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Conserved domains on  [gi|2027535381|ref|NP_001381338|]
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syntaxin-binding protein 5 isoform c [Homo sapiens]

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 ...
 275-384 7.03e-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: 7.03e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027535381  275 TITPHGkqlkdgkkPEPCKPILKVEFKTTRSGEPFIILSGGLSYDTVGRRPCLTVMHGKSTAVLEMDYSIVDFLTLCETP 354
Cdd:pfam08366    1 PTTPYG--------PFPCKAITKILWKTTKTGEPFIIFSGGMPRASYGDRHCITVMHGKKHTVFDFTSKVIDFFTLCESP 72

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2027535381  355 YPN-DFQEPYAVVVLLEKDLVLIDLAQNGYP 384
Cdd:pfam08366   73 DPNaEFDDPYALVVLLEEELVVIDLTTPGWP 103
R-SNARE_STXBP5 cd15893
SNARE domain of STXBP5; Syntaxin binding protein 5 (STXBP5, also called Tomosyn), as well as ...
 1068-1128 5.43e-37

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: 133.24  E-value: 5.43e-37
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2027535381 1068 PGGIEGVKGAASGVVGELARARLALDERGQKLGDLEERTAAMLSSAESFSKHAHEIMLKYK 1128
Cdd:cd15893      1 PGGIEGVKGAASGVVGELARARLALDERGQKLGELEERTAAMLASADSFSKHAHEMMLKYK 61
WD40 COG2319
WD40 repeat [General function prediction only];
48-280 1.57e-16

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 83.04  E-value: 1.57e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027535381   48 LCKTVRHGFPYQPSALAFDPVQKILAVGTQTGALRLFGRPGVECYCQ-HDSGAAVIQLQFLINEGALVSALADDTLHLWN 126
Cdd:COG2319    111 LLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTlTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWD 190

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027535381  127 LRQKRPaiLHSLKFCRERVTFCHLPFQSKWLYVGTERGNIHIVNVES----FTLSGyvimwnkaielssksHPGPV--VH 200
Cdd:COG2319    191 LATGKL--LRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATgkllRTLTG---------------HSGSVrsVA 253

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027535381  201 ISDNpmdeGKLLI-GFESGTVVLWDLKSKKADYRYT-YDEAIHSVAWHHEGKQFICSHSDGTLTIWNVRSPaKPVQTITP 278
Cdd:COG2319    254 FSPD----GRLLAsGSADGTVRLWDLATGELLRTLTgHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATG-KLLRTLTG 328


                   ..
gi 2027535381  279 HG 280
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 ...
 275-384 7.03e-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: 7.03e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027535381  275 TITPHGkqlkdgkkPEPCKPILKVEFKTTRSGEPFIILSGGLSYDTVGRRPCLTVMHGKSTAVLEMDYSIVDFLTLCETP 354
Cdd:pfam08366    1 PTTPYG--------PFPCKAITKILWKTTKTGEPFIIFSGGMPRASYGDRHCITVMHGKKHTVFDFTSKVIDFFTLCESP 72

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2027535381  355 YPN-DFQEPYAVVVLLEKDLVLIDLAQNGYP 384
Cdd:pfam08366   73 DPNaEFDDPYALVVLLEEELVVIDLTTPGWP 103
R-SNARE_STXBP5 cd15893
SNARE domain of STXBP5; Syntaxin binding protein 5 (STXBP5, also called Tomosyn), as well as ...
 1068-1128 5.43e-37

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: 133.24  E-value: 5.43e-37
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2027535381 1068 PGGIEGVKGAASGVVGELARARLALDERGQKLGDLEERTAAMLSSAESFSKHAHEIMLKYK 1128
Cdd:cd15893      1 PGGIEGVKGAASGVVGELARARLALDERGQKLGELEERTAAMLASADSFSKHAHEMMLKYK 61
WD40 COG2319
WD40 repeat [General function prediction only];
48-280 1.57e-16

