synaptosomal-associated protein 47 [Macaca mulatta]
Protein Classification
PH domain-containing protein; PH domain-containing RhoGEF family protein( domain architecture ID 10351657)
Pleckstrin homology (PH) domain-containing protein may be involved in targeting a protein to the appropriate cellular location or interacting with a binding partner; similar to the PH region of pleckstrin homology domain-containing family A member 2 (PLEKHA2/TAAP2) that binds specifically to phosphatidylinositol 3,4-diphosphate (PtdIns3,4P2)| PH domain-containing RhoGEF family protein may function as a guanine nucleotide exchange factor; similar to Homo sapiens pleckstrin homology domain-containing family G member 4B and Danio rerio quattro
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| SNARE_SNAP47N | cd15888 | N-terminal SNARE motif of SNAP47; N-terminal SNARE motif of SNAP47, a member of the Qb/Qc ... |
106-170 | 5.17e-33 | ||
N-terminal SNARE motif of SNAP47; N-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: 277241 Cd Length: 65 Bit Score: 118.63 E-value: 5.17e-33
|
||||||
| SNARE_SNAP47C | cd15854 | C-terminal SNARE motif of SNAP47; C-terminal SNARE motif of SNAP47, a member of the Qb/Qc ... |
359-417 | 8.13e-28 | ||
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: 104.56 E-value: 8.13e-28
|
||||||
| PH-like super family | cl17171 | Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ... |
42-98 | 2.72e-05 | ||
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like and IRS-like PTB domains, the ran-binding domain, the EVH1 domain, a domain in neurobeachin and the third domain of FERM. All of these domains have a PH fold, but lack significant sequence similarity. They are generally involved in targeting to protein to the appropriate cellular location or interacting with a binding partner. This domain family possesses multiple functions including the ability to bind inositol phosphates and to other proteins. The actual alignment was detected with superfamily member cd13220: Pssm-ID: 473070 Cd Length: 94 Bit Score: 42.49 E-value: 2.72e-05
|
||||||
| Name | Accession | Description | Interval | E-value | |||
| SNARE_SNAP47N | cd15888 | N-terminal SNARE motif of SNAP47; N-terminal SNARE motif of SNAP47, a member of the Qb/Qc ... |
106-170 | 5.17e-33 | |||
N-terminal SNARE motif of SNAP47; N-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: 277241 Cd Length: 65 Bit Score: 118.63 E-value: 5.17e-33
|
|||||||
| SNARE_SNAP47C | cd15854 | C-terminal SNARE motif of SNAP47; C-terminal SNARE motif of SNAP47, a member of the Qb/Qc ... |
359-417 | 8.13e-28 | |||
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: 104.56 E-value: 8.13e-28
|
|||||||
| PH-GRAM_GRAMDC | cd13220 | GRAM domain-containing protein (GRAMDC) Pleckstrin Homology-Glucosyltransferases, Rab-like ... |
42-98 | 2.72e-05 | |||
GRAM domain-containing protein (GRAMDC) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; The GRAMDC proteins are membrane proteins. Nothing is known about its function. Members include: GRAMDC1A, GRAMDC1B, GRAMDC1C, GRAMDC2, GRAMDC3, GRAMDC4, and GRAMDC-like proteins. All of the members, except for GRAMDC4 are included in this hierarchy. Each contains a single PH-GRAM domain at their N-terminus. The GRAM domain is found in glucosyltransferases, myotubularins and other putative membrane-associated proteins. The GRAM domain is part of a larger motif with a pleckstrin homology (PH) domain fold. Pssm-ID: 275406 Cd Length: 94 Bit Score: 42.49 E-value: 2.72e-05
|
|||||||
| GRAM | pfam02893 | GRAM domain; The GRAM domain is found in in glucosyltransferases, myotubularins and other ... |
6-99 | 6.37e-05 | |||
GRAM domain; The GRAM domain is found in in glucosyltransferases, myotubularins and other putative membrane-associated proteins. Note the alignment is lacking the last two beta strands and alpha helix. Pssm-ID: 397160 Cd Length: 112 Bit Score: 41.97 E-value: 6.37e-05
