N-terminal domain of syntaxin-10; Syntaxin-10 (STX10), also called Syn10, is part of a soluble NSF attachment protein receptor (SNARE) complex involved in vesicular transport from the late endosomes to the trans-Golgi network, such as the transport of mannose 6-phosphate receptors from endosomes to the Golgi after delivering lysosomal enzymes to the endocytic pathway. This model corresponds to the N-terminal domain of STX10, which is a regulatory domain named Habc.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507285    5 DPFFVVRGEVQKAVNTARGLYQRWCELLQESAAVGREELDWTTNELRNGLRSIEWDLEDLEETIGIVEANPGKFKLPAGD 84
Cdd:cd21446   1 DPFFVVKGEVQKAVNTARGLYQRWCELLQESVAVSKEELDWTTNELRNSLRSIEWDLEDLEETIGIVESNPRKFKIDPGE 80

                        90       100
                ....*....|....*....|...
gi 4507285   85 LQERKVFVERMREAVQEMKDHMV 107
Cdd:cd21446  81 LAERRAFVERTRESVKEMKDHMA 103

N-terminal domain of syntaxin-10; Syntaxin-10 (STX10), also called Syn10, is part of a soluble NSF attachment protein receptor (SNARE) complex involved in vesicular transport from the late endosomes to the trans-Golgi network, such as the transport of mannose 6-phosphate receptors from endosomes to the Golgi after delivering lysosomal enzymes to the endocytic pathway. This model corresponds to the N-terminal domain of STX10, which is a regulatory domain named Habc.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507285    5 DPFFVVRGEVQKAVNTARGLYQRWCELLQESAAVGREELDWTTNELRNGLRSIEWDLEDLEETIGIVEANPGKFKLPAGD 84
Cdd:cd21446   1 DPFFVVKGEVQKAVNTARGLYQRWCELLQESVAVSKEELDWTTNELRNSLRSIEWDLEDLEETIGIVESNPRKFKIDPGE 80

                        90       100
                ....*....|....*....|...
gi 4507285   85 LQERKVFVERMREAVQEMKDHMV 107
Cdd:cd21446  81 LAERRAFVERTRESVKEMKDHMA 103

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.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4507285  160 MDEQDQQLEMVSGSIQVLKHMSGRVGEELDEQGIMLDAFAQEMDHTQSRMDGVLRKLAKVSHMTSD 225
Cdd:cd15851   1 MREQDEQLDGVGGTVGNLREQAQLIGDELEEQAELLDDLDHEVDRTESRLDRGMKKMAKVIRKNED 66

SNARE domain; Most if not all vesicular membrane fusion events in eukaryotic cells are believed to be mediated by a conserved fusion machinery, the SNARE [soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein (SNAP) receptors] machinery. The SNARE domain is thought to act as a protein-protein interaction module in the assembly of a SNARE protein complex.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 4507285    194 MLDAFAQEMDHTQSRMDGVLRKLAKVSHMTSDRRQWCAIA 233
Cdd:pfam05739   2 MLDRIDTNVENAQSNVERAQKELKKAVKYQKSNRKLKCII 41

N-terminal domain of syntaxin-10; Syntaxin-10 (STX10), also called Syn10, is part of a soluble NSF attachment protein receptor (SNARE) complex involved in vesicular transport from the late endosomes to the trans-Golgi network, such as the transport of mannose 6-phosphate receptors from endosomes to the Golgi after delivering lysosomal enzymes to the endocytic pathway. This model corresponds to the N-terminal domain of STX10, which is a regulatory domain named Habc.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507285    5 DPFFVVRGEVQKAVNTARGLYQRWCELLQESAAVGREELDWTTNELRNGLRSIEWDLEDLEETIGIVEANPGKFKLPAGD 84
Cdd:cd21446   1 DPFFVVKGEVQKAVNTARGLYQRWCELLQESVAVSKEELDWTTNELRNSLRSIEWDLEDLEETIGIVESNPRKFKIDPGE 80

