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Conserved domains on  [gi|158749547|ref|NP_001074813|]
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syntaxin-binding protein 5 isoform 1 [Mus musculus]

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 ...
 276-385 5.90e-48

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: 165.83  E-value: 5.90e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749547   276 TITPHGkqlkdgkkPEPCKPILKVELKTTRSGEPFIILSGGLSYDTVGRRPCLTVMHGKSTAVLEMDYSIVDFLTLCETP 355
Cdd:pfam08366    1 PTTPYG--------PFPCKAITKILWKTTKTGEPFIIFSGGMPRASYGDRHCITVMHGKKHTVFDFTSKVIDFFTLCESP 72

                           90       100       110
                   ....*....|....*....|....*....|.
gi 158749547   356 YPN-DFQEPYAVVVLLEKDLVLIDLAQNGYP 385
Cdd:pfam08366   73 DPNaEFDDPYALVVLLEEELVVIDLTTPGWP 103
R-SNARE_STXBP5 cd15893
SNARE domain of STXBP5; Syntaxin binding protein 5 (STXBP5, also called Tomosyn), as well as ...
 1049-1109 7.43e-38

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: 135.55  E-value: 7.43e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158749547 1049 PGGIEGVKGAASGVVGELARARLALDERGQKLSDLEERTAAMMSSADSFSKHAHEMMLKYK 1109
Cdd:cd15893     1 PGGIEGVKGAASGVVGELARARLALDERGQKLGELEERTAAMLASADSFSKHAHEMMLKYK 61
WD40 COG2319
WD40 repeat [General function prediction only];
49-281 1.53e-16

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 83.04  E-value: 1.53e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749547   49 LCKTVRHGFPYQPSALAFDPVQKILAVGTQTGALRLFGRPGVECYCQ-HDSGAAVIQLQFLINEGALVSALADDTLHLWN 127
Cdd:COG2319   111 LLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTlTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWD 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749547  128 LRQKRPavLHSLKFCRERVTFCHLPFQSKWLYVGTERGNIHIVNVES----FTLSGyvimwnkaielsskaHPGPV--VH 201
Cdd:COG2319   191 LATGKL--LRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATgkllRTLTG---------------HSGSVrsVA 253

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749547  202 ISDNpmdeGKLLI-GFESGTVVLWDLKSKKADYRYT-YDEAIHSVAWHHEGKQFICSHSDGTLTIWNVRSPaKPVQTITP 279
Cdd:COG2319   254 FSPD----GRLLAsGSADGTVRLWDLATGELLRTLTgHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATG-KLLRTLTG 328


                  ..
gi 158749547  280 HG 281
Cdd:COG2319   329 HT 330
 
Name Accession Description Interval E-value
LLGL pfam08366
LLGL2; This domain is found in lethal giant larvae homolog 2 (LLGL2) proteins and ...
 276-385 5.90e-48

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: 165.83  E-value: 5.90e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749547   276 TITPHGkqlkdgkkPEPCKPILKVELKTTRSGEPFIILSGGLSYDTVGRRPCLTVMHGKSTAVLEMDYSIVDFLTLCETP 355
Cdd:pfam08366    1 PTTPYG--------PFPCKAITKILWKTTKTGEPFIIFSGGMPRASYGDRHCITVMHGKKHTVFDFTSKVIDFFTLCESP 72

                           90       100       110
                   ....*....|....*....|....*....|.
gi 158749547   356 YPN-DFQEPYAVVVLLEKDLVLIDLAQNGYP 385
Cdd:pfam08366   73 DPNaEFDDPYALVVLLEEELVVIDLTTPGWP 103
R-SNARE_STXBP5 cd15893
SNARE domain of STXBP5; Syntaxin binding protein 5 (STXBP5, also called Tomosyn), as well as ...
 1049-1109 7.43e-38

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: 135.55  E-value: 7.43e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158749547 1049 PGGIEGVKGAASGVVGELARARLALDERGQKLSDLEERTAAMMSSADSFSKHAHEMMLKYK 1109
Cdd:cd15893     1 PGGIEGVKGAASGVVGELARARLALDERGQKLGELEERTAAMLASADSFSKHAHEMMLKYK 61
WD40 COG2319
WD40 repeat [General function prediction only];
49-281 1.53e-16

