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.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19113982  94 NFLEMQEANSLDNSIRGTNELLERAYATREDFDYQNSVLGNVTNRINGAAMSIPFINQILRKTSIR 159
Cdd:cd15864   1 TELYLKEHEHLRNSDRLIDEQISIAMATKENLTSQRGMLKSITSRMNTLANRFPAINSLIQKINLR 66

SNARE motif of GS28; GS28 (also known as golgi SNAP receptor complex member 1 or GOSR1) forms complexes with syntaxin-5 (Qa), Ykt6 (R-SNARE) and either Bet1 (Qc) or GS15 (Qc). These complexes regulate the early secretory pathway of eukaryotic cells at the level of the transport from the ER-Golgi intermediate compartment (ERGIC) to the cis-Golgi and transport from the trans-Golgi network to the cis-Golgi, respectively. GS28 is a member of the Qb subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins which contain coiled-coil helices (called SNARE motifs) that 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.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19113982  94 NFLEMQEANSLDNSIRGTNELLERAYATREDFDYQNSVLGNVTNRINGAAMSIPFINQILRKTSIR 159
Cdd:cd15864   1 TELYLKEHEHLRNSDRLIDEQISIAMATKENLTSQRGMLKSITSRMNTLANRFPAINSLIQKINLR 66

SNARE motif of GS28; GS28 (also known as golgi SNAP receptor complex member 1 or GOSR1) forms complexes with syntaxin-5 (Qa), Ykt6 (R-SNARE) and either Bet1 (Qc) or GS15 (Qc). These complexes regulate the early secretory pathway of eukaryotic cells at the level of the transport from the ER-Golgi intermediate compartment (ERGIC) to the cis-Golgi and transport from the trans-Golgi network to the cis-Golgi, respectively. GS28 is a member of the Qb subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins which contain coiled-coil helices (called SNARE motifs) that 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.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19113982  94 NFLEMQEANSLDNSIRGTNELLERAYATREDFDYQNSVLGNVTNRINGAAMSIPFINQILRKTSIR 159
Cdd:cd15864   1 TELYLKEHEHLRNSDRLIDEQISIAMATKENLTSQRGMLKSITSRMNTLANRFPAINSLIQKINLR 66

Snare region anchored in the vesicle membrane C-terminus; Within the SNARE proteins interactions in the C-terminal half of the SNARE helix are critical to the driving of membrane fusion; whereas interactions in the N-terminal half of the SNARE domain are important for promoting priming or docking of the vesicle pfam05008.

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                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19113982    95 FLEMQEANSLDNSIRGTNELLERAYATREDFDYQNSVLGNVTNRINGAAMSIPFINQILRKTSIRR 160
Cdd:pfam12352   1 ERLLREHDRLKNSHRIADETISIGQAILEDLHSQRETLKRARNKLHNTDNRLGKSNSTLRLINRRR 66