUBMED:20188050)].

The ~180-amino acid PNPLA domain harbors the evolutionarily conserved consensus serine lipase motif Gly-X-Ser-X-Gly.It displays an alpha/beta class protein fold with approximately three layers, basically alpha/beta/alpha in content, in which a central six-stranded beta-sheet is sandwiched essentially between alpha-helices front and back. The central beta-sheet contains five parallel strands and an antiparallel strand at the edge of the sheet. The PNPLA domain has a Ser-Asp catalytic dyad. The catalytic Ser resides in a sharp nucleophile elbow turn loop which follows a beta-strand (beta5) of the central beta-sheet and precedes a helix (helix C) [(PUBMED:12779324), (PUBMED:25248161)].

GO process:lipid metabolic process (GO:0006629)

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