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        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196929748 258 IQNRADTMQNIESTIVELGSIFQQLAHMVKEQEETVHRIDANVEDTQLNVDLAHTEILKYFQSVSNNRWLLIKMFLVLVI 337
Cdd:cd15844     1 LQSRADAVQNIESTIVELGQIFQQLATMVAEQGEMVQRIDENVEDALANVEAAHSELLKYYRSISSNRWLILKIFGVLIV 80

                  ....*.
gi 1196929748 338 FFIVFV 343
Cdd:cd15844    81 FIVIFV 86

Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196929748  88 DFTLLAKRIGRDLSNTFAKLEKLT-----ILAKRKSLFDDKATE-IDELTYIVKQDINSLIKQIAGLQELVRSRSAQNGR 161
Cdd:pfam01442  34 ETEALRERLQKDLEEVRAKLEPYLeelqaKLGQNVEELRQRLEPyTEELRKRLNADAEELQEKLAPYGEELRERLEQNVD 113

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1196929748 162 HLQTHSNTIVVSLQSKLASMSSDFKSVLEVRTENLKQQ-RSRQEQFSQT 209
Cdd:pfam01442 114 ALRARLAPYAEELRQKLAERLEELKESLAPYAEEVQAQlSQRLQELREK 162

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        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196929748 258 IQNRADTMQNIESTIVELGSIFQQLAHMVKEQEETVHRIDANVEDTQLNVDLAHTEILKYFQSVSNNRWLLIKMFLVLVI 337
Cdd:cd15844     1 LQSRADAVQNIESTIVELGQIFQQLATMVAEQGEMVQRIDENVEDALANVEAAHSELLKYYRSISSNRWLILKIFGVLIV 80

                  ....*.
gi 1196929748 338 FFIVFV 343
Cdd:cd15844    81 FIVIFV 86

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196929748 173 SLQSKLASMSSDF---KSVLEVRTENLKQQRSRQE--QFSQTPASASAFHTNSFNNSVLMQDDSKKTDISIDMDLNSSQQ 247
Cdd:COG5325    96 ILKTKYKNLQSSFlqsKLLRDLNTECMEGQRIQQKsaQFRKYQVLQAKFLRNKNNDQHPLEEEEDEESLSSLGSQQTLQQ 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196929748 248 MQLVNERDSYIQN----RADTMQNIESTIVELGSIFQQLAHMVKEQEETVHRIDANVEDTQLNVDLAHTEILKYFQSVSN 323
Cdd:COG5325   176 QGLSNEELEYQQIliteRDEEIKNLARGIYELNEIFRDLGSLVGEQGELVDRIDFNIENTSDNLKNANKELEKAPAHQRR 255

                         170       180
                  ....*....|....*....|.
gi 1196929748 324 -NRWLLIKMFLVLVIFFIVFV 343
Cdd:COG5325   256 tKKCRFYLLLILLVVLLFVSL 276

Syntaxin-5 N-terminal, Sly1p-binding domain; Syntaxin-5_N is the Sed5 N-terminal and the N-terminus of Syntaxin-5-like proteins. It is the region of Syntaxin that interacts with Sly1p, a positive regulator of intracellular membrane fusion, allowing SM (cytosolic Sec1/munc18-like) proteins to stay associated with the assembling fusion machinery. This allows the SM proteins to participate in late fusion steps.

                          10        20
                  ....*....|....*....|...
gi 1196929748  47 TFSMSCRDRTGEFQSVCKSLQGR 69
Cdd:pfam11416   1 AAPTSIRDRTSEFQSIVKSLQKR 23

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        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196929748 258 IQNRADTMQNIESTIVELGSIFQQLAHMVKEQEETVHRIDANVEDTQLNVDLAHTEILKYFQSVSNNRWLLIKMFLVLVI 337
Cdd:cd15844     1 LQSRADAVQNIESTIVELGQIFQQLATMVAEQGEMVQRIDENVEDALANVEAAHSELLKYYRSISSNRWLILKIFGVLIV 80

                  ....*.
gi 1196929748 338 FFIVFV 343
Cdd:cd15844    81 FIVIFV 86

SNARE motif of syntaxin 7, 12 and related sequences; 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 7, syntaxin 12, TSNARE1 and related proteins.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1196929748 258 IQNRADTMQNIESTIVELGSIFQQLAHMVKEQEETVHRIDANVEDTQLNVDLAHTEILK 316
Cdd:cd15847     1 LLEREERIRQIESDILDVNQIFKDLATLVHEQGETIDSIEANIESAYVNVESGNSQLAK 59

