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Conserved domains on  [gi|1907078673|ref|XP_036012004|]
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syntaxin-binding protein 5 isoform X6 [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 5.97e-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: 5.97e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907078673  276 TITPHGkqlkdgkkPEPCKPILKVELKTTRSGEPFIILSGGLSYDTVGRRPCLTVMHGKSTAVLEMDYSIVDFLTLCETP 355
Cdd:pfam08366    1 PTTPYG--------PFPCKAITKILWKTTKTGEPFIIFSGGMPRASYGDRHCITVMHGKKHTVFDFTSKVIDFFTLCESP 72

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1907078673  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 ...
 1060-1120 7.50e-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: 7.50e-38
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907078673 1060 PGGIEGVKGAASGVVGELARARLALDERGQKLSDLEERTAAMMSSADSFSKHAHEMMLKYK 1120
Cdd:cd15893      1 PGGIEGVKGAASGVVGELARARLALDERGQKLGELEERTAAMLASADSFSKHAHEMMLKYK 61
WD40 COG2319
WD40 repeat [General function prediction only];
49-281 1.55e-16

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 83.04  E-value: 1.55e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907078673   49 LCKTVRHGFPYQPSALAFDPVQKILAVGTQTGALRLFGRPGVECYCQ-HDSGAAVIQLQFLINEGALVSALADDTLHLWN 127
Cdd:COG2319    111 LLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTlTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWD 190

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907078673  128 LRQKRPavLHSLKFCRERVTFCHLPFQSKWLYVGTERGNIHIVNVES----FTLSGyvimwnkaielsskaHPGPV--VH 201
Cdd:COG2319    191 LATGKL--LRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATgkllRTLTG---------------HSGSVrsVA 253

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907078673  202 ISDNpmdeGKLLI-GFESGTVVLWDLKSKKADYRYT-YDEAIHSVAWHHEGKQFICSHSDGTLTIWNVRSPaKPVQTITP 279
Cdd:COG2319    254 FSPD----GRLLAsGSADGTVRLWDLATGELLRTLTgHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATG-KLLRTLTG 328


                   ..
gi 1907078673  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 5.97e-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: 5.97e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907078673  276 TITPHGkqlkdgkkPEPCKPILKVELKTTRSGEPFIILSGGLSYDTVGRRPCLTVMHGKSTAVLEMDYSIVDFLTLCETP 355
Cdd:pfam08366    1 PTTPYG--------PFPCKAITKILWKTTKTGEPFIIFSGGMPRASYGDRHCITVMHGKKHTVFDFTSKVIDFFTLCESP 72

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1907078673  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 ...
 1060-1120 7.50e-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: 7.50e-38
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907078673 1060 PGGIEGVKGAASGVVGELARARLALDERGQKLSDLEERTAAMMSSADSFSKHAHEMMLKYK 1120
Cdd:cd15893      1 PGGIEGVKGAASGVVGELARARLALDERGQKLGELEERTAAMLASADSFSKHAHEMMLKYK 61
WD40 COG2319
WD40 repeat [General function prediction only];
49-281 1.55e-16

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 83.04  E-value: 1.55e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907078673   49 LCKTVRHGFPYQPSALAFDPVQKILAVGTQTGALRLFGRPGVECYCQ-HDSGAAVIQLQFLINEGALVSALADDTLHLWN 127
Cdd:COG2319    111 LLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTlTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWD 190

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907078673  128 LRQKRPavLHSLKFCRERVTFCHLPFQSKWLYVGTERGNIHIVNVES----FTLSGyvimwnkaielsskaHPGPV--VH 201
Cdd:COG2319    191 LATGKL--LRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATgkllRTLTG---------------HSGSVrsVA 253

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907078673  202 ISDNpmdeGKLLI-GFESGTVVLWDLKSKKADYRYT-YDEAIHSVAWHHEGKQFICSHSDGTLTIWNVRSPaKPVQTITP 279
Cdd:COG2319    254 FSPD----GRLLAsGSADGTVRLWDLATGELLRTLTgHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATG-KLLRTLTG 328


