SNARE domain of STXBP5; 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. Tomosyn contains an N-terminal WD40 repeat region and has been shown to form complexes with SNAP-25 and syntaxin 1a, as well as SNAP-23 and syntaxin 4. 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 688571455 1115 GGIEGMKAAAGGVVGDLARARIALDERGQRLGELEERTALMMTSAETFSKHAHELMLKCK 1174
Cdd:cd15893     2 GGIEGVKGAASGVVGELARARLALDERGQKLGELEERTAAMLASADSFSKHAHEMMLKYK 61

Facioscapulohumeral muscular dystrophy candidate 2; This family of proteins is found in eukaryotes. The family is localized close to the D4Z4 repeats on chromosome 4 and 10 that are associated with the autosomal dominant facioscapulohumeral muscular dystrophy (FSHD). FRG2 are transcriptionally upregulated in FSHD myoblast cultures suggesting involvement in the pathogenesis of FSHD.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688571455   688 KNRQSTSDFCMRGLSNFYSDSKKRIRTSYQSLT----ELSDnQVSLDLERSKSPTSDHVNGHCTSPTSQPCPSGR-ARVP 762
Cdd:pfam15315   17 KGRSSIAGSESESSSDRESSRKRKISSSDSSCQgtgnSPGD-ERSVTLEKKTRPVSDAGHSSEIQETADAHPRRNsRAGS 95

                           90       100
                   ....*....|....*....|.
gi 688571455   763 GGPEGPRLARRGPGRPPFRKA 783
Cdd:pfam15315   96 GRSRRRRSRSPGDRPPPLRKS 116

SNARE domain of STXBP5; 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. Tomosyn contains an N-terminal WD40 repeat region and has been shown to form complexes with SNAP-25 and syntaxin 1a, as well as SNAP-23 and syntaxin 4. 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 688571455 1115 GGIEGMKAAAGGVVGDLARARIALDERGQRLGELEERTALMMTSAETFSKHAHELMLKCK 1174
Cdd:cd15893     2 GGIEGVKGAASGVVGELARARLALDERGQKLGELEERTAAMLASADSFSKHAHEMMLKYK 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 688571455   67 TALAFDPVQKILAIGSRSGGIRILGRPGVDCHSQ---HESGaaVLQMQFLINEGALVTACADDTLHLWSLRQrlPAILHS 143
Cdd:cd00200    13 TCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTlkgHTGP--VRDVAASADGTYLASGSSDKTIRLWDLET--GECVRT 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688571455  144 LKfnreritfCHlpfQSKWLYVgtergntHIVNIESFILSGY----VIMWN---KAIELSTKTHPGPVVHLSDSPkdEGK 216
Cdd:cd00200    89 LT--------GH---TSYVSSV-------AFSPDGRILSSSSrdktIKVWDvetGKCLTTLRGHTDWVNSVAFSP--DGT 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 688571455  217 LLIGFES-GTIVMWDLRAKR--ADFRIYYDEaIHSVSWHHEGRQFMCSHSDGSLSMWNMR 273
Cdd:cd00200   149 FVASSSQdGTIKLWDLRTGKcvATLTGHTGE-VNSVAFSPDGEKLLSSSSDGTIKLWDLS 207

Facioscapulohumeral muscular dystrophy candidate 2; This family of proteins is found in eukaryotes. The family is localized close to the D4Z4 repeats on chromosome 4 and 10 that are associated with the autosomal dominant facioscapulohumeral muscular dystrophy (FSHD). FRG2 are transcriptionally upregulated in FSHD myoblast cultures suggesting involvement in the pathogenesis of FSHD.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688571455   688 KNRQSTSDFCMRGLSNFYSDSKKRIRTSYQSLT----ELSDnQVSLDLERSKSPTSDHVNGHCTSPTSQPCPSGR-ARVP 762
Cdd:pfam15315   17 KGRSSIAGSESESSSDRESSRKRKISSSDSSCQgtgnSPGD-ERSVTLEKKTRPVSDAGHSSEIQETADAHPRRNsRAGS 95

                           90       100
                   ....*....|....*....|.
gi 688571455   763 GGPEGPRLARRGPGRPPFRKA 783
Cdd:pfam15315   96 GRSRRRRSRSPGDRPPPLRKS 116

SNARE domain of STXBP5; 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. Tomosyn contains an N-terminal WD40 repeat region and has been shown to form complexes with SNAP-25 and syntaxin 1a, as well as SNAP-23 and syntaxin 4. 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 688571455 1115 GGIEGMKAAAGGVVGDLARARIALDERGQRLGELEERTALMMTSAETFSKHAHELMLKCK 1174
Cdd:cd15893     2 GGIEGVKGAASGVVGELARARLALDERGQKLGELEERTAAMLASADSFSKHAHEMMLKYK 61

