Syntaxin-like protein; This domain includes syntaxin-like domains including from the Vam3p protein.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972648  265 SANVFRINSSVTSLERSLQSLGTPSDTQELRDSLHTAQQETNKTIAASASSVKQMAELLRSSCPqerlQQERPQLDRLKT 344
Cdd:pfam14523   2 SSNLFKINSNVSTLEKLVKQLGTKRDTQELRDKLHKLIEKTNELIKETSELLKKLSSLENLSSD----SQQKLQKEKLSR 77

                          90       100
                  ....*....|....*....|..
gi 223972648  345 QLSDAIQCYGVVQKKIAEKSRA 366
Cdd:pfam14523  78 DFKEALQEFQKLQRQYAEKEKA 99

SNARE motif of TSNARE1; TSNARE1 is member of the Qa 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. Its function is unknown, but polymorphisms in human TSNARE1 have been associated with schizophrenia susceptibility. 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. TSNARE1 is part of a subgroup of the Qa SNAREs that also includes syntaxin 7, syntaxin 12 and related proteins.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223972648 416 LEAIRLREEAILQMESNLLDVNQIIKDLASMVSEQGEAVDSIEASLEAASSHAEAARQLLAGAS 479
Cdd:cd15877    1 LEAIRQREEAIQQIESDMLDVNQIIKDLASMVSEQGDTIDSIEANIEAASSHVESANQQLAKAS 64

Syntaxin-like protein; This domain includes syntaxin-like domains including from the Vam3p protein.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972648  265 SANVFRINSSVTSLERSLQSLGTPSDTQELRDSLHTAQQETNKTIAASASSVKQMAELLRSSCPqerlQQERPQLDRLKT 344
Cdd:pfam14523   2 SSNLFKINSNVSTLEKLVKQLGTKRDTQELRDKLHKLIEKTNELIKETSELLKKLSSLENLSSD----SQQKLQKEKLSR 77

                          90       100
                  ....*....|....*....|..
gi 223972648  345 QLSDAIQCYGVVQKKIAEKSRA 366
Cdd:pfam14523  78 DFKEALQEFQKLQRQYAEKEKA 99

SNARE motif of TSNARE1; TSNARE1 is member of the Qa 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. Its function is unknown, but polymorphisms in human TSNARE1 have been associated with schizophrenia susceptibility. 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. TSNARE1 is part of a subgroup of the Qa SNAREs that also includes syntaxin 7, syntaxin 12 and related proteins.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223972648 416 LEAIRLREEAILQMESNLLDVNQIIKDLASMVSEQGEAVDSIEASLEAASSHAEAARQLLAGAS 479
Cdd:cd15877    1 LEAIRQREEAIQQIESDMLDVNQIIKDLASMVSEQGDTIDSIEANIEAASSHVESANQQLAKAS 64

Syntaxin N-terminal domain; Three-helix domain that (in Sso1p) slows the rate of its reaction with the SNAP-25 homologue Sec9p

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972648   258 QELFQEMSANVFRINSSVTSLERSLQSLGTPSDT-QELRDSLHTAQQETNKTIAASASSVKQMAELL----RSSCPQERL 332
Cdd:smart00503   7 FEKVEEIRANIQKISQNVAELQKLHEELLTPPDAdKELREKLERLIDDIKRLAKEIRAKLKELEKENlenrASGSASDRT 86

                           90       100       110
                   ....*....|....*....|....*....|...
gi 223972648   333 QQErpQLDRLKTQLSDAIQCYGVVQKKIAEKSR 365
Cdd:smart00503  87 RKA--QTEKLRKKFKEVMNEFQRLQRKYREREK 117

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
                   ....*....|....*....|....*....|....*....|
gi 223972648   422 REEAILQMESNLLDVNQIIKDLASMVSEQGEAVDSIEASL 461
Cdd:smart00397  10 RDEELEQLEKSIQELKQIFLDMGTELEEQGEQLDRIEDNV 49

