vesicle transport through interaction with t-SNAREs homolog 1A isoform X3 [Canis lupus familiaris]
Protein Classification
V-SNARE and SNARE domain-containing protein( domain architecture ID 10523371)
V-SNARE and SNARE domain-containing protein
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 | 1.29e-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: 89.59 E-value: 1.29e-23
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| SNARE super family | cl22856 | SNARE motif; SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) ... |
129-153 | 5.92e-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. The actual alignment was detected with superfamily member cd15891: Pssm-ID: 473982 Cd Length: 62 Bit Score: 44.98 E-value: 5.92e-07
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| 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 | 1.29e-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: 89.59 E-value: 1.29e-23
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| SNARE_Vti1a | cd15891 | SNARE motif of Vti1b-like; Vti1a (vesicle transport through interaction with t-SNAREs homolog ... |
129-153 | 5.92e-07 | ||
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: 44.98 E-value: 5.92e-07
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| 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 | 1.29e-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: 89.59 E-value: 1.29e-23
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| SNARE_Vti1a | cd15891 | SNARE motif of Vti1b-like; Vti1a (vesicle transport through interaction with t-SNAREs homolog ... |
129-153 | 5.92e-07 | ||
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: 44.98 E-value: 5.92e-07
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| SNARE_Vti1 | cd15862 | SNARE motif of Vti1; Vti1 (vesicle transport through interaction with t-SNAREs homolog 1) ... |
129-150 | 4.36e-03 | ||
SNARE motif of Vti1; Vti1 (vesicle transport through interaction with t-SNAREs homolog 1) belongs to the Qb subgroup of SNAREs (soluble N-ethylmaleimide-sensitive factor attachment protein receptor). Vti1b interacts with syntaxin 7 (Qa), syntaxin 8 (Qc), and the lysosomal R-SNARE VAMP8 or VAMP7 to form the endosomal SNARE core complex that mediates transport from the early endosomes and the MVBs (multivesicular bodies), and from the MVBs to the lysosomes, respectively. 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: 277215 Cd Length: 62 Bit Score: 34.43 E-value: 4.36e-03
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