The domain within your query sequence starts at position 321 and ends at position 681; the E-value for the APG9 domain shown below is 1.2e-100.

EELSSVPWAEVQSRLLELQRSGGLCVQPRPLTELDVHHRILRYTNYQVALANKGLLPARC
PLPWGSSAAFLSRGLALNVDLLLFRGPFSLFRGGWELPEAYKRSDLRGVLANRWRRTVLL
LAAVNLALSPLVLAWQVLHAFYSHVELLRREPGAFGARRWSRLARLQLRHFNELPHELRA
RLGRAYRPAAAFLRAAEPPAPLRALLARQLVFFSGALFAALLVLTIYDEDVLAVEHVLTT
MTALGVTATVARSFIPEEQCQGRSSQLLLQAALAHMHYLPEEPGATGARASSYWQMAQLL
QYRAVSLLEELLSPLLTPLFLLFWFRPRALEIIDFFHHFTVDVAGVGDICSFALMDVKRH
G

APG9

APG9
PFAM accession number:PF04109
Interpro abstract (IPR007241): Macroautophagy is a bulk degradation process induced by starvation in eukaryotic cells. In yeast, 15 Atg proteins coordinate the formation of autophagosomes. The pre-autophagosomal structure contains at least five Atg proteins: Atg1p, Atg2p, Atg5p, Aut7p/Atg8p and Atg16p. It is found in the vacuole [(PUBMED:11689437)]. The C-terminal glycine of Atg12p is conjugated to a lysine residue of Atg5p via an isopeptide bond. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. Auotphagy protein 16 (Atg16) has been shown to be bind to Atg5 and is required for the function of the Atg12p-Atg5p conjugate [(PUBMED:10406794)]. Autophagy protein 5 (Atg5) is directly required for the import of aminopeptidase I via the cytoplasm-to-vacuole targeting pathway [(PUBMED:10712513)].

Apg9 plays a direct role in the formation of the cytoplasm to vacuole targeting and autophagic vesicles, possibly serving as a marker for a specialised compartment essential for these vesicle-mediated alternative targeting pathways [(PUBMED:10662773)].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry APG9