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 83.04  E-value: 1.57e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027535381   48 LCKTVRHGFPYQPSALAFDPVQKILAVGTQTGALRLFGRPGVECYCQ-HDSGAAVIQLQFLINEGALVSALADDTLHLWN 126
Cdd:COG2319    111 LLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTlTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWD 190

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027535381  127 LRQKRPaiLHSLKFCRERVTFCHLPFQSKWLYVGTERGNIHIVNVES----FTLSGyvimwnkaielssksHPGPV--VH 200
Cdd:COG2319    191 LATGKL--LRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATgkllRTLTG---------------HSGSVrsVA 253

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027535381  201 ISDNpmdeGKLLI-GFESGTVVLWDLKSKKADYRYT-YDEAIHSVAWHHEGKQFICSHSDGTLTIWNVRSPaKPVQTITP 278
Cdd:COG2319    254 FSPD----GRLLAsGSADGTVRLWDLATGELLRTLTgHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATG-KLLRTLTG 328


                   ..
gi 2027535381  279 HG 280
Cdd:COG2319    329 HT 330
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 61-279 1.27e-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: 1.27e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027535381   61 SALAFDPVQKILAVGTQTGALRLFGRPGVEC---YCQHDSgaAVIQLQFLINEGALVSALADDTLHLWNLRQKRPaiLHS 137
Cdd:cd00200     55 RDVAASADGTYLASGSSDKTIRLWDLETGECvrtLTGHTS--YVSSVAFSPDGRILSSSSRDKTIKVWDVETGKC--LTT 130

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027535381  138 LKFCRERVTFCHLPFQSKWLYVGTERGNIHIVNVESF----TLSGyvimwnkaielssksHPGPVVHISDNPmDEGKLLI 213
Cdd:cd00200    131 LRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGkcvaTLTG---------------HTGEVNSVAFSP-DGEKLLS 194

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2027535381  214 GFESGTVVLWDLKSKKADYRYTY-DEAIHSVAWHHEGKQFICSHSDGTLTIWNVRSPaKPVQTITPH 279
Cdd:cd00200    195 SSSDGTIKLWDLSTGKCLGTLRGhENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTG-ECVQTLSGH 260
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 237-265 1.00e-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: 1.00e-03
                            10        20
                    ....*....|....*....|....*....
gi 2027535381   237 DEAIHSVAWHHEGKQFICSHSDGTLTIWN 265
Cdd:smart00320   12 TGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
Synaptobrevin pfam00957
Synaptobrevin;
1094-1133 1.40e-03

Synaptobrevin;


Pssm-ID: 395764  Cd Length: 89  Bit Score: 39.06  E-value: 1.40e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 2027535381 1094 ERGQKLGDLEERTAAMLSSAESFSKHAHEIMLKY--KDKKWY 1133
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 ...
 275-384 7.03e-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: 7.03e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027535381  275 TITPHGkqlkdgkkPEPCKPILKVEFKTTRSGEPFIILSGGLSYDTVGRRPCLTVMHGKSTAVLEMDYSIVDFLTLCETP 354
Cdd:pfam08366    1 PTTPYG--------PFPCKAITKILWKTTKTGEPFIIFSGGMPRASYGDRHCITVMHGKKHTVFDFTSKVIDFFTLCESP 72

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2027535381  355 YPN-DFQEPYAVVVLLEKDLVLIDLAQNGYP 384
Cdd:pfam08366   73 DPNaEFDDPYALVVLLEEELVVIDLTTPGWP 103
R-SNARE_STXBP5 cd15893
SNARE domain of STXBP5; Syntaxin binding protein 5 (STXBP5, also called Tomosyn), as well as ...
 1068-1128 5.43e-37

