synaptosome associated protein 23.1 [Salmo salar]
Protein Classification
SNARE domain-containing protein; syntaxin( domain architecture ID 10429084)
SNARE domain-containing protein such as SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins, which interact to form a SNARE complex that mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation; syntaxin may be involved in neuronal exocytosis, ER-Golgi transport and Golgi-endosome transport
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| SNARE_SNAP23C | cd15884 | C-terminal SNARE motif of SNAP23; C-terminal SNARE motifs of SNAP23, a member of the Qb/Qc ... |
107-165 | 1.57e-26 | ||
C-terminal SNARE motif of SNAP23; C-terminal SNARE motifs of SNAP23, a member of the Qb/Qc subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins. SNAP23 interacts with Syntaxin-4 (Qa) and the R-SNARE VAMP8. The complex plays a role in exocytosis of secretory granule. Qb/Qc SNAREs consist of 2 coiled-coil helices (called SNARE motifs, one belonging to the Qb subgroup and one belonging to the Qc subgroup), which mediate the interactions with other SNARE proteins, and a transmembrane domain. In general, the SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles. Other members of the Qb/Qc SNAREs are SNAP25, SNAP29, SNAP47 and SEC9. : Pssm-ID: 277237 Cd Length: 59 Bit Score: 95.22 E-value: 1.57e-26
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| SNAP-25 | pfam00835 | SNAP-25 family; SNAP-25 (synaptosome-associated protein 25 kDa) proteins are components of ... |
39-106 | 2.85e-20 | ||
SNAP-25 family; SNAP-25 (synaptosome-associated protein 25 kDa) proteins are components of SNARE complexes. Members of this family contain a cluster of cysteine residues that can be palmitoylated for membrane attachment. : Pssm-ID: 459955 Cd Length: 56 Bit Score: 78.87 E-value: 2.85e-20
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| SNARE super family | cl22856 | SNARE motif; SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) ... |
3-28 | 5.71e-09 | ||
SNARE motif; SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins consist of coiled-coil helices (called SNARE motifs) which mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, Qb- and Qc-SNAREs are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles. The actual alignment was detected with superfamily member cd15889: Pssm-ID: 473982 Cd Length: 65 Bit Score: 49.94 E-value: 5.71e-09
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| Name | Accession | Description | Interval | E-value | ||
| SNARE_SNAP23C | cd15884 | C-terminal SNARE motif of SNAP23; C-terminal SNARE motifs of SNAP23, a member of the Qb/Qc ... |
107-165 | 1.57e-26 | ||
C-terminal SNARE motif of SNAP23; C-terminal SNARE motifs of SNAP23, a member of the Qb/Qc subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins. SNAP23 interacts with Syntaxin-4 (Qa) and the R-SNARE VAMP8. The complex plays a role in exocytosis of secretory granule. Qb/Qc SNAREs consist of 2 coiled-coil helices (called SNARE motifs, one belonging to the Qb subgroup and one belonging to the Qc subgroup), which mediate the interactions with other SNARE proteins, and a transmembrane domain. In general, the SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles. Other members of the Qb/Qc SNAREs are SNAP25, SNAP29, SNAP47 and SEC9. Pssm-ID: 277237 Cd Length: 59 Bit Score: 95.22 E-value: 1.57e-26
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| SNAP-25 | pfam00835 | SNAP-25 family; SNAP-25 (synaptosome-associated protein 25 kDa) proteins are components of ... |
39-106 | 2.85e-20 | ||
SNAP-25 family; SNAP-25 (synaptosome-associated protein 25 kDa) proteins are components of SNARE complexes. Members of this family contain a cluster of cysteine residues that can be palmitoylated for membrane attachment. Pssm-ID: 459955 Cd Length: 56 Bit Score: 78.87 E-value: 2.85e-20
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| t_SNARE | smart00397 | Helical region found in SNAREs; All alpha-helical motifs that form twisted and parallel ... |
101-166 | 2.29e-12 | ||
Helical region found in SNAREs; All alpha-helical motifs that form twisted and parallel four-helix bundles in target soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein (SNAP) receptor proteins. This motif found in "Q-SNAREs". Pssm-ID: 197699 [Multi-domain] Cd Length: 66 Bit Score: 58.75 E-value: 2.29e-12