|
|||||||
| Name | Accession | Description | Interval | E-value | |||
| SNARE_SNAP47N | cd15888 | N-terminal SNARE motif of SNAP47; N-terminal SNARE motif of SNAP47, a member of the Qb/Qc ... |
106-170 | 5.17e-33 | |||
N-terminal SNARE motif of SNAP47; N-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: 277241 Cd Length: 65 Bit Score: 118.63 E-value: 5.17e-33
|
|||||||
| SNARE_SNAP47C | cd15854 | C-terminal SNARE motif of SNAP47; C-terminal SNARE motif of SNAP47, a member of the Qb/Qc ... |
359-417 | 8.13e-28 | |||
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: 104.56 E-value: 8.13e-28
|
|||||||
| SNARE_SNAP29C | cd15856 | C-terminal SNARE motif of SNAP29; C-terminal SNARE motif of SNAP29, a member of the Qb/Qc ... |
363-417 | 7.98e-10 | |||
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: 54.49 E-value: 7.98e-10
|
|||||||
| SNARE_SNAP25N_23N_29N_SEC9N | cd15861 | N-terminal SNARE motif of SNAP25, SNAP23, SNAP29, and SEC9; N-terminal SNARE motif of members ... |
120-170 | 1.29e-09 | |||
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: 54.12 E-value: 1.29e-09
|
|||||||
| SNARE_Qc | cd15841 | SNARE motif, subgroup Qc; SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein ... |
368-417 | 2.06e-07 | |||
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: 47.55 E-value: 2.06e-07
|
|||||||
| SNARE_VAM7 | cd15858 | SNARE motif of VAM7; Fungal VAM7 (vacuolar morphogenesis protein 7) is a member of the Qc ... |
361-417 | 4.17e-07 | |||
SNARE motif of VAM7; Fungal VAM7 (vacuolar morphogenesis protein 7) is a member of the Qc subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) protein family involved in vacuolar protein transport and membrane fusion. 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: 277211 [Multi-domain] Cd Length: 59 Bit Score: 46.73 E-value: 4.17e-07
|
|||||||
| PH-GRAM_GRAMDC | cd13220 | GRAM domain-containing protein (GRAMDC) Pleckstrin Homology-Glucosyltransferases, Rab-like ... |
42-98 | 2.72e-05 | |||
GRAM domain-containing protein (GRAMDC) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; The GRAMDC proteins are membrane proteins. Nothing is known about its function. Members include: GRAMDC1A, GRAMDC1B, GRAMDC1C, GRAMDC2, GRAMDC3, GRAMDC4, and GRAMDC-like proteins. All of the members, except for GRAMDC4 are included in this hierarchy. Each contains a single PH-GRAM domain at their N-terminus. The GRAM domain is found in glucosyltransferases, myotubularins and other putative membrane-associated proteins. The GRAM domain is part of a larger motif with a pleckstrin homology (PH) domain fold. Pssm-ID: 275406 Cd Length: 94 Bit Score: 42.49 E-value: 2.72e-05
|
|||||||
| SNARE_SNAP29N | cd15887 | N-terminal SNARE motif of SNAP29; N-terminal SNARE motif of SNAP29, a member of the Qb/Qc ... |
124-169 | 3.89e-05 | |||
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: 41.10 E-value: 3.89e-05
|
|||||||
| GRAM | pfam02893 | GRAM domain; The GRAM domain is found in in glucosyltransferases, myotubularins and other ... |
6-99 | 6.37e-05 | |||
GRAM domain; The GRAM domain is found in in glucosyltransferases, myotubularins and other putative membrane-associated proteins. Note the alignment is lacking the last two beta strands and alpha helix. Pssm-ID: 397160 Cd Length: 112 Bit Score: 41.97 E-value: 6.37e-05
|
|||||||
| SNARE_SNAP25N_23N | cd15889 | N-terminal SNARE motif of SNAP25 and SNAP23; N-terminal SNARE motifs of SNAP25 and SNAP23, ... |
125-170 | 7.68e-04 | |||
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: 37.61 E-value: 7.68e-04
|
|||||||
| SNARE_SNAP23N | cd15895 | N-terminal SNARE motif of SNAP23; N-terminal SNARE motifs of SNAP23, a member of the Qb/Qc ... |
109-170 | 2.93e-03 | |||
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: 36.18 E-value: 2.93e-03
|
|||||||
| Blast search parameters | ||||
|