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: 133.24  E-value: 5.43e-37
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2027535381 1068 PGGIEGVKGAASGVVGELARARLALDERGQKLGDLEERTAAMLSSAESFSKHAHEIMLKYK 1128
Cdd:cd15893      1 PGGIEGVKGAASGVVGELARARLALDERGQKLGELEERTAAMLASADSFSKHAHEMMLKYK 61
R-SNARE_STXBP5_6 cd15873
SNARE domain of STXBP5, STXBP6 and related proteins; Syntaxin binding protein 5 (STXBP5, also ...
 1068-1128 5.86e-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: 93.09  E-value: 5.86e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2027535381 1068 PGGIEGVKGAASGVVGELARARLALDERGQKLGDLEERTAAMLSSAESFSKHAHEIMLKYK 1128
Cdd:cd15873      1 GGGMKALRAKAGSAASAAARARQALNERGEKLSELEDRTAEMEDNAESFASTAKELAKKYK 61
WD40 COG2319
WD40 repeat [General function prediction only];
48-280 1.57e-16

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 83.04  E-value: 1.57e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027535381   48 LCKTVRHGFPYQPSALAFDPVQKILAVGTQTGALRLFGRPGVECYCQ-HDSGAAVIQLQFLINEGALVSALADDTLHLWN 126
Cdd:COG2319    111 LLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTlTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWD 190

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027535381  127 LRQKRPaiLHSLKFCRERVTFCHLPFQSKWLYVGTERGNIHIVNVES----FTLSGyvimwnkaielssksHPGPV--VH 200
Cdd:COG2319    191 LATGKL--LRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATgkllRTLTG---------------HSGSVrsVA 253

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027535381  201 ISDNpmdeGKLLI-GFESGTVVLWDLKSKKADYRYT-YDEAIHSVAWHHEGKQFICSHSDGTLTIWNVRSPaKPVQTITP 278
Cdd:COG2319    254 FSPD----GRLLAsGSADGTVRLWDLATGELLRTLTgHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATG-KLLRTLTG 328


                   ..
gi 2027535381  279 HG 280
Cdd:COG2319    329 HT 330
WD40 COG2319
WD40 repeat [General function prediction only];
61-268 1.63e-16

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 83.04  E-value: 1.63e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027535381   61 SALAFDPVQKILAVGTQTGALRLFGRPGVEC-YCQHDSGAAVIQLQFLINEGALVSALADDTLHLWNLRQKRPaiLHSLK 139
Cdd:COG2319    208 RSVAFSPDGKLLASGSADGTVRLWDLATGKLlRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGEL--LRTLT 285

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027535381  140 FCRERVTFCHLPFQSKWLYVGTERGNIHIVNVES----FTLSGyvimwnkaielssksHPGPVVHISDNPmDEGKLLIGF 215
Cdd:COG2319    286 GHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATgkllRTLTG---------------HTGAVRSVAFSP-DGKTLASGS 349

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2027535381  216 ESGTVVLWDLKSKKADYRYT-YDEAIHSVAWHHEGKQFICSHSDGTLTIWNVRS 268
Cdd:COG2319    350 DDGTVRLWDLATGELLRTLTgHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
WD40 COG2319
WD40 repeat [General function prediction only];
47-280 3.46e-16

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 82.27  E-value: 3.46e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027535381   47 QLCKTVRHGFPYQPSALAFDPVQKILAVGTQTGALRLFGRPGVECYCQ-HDSGAAVIQLQFLINEGALVSALADDTLHLW 125
Cdd:COG2319     68 GALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTlTGHTGAVRSVAFSPDGKTLASGSADGTVRLW 147

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027535381  126 NLRQKRPaiLHSLKFCRERVTfcHLPF--QSKWLYVGTERGNIHIVNVES----FTLSGyvimwnkaielssksHPGPVV 199
Cdd:COG2319    148 DLATGKL--LRTLTGHSGAVT--SVAFspDGKLLASGSDDGTVRLWDLATgkllRTLTG---------------HTGAVR 208

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027535381  200 HISDNPmdEGKLLI-GFESGTVVLWDLKSKKADYRYT-YDEAIHSVAWHHEGKQFICSHSDGTLTIWNVRSPaKPVQTIT 277
Cdd:COG2319    209 SVAFSP--DGKLLAsGSADGTVRLWDLATGKLLRTLTgHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATG-ELLRTLT 285