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| SNARE_SNAP25N_23N | cd15889 | N-terminal SNARE motif of SNAP25 and SNAP23; N-terminal SNARE motifs of SNAP25 and SNAP23, ... |
3-28 | 5.71e-09 | ||
N-terminal SNARE motif of SNAP25 and SNAP23; N-terminal SNARE motifs of SNAP25 and SNAP23, members of the Qb/Qc subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins. SNAP23 interacts with STX4 (Qa) and the lysosomal R-SNARE VAMP8. The complex plays a role in transport of secretory granule from trans-Golgi network to the plasma membrane. SNAP25 interacts with Syntaxin-1 (Qa) and the R-SNARE VAMP2 (also called synaptobrevin-2). The complex plays a role in transport of secretory granule from trans-Golgi network to the plasma membrane. Qb/Qc SNAREs consist of 2 coiled-coil helices (called SNARE motifs, one belonging to the Qb subgroup and one belonging to the Qc subgroup), which mediate the interactions with other SNARE proteins, and a transmembrane domain. In general, the SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles. Other members of the Qb/Qc SNAREs are SNAP29, SNAP47 and SEC9. Pssm-ID: 277242 Cd Length: 65 Bit Score: 49.94 E-value: 5.71e-09
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| Name | Accession | Description | Interval | E-value | ||
| SNARE_SNAP23C | cd15884 | C-terminal SNARE motif of SNAP23; C-terminal SNARE motifs of SNAP23, a member of the Qb/Qc ... |
107-165 | 1.57e-26 | ||
C-terminal SNARE motif of SNAP23; C-terminal SNARE motifs of SNAP23, a member of the Qb/Qc subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins. SNAP23 interacts with Syntaxin-4 (Qa) and the R-SNARE VAMP8. The complex plays a role in exocytosis of secretory granule. Qb/Qc SNAREs consist of 2 coiled-coil helices (called SNARE motifs, one belonging to the Qb subgroup and one belonging to the Qc subgroup), which mediate the interactions with other SNARE proteins, and a transmembrane domain. In general, the SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles. Other members of the Qb/Qc SNAREs are SNAP25, SNAP29, SNAP47 and SEC9. Pssm-ID: 277237 Cd Length: 59 Bit Score: 95.22 E-value: 1.57e-26
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| SNARE_SNAP25C | cd15885 | C-terminal SNARE motif of SNAP25; C-terminal SNARE motifs of SNAP25, a member of the Qb/Qc ... |
107-165 | 2.09e-25 | ||
C-terminal SNARE motif of SNAP25; C-terminal SNARE motifs of SNAP25, a member of the Qb/Qc subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins. SNAP25 interacts with Syntaxin-1 (Qa) and the R-SNARE VAMP2 (also called synaptobrevin-2). The complex plays a role in transport of secretory granule from trans-Golgi network to the plasma membrane. Qb/Qc SNAREs consist of 2 coiled-coil helices (called SNARE motifs, one belonging to the Qb subgroup and one belonging to the Qc subgroup), which mediate the interactions with other SNARE proteins, and a transmembrane domain. In general, the SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles. Other members of the Qb/Qc SNAREs are SNAP23, SNAP29, SNAP47 and SEC9. Pssm-ID: 277238 Cd Length: 59 Bit Score: 92.41 E-value: 2.09e-25
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| SNARE_SNAP25C_23C | cd15855 | C-terminal SNARE motif of SNAP25 and SNAP23; C-terminal SNARE motifs of SNAP25 and SNAP23, ... |
107-165 | 2.14e-20 | ||
C-terminal SNARE motif of SNAP25 and SNAP23; C-terminal SNARE motifs of SNAP25 and SNAP23, members of the Qb/Qc subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins. SNAP23 interacts with STX4 (Qa) and the lysosomal R-SNARE VAMP8. The complex plays a role in transport of secretory granule from trans-Golgi network to the plasma membrane. SNAP25 interacts with Syntaxin-1 (Qa) and the R-SNARE VAMP2 (also called synaptobrevin-2). The complex plays a role in transport of secretory granule from trans-Golgi network to the plasma membrane. Qb/Qc SNAREs consist of 2 coiled-coil helices (called SNARE motifs, one belonging to the Qb subgroup and one belonging to the Qc subgroup), which mediate the interactions with other SNARE proteins, and a transmembrane domain. In general, the SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles. Other members of the Qb/Qc SNAREs are SNAP29, SNAP47 and SEC9. Pssm-ID: 277208 Cd Length: 59 Bit Score: 79.48 E-value: 2.14e-20
