The domain within your query sequence starts at position 4 and ends at position 207; the E-value for the Frag1 domain shown below is 7.1e-52.

YLSLLPVILFLWAIAGIWIVFAIAVVNGSVDLNEGFPFISICGSYAPQSCIFGQVLNIGA
ALTVWICIVRHHQLRDWGVKTWQNQLILWSGILCALGTSIVGNFQDKNQKPTHLAGAFLA
FILGNLYFWLQFFLSWWVKGLPQPGPHWIKSLRLSLCSLSTILIVAMIVLHALHMRSASA
ICEWVVAMLLFMLFGFFAVDFSIL

Frag1

Frag1
PFAM accession number:PF10277
Interpro abstract (IPR019402):

This entry includes Frag1, DRAM and Sfk1 proteins. Frag1 (FGF receptor activating protein 1, also known as post-GPI attachment to proteins factor 2) is a protein that is conserved from fungi to humans. There are four potential iso-prenylation sites throughout the peptide, CILW (x2), CIIW and CIGL. Frag1 is a membrane-spanning protein that is ubiquitously expressed in adult tissues suggesting an important cellular function [(PUBMED:10585768)]. DRAM is a family of proteins conserved from nematodes to humans with six hydrophobic transmembrane regions and an endoplasmic reticulum signal peptide. It is a lysosomal protein that induces macro-autophagy as an effector of p53-mediated death, where p53 is the tumour-suppressor gene that is frequently mutated in cancer. Expression of DRAM is stress-induced [(PUBMED:16839881)]. DRAM-3 (also known as modulator of macroautophagy TMEM150B) has been shown to be a modulator of both macroautophagy and cell survival under starvation conditions [(PUBMED:25929859)]. This region is also part of a family of small plasma membrane proteins, referred to as Sfk1, that may act together with or upstream of Stt4p to generate normal levels of the essential phospholipid PI4P, thus allowing proper localisation of Stt4p to the actin cytoskeleton [(PUBMED:12837385), (PUBMED:12015967)].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Frag1