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Conserved domains on  [gi|1207184993|ref|XP_021334414|]
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syntaxin-binding protein 5-like isoform X14 [Danio rerio]

Protein Classification

LLGL and R-SNARE_STXBP5 domain-containing protein( domain architecture ID 11456851)

protein containing domains WD40, LLGL, and R-SNARE_STXBP5

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LLGL pfam08366
LLGL2; This domain is found in lethal giant larvae homolog 2 (LLGL2) proteins and ...
 281-390 1.38e-40

LLGL2; This domain is found in lethal giant larvae homolog 2 (LLGL2) proteins and syntaxin-binding proteins like tomosyn. It has been identified in eukaryotes and tends to be found together with WD repeats (pfam00400).


:

Pssm-ID: 462446  Cd Length: 103  Bit Score: 144.64  E-value: 1.38e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207184993  281 VTFPHGKtqrdgrkESCKPILKVEYKTSRNSSEaFVIFSGGLSYDKAGRRPTLTIMHGKAITVLEMDYPIVDFMVLCETP 360
Cdd:pfam08366    1 PTTPYGP-------FPCKAITKILWKTTKTGEP-FIIFSGGMPRASYGDRHCITVMHGKKHTVFDFTSKVIDFFTLCESP 72

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1207184993  361 YLN-EVQEPYAVVVLLEKDFVVVDLTQSNFP 390
Cdd:pfam08366   73 DPNaEFDDPYALVVLLEEELVVIDLTTPGWP 103
R-SNARE_STXBP5 cd15893
SNARE domain of STXBP5; Syntaxin binding protein 5 (STXBP5, also called Tomosyn), as well as ...
 1054-1113 1.46e-31

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.


:

Pssm-ID: 277246  Cd Length: 61  Bit Score: 117.45  E-value: 1.46e-31
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207184993 1054 GGIEGMKAAAGGVVGDLARARIALDERGQRLGELEERTALMMTSAETFSKHAHELMLKCK 1113
Cdd:cd15893      2 GGIEGVKGAASGVVGELARARLALDERGQKLGELEERTAAMLASADSFSKHAHEMMLKYK 61
WD40 COG2319
WD40 repeat [General function prediction only];
67-274 9.28e-11

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 65.32  E-value: 9.28e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207184993   67 TALAFDPVQKILAIGSRSGGIRILGRPGVDC-HSQHESGAAVLQMQFLINEGALVTACADDTLHLWSLRQRlpAILHSLK 145
Cdd:COG2319    208 RSVAFSPDGKLLASGSADGTVRLWDLATGKLlRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATG--ELLRTLT 285

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207184993  146 FNRERITFCHLPFQSKWLYVGTERGNTHIVNIES----FILSGyvimwnkaielstktHPGPVVHLSDSPkDEGKLLIGF 221
Cdd:COG2319    286 GHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATgkllRTLTG---------------HTGAVRSVAFSP-DGKTLASGS 349

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1207184993  222 ESGTIVMWDLRAKRADFRIY-YDEAIHSVSWHHEGRQFMCSHSDGSLSMWNMRN 274
Cdd:COG2319    350 DDGTVRLWDLATGELLRTLTgHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
 
Name Accession Description Interval E-value
LLGL pfam08366
LLGL2; This domain is found in lethal giant larvae homolog 2 (LLGL2) proteins and ...
 281-390 1.38e-40

LLGL2; This domain is found in lethal giant larvae homolog 2 (LLGL2) proteins and syntaxin-binding proteins like tomosyn. It has been identified in eukaryotes and tends to be found together with WD repeats (pfam00400).


Pssm-ID: 462446  Cd Length: 103  Bit Score: 144.64  E-value: 1.38e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207184993  281 VTFPHGKtqrdgrkESCKPILKVEYKTSRNSSEaFVIFSGGLSYDKAGRRPTLTIMHGKAITVLEMDYPIVDFMVLCETP 360
Cdd:pfam08366    1 PTTPYGP-------FPCKAITKILWKTTKTGEP-FIIFSGGMPRASYGDRHCITVMHGKKHTVFDFTSKVIDFFTLCESP 72

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1207184993  361 YLN-EVQEPYAVVVLLEKDFVVVDLTQSNFP 390
Cdd:pfam08366   73 DPNaEFDDPYALVVLLEEELVVIDLTTPGWP 103
R-SNARE_STXBP5 cd15893
SNARE domain of STXBP5; Syntaxin binding protein 5 (STXBP5, also called Tomosyn), as well as ...
 1054-1113 1.46e-31

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.


