The domain within your query sequence starts at position 41 and ends at position 632; the E-value for the Sec1 domain shown below is 1.6e-109.
KVLIYDRFGQDIISPLLSVKELRDMGITLHLLLHSDRDPIPDVPAVYFVMPTEENIDRLC QDLRNQLYESYYLNFISAISRSKLEDIANAALAASAVTQVAKVFDQYLNFITLEDDMFVL CNQNKELVSYRAINRPDITDTEMETVMDTIVDSLFCFFVTLGAVPIIRCSRGTAAEMVAV KLDKKLRENLRDARNSLFTGDPLGTGQFSFQRPLLVLVDRNIDLATPLHHTWTYQALVHD VLDFHLNRVNLEESTGVENSPAGARPKRKNKKSYDLTPVDKFWQKHKGSPFPEVAESVQQ ELESYRAQEDEVKRLKSIMGLEGEDEGAISMLSDNTAKLTSAVSSLPELLEKKRLIDLHT NVATAVLEHIKARKLDVYFEYEEKIMSKTTLDKSLLDVISDPDAGTPEDKMRLFLIYYIS AQQAPSEVDLEQYKKALTDAGCNLSPLQYIKQWKAFAKMASTPASYGNTTTKPMGLLSRV MNTGSQFVMEGVKNLVLKQQNLPVTRILDNLMEMKSNPETDDYRYFDPKMLRSNDSSVPR NKSPFQEAIVFVVGGGNYIEYQNLVDYIKAKQGKHILYGCSEIFNATQFIKQ
Sec1 |
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PFAM accession number: | PF00995 |
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Interpro abstract (IPR001619): | Sec1-like molecules have been implicated in a variety of eukaryotic vesicle transport processes including neurotransmitter release by exocytosis [ (PUBMED:8769846) ]. They regulate vesicle transport by binding to a t-SNARE from the syntaxin family. This process is thought to prevent SNARE complex formation, a protein complex required for membrane fusion. Whereas Sec1 molecules are essential for neurotransmitter release and other secretory events, their interaction with syntaxin molecules seems to represent a negative regulatory step in secretion [ (PUBMED:10903948) ]. |
GO process: | vesicle docking involved in exocytosis (GO:0006904), vesicle-mediated transport (GO:0016192) |
This is a PFAM domain. For full annotation and more information, please see the PFAM entry Sec1