                   ...
gi 2027535381  278 PHG 280
Cdd:COG2319    286 GHS 288
WD40 COG2319
WD40 repeat [General function prediction only];
51-280 2.12e-14

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 76.49  E-value: 2.12e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027535381   51 TVRHGFPYQPSALAFDPVQKILAVGTQTGALRLFGRPGVECYCQHDSGAAVIQLQFLINEGALVSALADDTLHLWNLRQK 130
Cdd:COG2319     31 LLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATG 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027535381  131 RPaiLHSLKFCRERVTFCHLPFQSKWLYVGTERGNIHIVNVES----FTLSGyvimwnkaielssksHPGPV--VHISDN 204
Cdd:COG2319    111 LL--LRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATgkllRTLTG---------------HSGAVtsVAFSPD 173

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2027535381  205 pmdeGKLLI-GFESGTVVLWDLKSKKADYRYT-YDEAIHSVAWHHEGKQFICSHSDGTLTIWNVRSPaKPVQTITPHG 280
Cdd:COG2319    174 ----GKLLAsGSDDGTVRLWDLATGKLLRTLTgHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATG-KLLRTLTGHS 246
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 61-279 1.27e-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: 1.27e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027535381   61 SALAFDPVQKILAVGTQTGALRLFGRPGVEC---YCQHDSgaAVIQLQFLINEGALVSALADDTLHLWNLRQKRPaiLHS 137
Cdd:cd00200     55 RDVAASADGTYLASGSSDKTIRLWDLETGECvrtLTGHTS--YVSSVAFSPDGRILSSSSRDKTIKVWDVETGKC--LTT 130

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027535381  138 LKFCRERVTFCHLPFQSKWLYVGTERGNIHIVNVESF----TLSGyvimwnkaielssksHPGPVVHISDNPmDEGKLLI 213
Cdd:cd00200    131 LRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGkcvaTLTG---------------HTGEVNSVAFSP-DGEKLLS 194

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2027535381  214 GFESGTVVLWDLKSKKADYRYTY-DEAIHSVAWHHEGKQFICSHSDGTLTIWNVRSPaKPVQTITPH 279
Cdd:cd00200    195 SSSDGTIKLWDLSTGKCLGTLRGhENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTG-ECVQTLSGH 260
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 61-279 2.83e-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: 71.60  E-value: 2.83e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027535381   61 SALAFDPVQKILAVGTQTGALRLFGRPGVEC---YCQHDSGaaVIQLQFLINEGALVSALADDTLHLWNLRQKRPaiLHS 137
Cdd:cd00200     13 TCVAFSPDGKLLATGSGDGTIKVWDLETGELlrtLKGHTGP--VRDVAASADGTYLASGSSDKTIRLWDLETGEC--VRT 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027535381  138 LKFCRERVTFCHLPFQSKWLYVGTERGNIHIVNVESFTLSgYVImwnkaielssKSHPGPVVHISDNPmdEGKLLIGFES 217
Cdd:cd00200     89 LTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCL-TTL----------RGHTDWVNSVAFSP--DGTFVASSSQ 155

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2027535381  218 -GTVVLWDLKSKKADYRYT-YDEAIHSVAWHHEGKQFICSHSDGTLTIWNVRSpAKPVQTITPH 279
Cdd:cd00200    156 dGTIKLWDLRTGKCVATLTgHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLST-GKCLGTLRGH 218
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 61-265 5.81e-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: 70.83  E-value: 5.81e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027535381   61 SALAFDPVQKILAVGTQTGALRLF-GRPGVECYCQHDSGAAVIQLQFLINEGALVSALADDTLHLWNLRQKRPaiLHSLK 139
Cdd:cd00200     97 SSVAFSPDGRILSSSSRDKTIKVWdVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKC--VATLT 174

