The domain within your query sequence starts at position 35 and ends at position 96; the E-value for the EMP24_GP25L domain shown below is 2.4e-14.
DFTFTLPAGRKECFYQPMPLKASLEIEYQVLDGGELDIDFHLTSPEGRTLVFEQRKSDGV HT
EMP24_GP25L |
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PFAM accession number: | PF01105 |
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Interpro abstract (IPR009038): | The GOLD (for Golgi dynamics) domain is a protein module found in several eukaryotic Golgi and lipid-traffic proteins. It is typically between 90 and 150 amino acids long. Most of the size difference observed in the GOLD-domain superfamily is traceable to a single large low-complexity insert that is seen in some versions of the domain. With the exception of the p24 proteins, which have a simple architecture with the GOLD domain as their only globular domain, all other GOLD-domain proteins contain additional conserved globular domains. In these proteins, the GOLD domain co-occurs with lipid-, sterol- or fatty acid-binding domains such as PH, CRAL-TRIO, FYVE oxysterol binding- and acyl CoA-binding domains, suggesting that these proteins may interact with membranes. The GOLD domain can also be found associated with a RUN domain, which may have a role in the interaction of various proteins with cytoskeletal filaments. The GOLD domain is predicted to mediate diverse protein-protein interactions [ (PUBMED:12049664) ]. A secondary structure prediction for the GOLD domain reveals that it is likely to adopt a compact all-beta-fold structure with six to seven strands. Most of the sequence conservation is centred on the hydrophobic cores that support these predicted strands. The predicted secondary-structure elements and the size of the conserved core of the domain suggests that it may form a beta- sandwich fold with the strands arranged in two beta sheets stacked on each other [ (PUBMED:12049664) ]. Some proteins known to contain a GOLD domain are listed below:
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This is a PFAM domain. For full annotation and more information, please see the PFAM entry EMP24_GP25L