Syntaxin-like protein; This domain includes syntaxin-like domains including from the Vam3p protein.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972648  265 SANVFRINSSVTSLERSLQSLGTPSDTQELRDSLHTAQQETNKTIAASASSVKQMAELLRSSCPqerlQQERPQLDRLKT 344
Cdd:pfam14523   2 SSNLFKINSNVSTLEKLVKQLGTKRDTQELRDKLHKLIEKTNELIKETSELLKKLSSLENLSSD----SQQKLQKEKLSR 77

                          90       100
                  ....*....|....*....|..
gi 223972648  345 QLSDAIQCYGVVQKKIAEKSRA 366
Cdd:pfam14523  78 DFKEALQEFQKLQRQYAEKEKA 99

SNARE motif of TSNARE1; TSNARE1 is member of the Qa 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. Its function is unknown, but polymorphisms in human TSNARE1 have been associated with schizophrenia susceptibility. 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. TSNARE1 is part of a subgroup of the Qa SNAREs that also includes syntaxin 7, syntaxin 12 and related proteins.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223972648 416 LEAIRLREEAILQMESNLLDVNQIIKDLASMVSEQGEAVDSIEASLEAASSHAEAARQLLAGAS 479
Cdd:cd15877    1 LEAIRQREEAIQQIESDMLDVNQIIKDLASMVSEQGDTIDSIEANIEAASSHVESANQQLAKAS 64

SNARE motif of syntaxin 7; Syntaxin 7 forms a complex with syntaxin 8 (Qc), Vti1b (Qb) and either VAMP7 or VAMP8 (R-SNARE) and is involved in the transport from early endosomes to the lysosome. Syntaxin 7 is member of the Qa 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 223972648 419 IRLREEAILQMESNLLDVNQIIKDLASMVSEQGEAVDSIEASLEAASSHAEAARQLLAGA 478
Cdd:cd15875    1 LEERERSIRQLESDIMDVNQIFKDLGMLVHEQGEVIDSIEANVETAAVHVEEANQQLSQA 60

SNARE motif, subgroup Qa; 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-, 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. Examples for members of the Qa SNAREs are syntaxin 18, syntaxin 5, syntaxin 16, and syntaxin 1.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 223972648 419 IRLREEAILQMESNLLDVNQIIKDLASMVSEQGEAVDSIEASL 461
Cdd:cd15840    1 IEEREEEIREIESSIGEVNEIFKDLATLVTEQGEQIDNIENNI 43

Syntaxin N-terminal domain; Three-helix domain that (in Sso1p) slows the rate of its reaction with the SNAP-25 homologue Sec9p

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223972648   258 QELFQEMSANVFRINSSVTSLERSLQSLGTPSDT-QELRDSLHTAQQETNKTIAASASSVKQMAELL----RSSCPQERL 332
Cdd:smart00503   7 FEKVEEIRANIQKISQNVAELQKLHEELLTPPDAdKELREKLERLIDDIKRLAKEIRAKLKELEKENlenrASGSASDRT 86

                           90       100       110
                   ....*....|....*....|....*....|...
gi 223972648   333 QQErpQLDRLKTQLSDAIQCYGVVQKKIAEKSR 365
Cdd:smart00503  87 RKA--QTEKLRKKFKEVMNEFQRLQRKYREREK 117

SNARE motif of syntaxin 1 and related proteins; 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-, 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. This subgroup of the Qa SNAREs includes syntaxin 1, syntaxin 11, syntaxin 19, syntaxin 2, syntaxin 3, syntaxin 4 and related proteins.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 223972648 416 LEAIRLREEAILQMESNLLDVNQIIKDLASMVSEQGEAVDSIE 458
Cdd:cd15848    2 LADIEERHQDILKLEKSIRELHQMFLDMAVLVESQGELIDNIE 44

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
                   ....*....|....*....|....*....|....*....|
gi 223972648   422 REEAILQMESNLLDVNQIIKDLASMVSEQGEAVDSIEASL 461
Cdd:smart00397  10 RDEELEQLEKSIQELKQIFLDMGTELEEQGEQLDRIEDNV 49