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| SNAP-25 | pfam00835 | SNAP-25 family; SNAP-25 (synaptosome-associated protein 25 kDa) proteins are components of ... |
39-106 | 2.85e-20 | ||
SNAP-25 family; SNAP-25 (synaptosome-associated protein 25 kDa) proteins are components of SNARE complexes. Members of this family contain a cluster of cysteine residues that can be palmitoylated for membrane attachment. Pssm-ID: 459955 Cd Length: 56 Bit Score: 78.87 E-value: 2.85e-20
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| t_SNARE | smart00397 | Helical region found in SNAREs; All alpha-helical motifs that form twisted and parallel ... |
101-166 | 2.29e-12 | ||
Helical region found in SNAREs; All alpha-helical motifs that form twisted and parallel four-helix bundles in target soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein (SNAP) receptor proteins. This motif found in "Q-SNAREs". Pssm-ID: 197699 [Multi-domain] Cd Length: 66 Bit Score: 58.75 E-value: 2.29e-12
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| SNARE_SEC9C | cd15857 | C-terminal SNARE motif of SEC9; C-terminal SNARE motif of fungal SEC9, a member of the Qb/Qc ... |
107-150 | 2.39e-12 | ||
C-terminal SNARE motif of SEC9; C-terminal SNARE motif of fungal SEC9, a member of the Qb/Qc subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins. SEC9 interacts with Sso1(Qa) and the lysosomal R-SNARE Snc1. The complex plays a role in post-Golgi transport. Qb/Qc SNAREs consist of 2 coiled-coil helices (called SNARE motifs, one belonging to the Qb subgroup and one belonging to the Qc subgroup), which mediate the interactions with other SNARE proteins, and a transmembrane domain. In general, the SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles. Other members of the Qb/Qc SNAREs are SNAP23, SNAP25, SNAP47 and SNAP29. Pssm-ID: 277210 Cd Length: 59 Bit Score: 58.74 E-value: 2.39e-12
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| SNARE_SNAP29C | cd15856 | C-terminal SNARE motif of SNAP29; C-terminal SNARE motif of SNAP29, a member of the Qb/Qc ... |
107-165 | 3.51e-09 | ||
C-terminal SNARE motif of SNAP29; C-terminal SNARE motif of SNAP29, a member of the Qb/Qc subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins. SNAP29 interacts with STX17 (Qa) and the lysosomal R-SNARE VAMP8. The complex plays a role in autophagosome-lysosome fusion. Autophagosome transports cytoplasmic materials including cytoplasmic proteins, glycogen, lipids, organelles, and invading bacteria to the lysosome for degradation. Qb/Qc SNAREs consist of 2 coiled-coil helices (called SNARE motifs, one belonging to the Qb subgroup and one belonging to the Qc subgroup), which mediate the interactions with other SNARE proteins, and a transmembrane domain. In general, the SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles. Other members of the Qb/Qc SNAREs are SNAP23, SNAP25, SNAP47 and SEC9. Pssm-ID: 277209 Cd Length: 59 Bit Score: 50.25 E-value: 3.51e-09
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| SNARE_SNAP25N_23N | cd15889 | N-terminal SNARE motif of SNAP25 and SNAP23; N-terminal SNARE motifs of SNAP25 and SNAP23, ... |
3-28 | 5.71e-09 | ||
N-terminal SNARE motif of SNAP25 and SNAP23; N-terminal SNARE motifs of SNAP25 and SNAP23, members of the Qb/Qc subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins. SNAP23 interacts with STX4 (Qa) and the lysosomal R-SNARE VAMP8. The complex plays a role in transport of secretory granule from trans-Golgi network to the plasma membrane. SNAP25 interacts with Syntaxin-1 (Qa) and the R-SNARE VAMP2 (also called synaptobrevin-2). The complex plays a role in transport of secretory granule from trans-Golgi network to the plasma membrane. Qb/Qc SNAREs consist of 2 coiled-coil helices (called SNARE motifs, one belonging to the Qb subgroup and one belonging to the Qc subgroup), which mediate the interactions with other SNARE proteins, and a transmembrane domain. In general, the SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles. Other members of the Qb/Qc SNAREs are SNAP29, SNAP47 and SEC9. Pssm-ID: 277242 Cd Length: 65 Bit Score: 49.94 E-value: 5.71e-09
