SNARE domain of STXBP5, STXBP6 and related proteins; Syntaxin binding protein 5 (STXBP5, also called Tomosyn), as well as its relative Syntaxin binding protein 6 (STXBP6, also called Amisyn) contains a C-terminal R-SNARE-like domain, which allows it to assemble into SNARE complexes, which in turn makes the complexes inactive and inhibits exocytosis. In general, 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.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 193203016 1066 SVQMDRAQAGGVSAGQAAAMALQNLNERTEKLNATVDATENLKNNAMSLSSRTGKLVEKYE 1126
Cdd:cd15873     1 GGGMKALRAKAGSAASAAARARQALNERGEKLSELEDRTAEMEDNAESFASTAKELAKKYK 61

SNARE domain of STXBP5, STXBP6 and related proteins; Syntaxin binding protein 5 (STXBP5, also called Tomosyn), as well as its relative Syntaxin binding protein 6 (STXBP6, also called Amisyn) contains a C-terminal R-SNARE-like domain, which allows it to assemble into SNARE complexes, which in turn makes the complexes inactive and inhibits exocytosis. In general, 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.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 193203016 1066 SVQMDRAQAGGVSAGQAAAMALQNLNERTEKLNATVDATENLKNNAMSLSSRTGKLVEKYE 1126
Cdd:cd15873     1 GGGMKALRAKAGSAASAAARARQALNERGEKLSELEDRTAEMEDNAESFASTAKELAKKYK 61

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193203016   50 RCFAYDPVQRLIAIGTGRGHIRIIgDAGVDYLLKHESG--EPVLHMQFLVNeGGLITSCGTDS-IHLWNYrqKTAEIVHT 126
Cdd:cd00200    13 TCVAFSPDGKLLATGSGDGTIKVW-DLETGELLRTLKGhtGPVRDVAASAD-GTYLASGSSDKtIRLWDL--ETGECVRT 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193203016  127 VQLSKESVSCIHLPVAGKWLFIGTDKGNVYFLCLNSFLLSpyvinwnkaidLSCRVHPGPVRQLAVSPaenTKLLIV--- 203
Cdd:cd00200    89 LTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCL-----------TTLRGHTDWVNSVAFSP---DGTFVAsss 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 193203016  204 YDKGIVVqWNLGT-REVDRYPL-DPPIKSVNWHFDGRQILTGNVDGSISLYNHKK 256
Cdd:cd00200   155 QDGTIKL-WDLRTgKCVATLTGhTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLST 208

SNARE domain of STXBP5, STXBP6 and related proteins; Syntaxin binding protein 5 (STXBP5, also called Tomosyn), as well as its relative Syntaxin binding protein 6 (STXBP6, also called Amisyn) contains a C-terminal R-SNARE-like domain, which allows it to assemble into SNARE complexes, which in turn makes the complexes inactive and inhibits exocytosis. In general, 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.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 193203016 1066 SVQMDRAQAGGVSAGQAAAMALQNLNERTEKLNATVDATENLKNNAMSLSSRTGKLVEKYE 1126
Cdd:cd15873     1 GGGMKALRAKAGSAASAAARARQALNERGEKLSELEDRTAEMEDNAESFASTAKELAKKYK 61

WD40 repeat [General function prediction only];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193203016   50 RCFAYDPVQRLIAIGTGRGHIRI--IGDAGVDYLLKHESGePVLHMQFLVNeGGLITSCGTD-SIHLWNYRqkTAEIVHT 126
Cdd:COG2319   166 TSVAFSPDGKLLASGSDDGTVRLwdLATGKLLRTLTGHTG-AVRSVAFSPD-GKLLASGSADgTVRLWDLA--TGKLLRT 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193203016  127 VQLSKESVSCIHLPVAGKWLFIGTDKGNVYFlclnsfllspyvinWN---KAIDLSCRVHPGPVRQLAVSPaeNTKLLIV 203
Cdd:COG2319   242 LTGHSGSVRSVAFSPDGRLLASGSADGTVRL--------------WDlatGELLRTLTGHSGGVNSVAFSP--DGKLLAS 305

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193203016  204 --YDKGIVVqWNLGTREVdRYPLDP---PIKSVNWHFDGRQILTGNVDGSISLYNhKKSTEAIQRTTPHGSG 270
Cdd:COG2319   306 gsDDGTVRL-WDLATGKL-LRTLTGhtgAVRSVAFSPDGKTLASGSDDGTVRLWD-LATGELLRTLTGHTGA 374

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193203016   50 RCFAYDPVQRLIAIGTGRGHIRIIgDAGVDYLLKHESG--EPVLHMQFLVNeGGLITSCGTDS-IHLWNYrqKTAEIVHT 126
Cdd:cd00200    13 TCVAFSPDGKLLATGSGDGTIKVW-DLETGELLRTLKGhtGPVRDVAASAD-GTYLASGSSDKtIRLWDL--ETGECVRT 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193203016  127 VQLSKESVSCIHLPVAGKWLFIGTDKGNVYFLCLNSFLLSpyvinwnkaidLSCRVHPGPVRQLAVSPaenTKLLIV--- 203
Cdd:cd00200    89 LTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCL-----------TTLRGHTDWVNSVAFSP---DGTFVAsss 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 193203016  204 YDKGIVVqWNLGT-REVDRYPL-DPPIKSVNWHFDGRQILTGNVDGSISLYNHKK 256
Cdd:cd00200   155 QDGTIKL-WDLRTgKCVATLTGhTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLST 208

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193203016   50 RCFAYDPVQRLIAIGTGRGHIRI--IGDAGVDYLLKHESGePVLHMQFLVNEGGLITSCGTDSIHLWNYRqkTAEIVHTV 127
Cdd:cd00200   139 NSVAFSPDGTFVASSSQDGTIKLwdLRTGKCVATLTGHTG-EVNSVAFSPDGEKLLSSSSDGTIKLWDLS--TGKCLGTL 215

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193203016  128 QLSKESVSCIHLPVAGKWLFIGTDKGNVYFlclnsfllspyvinWN---KAIDLSCRVHPGPVRQLAVSP 194
Cdd:cd00200   216 RGHENGVNSVAFSPDGYLLASGSEDGTIRV--------------WDlrtGECVQTLSGHTNSVTSLAWSP 271