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 18396813   5 QDPFYIVKEEIQDSIDKLQSTFHKWERISPDMGDQAHVAKELVATCGSIEWQVDELEKAITVAAKDPSWYGIDEAELEKR 84
Cdd:cd21445   1 QDPFYLVRDEIQESVDKLQQSFRRWEGLPAGSAERARLARELESDCESLEWQVDELDRAVDVAERDPARFGLSAAELESR 80

                        90
                ....*....|....*...
gi 18396813  85 RRWTSNARTQVRNVKSGV 102
Cdd:cd21445  81 RRWTSATRDQVSGIKEAL 98

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        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 18396813   189 RIIDELDTEMDSTKNRLEFVQKKVGMVMKKAGAKGQMMMICFLLVLFIILFV 240
Cdd:pfam05739   1 EMLDRIDTNVENAQSNVERAQKELKKAVKYQKSNRKLKCIILLILVIILLVV 52

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 18396813   5 QDPFYIVKEEIQDSIDKLQSTFHKWERISPDMGDQAHVAKELVATCGSIEWQVDELEKAITVAAKDPSWYGIDEAELEKR 84
Cdd:cd21445   1 QDPFYLVRDEIQESVDKLQQSFRRWEGLPAGSAERARLARELESDCESLEWQVDELDRAVDVAERDPARFGLSAAELESR 80

                        90
                ....*....|....*...
gi 18396813  85 RRWTSNARTQVRNVKSGV 102
Cdd:cd21445  81 RRWTSATRDQVSGIKEAL 98

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.

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 18396813 156 IKQQDEELDELSKSVQRIGGVGLTIHDELVAQERIIDELDTEMDSTKNRLEFVQKKV 212
Cdd:cd15841   1 MKEQDEQLDELSGSVGRLKNIALAINEELDLQNRLLDDLDEDVDKTQSRLKKVNKKL 57

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".

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18396813    150 DRQMLLIKQQDEELDELSKSVQRIGGVGLTIHDELVAQERIIDELDTEMDSTKNRLEFVQKKV 212
Cdd:smart00397   1 QQALAREEERDEELEQLEKSIQELKQIFLDMGTELEEQGEQLDRIEDNVDDADVNLKKANKRL 63

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 18396813   5 QDPFYIVKEEIQDSIDKLQSTFHKWERISPDMGDQAHVAKELVATCGSIEWQVDELEKAITVAAKDPSWYGIDEAELEKR 84
Cdd:cd21445   1 QDPFYLVRDEIQESVDKLQQSFRRWEGLPAGSAERARLARELESDCESLEWQVDELDRAVDVAERDPARFGLSAAELESR 80

                        90
                ....*....|....*...
gi 18396813  85 RRWTSNARTQVRNVKSGV 102
Cdd:cd21445  81 RRWTSATRDQVSGIKEAL 98

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 18396813   6 DPFYIVKEEIQDSIDKLQSTFHKWERI-----SPDMGDQAHVAKELVATCGSIEWQVDELEKAITVAAKDPSWYGIDEAE 80
Cdd:cd21442   1 DPFFEAKEEVQASLDRAESLYRSWLRIrktaqSGSSEELSDARNELKTTLGTLEWDLEDLEESVRVVEADGKRFGISEDE 80

                        90       100
                ....*....|....*....|...
gi 18396813  81 LEKRRRWTSNARTQVRNVKSGVL 103
Cdd:cd21442  81 VSRRRQFVRRIRQQIEAMKKDVK 103

N-terminal domain of syntaxin-6, syntaxin-10, and similar proteins; This subfamily includes two soluble NSF attachment protein receptor (SNARE) proteins, syntaxin-6 (STX6) and syntaxin-10 (STX10). 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. This model corresponds to the N-terminal domain of STX6 and STX10, which is a regulatory domain named Habc.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396813   6 DPFYIVKEEIQDSIDKLQSTFHKWERISPDMGDQA-----HVAKELVATCGSIEWQVDELEKAITVAAKDPSWYGIDEAE 80
Cdd:cd21443   1 DPFFVVKDEVEKALNKAQELYERWRELQDEDSTSSneeleWTTNELRNSLRSIEWDLEDLEETIGIVEKNPSKFKLDAEE 80

                        90       100
                ....*....|....*....|..
gi 18396813  81 LEKRRRWTSNARTQVRNVKSGV 102
Cdd:cd21443  81 IQARRQFIEETRQEVKEIKDEL 102

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.

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 18396813 156 IKQQDEELDELSKSVQRIGGVGLTIHDELVAQERIIDELDTEMDSTKNRLEFVQKKVG 213
Cdd:cd15858   1 MQEQDQQLEQLRKIVQRQKELGLAINQELEEQNELLDELDEDVDRTGGKLRVANKRAK 58

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 18396813 156 IKQQDEELDELSKSVQRIGGVGLTIHDELVAQERIIDELDTEMDSTKNRLEFVQKKVGMVMKKAGAKG 223
Cdd:cd15859   1 LLEQDEHLDHLSASIRRQHELSLQINDELDEQNELLDDLENGVDRTGRRLNRARRRLDKFRRKARENG 68

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 18396813 156 IKQQDEELDELSKSVQRIGGVGLTIHDELVAQERIIDELDTEMDSTKNRLE 206
Cdd:cd15852   1 IQEQDQGLDALSSIISRQKQIGQAIGDEVDDQNEIIDDLADGMDRTDARLR 51

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 18396813   6 DPFYIVKEEIQDSIDKLQSTFHKWERISPDmgDQAH----VAKELVATcgsiewqVDELEKAITVAAKDPSWYGIDEAEL 81
Cdd:cd21444   1 DPFNQVQEDAWSQLERLRQLLTSYLRIPTN--EAKSdfenNIQELEET-------IEDLKQSVEISEADPERFGLDEEEI 71

                        90
                ....*....|....*....
gi 18396813  82 EKRRRWTSNARTQVRNVKS 100
Cdd:cd21444  72 SERERIVAELESQLDDLKE 90

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
                ....*....|....*....|....*....|....*....|....*...
gi 18396813 158 QQDEELDELSKSVQRIGGVGLTIHDELVAQERIIDELDTEMDSTKNRL 205
Cdd:cd15853   3 QNDRRLDELSSKVSALKSLTIDIGDEVRDQNKLLDGMGDDFDSTGGLL 50

t-SNARE complex subunit, syntaxin [Intracellular trafficking and secretion];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18396813 142 DGFVQSESDRQMLLIKQQDEELDELSKSVQRIGGVGLTIHDELVAQERIIDELDTEMDSTKNRLEFVQKKVGMVMKKAGA 221
Cdd:COG5325 176 QGLSNEELEYQQILITERDEEIKNLARGIYELNEIFRDLGSLVGEQGELVDRIDFNIENTSDNLKNANKELEKAPAHQRR 255

                        90       100
                ....*....|....*....|.
gi 18396813 222 KGQMMMICFLLVLFIILFVLV 242
Cdd:COG5325 256 TKKCRFYLLLILLVVLLFVSL 276