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196929748 173 SLQSKLASMSSDF---KSVLEVRTENLKQQRSRQE--QFSQTPASASAFHTNSFNNSVLMQDDSKKTDISIDMDLNSSQQ 247
Cdd:COG5325    96 ILKTKYKNLQSSFlqsKLLRDLNTECMEGQRIQQKsaQFRKYQVLQAKFLRNKNNDQHPLEEEEDEESLSSLGSQQTLQQ 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196929748 248 MQLVNERDSYIQN----RADTMQNIESTIVELGSIFQQLAHMVKEQEETVHRIDANVEDTQLNVDLAHTEILKYFQSVSN 323
Cdd:COG5325   176 QGLSNEELEYQQIliteRDEEIKNLARGIYELNEIFRDLGSLVGEQGELVDRIDFNIENTSDNLKNANKELEKAPAHQRR 255

                         170       180
                  ....*....|....*....|.
gi 1196929748 324 -NRWLLIKMFLVLVIFFIVFV 343
Cdd:COG5325   256 tKKCRFYLLLILLVVLLFVSL 276

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        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1196929748 258 IQNRADTMQNIESTIVELGSIFQQLAHMVKEQEETVHRIDANVEDTQLNVDLAHTEI 314
Cdd:cd15849     4 VQARHNEIQRIEQTLTELAQLFNDMATLVEQQDEVIQQIEQNAEEVETDLEKGNVHL 60

SNARE motif of syntaxin 16; Syntaxin 16 is located in trans-Golgi network (TGN) and regulated by the SM protein Vps45p. It forms a complex with syntaxin 6 (Qc), Vti1a (Qb) and VAMP4 (R-SNARE) and is involved in the regulation of recycling of early endosomes to the trans-Golgi network (TGN). Syntaxin 16 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        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1196929748 258 IQNRADTMQNIESTIVELGSIFQQLAHMVKEQEETVHRIDANVEDTQLNVDLAHTEILK 316
Cdd:cd15845     1 IQERDREIAKIVESINELAEIFKDLATLVIEQGTILDRIDYNIEQTATRVEKGVKELKK 59

SNARE motif of syntaxin 17; Synthaxin 17 (STX17) belongs to the Qa subgroup of SNAREs and interacts with SNAP29 (Qb/Qc) and the lysosomal R-SNARE VAMP8. The complex plays a role in autophagosome-lysosome fusion. Autophagosome transports cytoplasmic materials, including cytoplasmic proteins, glycogen, lipids, organelles, and invading bacteria to the lysosome for degradation. 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 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 1196929748 259 QNRADTMQNIESTIVELGSIFQQLAHMVKEQEETVHRIDANVEDTQLNV 307
Cdd:cd15846     5 QACLESWETLQQDLEDLHGLFTDFHQLVHDQGEQVDTIEDNVEEALENV 53

Syntaxin-5 N-terminal, Sly1p-binding domain; Syntaxin-5_N is the Sed5 N-terminal and the N-terminus of Syntaxin-5-like proteins. It is the region of Syntaxin that interacts with Sly1p, a positive regulator of intracellular membrane fusion, allowing SM (cytosolic Sec1/munc18-like) proteins to stay associated with the assembling fusion machinery. This allows the SM proteins to participate in late fusion steps.

                          10        20
                  ....*....|....*....|...
gi 1196929748  47 TFSMSCRDRTGEFQSVCKSLQGR 69
Cdd:pfam11416   1 AAPTSIRDRTSEFQSIVKSLQKR 23

SNARE motif of syntaxin 4; Syntaxin-4 forms a complex with SNAP-23 (Qb/Qc) and R-SNAREs VAMP8, VAMP2 and VAMP7 which plays a role in exocytosis of secetory granule. Syntaxin 4 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
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1196929748 258 IQNRADTMQNIESTIVELGSIFQQLAHMVKEQEETVHRIDANVEDTQLNVDLAHTEI 314
Cdd:cd15883     5 IEARHSEIQKLERSIRELHDMFTYLAMEVEAQGEMIDRIEKNILSSADYVEKAQEHV 61

Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196929748  88 DFTLLAKRIGRDLSNTFAKLEKLT-----ILAKRKSLFDDKATE-IDELTYIVKQDINSLIKQIAGLQELVRSRSAQNGR 161
Cdd:pfam01442  34 ETEALRERLQKDLEEVRAKLEPYLeelqaKLGQNVEELRQRLEPyTEELRKRLNADAEELQEKLAPYGEELRERLEQNVD 113

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1196929748 162 HLQTHSNTIVVSLQSKLASMSSDFKSVLEVRTENLKQQ-RSRQEQFSQT 209
Cdd:pfam01442 114 ALRARLAPYAEELRQKLAERLEELKESLAPYAEEVQAQlSQRLQELREK 162