SNARE motif of syntaxin 5; Syntaxin 5 (Syn5) regulates the transport from the ER to the Golgi, as well as the early/recycling endosomes to the trans-Golgi network and participates in the assembly of transitional ER and the Golgi, lipid droplet fusion, and cytokinesis. Syn5 exists in 2 isoforms, long (42 kDa) and short (35 kDa). The short form is localized in the Golgi complex, whereas the long form is additionally found in the endoplasmic reticulum (ER). The syntaxin-5 SNARE complexes, which also contain Bet1 (Qc) and either GS27 (Qb) and Sec22B (R-SNARE) or GS28 (Qb) and Ykt6 (R-SNARE), regulate the early secretory pathway of eukaryotic cells at the level of endoplasmic reticulum (ER) to Golgi transport. The syntaxin-5 SNARE complex, which also contains GS15 (Qc), GS28 (Qb) and Ykt6 (R-SNAREs) is involved in the transport from the trans-Golgi network to the cis-Golgi. Syn5 is member of the Qa 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 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.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 223972648 419 IRLREEAILQMESNLLDVNQIIKDLASMVSEQGEAVDSIEA 459
Cdd:cd15844    1 LQSRADAVQNIESTIVELGQIFQQLATMVAEQGEMVQRIDE 41

SNARE motif of Sso1; Saccharomyces cerevisiae SNARE protein Sso1p forms a complex with synaptobrevin homolog Snc1p (R-SNARE) and the SNAP-25 homolog Sec9p (Qb/c) which is involved in exocytosis. Sso1 is member of the Qa 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
                 ....*....|....*....|....*....|....*....|...
gi 223972648 416 LEAIRLREEAILQMESNLLDVNQIIKDLASMVSEQGEAVDSIE 458
Cdd:cd15849    1 LGEVQARHNEIQRIEQTLTELAQLFNDMATLVEQQDEVIQQIE 43

SNARE motif of syntaxin 2; Syntaxin 2 (STX2), also known as epimorphin (EPM or EPIM), may interact with SNAP-23 (Qb/c) and genetic varioations are associated with type 1 von Willebrand disease (VWD). Syntaxin 2 is a member of the Qa 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
                 ....*....|....*....|....*....|....*....|...
gi 223972648 416 LEAIRLREEAILQMESNLLDVNQIIKDLASMVSEQGEAVDSIE 458
Cdd:cd15882    2 LNEIESRHKDIMKLESSIRELHDMFVDMAMLVETQGEMINNIE 44

SNARE motif of syntaxin 1; Syntaxin-1 belongs to the Qa subgroup of SNAREs and interacts with SNAP-25 (Qb/Qc) and the R-SNARE VAMP2 (also called synaptobrevin-2). The complex plays a role in exocytosis of synaptic vesicles. 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
                 ....*....|....*....|....*....|....*....|....
gi 223972648 415 DLEAirlREEAILQMESNLLDVNQIIKDLASMVSEQGEAVDSIE 458
Cdd:cd15880    4 EIEA---RHNDIIKLENSIRELHDMFMDMAMLVESQGEMIDRIE 44

SNARE motif of syntaxin 11; Syntaxin 11 (also known as STX11, FHL4, HLH4, HPLH4) is present on endosomal membranes, including late endosomes and lysosomes in macrophages, and has been shown to bind Vti1b and regulate the availability of Vti1b to form other SNARE-complexes. Mutations in human STX11 has been linked to familial hemophagocytic lymphohistiocytosis type-4 (FHL-4), an autosomal recessive disorder of immune dysregulation. Syntaxin 11 is a member of the Qa 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
                 ....*....|....*....|....*....|....*....|....*.
gi 223972648 416 LEAIRLREEAILQMESNLLDVNQIIKDLASMVSEQGEAVDSIEASL 461
Cdd:cd15878    2 LNEIETRHKELLELESRIREVHELFLQMALLVEEQADTLNNIELNV 47