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| SNARE_SNAP25N | cd15894 | N-terminal SNARE motif of SNAP25; N-terminal SNARE motifs of SNAP25, a member of the Qb/Qc ... |
3-29 | 1.13e-08 | ||
N-terminal SNARE motif of SNAP25; N-terminal SNARE motifs of SNAP25, a member of the Qb/Qc subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins. SNAP25 interacts with Syntaxin-1 (Qa) and the R-SNARE VAMP2 (also called synaptobrevin-2). The complex plays a role in transport of secretory granule from trans-Golgi network to the plasma membrane. Qb/Qc SNAREs consist of 2 coiled-coil helices (called SNARE motifs, one belonging to the Qb subgroup and one belonging to the Qc subgroup), which mediate the interactions with other SNARE proteins, and a transmembrane domain. In general, the SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles. Other members of the Qb/Qc SNAREs are SNAP23, SNAP29, SNAP47 and SEC9. Pssm-ID: 277247 Cd Length: 73 Bit Score: 49.61 E-value: 1.13e-08
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| SNARE_Qc | cd15841 | SNARE motif, subgroup Qc; SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein ... |
108-165 | 1.93e-08 | ||
SNARE motif, subgroup Qc; SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins consist of coiled-coil helices (called SNARE motifs) which mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qc-, as well as Qa- and Qb-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles. Examples for members of the Qc SNAREs are C-terminal domains of SNAP23 and SNAP25, syntaxin 8, syntaxin 6, and Bet1. Pssm-ID: 277194 [Multi-domain] Cd Length: 59 Bit Score: 48.32 E-value: 1.93e-08
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| SNARE | cd00193 | SNARE motif; SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) ... |
112-165 | 4.45e-07 | ||
SNARE motif; SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins consist of coiled-coil helices (called SNARE motifs) which mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, Qb- and Qc-SNAREs are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles. Pssm-ID: 277192 Cd Length: 54 Bit Score: 44.69 E-value: 4.45e-07
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| SNARE_SNAP23N | cd15895 | N-terminal SNARE motif of SNAP23; N-terminal SNARE motifs of SNAP23, a member of the Qb/Qc ... |
3-28 | 1.80e-06 | ||
N-terminal SNARE motif of SNAP23; N-terminal SNARE motifs of SNAP23, a member of the Qb/Qc subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins. SNAP23 interacts with Syntaxin-4 (Qa) and the R-SNARE VAMP8. The complex plays a role in exocytosis of secretory granule. Qb/Qc SNAREs consist of 2 coiled-coil helices (called SNARE motifs, one belonging to the Qb subgroup and one belonging to the Qc subgroup), which mediate the interactions with other SNARE proteins, and a transmembrane domain. In general, the SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles. Other members of the Qb/Qc SNAREs are SNAP25, SNAP29, SNAP47 and SEC9. Pssm-ID: 277248 Cd Length: 67 Bit Score: 43.50 E-value: 1.80e-06
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| SNARE_SNAP47C | cd15854 | C-terminal SNARE motif of SNAP47; C-terminal SNARE motif of SNAP47, a member of the Qb/Qc ... |
111-165 | 1.37e-05 | ||
C-terminal SNARE motif of SNAP47; C-terminal SNARE motif of SNAP47, a member of the Qb/Qc subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins. The exact funtion of SNAP47 is unknown. Qb/Qc SNAREs consist of 2 coiled-coil helices (called SNARE motifs, one belonging to the Qb subgroup and one belonging to the Qc subgroup), which mediate the interactions with other SNARE proteins, and a transmembrane domain. In general, the SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles. Other members of the Qb/Qc SNAREs are SNAP23, SNAP25, SNAP29 and SEC9. Pssm-ID: 277207 Cd Length: 59 Bit Score: 41.00 E-value: 1.37e-05
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| SNARE_Syntaxin6 | cd15851 | SNARE motif of syntaxin 6; Syntaxin 6 forms a complex with syntaxin 16 (Qa), Vti1a (Qb) and ... |