                        90       100
                ....*....|....*....|...
gi 4507285   85 LQERKVFVERMREAVQEMKDHMV 107
Cdd:cd21446  81 LAERRAFVERTRESVKEMKDHMA 103

N-terminal domain of syntaxin-6; Syntaxin-6 (STX6) is a component of a soluble NSF attachment protein receptor (SNARE) complex involved in intracellular vesicle trafficking and in the fusion of retrograde transport carriers with the trans-Golgi network (TGN). This model corresponds to N-terminal domain of STX6, which is a regulatory domain named Habc.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507285    5 DPFFVVRGEVQKAVNTARGLYQRWCELLQESAAVGREELDWTTNELRNGLRSIEWDLEDLEETIGIVEANPGKFKLPAGD 84
Cdd:cd21447   1 DPFFVVKGEVQKAVNTAQGLFQRWTELLQDPSSATKEEIDWTTNELRNSLRSIEWDLEDLDETISIVEANPRKFNLDPTE 80

                        90       100
                ....*....|....*....|..
gi 4507285   85 LQERKVFVERMREAVQEMKDHM 106
Cdd:cd21447  81 LSIRKAFITSTRQVVREMKDQM 102

N-terminal domain of syntaxin-6 and similar proteins; The family includes soluble NSF attachment protein receptor (SNARE) proteins, syntaxin-6 (STX6) and syntaxin-10 (STX10), and their homologs found in fungi and plants, such as Tlg1p, AtSYP61, and similar proteins. STX6 is involved in intracellular vesicle trafficking. STX10, also called Syn10, is involved in vesicular transport from the late endosomes to the trans-Golgi network. Tlg1p, also called syntaxin TLG1, is a SNARE protein (of Qc type) involved in membrane fusion probably in retrograde traffic of cytosolic double-membrane vesicles derived from both, early and possibly late endosomes/PVC (prevacuolar compartment) back to the trans-Golgi network (TGN or late Golgi). It has been reported to function both as a (target membrane) t-SNARE and as a (vesicle) v-SNARE. AtSYP61, also called osmotic stress-sensitive mutant 1 (OSM1), is a vesicle trafficking syntaxin protein that functions in the secretory pathway. It is involved in osmotic stress tolerance and in abscisic acid (ABA) regulation of stomatal responses in Arabidopsis.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507285    5 DPFFVVRGEVQKAVNTARGLYQRWCELLQESAAVGREELDWTTNELRNGLRSIEWDLEDLEETIGIVEANPGKFKLPAGD 84
Cdd:cd21442   1 DPFFEAKEEVQASLDRAESLYRSWLRIRKTAQSGSSEELSDARNELKTTLGTLEWDLEDLEESVRVVEADGKRFGISEDE 80

                        90       100
                ....*....|....*....|..
gi 4507285   85 LQERKVFVERMREAVQEMKDHM 106
Cdd:cd21442  81 VSRRRQFVRRIRQQIEAMKKDV 102

N-terminal domain of Arabidopsis thaliana syntaxin-61 and similar proteins; Arabidopsis thaliana syntaxin-61 (AtSYP61), also called osmotic stress-sensitive mutant 1 (OSM1), is a vesicle trafficking syntaxin protein that functions in the secretory pathway. It is involved in osmotic stress tolerance and in abscisic acid (ABA) regulation of stomatal responses in Arabidopsis. This model corresponds to the N-terminal domain of AtSYP61, which shows high sequence similarity with the N-terminal domain of yeast Tlg1p, a soluble NSF attachment protein receptor (SNARE) protein (of Qc type) involved in membrane fusion.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507285    5 DPFFVVRGEVQKAVNTARGLYQRWcELLQESAAvgreELDWTTNELRNGLRSIEWDLEDLEETIGIVEANPGKFKLPAGD 84
Cdd:cd21445   2 DPFYLVRDEIQESVDKLQQSFRRW-EGLPAGSA----ERARLARELESDCESLEWQVDELDRAVDVAERDPARFGLSAAE 76