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 83.04  E-value: 1.53e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749547   49 LCKTVRHGFPYQPSALAFDPVQKILAVGTQTGALRLFGRPGVECYCQ-HDSGAAVIQLQFLINEGALVSALADDTLHLWN 127
Cdd:COG2319   111 LLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTlTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWD 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749547  128 LRQKRPavLHSLKFCRERVTFCHLPFQSKWLYVGTERGNIHIVNVES----FTLSGyvimwnkaielsskaHPGPV--VH 201
Cdd:COG2319   191 LATGKL--LRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATgkllRTLTG---------------HSGSVrsVA 253

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749547  202 ISDNpmdeGKLLI-GFESGTVVLWDLKSKKADYRYT-YDEAIHSVAWHHEGKQFICSHSDGTLTIWNVRSPaKPVQTITP 279
Cdd:COG2319   254 FSPD----GRLLAsGSADGTVRLWDLATGELLRTLTgHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATG-KLLRTLTG 328


                  ..
gi 158749547  280 HG 281
Cdd:COG2319   329 HT 330
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 62-280 1.24e-13

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: 72.75  E-value: 1.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749547   62 SALAFDPVQKILAVGTQTGALRLFGRPGVEC---YCQHDSgaAVIQLQFLINEGALVSALADDTLHLWNLRQKRPavLHS 138
Cdd:cd00200    55 RDVAASADGTYLASGSSDKTIRLWDLETGECvrtLTGHTS--YVSSVAFSPDGRILSSSSRDKTIKVWDVETGKC--LTT 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749547  139 LKFCRERVTFCHLPFQSKWLYVGTERGNIHIVNVESF----TLSGyvimwnkaielsskaHPGPVVHISDNPmDEGKLLI 214
Cdd:cd00200   131 LRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGkcvaTLTG---------------HTGEVNSVAFSP-DGEKLLS 194

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158749547  215 GFESGTVVLWDLKSKKADYRYTY-DEAIHSVAWHHEGKQFICSHSDGTLTIWNVRSPaKPVQTITPH 280
Cdd:cd00200   195 SSSDGTIKLWDLSTGKCLGTLRGhENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTG-ECVQTLSGH 260
Synaptobrevin pfam00957
Synaptobrevin;
1075-1114 1.32e-04

Synaptobrevin;


Pssm-ID: 395764  Cd Length: 89  Bit Score: 41.75  E-value: 1.32e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 158749547  1075 ERGQKLSDLEERTAAMMSSADSFSKHAHEMMLKY--KDKKWY 1114
Cdd:pfam00957   28 ERGEKLDLLVDKTENLQSSAQQFRRQARKLKRKMwwKNMKLY 69
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 238-266 9.83e-04

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 37.68  E-value: 9.83e-04
                            10        20
                    ....*....|....*....|....*....
gi 158749547    238 DEAIHSVAWHHEGKQFICSHSDGTLTIWN 266
Cdd:smart00320   12 TGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
 
Name Accession Description Interval E-value
LLGL pfam08366
LLGL2; This domain is found in lethal giant larvae homolog 2 (LLGL2) proteins and ...
 276-385 5.90e-48

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: 165.83  E-value: 5.90e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749547   276 TITPHGkqlkdgkkPEPCKPILKVELKTTRSGEPFIILSGGLSYDTVGRRPCLTVMHGKSTAVLEMDYSIVDFLTLCETP 355
Cdd:pfam08366    1 PTTPYG--------PFPCKAITKILWKTTKTGEPFIIFSGGMPRASYGDRHCITVMHGKKHTVFDFTSKVIDFFTLCESP 72

                           90       100       110
                   ....*....|....*....|....*....|.
gi 158749547   356 YPN-DFQEPYAVVVLLEKDLVLIDLAQNGYP 385
Cdd:pfam08366   73 DPNaEFDDPYALVVLLEEELVVIDLTTPGWP 103
R-SNARE_STXBP5 cd15893
SNARE domain of STXBP5; Syntaxin binding protein 5 (STXBP5, also called Tomosyn), as well as ...
 1049-1109 7.43e-38

