hypothetical protein MATL_G00235480 [Megalops atlanticus]
Protein Classification
SNARE domain- containing protein( domain architecture ID 10205159)
SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) domain-containing protein such as Bet1, which forms complexes with GS27 (Qb), syntaxin-5 (Qa) and Sec22B (R-SNARE) or GS28 (Qb), syntaxin-5 (Qa) and Ykt6 (R-SNARE); these complexes regulate the early secretory pathway of eukaryotic cells at the level of the transport from endoplasmic reticulum (ER) to the ER-Golgi intermediate compartment (ERGIC) and from ERGIC to the cis-Golgi, respectively.
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| SNARE_Bet1 | cd15853 | SNARE motif of Bet1; Bet1 forms a complexes with GS27 (Qb), syntaxin-5 (Qa) and Sec22B ... |
24-81 | 1.53e-27 | ||
SNARE motif of Bet1; Bet1 forms a complexes with GS27 (Qb), syntaxin-5 (Qa) and Sec22B (R-SNARE) or GS28 (Qb), syntaxin-5 (Qa) and Ykt6 (R-SNARE). These complexes regulates the early secretory pathway of eukaryotic cells at the level of the transport from endoplasmic reticulum (ER) to the ER-Golgi intermediate compartment (ERGIC) and from ERGIC to the cis-Golgi, respectively. Bet1 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) which 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: 277206 Cd Length: 59 Bit Score: 95.65 E-value: 1.53e-27
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| Name | Accession | Description | Interval | E-value | |||
| SNARE_Bet1 | cd15853 | SNARE motif of Bet1; Bet1 forms a complexes with GS27 (Qb), syntaxin-5 (Qa) and Sec22B ... |
24-81 | 1.53e-27 | |||
SNARE motif of Bet1; Bet1 forms a complexes with GS27 (Qb), syntaxin-5 (Qa) and Sec22B (R-SNARE) or GS28 (Qb), syntaxin-5 (Qa) and Ykt6 (R-SNARE). These complexes regulates the early secretory pathway of eukaryotic cells at the level of the transport from endoplasmic reticulum (ER) to the ER-Golgi intermediate compartment (ERGIC) and from ERGIC to the cis-Golgi, respectively. Bet1 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) which 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: 277206 Cd Length: 59 Bit Score: 95.65 E-value: 1.53e-27
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| t_SNARE | smart00397 | Helical region found in SNAREs; All alpha-helical motifs that form twisted and parallel ... |
23-81 | 5.85e-09 | |||
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: 48.35 E-value: 5.85e-09
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| COG5074 | COG5074 | t-SNARE complex subunit, syntaxin [Intracellular trafficking, secretion, and vesicular ... |
24-105 | 2.22e-03 | |||
t-SNARE complex subunit, syntaxin [Intracellular trafficking, secretion, and vesicular transport]; Pssm-ID: 227406 [Multi-domain] Cd Length: 280 Bit Score: 36.02 E-value: 2.22e-03
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| Name | Accession | Description | Interval | E-value | |||
| SNARE_Bet1 | cd15853 | SNARE motif of Bet1; Bet1 forms a complexes with GS27 (Qb), syntaxin-5 (Qa) and Sec22B ... |
24-81 | 1.53e-27 | |||
SNARE motif of Bet1; Bet1 forms a complexes with GS27 (Qb), syntaxin-5 (Qa) and Sec22B (R-SNARE) or GS28 (Qb), syntaxin-5 (Qa) and Ykt6 (R-SNARE). These complexes regulates the early secretory pathway of eukaryotic cells at the level of the transport from endoplasmic reticulum (ER) to the ER-Golgi intermediate compartment (ERGIC) and from ERGIC to the cis-Golgi, respectively. Bet1 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) which 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: 277206 Cd Length: 59 Bit Score: 95.65 E-value: 1.53e-27
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| SNARE_Qc | cd15841 | SNARE motif, subgroup Qc; SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein ... |
23-81 | 2.35e-14 | |||
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: 62.19 E-value: 2.35e-14
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| SNARE_VAM7 | cd15858 | SNARE motif of VAM7; Fungal VAM7 (vacuolar morphogenesis protein 7) is a member of the Qc ... |
24-81 | 1.91e-10 | |||
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: 52.12 E-value: 1.91e-10
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| SNARE_SYN8 | cd15859 | SNARE motif of SYN8; Fungal SYN8 is a member of the Qc subfamily of SNARE (soluble ... |
24-85 | 5.22e-10 | |||
SNARE motif of SYN8; Fungal SYN8 is a member of the Qc subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) protein family presetn in the endosomes. 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: 277212 Cd Length: 68 Bit Score: 51.39 E-value: 5.22e-10
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| t_SNARE | smart00397 | Helical region found in SNAREs; All alpha-helical motifs that form twisted and parallel ... |
23-81 | 5.85e-09 | |||
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: 48.35 E-value: 5.85e-09
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| SNARE_Syntaxin6 | cd15851 | SNARE motif of syntaxin 6; Syntaxin 6 forms a complex with syntaxin 16 (Qa), Vti1a (Qb) and ... |
24-85 | 3.82e-07 | |||
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: 43.63 E-value: 3.82e-07
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| SNARE_Syntaxin8 | cd15852 | SNARE motif of syntaxin 8; Syntaxin 8 forms a complex with syntaxin 7 (Qa), Vti1b (Qb) and ... |
24-69 | 1.57e-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: 34.13 E-value: 1.57e-03
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| COG5074 | COG5074 | t-SNARE complex subunit, syntaxin [Intracellular trafficking, secretion, and vesicular ... |
24-105 | 2.22e-03 | |||
t-SNARE complex subunit, syntaxin [Intracellular trafficking, secretion, and vesicular transport]; Pssm-ID: 227406 [Multi-domain] Cd Length: 280 Bit Score: 36.02 E-value: 2.22e-03
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