Pssm-ID: 277246  Cd Length: 61  Bit Score: 117.45  E-value: 1.46e-31
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207184993 1054 GGIEGMKAAAGGVVGDLARARIALDERGQRLGELEERTALMMTSAETFSKHAHELMLKCK 1113
Cdd:cd15893      2 GGIEGVKGAASGVVGELARARLALDERGQKLGELEERTAAMLASADSFSKHAHEMMLKYK 61
WD40 COG2319
WD40 repeat [General function prediction only];
67-274 9.28e-11

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 65.32  E-value: 9.28e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207184993   67 TALAFDPVQKILAIGSRSGGIRILGRPGVDC-HSQHESGAAVLQMQFLINEGALVTACADDTLHLWSLRQRlpAILHSLK 145
Cdd:COG2319    208 RSVAFSPDGKLLASGSADGTVRLWDLATGKLlRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATG--ELLRTLT 285

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207184993  146 FNRERITFCHLPFQSKWLYVGTERGNTHIVNIES----FILSGyvimwnkaielstktHPGPVVHLSDSPkDEGKLLIGF 221
Cdd:COG2319    286 GHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATgkllRTLTG---------------HTGAVRSVAFSP-DGKTLASGS 349

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1207184993  222 ESGTIVMWDLRAKRADFRIY-YDEAIHSVSWHHEGRQFMCSHSDGSLSMWNMRN 274
Cdd:COG2319    350 DDGTVRLWDLATGELLRTLTgHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 67-273 2.82e-10

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.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 62.74  E-value: 2.82e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207184993   67 TALAFDPVQKILAIGSRSGGIRILGRPGVDCHSQ---HESGaaVLQMQFLINEGALVTACADDTLHLWSLRQrlPAILHS 143
Cdd:cd00200     13 TCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTlkgHTGP--VRDVAASADGTYLASGSSDKTIRLWDLET--GECVRT 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207184993  144 LKfnreritfCHlpfQSKWLYVgtergntHIVNIESFILSGY----VIMWN---KAIELSTKTHPGPVVHLSDSPkdEGK 216
Cdd:cd00200     89 LT--------GH---TSYVSSV-------AFSPDGRILSSSSrdktIKVWDvetGKCLTTLRGHTDWVNSVAFSP--DGT 148

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207184993  217 LLIGFES-GTIVMWDLRAKR--ADFRIYYDEaIHSVSWHHEGRQFMCSHSDGSLSMWNMR 273
Cdd:cd00200    149 FVASSSQdGTIKLWDLRTGKcvATLTGHTGE-VNSVAFSPDGEKLLSSSSDGTIKLWDLS 207
Synaptobrevin pfam00957
Synaptobrevin;
1079-1118 6.96e-04

Synaptobrevin;


Pssm-ID: 395764  Cd Length: 89  Bit Score: 39.83  E-value: 6.96e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1207184993 1079 ERGQRLGELEERTALMMTSAETFSKHAHELMLK--CKDKKWY 1118
Cdd:pfam00957   28 ERGEKLDLLVDKTENLQSSAQQFRRQARKLKRKmwWKNMKLY 69
 
Name Accession Description Interval E-value
LLGL pfam08366
LLGL2; This domain is found in lethal giant larvae homolog 2 (LLGL2) proteins and ...
 281-390 1.38e-40

LLGL2; This domain is found in lethal giant larvae homolog 2 (LLGL2) proteins and syntaxin-binding proteins like tomosyn. It has been identified in eukaryotes and tends to be found together with WD repeats (pfam00400).