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: 135.55  E-value: 7.43e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158749547 1049 PGGIEGVKGAASGVVGELARARLALDERGQKLSDLEERTAAMMSSADSFSKHAHEMMLKYK 1109
Cdd:cd15893     1 PGGIEGVKGAASGVVGELARARLALDERGQKLGELEERTAAMLASADSFSKHAHEMMLKYK 61
R-SNARE_STXBP5_6 cd15873
SNARE domain of STXBP5, STXBP6 and related proteins; Syntaxin binding protein 5 (STXBP5, also ...
 1049-1109 2.26e-23

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: 94.25  E-value: 2.26e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158749547 1049 PGGIEGVKGAASGVVGELARARLALDERGQKLSDLEERTAAMMSSADSFSKHAHEMMLKYK 1109
Cdd:cd15873     1 GGGMKALRAKAGSAASAAARARQALNERGEKLSELEDRTAEMEDNAESFASTAKELAKKYK 61
WD40 COG2319
WD40 repeat [General function prediction only];
49-281 1.53e-16

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 83.04  E-value: 1.53e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749547   49 LCKTVRHGFPYQPSALAFDPVQKILAVGTQTGALRLFGRPGVECYCQ-HDSGAAVIQLQFLINEGALVSALADDTLHLWN 127
Cdd:COG2319   111 LLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTlTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWD 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749547  128 LRQKRPavLHSLKFCRERVTFCHLPFQSKWLYVGTERGNIHIVNVES----FTLSGyvimwnkaielsskaHPGPV--VH 201
Cdd:COG2319   191 LATGKL--LRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATgkllRTLTG---------------HSGSVrsVA 253

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749547  202 ISDNpmdeGKLLI-GFESGTVVLWDLKSKKADYRYT-YDEAIHSVAWHHEGKQFICSHSDGTLTIWNVRSPaKPVQTITP 279
Cdd:COG2319   254 FSPD----GRLLAsGSADGTVRLWDLATGELLRTLTgHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATG-KLLRTLTG 328


                  ..
gi 158749547  280 HG 281
Cdd:COG2319   329 HT 330
WD40 COG2319
WD40 repeat [General function prediction only];
62-269 1.59e-16

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 83.04  E-value: 1.59e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749547   62 SALAFDPVQKILAVGTQTGALRLFGRPGVEC-YCQHDSGAAVIQLQFLINEGALVSALADDTLHLWNLRQKRPavLHSLK 140
Cdd:COG2319   208 RSVAFSPDGKLLASGSADGTVRLWDLATGKLlRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGEL--LRTLT 285

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749547  141 FCRERVTFCHLPFQSKWLYVGTERGNIHIVNVES----FTLSGyvimwnkaielsskaHPGPVVHISDNPmDEGKLLIGF 216
Cdd:COG2319   286 GHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATgkllRTLTG---------------HTGAVRSVAFSP-DGKTLASGS 349

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 158749547  217 ESGTVVLWDLKSKKADYRYT-YDEAIHSVAWHHEGKQFICSHSDGTLTIWNVRS 269
Cdd:COG2319   350 DDGTVRLWDLATGELLRTLTgHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
WD40 COG2319
WD40 repeat [General function prediction only];
48-281 2.80e-16

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 82.27  E-value: 2.80e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749547   48 QLCKTVRHGFPYQPSALAFDPVQKILAVGTQTGALRLFGRPGVECYCQ-HDSGAAVIQLQFLINEGALVSALADDTLHLW 126
Cdd:COG2319    68 GALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTlTGHTGAVRSVAFSPDGKTLASGSADGTVRLW 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749547  127 NLRQKRP-AVLHSLKFCRERVTFCHlpfQSKWLYVGTERGNIHIVNVES----FTLSGyvimwnkaielsskaHPGPVVH 201
Cdd:COG2319   148 DLATGKLlRTLTGHSGAVTSVAFSP---DGKLLASGSDDGTVRLWDLATgkllRTLTG---------------HTGAVRS 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749547  202 ISDNPmdEGKLLI-GFESGTVVLWDLKSKKADYRYT-YDEAIHSVAWHHEGKQFICSHSDGTLTIWNVRSPaKPVQTITP 279
Cdd:COG2319   210 VAFSP--DGKLLAsGSADGTVRLWDLATGKLLRTLTgHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATG-ELLRTLTG 286