                   ..
gi 1907078673  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 1.25e-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: 1.25e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907078673   62 SALAFDPVQKILAVGTQTGALRLFGRPGVEC---YCQHDSgaAVIQLQFLINEGALVSALADDTLHLWNLRQKRPavLHS 138
Cdd:cd00200     55 RDVAASADGTYLASGSSDKTIRLWDLETGECvrtLTGHTS--YVSSVAFSPDGRILSSSSRDKTIKVWDVETGKC--LTT 130

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907078673  139 LKFCRERVTFCHLPFQSKWLYVGTERGNIHIVNVESF----TLSGyvimwnkaielsskaHPGPVVHISDNPmDEGKLLI 214
Cdd:cd00200    131 LRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGkcvaTLTG---------------HTGEVNSVAFSP-DGEKLLS 194

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907078673  215 GFESGTVVLWDLKSKKADYRYTY-DEAIHSVAWHHEGKQFICSHSDGTLTIWNVRSPaKPVQTITPH 280
Cdd:cd00200    195 SSSDGTIKLWDLSTGKCLGTLRGhENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTG-ECVQTLSGH 260
Synaptobrevin pfam00957
Synaptobrevin;
1086-1125 1.33e-04

Synaptobrevin;


Pssm-ID: 395764  Cd Length: 89  Bit Score: 41.75  E-value: 1.33e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1907078673 1086 ERGQKLSDLEERTAAMMSSADSFSKHAHEMMLKY--KDKKWY 1125
Cdd:pfam00957   28 ERGEKLDLLVDKTENLQSSAQQFRRQARKLKRKMwwKNMKLY 69
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 238-266 1.10e-03

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: 1.10e-03
                            10        20
                    ....*....|....*....|....*....
gi 1907078673   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 5.97e-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: 5.97e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907078673  276 TITPHGkqlkdgkkPEPCKPILKVELKTTRSGEPFIILSGGLSYDTVGRRPCLTVMHGKSTAVLEMDYSIVDFLTLCETP 355
Cdd:pfam08366    1 PTTPYG--------PFPCKAITKILWKTTKTGEPFIIFSGGMPRASYGDRHCITVMHGKKHTVFDFTSKVIDFFTLCESP 72

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1907078673  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 ...
 1060-1120 7.50e-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: 7.50e-38
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907078673 1060 PGGIEGVKGAASGVVGELARARLALDERGQKLSDLEERTAAMMSSADSFSKHAHEMMLKYK 1120
Cdd:cd15893      1 PGGIEGVKGAASGVVGELARARLALDERGQKLGELEERTAAMLASADSFSKHAHEMMLKYK 61
R-SNARE_STXBP5_6 cd15873
SNARE domain of STXBP5, STXBP6 and related proteins; Syntaxin binding protein 5 (STXBP5, also ...
 1060-1120 2.29e-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: 2.29e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907078673 1060 PGGIEGVKGAASGVVGELARARLALDERGQKLSDLEERTAAMMSSADSFSKHAHEMMLKYK 1120
Cdd:cd15873      1 GGGMKALRAKAGSAASAAARARQALNERGEKLSELEDRTAEMEDNAESFASTAKELAKKYK 61
WD40 COG2319
WD40 repeat [General function prediction only];
49-281 1.55e-16

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 83.04  E-value: 1.55e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907078673   49 LCKTVRHGFPYQPSALAFDPVQKILAVGTQTGALRLFGRPGVECYCQ-HDSGAAVIQLQFLINEGALVSALADDTLHLWN 127
Cdd:COG2319    111 LLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTlTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWD 190

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907078673  128 LRQKRPavLHSLKFCRERVTFCHLPFQSKWLYVGTERGNIHIVNVES----FTLSGyvimwnkaielsskaHPGPV--VH 201
Cdd:COG2319    191 LATGKL--LRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATgkllRTLTG---------------HSGSVrsVA 253

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907078673  202 ISDNpmdeGKLLI-GFESGTVVLWDLKSKKADYRYT-YDEAIHSVAWHHEGKQFICSHSDGTLTIWNVRSPaKPVQTITP 279
Cdd:COG2319    254 FSPD----GRLLAsGSADGTVRLWDLATGELLRTLTgHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATG-KLLRTLTG 328