Pssm-ID: 462446  Cd Length: 103  Bit Score: 144.64  E-value: 1.38e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207184993  281 VTFPHGKtqrdgrkESCKPILKVEYKTSRNSSEaFVIFSGGLSYDKAGRRPTLTIMHGKAITVLEMDYPIVDFMVLCETP 360
Cdd:pfam08366    1 PTTPYGP-------FPCKAITKILWKTTKTGEP-FIIFSGGMPRASYGDRHCITVMHGKKHTVFDFTSKVIDFFTLCESP 72

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1207184993  361 YLN-EVQEPYAVVVLLEKDFVVVDLTQSNFP 390
Cdd:pfam08366   73 DPNaEFDDPYALVVLLEEELVVIDLTTPGWP 103
R-SNARE_STXBP5 cd15893
SNARE domain of STXBP5; Syntaxin binding protein 5 (STXBP5, also called Tomosyn), as well as ...
 1054-1113 1.46e-31

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.


Pssm-ID: 277246  Cd Length: 61  Bit Score: 117.45  E-value: 1.46e-31
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207184993 1054 GGIEGMKAAAGGVVGDLARARIALDERGQRLGELEERTALMMTSAETFSKHAHELMLKCK 1113
Cdd:cd15893      2 GGIEGVKGAASGVVGELARARLALDERGQKLGELEERTAAMLASADSFSKHAHEMMLKYK 61
R-SNARE_STXBP5_6 cd15873
SNARE domain of STXBP5, STXBP6 and related proteins; Syntaxin binding protein 5 (STXBP5, also ...
 1053-1113 1.40e-20

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.


Pssm-ID: 277226  Cd Length: 61  Bit Score: 86.16  E-value: 1.40e-20
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207184993 1053 QGGIEGMKAAAGGVVGDLARARIALDERGQRLGELEERTALMMTSAETFSKHAHELMLKCK 1113
Cdd:cd15873      1 GGGMKALRAKAGSAASAAARARQALNERGEKLSELEDRTAEMEDNAESFASTAKELAKKYK 61
R-SNARE_STXBP6 cd15892
SNARE domain of STXBP6; Syntaxin binding protein 6 (STXBP6, also called Amisyn), as well as ...
 1054-1113 4.50e-11

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.


Pssm-ID: 277245  Cd Length: 62  Bit Score: 59.40  E-value: 4.50e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207184993 1054 GGIEGMKAAAGGVVGDLARARIALDERGQRLGELEERTALMMTSAETFSKHAHELMLKCK 1113
Cdd:cd15892      2 GGNSILHSAADSVTSAVQKASQALNERGERLGRAEEKTEDMKNSAQQFAETAHKLAMKHK 61
WD40 COG2319
WD40 repeat [General function prediction only];
67-274 9.28e-11

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 65.32  E-value: 9.28e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207184993   67 TALAFDPVQKILAIGSRSGGIRILGRPGVDC-HSQHESGAAVLQMQFLINEGALVTACADDTLHLWSLRQRlpAILHSLK 145
Cdd:COG2319    208 RSVAFSPDGKLLASGSADGTVRLWDLATGKLlRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATG--ELLRTLT 285

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207184993  146 FNRERITFCHLPFQSKWLYVGTERGNTHIVNIES----FILSGyvimwnkaielstktHPGPVVHLSDSPkDEGKLLIGF 221
Cdd:COG2319    286 GHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATgkllRTLTG---------------HTGAVRSVAFSP-DGKTLASGS 349

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1207184993  222 ESGTIVMWDLRAKRADFRIY-YDEAIHSVSWHHEGRQFMCSHSDGSLSMWNMRN 274
Cdd:COG2319    350 DDGTVRLWDLATGELLRTLTgHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 67-273 2.82e-10

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.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 62.74  E-value: 2.82e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207184993   67 TALAFDPVQKILAIGSRSGGIRILGRPGVDCHSQ---HESGaaVLQMQFLINEGALVTACADDTLHLWSLRQrlPAILHS 143
Cdd:cd00200     13 TCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTlkgHTGP--VRDVAASADGTYLASGSSDKTIRLWDLET--GECVRT 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207184993  144 LKfnreritfCHlpfQSKWLYVgtergntHIVNIESFILSGY----VIMWN---KAIELSTKTHPGPVVHLSDSPkdEGK 216
Cdd:cd00200     89 LT--------GH---TSYVSSV-------AFSPDGRILSSSSrdktIKVWDvetGKCLTTLRGHTDWVNSVAFSP--DGT 148