                  ..
gi 158749547  280 HG 281
Cdd:COG2319   287 HS 288
WD40 COG2319
WD40 repeat [General function prediction only];
52-281 2.07e-14

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 76.49  E-value: 2.07e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749547   52 TVRHGFPYQPSALAFDPVQKILAVGTQTGALRLFGRPGVECYCQHDSGAAVIQLQFLINEGALVSALADDTLHLWNLRQK 131
Cdd:COG2319    31 LLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATG 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749547  132 RPavLHSLKFCRERVTFCHLPFQSKWLYVGTERGNIHIVNVES----FTLSGyvimwnkaielsskaHPGPV--VHISDN 205
Cdd:COG2319   111 LL--LRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATgkllRTLTG---------------HSGAVtsVAFSPD 173

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158749547  206 pmdeGKLLI-GFESGTVVLWDLKSKKADYRYT-YDEAIHSVAWHHEGKQFICSHSDGTLTIWNVRSPaKPVQTITPHG 281
Cdd:COG2319   174 ----GKLLAsGSDDGTVRLWDLATGKLLRTLTgHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATG-KLLRTLTGHS 246
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 62-280 1.24e-13

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: 72.75  E-value: 1.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749547   62 SALAFDPVQKILAVGTQTGALRLFGRPGVEC---YCQHDSgaAVIQLQFLINEGALVSALADDTLHLWNLRQKRPavLHS 138
Cdd:cd00200    55 RDVAASADGTYLASGSSDKTIRLWDLETGECvrtLTGHTS--YVSSVAFSPDGRILSSSSRDKTIKVWDVETGKC--LTT 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749547  139 LKFCRERVTFCHLPFQSKWLYVGTERGNIHIVNVESF----TLSGyvimwnkaielsskaHPGPVVHISDNPmDEGKLLI 214
Cdd:cd00200   131 LRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGkcvaTLTG---------------HTGEVNSVAFSP-DGEKLLS 194

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158749547  215 GFESGTVVLWDLKSKKADYRYTY-DEAIHSVAWHHEGKQFICSHSDGTLTIWNVRSPaKPVQTITPH 280
Cdd:cd00200   195 SSSDGTIKLWDLSTGKCLGTLRGhENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTG-ECVQTLSGH 260
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 62-280 1.97e-13

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: 71.98  E-value: 1.97e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749547   62 SALAFDPVQKILAVGTQTGALRLFGRPGVEC---YCQHDSGaaVIQLQFLINEGALVSALADDTLHLWNLRQKRpaVLHS 138
Cdd:cd00200    13 TCVAFSPDGKLLATGSGDGTIKVWDLETGELlrtLKGHTGP--VRDVAASADGTYLASGSSDKTIRLWDLETGE--CVRT 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749547  139 LKFCRERVTFCHLPFQSKWLYVGTERGNIHIVNVESFTLSgYVImwnkaielssKAHPGPVVHISDNPmdEGKLLIGFES 218
Cdd:cd00200    89 LTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCL-TTL----------RGHTDWVNSVAFSP--DGTFVASSSQ 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158749547  219 -GTVVLWDLKSKKADYRYT-YDEAIHSVAWHHEGKQFICSHSDGTLTIWNVRSpAKPVQTITPH 280
Cdd:cd00200   156 dGTIKLWDLRTGKCVATLTgHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLST-GKCLGTLRGH 218
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 62-266 7.65e-13