                   ..
gi 1907078673  280 HG 281
Cdd:COG2319    329 HT 330
WD40 COG2319
WD40 repeat [General function prediction only];
62-269 1.61e-16

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 83.04  E-value: 1.61e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907078673   62 SALAFDPVQKILAVGTQTGALRLFGRPGVEC-YCQHDSGAAVIQLQFLINEGALVSALADDTLHLWNLRQKRPavLHSLK 140
Cdd:COG2319    208 RSVAFSPDGKLLASGSADGTVRLWDLATGKLlRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGEL--LRTLT 285

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907078673  141 FCRERVTFCHLPFQSKWLYVGTERGNIHIVNVES----FTLSGyvimwnkaielsskaHPGPVVHISDNPmDEGKLLIGF 216
Cdd:COG2319    286 GHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATgkllRTLTG---------------HTGAVRSVAFSP-DGKTLASGS 349

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907078673  217 ESGTVVLWDLKSKKADYRYT-YDEAIHSVAWHHEGKQFICSHSDGTLTIWNVRS 269
Cdd:COG2319    350 DDGTVRLWDLATGELLRTLTgHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
WD40 COG2319
WD40 repeat [General function prediction only];
48-281 2.84e-16

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 82.27  E-value: 2.84e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907078673   48 QLCKTVRHGFPYQPSALAFDPVQKILAVGTQTGALRLFGRPGVECYCQ-HDSGAAVIQLQFLINEGALVSALADDTLHLW 126
Cdd:COG2319     68 GALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTlTGHTGAVRSVAFSPDGKTLASGSADGTVRLW 147

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907078673  127 NLRQKRP-AVLHSLKFCRERVTFCHlpfQSKWLYVGTERGNIHIVNVES----FTLSGyvimwnkaielsskaHPGPVVH 201
Cdd:COG2319    148 DLATGKLlRTLTGHSGAVTSVAFSP---DGKLLASGSDDGTVRLWDLATgkllRTLTG---------------HTGAVRS 209

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907078673  202 ISDNPmdEGKLLI-GFESGTVVLWDLKSKKADYRYT-YDEAIHSVAWHHEGKQFICSHSDGTLTIWNVRSPaKPVQTITP 279
Cdd:COG2319    210 VAFSP--DGKLLAsGSADGTVRLWDLATGKLLRTLTgHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATG-ELLRTLTG 286


                   ..
gi 1907078673  280 HG 281
Cdd:COG2319    287 HS 288
WD40 COG2319
WD40 repeat [General function prediction only];
52-281 2.10e-14

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 76.49  E-value: 2.10e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907078673   52 TVRHGFPYQPSALAFDPVQKILAVGTQTGALRLFGRPGVECYCQHDSGAAVIQLQFLINEGALVSALADDTLHLWNLRQK 131
Cdd:COG2319     31 LLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATG 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907078673  132 RPavLHSLKFCRERVTFCHLPFQSKWLYVGTERGNIHIVNVES----FTLSGyvimwnkaielsskaHPGPV--VHISDN 205
Cdd:COG2319    111 LL--LRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATgkllRTLTG---------------HSGAVtsVAFSPD 173

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907078673  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 1.25e-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: 1.25e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907078673   62 SALAFDPVQKILAVGTQTGALRLFGRPGVEC---YCQHDSgaAVIQLQFLINEGALVSALADDTLHLWNLRQKRPavLHS 138
Cdd:cd00200     55 RDVAASADGTYLASGSSDKTIRLWDLETGECvrtLTGHTS--YVSSVAFSPDGRILSSSSRDKTIKVWDVETGKC--LTT 130

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907078673  139 LKFCRERVTFCHLPFQSKWLYVGTERGNIHIVNVESF----TLSGyvimwnkaielsskaHPGPVVHISDNPmDEGKLLI 214
Cdd:cd00200    131 LRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGkcvaTLTG---------------HTGEVNSVAFSP-DGEKLLS 194