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027535381  140 FCRERVTFCHLPFQSKWLYVGTERGNIHIVNVESFTLSGYVImwnkaielsskSHPGPVVHISDNPmdEGKLLI-GFESG 218
Cdd:cd00200    175 GHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLR-----------GHENGVNSVAFSP--DGYLLAsGSEDG 241

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2027535381  219 TVVLWDLKSKKADYRYT-YDEAIHSVAWHHEGKQFICSHSDGTLTIWN 265
Cdd:cd00200    242 TIRVWDLRTGECVQTLSgHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 95-279 3.30e-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: 65.43  E-value: 3.30e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027535381   95 HDSGaaVIQLQFLINEGALVSALADDTLHLWNLRQKRPAI---LHSLKfcrerVTFCHLPFQSKWLYVGTERGNIHIVNV 171
Cdd:cd00200      8 HTGG--VTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRtlkGHTGP-----VRDVAASADGTYLASGSSDKTIRLWDL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027535381  172 ESFTLSGYVimwnkaielssKSHPGPV--VHISDNpmdeGKLLIG-FESGTVVLWDLKSKKADYRYTY-DEAIHSVAWHH 247
Cdd:cd00200     81 ETGECVRTL-----------TGHTSYVssVAFSPD----GRILSSsSRDKTIKVWDVETGKCLTTLRGhTDWVNSVAFSP 145

                          170       180       190
                   ....*....|....*....|....*....|..
gi 2027535381  248 EGKQFICSHSDGTLTIWNVRSpAKPVQTITPH 279
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 ...
 1069-1128 4.20e-10

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: 56.70  E-value: 4.20e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2027535381 1069 GGIEGVKGAASGVVGELARARLALDERGQKLGDLEERTAAMLSSAESFSKHAHEIMLKYK 1128
Cdd:cd15892      2 GGNSILHSAADSVTSAVQKASQALNERGERLGRAEEKTEDMKNSAQQFAETAHKLAMKHK 61
R-SNARE cd15843
SNARE motif, subgroup R-SNARE; SNARE (soluble N-ethylmaleimide-sensitive factor attachment ...
 1094-1128 5.70e-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: 39.02  E-value: 5.70e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 2027535381 1094 ERGQKLGDLEERTAAMLSSAESFSKHAHEIMLKYK 1128
Cdd:cd15843     26 ERGEKLEDLVDKTENLNESANAFKKQARKLKRKMW 60
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 237-265 1.00e-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: 1.00e-03
                            10        20
                    ....*....|....*....|....*....
gi 2027535381   237 DEAIHSVAWHHEGKQFICSHSDGTLTIWN 265
Cdd:smart00320   12 TGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
Synaptobrevin pfam00957
Synaptobrevin;
1094-1133 1.40e-03

Synaptobrevin;


Pssm-ID: 395764  Cd Length: 89  Bit Score: 39.06  E-value: 1.40e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 2027535381 1094 ERGQKLGDLEERTAAMLSSAESFSKHAHEIMLKY--KDKKWY 1133
Cdd:pfam00957   28 ERGEKLDLLVDKTENLQSSAQQFRRQARKLKRKMwwKNMKLY 69
R-SNARE_VAMP5 cd15872
SNARE motif of VAMP5; The VAMP-5 (vesicle-associated membrane protein 5) protein belongs to ...
 1093-1132 5.23e-03

SNARE motif of VAMP5; The VAMP-5 (vesicle-associated membrane protein 5) protein belongs to the R-SNARE subgroup of SNAREs. Its function is unknown. SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins contain coiled-coil helices (called SNARE motifs) which mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles.


Pssm-ID: 277225 [Multi-domain]  Cd Length: 68  Bit Score: 36.62  E-value: 5.23e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2027535381 1093 DERGQKLGDLEERTAAMLSSAESFSKHAHEIMLKYKDKKW 1132
Cdd:cd15872     26 LEREGKLSDLEDRADELLNMSKAFEKTTQTVAQKKRWENI 65
 
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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