Summary: SNARE domain
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Most if not all vesicular membrane fusion events in eukaryotic cells are believed to be mediated by a conserved fusion machinery, the SNARE [soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein (SNAP) receptors] machinery. The SNARE domain is thought to act as a protein-protein interaction module in the assembly of a SNARE protein complex .
Weimbs T, Low SH, Chapin SJ, Mostov KE, Bucher P, Hofmann K; , Proc Natl Acad Sci U S A 1997;94:3046-3051.: A conserved domain is present in different families of vesicular fusion proteins: a new superfamily. PUBMED:9096343 EPMC:9096343
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This tab holds annotation information from the InterPro database.
InterPro entry IPR000727
The process of vesicular fusion with target membranes depends on a set of SNAREs (SNAP-Receptors), which are associated with the fusing membranes [PUBMED:9239749, PUBMED:9232812]. Target SNAREs (t-SNAREs) are localised on the target membrane and belong to two different families, the syntaxin-like family and the SNAP-25 like family. One member of each family, together with a v-SNARE localised on the vesicular membrane, are required for fusion.
The Syntaxins are type-I transmembrane proteins that contain several regions with coiled-coil propensity in their cytosolic part, the SNARE motif. SNAP-25 (INTERPRO) is a protein consisting of two coiled-coil regions, which is associated with the membrane by lipid anchors. SNARE motifs assemble into parallel four helix bundles stabilised by the burial of these hydrophobic helix faces in the bundle core. Monomeric SNARE motifs are disordered so this assembly reaction is accompanied by a dramatic increase in alpha-helical secondary structure [PUBMED:14570579]. The parallel arrangement of SNARE motifs within complexes bring the transmembrane anchors, and the two membranes, into close proximity. Recently, it was shown that the two coiled-coil regions of SNAP-25 and one of the coiled-coil regions of the syntaxins are related [PUBMED:9096343]. This domain is found in both Syntaxin and SNAP-25 families as well as in other proteins.
|Molecular function||protein binding (GO:0005515)|
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Curation and family details
|Seed source:||Pfam-B_6285 (release 8.0)|
|Number in seed:||105|
|Number in full:||4036|
|Average length of the domain:||61.80 aa|
|Average identity of full alignment:||22 %|
|Average coverage of the sequence by the domain:||22.43 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||14|
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There are 2 interactions for this family. More...
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the SNARE domain has been found. There are 62 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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