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207184993  217 LLIGFES-GTIVMWDLRAKR--ADFRIYYDEaIHSVSWHHEGRQFMCSHSDGSLSMWNMR 273
Cdd:cd00200    149 FVASSSQdGTIKLWDLRTGKcvATLTGHTGE-VNSVAFSPDGEKLLSSSSDGTIKLWDLS 207
WD40 COG2319
WD40 repeat [General function prediction only];
67-286 1.52e-09

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 61.47  E-value: 1.52e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207184993   67 TALAFDPVQKILAIGSRSGGIRIL-GRPGVDCHSQHESGAAVLQMQFLINEGALVTACADDTLHLWSLRQRLPaiLHSLK 145
Cdd:COG2319    166 TSVAFSPDGKLLASGSDDGTVRLWdLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKL--LRTLT 243

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207184993  146 FNRERITFCHLPFQSKWLYVGTERGNTHIVNIESfilsgyvimwnKAIELSTKTHPGPVVHLSDSPkdEGKLLI-GFESG 224
Cdd:COG2319    244 GHSGSVRSVAFSPDGRLLASGSADGTVRLWDLAT-----------GELLRTLTGHSGGVNSVAFSP--DGKLLAsGSDDG 310

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207184993  225 TIVMWDLRAKRAdFRIY--YDEAIHSVSWHHEGRQFMCSHSDGSLSMWNmRNTAKPFQVTFPHG 286
Cdd:COG2319    311 TVRLWDLATGKL-LRTLtgHTGAVRSVAFSPDGKTLASGSDDGTVRLWD-LATGELLRTLTGHT 372
WD40 COG2319
WD40 repeat [General function prediction only];
55-271 3.50e-09

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 60.31  E-value: 3.50e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207184993   55 CKTVRHGFPYQPTALAFDPVQKILAIGSRSGGIRILG-RPGVDCHSQHESGAAVLQMQFLINEGALVTACADDTLHLWSL 133
Cdd:COG2319     70 LLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDlATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDL 149

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207184993  134 RQrlPAILHSLKFNRERITfcHLPF--QSKWLYVGTERGNTHIVNIES----FILSGyvimwnkaielstktHPGPVVHL 207
Cdd:COG2319    150 AT--GKLLRTLTGHSGAVT--SVAFspDGKLLASGSDDGTVRLWDLATgkllRTLTG---------------HTGAVRSV 210

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207184993  208 SDSPkdEGKLLI-GFESGTIVMWDLRAKRADFRI-YYDEAIHSVSWHHEGRQFMCSHSDGSLSMWN 271
Cdd:COG2319    211 AFSP--DGKLLAsGSADGTVRLWDLATGKLLRTLtGHSGSVRSVAFSPDGRLLASGSADGTVRLWD 274
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 67-271 2.20e-08

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.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 56.96  E-value: 2.20e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207184993   67 TALAFDPVQKILAIGSRSGGIRIL-GRPGVDCHSQHESGAAVLQMQFLINEGALVTACADDTLHLWSLRQRLPaiLHSLK 145
Cdd:cd00200     97 SSVAFSPDGRILSSSSRDKTIKVWdVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKC--VATLT 174

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207184993  146 FNRERITFCHLPFQSKWLYVGTERGNthivniesfilsgyVIMWNKAIELSTKT---HPGPVVHLSDSPKdeGKLLI-GF 221
Cdd:cd00200    175 GHTGEVNSVAFSPDGEKLLSSSSDGT--------------IKLWDLSTGKCLGTlrgHENGVNSVAFSPD--GYLLAsGS 238

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1207184993  222 ESGTIVMWDLRAKRADFRIY-YDEAIHSVSWHHEGRQFMCSHSDGSLSMWN 271
Cdd:cd00200    239 EDGTIRVWDLRTGECVQTLSgHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 101-274 2.81e-07