                        90       100
                ....*....|....*....|
gi 4507285   85 LQERKVFVERMREAVQEMKD 104
Cdd:cd21445  77 LESRRRWTSATRDQVSGIKE 96

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.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4507285  160 MDEQDQQLEMVSGSIQVLKHMSGRVGEELDEQGIMLDAFAQEMDHTQSRMDGVLRKLAKVSHMTSD 225
Cdd:cd15859   1 LLEQDEHLDHLSASIRRQHELSLQINDELDEQNELLDDLENGVDRTGRRLNRARRRLDKFRRKARE 66

N-terminal domain of t-SNARE affecting a late Golgi compartment protein 1 and similar proteins; t-SNARE affecting a late Golgi compartment protein 1 (Tlg1p), also called syntaxin TLG1, is a soluble NSF attachment protein receptor (SNARE) protein (of Qc type) involved in membrane fusion, probably in retrograde traffic of cytosolic double-membrane vesicles derived from both, early and possibly late endosomes/PVC (prevacuolar compartment) back to the trans-Golgi network (TGN or late Golgi). It has been reported to function both as a (target membrane) t-SNARE and as a (vesicle) v-SNARE. The model corresponds to the N-terminal domain of Tlg1p, which consists of a three-helix bundle.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507285    5 DPFFVVRGEVQKAVNTARGLYQRWcellqesaavGREELDWTTNELRNGLRSIEWDLEDLEETIGIVEANPGKFKLPAGD 84
Cdd:cd21444   1 DPFNQVQEDAWSQLERLRQLLTSY----------LRIPTNEAKSDFENNIQELEETIEDLKQSVEISEADPERFGLDEEE 70

                        90       100
                ....*....|....*....|..
gi 4507285   85 LQERKVFVERMREAVQEMKDHM 106
Cdd:cd21444  71 ISERERIVAELESQLDDLKEEW 92

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.

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 4507285  160 MDEQDQQLEMVSGSIQVLKHMSGRVGEELDEQGIMLDAFAQEMDHTQSRM 209
Cdd:cd15852   1 IQEQDQGLDALSSIISRQKQIGQAIGDEVDDQNEIIDDLADGMDRTDARL 50

SNARE domain; Most if not all vesicular membrane fusion events in eukaryotic cells are believed to be mediated by a conserved fusion machinery, the SNARE [soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein (SNAP) receptors] machinery. The SNARE domain is thought to act as a protein-protein interaction module in the assembly of a SNARE protein complex.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 4507285    194 MLDAFAQEMDHTQSRMDGVLRKLAKVSHMTSDRRQWCAIA 233
Cdd:pfam05739   2 MLDRIDTNVENAQSNVERAQKELKKAVKYQKSNRKLKCII 41

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.

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 4507285  161 DEQDQQLEMVSGSIQVLKHMSGRVGEELDEQGIMLDAFAQEMDHTQSRMDGVLRKL 216
Cdd:cd15853   2 SQNDRRLDELSSKVSALKSLTIDIGDEVRDQNKLLDGMGDDFDSTGGLLGGTMKRL 57

C-terminal SNARE motif of SNAP25; C-terminal SNARE motifs of SNAP25, a member of the Qb/Qc subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins. SNAP25 interacts with Syntaxin-1 (Qa) and the R-SNARE VAMP2 (also called synaptobrevin-2). The complex plays a role in transport of secretory granule from trans-Golgi network to the plasma membrane. Qb/Qc SNAREs consist of 2 coiled-coil helices (called SNARE motifs, one belonging to the Qb subgroup and one belonging to the Qc subgroup), which mediate the interactions with other SNARE proteins, and a transmembrane domain. In general, 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. Other members of the Qb/Qc SNAREs are SNAP23, SNAP29, SNAP47 and SEC9.

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 4507285  161 DEQDQQLEMVSGSIQVLKHMSGRVGEELDEQGIMLDAFAQEMDHTQSRMD 210
Cdd:cd15885   2 DEMEENLGQVSGMIGNLRNMAIDMGSEIESQNRQIDRINEKAESNETRID 51