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: 70.44  E-value: 7.65e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749547   62 SALAFDPVQKILAVGTQTGALRLF-GRPGVECYCQHDSGAAVIQLQFLINEGALVSALADDTLHLWNLRQKRPavLHSLK 140
Cdd:cd00200    97 SSVAFSPDGRILSSSSRDKTIKVWdVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKC--VATLT 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749547  141 FCRERVTFCHLPFQSKWLYVGTERGNIHIVNVESFTLSGyvimwnkaiELSSkaHPGPVVHISDNPmdEGKLLI-GFESG 219
Cdd:cd00200   175 GHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLG---------TLRG--HENGVNSVAFSP--DGYLLAsGSEDG 241

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 158749547  220 TVVLWDLKSKKADYRYT-YDEAIHSVAWHHEGKQFICSHSDGTLTIWN 266
Cdd:cd00200   242 TIRVWDLRTGECVQTLSgHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 96-280 2.62e-11

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: 65.82  E-value: 2.62e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749547   96 HDSGaaVIQLQFLINEGALVSALADDTLHLWNLRQKRPA---VLHSLKfcrerVTFCHLPFQSKWLYVGTERGNIHIVNV 172
Cdd:cd00200     8 HTGG--VTCVAFSPDGKLLATGSGDGTIKVWDLETGELLrtlKGHTGP-----VRDVAASADGTYLASGSSDKTIRLWDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749547  173 ESFTLSGYVimwnkaielssKAHPGPV--VHISDNpmdeGKLLIG-FESGTVVLWDLKSKKADYRYTY-DEAIHSVAWHH 248
Cdd:cd00200    81 ETGECVRTL-----------TGHTSYVssVAFSPD----GRILSSsSRDKTIKVWDVETGKCLTTLRGhTDWVNSVAFSP 145

                         170       180       190
                  ....*....|....*....|....*....|..
gi 158749547  249 EGKQFICSHSDGTLTIWNVRSpAKPVQTITPH 280
Cdd:cd00200   146 DGTFVASSSQDGTIKLWDLRT-GKCVATLTGH 176
R-SNARE_STXBP6 cd15892
SNARE domain of STXBP6; Syntaxin binding protein 6 (STXBP6, also called Amisyn), as well as ...
 1050-1109 2.89e-09

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: 54.00  E-value: 2.89e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 158749547 1050 GGIEGVKGAASGVVGELARARLALDERGQKLSDLEERTAAMMSSADSFSKHAHEMMLKYK 1109
Cdd:cd15892     2 GGNSILHSAADSVTSAVQKASQALNERGERLGRAEEKTEDMKNSAQQFAETAHKLAMKHK 61
R-SNARE cd15843
SNARE motif, subgroup R-SNARE; SNARE (soluble N-ethylmaleimide-sensitive factor attachment ...
 1075-1109 2.21e-05

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: 42.87  E-value: 2.21e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 158749547 1075 ERGQKLSDLEERTAAMMSSADSFSKHAHEMMLKYK 1109
Cdd:cd15843    26 ERGEKLEDLVDKTENLNESANAFKKQARKLKRKMW 60
Synaptobrevin pfam00957
Synaptobrevin;
1075-1114 1.32e-04

Synaptobrevin;


Pssm-ID: 395764  Cd Length: 89  Bit Score: 41.75  E-value: 1.32e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 158749547  1075 ERGQKLSDLEERTAAMMSSADSFSKHAHEMMLKY--KDKKWY 1114
Cdd:pfam00957   28 ERGEKLDLLVDKTENLQSSAQQFRRQARKLKRKMwwKNMKLY 69
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 238-266 9.83e-04

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 37.68  E-value: 9.83e-04
                            10        20
                    ....*....|....*....|....*....
gi 158749547    238 DEAIHSVAWHHEGKQFICSHSDGTLTIWN 266
Cdd:smart00320   12 TGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 COG2319
WD40 repeat [General function prediction only];
56-129 8.18e-03

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 39.89  E-value: 8.18e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158749547   56 GFPYQPSALAFDPVQKILAVGTQTGALRLFGRPGVECYC---QHDsgAAVIQLQFLINEGALVSALADDTLHLWNLR 129
Cdd:COG2319   328 GHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRtltGHT--GAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
 
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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