vesicle transport through interaction with t-SNAREs homolog 1A isoform X11 [Rattus norvegicus]
Protein Classification
v-SNARE domain-containing protein( domain architecture ID 10523371)
v-SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) domain-containing protein is part of various SNARE complexes involved in multiple transport pathways
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| V-SNARE | pfam05008 | Vesicle transport v-SNARE protein N-terminus; V-SNARE proteins are required for protein ... |
12-90 | 2.07e-23 | ||
Vesicle transport v-SNARE protein N-terminus; V-SNARE proteins are required for protein traffic between eukaryotic organelles. The v-SNAREs on transport vesicles interact with t-SNAREs on target membranes in order to facilitate this. This domain is the N-terminal half of the V-Snare proteins. : Pssm-ID: 461516 Cd Length: 79 Bit Score: 87.28 E-value: 2.07e-23
|
||||||
| SNARE super family | cl22856 | SNARE motif; SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) ... |
129-149 | 2.61e-05 | ||
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 cd15891: Pssm-ID: 473982 Cd Length: 62 Bit Score: 39.97 E-value: 2.61e-05
|
||||||
| Name | Accession | Description | Interval | E-value | ||
| V-SNARE | pfam05008 | Vesicle transport v-SNARE protein N-terminus; V-SNARE proteins are required for protein ... |
12-90 | 2.07e-23 | ||
Vesicle transport v-SNARE protein N-terminus; V-SNARE proteins are required for protein traffic between eukaryotic organelles. The v-SNAREs on transport vesicles interact with t-SNAREs on target membranes in order to facilitate this. This domain is the N-terminal half of the V-Snare proteins. Pssm-ID: 461516 Cd Length: 79 Bit Score: 87.28 E-value: 2.07e-23
|
||||||
| SNARE_Vti1a | cd15891 | SNARE motif of Vti1b-like; Vti1a (vesicle transport through interaction with t-SNAREs homolog ... |
129-149 | 2.61e-05 | ||
SNARE motif of Vti1b-like; Vti1a (vesicle transport through interaction with t-SNAREs homolog 1A) belongs to the Qb subgroup of SNAREs (soluble N-ethylmaleimide-sensitive factor attachment protein receptor). Vti1a interacts with syntaxin 16 (Qa), syntaxin 6 (Qc), and the lysosomal R-SNARE VAMP4 to form an endosomal SNARE core complex that mediates transport from the early endosomes to the TGN (trans-Golgi network). 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). 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 SNAREs are N-terminal domains of SNAP23 and SNAP25, Vti1, Sec20 and GS27. Pssm-ID: 277244 Cd Length: 62 Bit Score: 39.97 E-value: 2.61e-05
|
||||||
| Name | Accession | Description | Interval | E-value | ||
| V-SNARE | pfam05008 | Vesicle transport v-SNARE protein N-terminus; V-SNARE proteins are required for protein ... |
12-90 | 2.07e-23 | ||
Vesicle transport v-SNARE protein N-terminus; V-SNARE proteins are required for protein traffic between eukaryotic organelles. The v-SNAREs on transport vesicles interact with t-SNAREs on target membranes in order to facilitate this. This domain is the N-terminal half of the V-Snare proteins. Pssm-ID: 461516 Cd Length: 79 Bit Score: 87.28 E-value: 2.07e-23
|
||||||
| SNARE_Vti1a | cd15891 | SNARE motif of Vti1b-like; Vti1a (vesicle transport through interaction with t-SNAREs homolog ... |
129-149 | 2.61e-05 | ||
SNARE motif of Vti1b-like; Vti1a (vesicle transport through interaction with t-SNAREs homolog 1A) belongs to the Qb subgroup of SNAREs (soluble N-ethylmaleimide-sensitive factor attachment protein receptor). Vti1a interacts with syntaxin 16 (Qa), syntaxin 6 (Qc), and the lysosomal R-SNARE VAMP4 to form an endosomal SNARE core complex that mediates transport from the early endosomes to the TGN (trans-Golgi network). 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). 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 SNAREs are N-terminal domains of SNAP23 and SNAP25, Vti1, Sec20 and GS27. Pssm-ID: 277244 Cd Length: 62 Bit Score: 39.97 E-value: 2.61e-05
|
||||||
| Blast search parameters | ||||
|