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907078673  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 1.99e-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: 1.99e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907078673   62 SALAFDPVQKILAVGTQTGALRLFGRPGVEC---YCQHDSGaaVIQLQFLINEGALVSALADDTLHLWNLRQKRpaVLHS 138
Cdd:cd00200     13 TCVAFSPDGKLLATGSGDGTIKVWDLETGELlrtLKGHTGP--VRDVAASADGTYLASGSSDKTIRLWDLETGE--CVRT 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907078673  139 LKFCRERVTFCHLPFQSKWLYVGTERGNIHIVNVESFTLSgYVImwnkaielssKAHPGPVVHISDNPmdEGKLLIGFES 218
Cdd:cd00200     89 LTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCL-TTL----------RGHTDWVNSVAFSP--DGTFVASSSQ 155

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907078673  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 7.74e-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: 7.74e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907078673   62 SALAFDPVQKILAVGTQTGALRLF-GRPGVECYCQHDSGAAVIQLQFLINEGALVSALADDTLHLWNLRQKRPavLHSLK 140
Cdd:cd00200     97 SSVAFSPDGRILSSSSRDKTIKVWdVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKC--VATLT 174

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907078673  141 FCRERVTFCHLPFQSKWLYVGTERGNIHIVNVESFTLSGyvimwnkaiELSSkaHPGPVVHISDNPmdEGKLLI-GFESG 219
Cdd:cd00200    175 GHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLG---------TLRG--HENGVNSVAFSP--DGYLLAsGSEDG 241

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1907078673  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 2.65e-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: 2.65e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907078673   96 HDSGaaVIQLQFLINEGALVSALADDTLHLWNLRQKRPA---VLHSLKfcrerVTFCHLPFQSKWLYVGTERGNIHIVNV 172
Cdd:cd00200      8 HTGG--VTCVAFSPDGKLLATGSGDGTIKVWDLETGELLrtlKGHTGP-----VRDVAASADGTYLASGSSDKTIRLWDL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907078673  173 ESFTLSGYVimwnkaielssKAHPGPV--VHISDNpmdeGKLLIG-FESGTVVLWDLKSKKADYRYTY-DEAIHSVAWHH 248
Cdd:cd00200     81 ETGECVRTL-----------TGHTSYVssVAFSPD----GRILSSsSRDKTIKVWDVETGKCLTTLRGhTDWVNSVAFSP 145

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1907078673  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 ...
 1061-1120 2.92e-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: 2.92e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907078673 1061 GGIEGVKGAASGVVGELARARLALDERGQKLSDLEERTAAMMSSADSFSKHAHEMMLKYK 1120
Cdd:cd15892      2 GGNSILHSAADSVTSAVQKASQALNERGERLGRAEEKTEDMKNSAQQFAETAHKLAMKHK 61
R-SNARE cd15843
SNARE motif, subgroup R-SNARE; SNARE (soluble N-ethylmaleimide-sensitive factor attachment ...
 1086-1120 2.23e-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: 2.23e-05
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1907078673 1086 ERGQKLSDLEERTAAMMSSADSFSKHAHEMMLKYK 1120
Cdd:cd15843     26 ERGEKLEDLVDKTENLNESANAFKKQARKLKRKMW 60
Synaptobrevin pfam00957
Synaptobrevin;
1086-1125 1.33e-04

Synaptobrevin;


Pssm-ID: 395764  Cd Length: 89  Bit Score: 41.75  E-value: 1.33e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1907078673 1086 ERGQKLSDLEERTAAMMSSADSFSKHAHEMMLKY--KDKKWY 1125
Cdd:pfam00957   28 ERGEKLDLLVDKTENLQSSAQQFRRQARKLKRKMwwKNMKLY 69
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 238-266 1.10e-03

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: 1.10e-03
                            10        20
                    ....*....|....*....|....*....
gi 1907078673   238 DEAIHSVAWHHEGKQFICSHSDGTLTIWN 266
Cdd:smart00320   12 TGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 COG2319
WD40 repeat [General function prediction only];
56-129 8.28e-03

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 39.89  E-value: 8.28e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907078673   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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