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.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 53.49  E-value: 2.81e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207184993  101 HESGaaVLQMQFLINEGALVTACADDTLHLWSLRQRLPaiLHSLKFNRERITFCHLPFQSKWLYVGterGNTHIVNIesf 180
Cdd:cd00200      8 HTGG--VTCVAFSPDGKLLATGSGDGTIKVWDLETGEL--LRTLKGHTGPVRDVAASADGTYLASG---SSDKTIRL--- 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207184993  181 ilsgyvimWNKAIELSTKT---HPGPVVHLSDSPKdeGKLLIG-FESGTIVMWDLRAKRADFRIYY-DEAIHSVSWHHEG 255
Cdd:cd00200     78 --------WDLETGECVRTltgHTSYVSSVAFSPD--GRILSSsSRDKTIKVWDVETGKCLTTLRGhTDWVNSVAFSPDG 147

                          170
                   ....*....|....*....
gi 1207184993  256 RQFMCSHSDGSLSMWNMRN 274
Cdd:cd00200    148 TFVASSSQDGTIKLWDLRT 166
WD40 COG2319
WD40 repeat [General function prediction only];
55-232 3.82e-07

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 53.76  E-value: 3.82e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207184993   55 CKTVRHGFPYQPTALAFDPVQKILAIGSRSGGIRILGRPGVDC-HSQHESGAAVLQMQFLINEGALVTACADDTLHLWSL 133
Cdd:COG2319    238 LLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELlRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDL 317

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207184993  134 RQRlpAILHSLKFNRERITFCHLPFQSKWLYVGTERGNTHIVNIESFILSGyvimwnkaielSTKTHPGPVVHLSDSPkD 213
Cdd:COG2319    318 ATG--KLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLR-----------TLTGHTGAVTSVAFSP-D 383

                          170
                   ....*....|....*....
gi 1207184993  214 EGKLLIGFESGTIVMWDLR 232
Cdd:COG2319    384 GRTLASGSADGTVRLWDLA 402
R-SNARE cd15843
SNARE motif, subgroup R-SNARE; SNARE (soluble N-ethylmaleimide-sensitive factor attachment ...
 1079-1117 2.80e-04

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.


Pssm-ID: 277196 [Multi-domain]  Cd Length: 60  Bit Score: 39.79  E-value: 2.80e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1207184993 1079 ERGQRLGELEERTALMMTSAETFSKHAHELmlkcKDKKW 1117
Cdd:cd15843     26 ERGEKLEDLVDKTENLNESANAFKKQARKL----KRKMW 60
Synaptobrevin pfam00957
Synaptobrevin;
1079-1118 6.96e-04

Synaptobrevin;


Pssm-ID: 395764  Cd Length: 89  Bit Score: 39.83  E-value: 6.96e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1207184993 1079 ERGQRLGELEERTALMMTSAETFSKHAHELMLK--CKDKKWY 1118
Cdd:pfam00957   28 ERGEKLDLLVDKTENLQSSAQQFRRQARKLKRKmwWKNMKLY 69
WD40 COG2319
WD40 repeat [General function prediction only];
70-274 9.90e-04

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 42.98  E-value: 9.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207184993   70 AFDPVQKILAIGSRSGGIRILGRPGVDCHSQHESGAAVLQMQFLINEGALVTACADDTLHLWSLRQRlPAILHSLKFNRE 149
Cdd:COG2319      1 ALSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAA-GALLATLLGHTA 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207184993  150 RITFCHLPFQSKWLYVGTERGNTHIVNIESfilsgyvimwnKAIELSTKTHPGPVVHLSDSPkDEGKLLIGFESGTIVMW 229
Cdd:COG2319     80 AVLSVAFSPDGRLLASASADGTVRLWDLAT-----------GLLLRTLTGHTGAVRSVAFSP-DGKTLASGSADGTVRLW 147

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1207184993  230 DLRAKRADFRIY-YDEAIHSVSWHHEGRQFMCSHSDGSLSMWNMRN 274
Cdd:COG2319    148 DLATGKLLRTLTgHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLAT 193
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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