Membrane fusion protein Use1 [Arabidopsis thaliana]
SNARE domain-containing protein( domain architecture ID 366304)
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
List of domain hits
Name | Accession | Description | Interval | E-value | |||||
Use1 super family | cl48070 | Membrane fusion protein Use1; This entry is of a family of proteins all approximately 300 ... |
5-236 | 4.34e-63 | |||||
Membrane fusion protein Use1; This entry is of a family of proteins all approximately 300 residues in length. The proteins have a single C-terminal trans-membrane domain and a SNARE [soluble NSF (N-ethylmaleimide-sensitive fusion protein) attachment protein receptor] domain of approximately 60 residues. The SNARE domains are essential for membrane fusion and are conserved from yeasts to humans. Use1 is one of the three protein subunits that make up the SNARE complex and it is specifically required for Golgi-endoplasmic reticulum retrograde transport. The actual alignment was detected with superfamily member pfam09753: Pssm-ID: 462882 [Multi-domain] Cd Length: 245 Bit Score: 196.78 E-value: 4.34e-63
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Name | Accession | Description | Interval | E-value | |||||
Use1 | pfam09753 | Membrane fusion protein Use1; This entry is of a family of proteins all approximately 300 ... |
5-236 | 4.34e-63 | |||||
Membrane fusion protein Use1; This entry is of a family of proteins all approximately 300 residues in length. The proteins have a single C-terminal trans-membrane domain and a SNARE [soluble NSF (N-ethylmaleimide-sensitive fusion protein) attachment protein receptor] domain of approximately 60 residues. The SNARE domains are essential for membrane fusion and are conserved from yeasts to humans. Use1 is one of the three protein subunits that make up the SNARE complex and it is specifically required for Golgi-endoplasmic reticulum retrograde transport. Pssm-ID: 462882 [Multi-domain] Cd Length: 245 Bit Score: 196.78 E-value: 4.34e-63
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SNARE_USE1 | cd15860 | SNARE motif of USE1; USE1 (unconventional SNARE in the ER 1 homolog, also known as SNARE-like ... |
144-203 | 4.68e-12 | |||||
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: 59.12 E-value: 4.68e-12
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Name | Accession | Description | Interval | E-value | |||||
Use1 | pfam09753 | Membrane fusion protein Use1; This entry is of a family of proteins all approximately 300 ... |
5-236 | 4.34e-63 | |||||
Membrane fusion protein Use1; This entry is of a family of proteins all approximately 300 residues in length. The proteins have a single C-terminal trans-membrane domain and a SNARE [soluble NSF (N-ethylmaleimide-sensitive fusion protein) attachment protein receptor] domain of approximately 60 residues. The SNARE domains are essential for membrane fusion and are conserved from yeasts to humans. Use1 is one of the three protein subunits that make up the SNARE complex and it is specifically required for Golgi-endoplasmic reticulum retrograde transport. Pssm-ID: 462882 [Multi-domain] Cd Length: 245 Bit Score: 196.78 E-value: 4.34e-63
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SNARE_USE1 | cd15860 | SNARE motif of USE1; USE1 (unconventional SNARE in the ER 1 homolog, also known as SNARE-like ... |
144-203 | 4.68e-12 | |||||
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: 59.12 E-value: 4.68e-12
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Blast search parameters | ||||
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