109-168 | 1.45e-05 | ||
SNARE motif of syntaxin 6; Syntaxin 6 forms a complex with syntaxin 16 (Qa), Vti1a (Qb) and VAMP4 (R-SNARE) and is involved in the regulation of recycling of early endosomes to the trans-Golgi network (TGN). Syntaxin 6 and its yeast homolog TLG1 are members of the Qc subgroup of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins, which consist of coiled-coil helices (called SNARE motifs) that mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complexes mediate membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Pssm-ID: 277204 Cd Length: 66 Bit Score: 40.93 E-value: 1.45e-05
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| SNARE_Syntaxin8 | cd15852 | SNARE motif of syntaxin 8; Syntaxin 8 forms a complex with syntaxin 7 (Qa), Vti1b (Qb) and ... |
108-163 | 2.15e-03 | ||
SNARE motif of syntaxin 8; Syntaxin 8 forms a complex with syntaxin 7 (Qa), Vti1b (Qb) and either VAMP7 or VAMP8 (R-SNARE) and is involved in the transport from early endosomes to the lysosome. Syntaxin 8 is a member of the Qc subgroup of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins, which consist of coiled-coil helices (called SNARE motifs) that mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complexes mediate membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Pssm-ID: 277205 [Multi-domain] Cd Length: 59 Bit Score: 34.90 E-value: 2.15e-03
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| SNARE_SNAP25N_23N_29N_SEC9N | cd15861 | N-terminal SNARE motif of SNAP25, SNAP23, SNAP29, and SEC9; N-terminal SNARE motif of members ... |
2-28 | 2.42e-03 | ||
N-terminal SNARE motif of SNAP25, SNAP23, SNAP29, and SEC9; N-terminal SNARE motif of members of the Qb/Qc subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins. Qb/Qc SNAREs consist of 2 coiled-coil helices (called SNARE motifs, one belonging to the Qb subgroup and one belonging to the Qc subgroup), which mediate the interactions with other SNARE proteins, and a transmembrane domain. In general, the SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles. Examples for members of the Qb/Qc SNAREs are SNAP23, SNAP25, SNAP29, SNAP47 and SEC9. Pssm-ID: 277214 Cd Length: 65 Bit Score: 34.86 E-value: 2.42e-03
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| SNARE_USE1 | cd15860 | SNARE motif of USE1; USE1 (unconventional SNARE in the ER 1 homolog, also known as SNARE-like ... |
107-165 | 3.12e-03 | ||
SNARE motif of USE1; USE1 (unconventional SNARE in the ER 1 homolog, also known as SNARE-like tail-anchored protein 1 or SLT1) is involved in retrograde transport of CopI coatomer coated vesicles from the Golgi to the ER. It forms a complex with syntaxin18 (Ufe1p, Qa), Bnip1 (Sec20p, Qb) and Sec22b (R-SNARE). USE1 is a member of the Qc subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) protein family. SNARE proteins consist of coiled-coil helices (called SNARE motifs) which mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qc-, as well as Qa- and Qb-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles. Pssm-ID: 277213 Cd Length: 60 Bit Score: 34.46 E-value: 3.12e-03
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| SNARE_SNAP29N | cd15887 | N-terminal SNARE motif of SNAP29; N-terminal SNARE motif of SNAP29, a member of the Qb/Qc ... |
3-27 | 7.24e-03 | ||
N-terminal SNARE motif of SNAP29; N-terminal SNARE motif of SNAP29, a member of the Qb/Qc subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins. SNAP29 interacts with STX17 (Qa) and the lysosomal R-SNARE VAMP8. The complex plays a role in autophagosome-lysosome fusion. Autophagosome transports cytoplasmic materials including cytoplasmic proteins, glycogen, lipids, organelles, and invading bacteria to the lysosome for degradation. Qb/Qc SNAREs consist of 2 coiled-coil helices (called SNARE motifs, one belonging to the Qb subgroup and one belonging to the Qc subgroup), which mediate the interactions with other SNARE proteins, and a transmembrane domain. In general, the SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles. Other members of the Qb/Qc SNAREs are SNAP23, SNAP25, SNAP47 and SEC9. Pssm-ID: 277240 Cd Length: 65 Bit Score: 33.40 E-value: 7.24e-03
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