SNARE domain of STXBP6; Syntaxin binding protein 6 (STXBP6, also called Amisyn), as well as its relative Syntaxin binding protein 5 (STXBP5, also called Tomosyn), 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 688571455 1115 GGIEGMKAAAGGVVGDLARARIALDERGQRLGELEERTALMMTSAETFSKHAHELMLKCK 1174
Cdd:cd15892     2 GGNSILHSAADSVTSAVQKASQALNERGERLGRAEEKTEDMKNSAQQFAETAHKLAMKHK 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 688571455   67 TALAFDPVQKILAIGSRSGGIRILGRPGVDCHSQ---HESGaaVLQMQFLINEGALVTACADDTLHLWSLRQrlPAILHS 143
Cdd:cd00200    13 TCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTlkgHTGP--VRDVAASADGTYLASGSSDKTIRLWDLET--GECVRT 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688571455  144 LKfnreritfCHlpfQSKWLYVgtergntHIVNIESFILSGY----VIMWN---KAIELSTKTHPGPVVHLSDSPkdEGK 216
Cdd:cd00200    89 LT--------GH---TSYVSSV-------AFSPDGRILSSSSrdktIKVWDvetGKCLTTLRGHTDWVNSVAFSP--DGT 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 688571455  217 LLIGFES-GTIVMWDLRAKR--ADFRIYYDEaIHSVSWHHEGRQFMCSHSDGSLSMWNMR 273
Cdd:cd00200   149 FVASSSQdGTIKLWDLRTGKcvATLTGHTGE-VNSVAFSPDGEKLLSSSSDGTIKLWDLS 207

WD40 repeat [General function prediction only];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688571455   55 CKTVRHGFPYQPTALAFDPVQKILAIGSRSGGIRILG-RPGVDCHSQHESGAAVLQMQFLINEGALVTACADDTLHLWSL 133
Cdd:COG2319    70 LLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDlATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDL 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688571455  134 RQrlPAILHSLKFNRERITfcHLPF--QSKWLYVGTERGNTHIVNIES----FILSGyvimwnkaielstktHPGPVVHL 207
Cdd:COG2319   150 AT--GKLLRTLTGHSGAVT--SVAFspDGKLLASGSDDGTVRLWDLATgkllRTLTG---------------HTGAVRSV 210

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688571455  208 SDSPkdEGKLLI-GFESGTIVMWDLRAKRADFRI-YYDEAIHSVSWHHEGRQFMCSHSDGSLSMWN 271
Cdd:COG2319   211 AFSP--DGKLLAsGSADGTVRLWDLATGKLLRTLtGHSGSVRSVAFSPDGRLLASGSADGTVRLWD 274

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 688571455  101 HESGaaVLQMQFLINEGALVTACADDTLHLWSLRQRLPaiLHSLKFNRERITFCHLPFQSKWLYVGterGNTHIVNIesf 180
Cdd:cd00200     8 HTGG--VTCVAFSPDGKLLATGSGDGTIKVWDLETGEL--LRTLKGHTGPVRDVAASADGTYLASG---SSDKTIRL--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688571455  181 ilsgyvimWNKAIELSTKT---HPGPVVHLSDSPKdeGKLLIG-FESGTIVMWDLRAKRADFRIYY-DEAIHSVSWHHEG 255
Cdd:cd00200    78 --------WDLETGECVRTltgHTSYVSSVAFSPD--GRILSSsSRDKTIKVWDVETGKCLTTLRGhTDWVNSVAFSPDG 147

                         170
                  ....*....|....*....
gi 688571455  256 RQFMCSHSDGSLSMWNMRN 274
Cdd:cd00200   148 TFVASSSQDGTIKLWDLRT 166

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 688571455 1140 ERGQRLGELEERTALMMTSAETFSKHAHELmlkcKDKKW 1178
Cdd:cd15843    26 ERGEKLEDLVDKTENLNESANAFKKQARKL----KRKMW 60

WD40 repeat [General function prediction only];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688571455   70 AFDPVQKILAIGSRSGGIRILGRPGVDCHSQHESGAAVLQMQFLINEGALVTACADDTLHLWSLRQRlPAILHSLKFNRE 149
Cdd:COG2319     1 ALSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAA-GALLATLLGHTA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688571455  150 RITFCHLPFQSKWLYVGTERGNTHIVNIESfilsgyvimwnKAIELSTKTHPGPVVHLSDSPkDEGKLLIGFESGTIVMW 229
Cdd:COG2319    80 AVLSVAFSPDGRLLASASADGTVRLWDLAT-----------GLLLRTLTGHTGAVRSVAFSP-DGKTLASGSADGTVRLW 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 688571455  230 DLRAKRADFRIY-YDEAIHSVSWHHEGRQFMCSHSDGSLSMWNMRN 274
Cdd:COG2319   148 DLATGKLLRTLTgHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLAT 193