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
                   ....*....|....*....|....*....|....*....|
gi 1002284285 1054 KDKLMQRQEKLERISQRTAELESGAENFASLAQELAKSME 1093
Cdd:cd15873     22 RQALNERGEKLSELEDRTAEMEDNAESFASTAKELAKKYK 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
                   ....*....|....*....|....*....|....*....|
gi 1002284285 1054 KDKLMQRQEKLERISQRTAELESGAENFASLAQELAKSME 1093
Cdd:cd15873     22 RQALNERGEKLSELEDRTAEMEDNAESFASTAKELAKKYK 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 1002284285  489 RIYIAGYQDSSVRIWDatfpvltpmfVLDGKVVGVnMDGENSAVSSLAFCSLNMTLAVGTTSGLVRIYKLRE-------- 560
Cdd:cd00200    106 RILSSSSRDKTIKVWD----------VETGKCLTT-LRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTgkcvatlt 174

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002284285  561 -HTG---GSSFH------FVSESKQEVHVVQHgRGFHCHVAFLASNSPVRSLRFTASGEVLAVGYQNGQLASFDANQLSI 630
Cdd:cd00200    175 gHTGevnSVAFSpdgeklLSSSSDGTIKLWDL-STGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGEC 253

                          170       180       190
                   ....*....|....*....|....*....|
gi 1002284285  631 MFTVdcaSGTNSPVVSLS---NYNVVTSAA 657
Cdd:cd00200    254 VQTL---SGHTNSVTSLAwspDGKRLASGS 280

Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped WD40 domain.The N-terminus of Afi1 serves to stabilize the union between Apc4 and Apc5, both of which lie towards the bottom-front of the APC,

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1002284285  594 ASNSPVRSLRFTASGEVLAVGYQNGQLASFDANQLSIMFTVDCASG 639
Cdd:pfam12894   36 KEDLEVTSLAWRPDGKLLAVGYSDGTVRLLDAENGKIVHHFSAGSD 81

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
                   ....*....|....*....|....*....|....*....|
gi 1002284285 1054 KDKLMQRQEKLERISQRTAELESGAENFASLAQELAKSME 1093
Cdd:cd15873     22 RQALNERGEKLSELEDRTAEMEDNAESFASTAKELAKKYK 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 1002284285  489 RIYIAGYQDSSVRIWDatfpvltpmfVLDGKVVGVnMDGENSAVSSLAFCSLNMTLAVGTTSGLVRIYKLRE-------- 560
Cdd:cd00200    106 RILSSSSRDKTIKVWD----------VETGKCLTT-LRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTgkcvatlt 174

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002284285  561 -HTG---GSSFH------FVSESKQEVHVVQHgRGFHCHVAFLASNSPVRSLRFTASGEVLAVGYQNGQLASFDANQLSI 630
Cdd:cd00200    175 gHTGevnSVAFSpdgeklLSSSSDGTIKLWDL-STGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGEC 253

                          170       180       190
                   ....*....|....*....|....*....|
gi 1002284285  631 MFTVdcaSGTNSPVVSLS---NYNVVTSAA 657
Cdd:cd00200    254 VQTL---SGHTNSVTSLAwspDGKRLASGS 280

SNARE motif of VAMP2; The VAMP-2 (vesicle-associated membrane protein 2, also called synaptobrevin-2) protein belongs to the R-SNARE subgroup of SNAREs and interacts with Syntaxin-1 (Qa) and SNAP-25(Qb/Qc), as well as syntaxin 12 (Qa) and SNAP23 (Qb/Qc). The complexes play a role in transport of secretory granule from trans-Golgi network to the plasma membrane, and in the transport from early endosomes to and from the plasma membrane, respectively. SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins contain 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.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1002284285 1055 DKLMQRQEKLERISQRTAELESGAENFASLAQELaksmENKKWWK 1099
Cdd:cd15870     22 DKVLERDQKLSELDDRADALQAGASQFETSAGKL----KRKYWWK 62

SNARE motif, subgroup R-SNARE; 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). In contrast to Qa-, Qb- and Qc-SNAREs that are localized to target organelle membranes, R-SNAREs are 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
                   ....*....|....*....|....*....|....*...
gi 1002284285 1055 DKLMQRQEKLERISQRTAELESGAENFASLAQELAKSM 1092
Cdd:cd15843     22 DKVLERGEKLEDLVDKTENLNESANAFKKQARKLKRKM 59

WD40 repeat [General function prediction only];

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002284285  492 IAGYQDSSVRIWDATfpvltpmfvlDGKVVGVnMDGENSAVSSLAFCSLNMTLAVGTTSGLVRIYKLRehTGgssfhfvs 571
Cdd:COG2319    136 ASGSADGTVRLWDLA----------TGKLLRT-LTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLA--TG-------- 194

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002284285  572 eskQEVHVvqhgrgfhchvaFLASNSPVRSLRFTASGEVLAVGYQNGQLASFDANQLSIMFTVDcasGTNSPVVSLS 648
Cdd:COG2319    195 ---KLLRT------------LTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLT---GHSGSVRSVA 253

WD40 repeat [General function prediction only];

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002284285  489 RIYIAGYQDSSVRIWDatfpvltpmfvLDGKVVGVNMDGENSAVSSLAFCSLNMTLAVGTTSGLVRIYKLrehtggssfh 568
Cdd:COG2319     91 RLLASASADGTVRLWD-----------LATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDL---------- 149

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002284285  569 fvsESKQEVHVVQHGRGfhchvaflasnsPVRSLRFTASGEVLAVGYQNGQLASFDANQLSIMFTVDcasGTNSPVVSLS 648
Cdd:COG2319    150 ---ATGKLLRTLTGHSG------------AVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLT---GHTGAVRSVA 211

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
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002284285  489 RIYIAGYQDSSVRIWDATFPVLTPMFVldgkvvgvnmdGENSAVSSLAFCSLNMTLAVGTTSGLVRIYK 557
Cdd:cd00200    232 YLLASGSEDGTIRVWDLRTGECVQTLS-----------GHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289