The domain within your query sequence starts at position 65 and ends at position 298; the E-value for the DUF974 domain shown below is 1.3e-87.

LTLPQNFGNIFLGETFSSYISVHNDSNQVVKDILVKADLQTSSQRLNLSASNAAVAELKP
DCCIDDVIHHEVKEIGTHILVCAVSYTTQGGEKMYFRKFFKFQVLKPLDVKTKFYNAESD
LSSVTDEVFLEAQIQNITTSPMFMEKVSLEPSIMYNVTELNSVTQAGECISTFGSRGYLQ
PMDTRQYLYCLKPKKEFAEKAGIIKGVTVIGKLDIVWKTNLGERGRLQTSQLQR

DUF974

DUF974
PFAM accession number:PF06159
Interpro abstract (IPR010378):

Three transport protein particle (TRAPP) complexes exist in yeast (TRAPPI-TRAPPIII), which share a common core in addition to unique subunits. TRAPPI-TRAPPIII regulate endoplasmic reticulum (ER)-to-Golgi transport, intra-Golgi transport and autophagy, respectively. TRAPPC composition seems to be more complex in higher eukaryotes than in yeast, and its roles are less clear.

Mammalian TRAPPC13 is involved in regulating autophagy and survival in response to small molecule compound-induced Golgi stress [ (PUBMED:28536105) ]. The overall architecture of TRAPPC is not disrupted upon TRAPPC13 depletion. This is also the case for yeast TRAPP II Trs65 subunit, which was previously reported to be specific to yeast. However, Trs65 has been shown to have homology to TRAPPC13 and they are now thought to be orthologues [ (PUBMED:21453443) ]. This entry consists of high eukaryotes TRAPPC13 and some related yeast proteins, but it does not include S. cerevisiae Trs65 (see IPR024662 ).

This is a PFAM domain. For full annotation and more information, please see the PFAM entry DUF974