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Conserved domains on  [gi|189217897|ref|NP_640337|]
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syntaxin-binding protein 5 isoform a [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 7.89e-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: 165.44  E-value: 7.89e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189217897   275 TITPHGkqlkdgkkPEPCKPILKVEFKTTRSGEPFIILSGGLSYDTVGRRPCLTVMHGKSTAVLEMDYSIVDFLTLCETP 354
Cdd:pfam08366    1 PTTPYG--------PFPCKAITKILWKTTKTGEPFIIFSGGMPRASYGDRHCITVMHGKKHTVFDFTSKVIDFFTLCESP 72

                           90       100       110
                   ....*....|....*....|....*....|.
gi 189217897   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 ...
 1048-1108 5.33e-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: 5.33e-37
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 189217897 1048 PGGIEGVKGAASGVVGELARARLALDERGQKLGDLEERTAAMLSSAESFSKHAHEIMLKYK 1108
Cdd:cd15893     1 PGGIEGVKGAASGVVGELARARLALDERGQKLGELEERTAAMLASADSFSKHAHEMMLKYK 61
WD40 COG2319
WD40 repeat [General function prediction only];
48-280 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 189217897   48 LCKTVRHGFPYQPSALAFDPVQKILAVGTQTGALRLFGRPGVECYCQ-HDSGAAVIQLQFLINEGALVSALADDTLHLWN 126
Cdd:COG2319   111 LLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTlTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWD 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189217897  127 LRQKRPaiLHSLKFCRERVTFCHLPFQSKWLYVGTERGNIHIVNVES----FTLSGyvimwnkaielssksHPGPV--VH 200
Cdd:COG2319   191 LATGKL--LRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATgkllRTLTG---------------HSGSVrsVA 253

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189217897  201 ISDNpmdeGKLLI-GFESGTVVLWDLKSKKADYRYT-YDEAIHSVAWHHEGKQFICSHSDGTLTIWNVRSPaKPVQTITP 278
Cdd:COG2319   254 FSPD----GRLLAsGSADGTVRLWDLATGELLRTLTgHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATG-KLLRTLTG 328


                  ..
gi 189217897  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 7.89e-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: 165.44  E-value: 7.89e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189217897   275 TITPHGkqlkdgkkPEPCKPILKVEFKTTRSGEPFIILSGGLSYDTVGRRPCLTVMHGKSTAVLEMDYSIVDFLTLCETP 354
Cdd:pfam08366    1 PTTPYG--------PFPCKAITKILWKTTKTGEPFIIFSGGMPRASYGDRHCITVMHGKKHTVFDFTSKVIDFFTLCESP 72

                           90       100       110
                   ....*....|....*....|....*....|.
gi 189217897   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 ...
 1048-1108 5.33e-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: 5.33e-37
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 189217897 1048 PGGIEGVKGAASGVVGELARARLALDERGQKLGDLEERTAAMLSSAESFSKHAHEIMLKYK 1108
Cdd:cd15893     1 PGGIEGVKGAASGVVGELARARLALDERGQKLGELEERTAAMLASADSFSKHAHEMMLKYK 61
WD40 COG2319
WD40 repeat [General function prediction only];
48-280 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 189217897   48 LCKTVRHGFPYQPSALAFDPVQKILAVGTQTGALRLFGRPGVECYCQ-HDSGAAVIQLQFLINEGALVSALADDTLHLWN 126
Cdd:COG2319   111 LLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTlTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWD 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189217897  127 LRQKRPaiLHSLKFCRERVTFCHLPFQSKWLYVGTERGNIHIVNVES----FTLSGyvimwnkaielssksHPGPV--VH 200
Cdd:COG2319   191 LATGKL--LRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATgkllRTLTG---------------HSGSVrsVA 253

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189217897  201 ISDNpmdeGKLLI-GFESGTVVLWDLKSKKADYRYT-YDEAIHSVAWHHEGKQFICSHSDGTLTIWNVRSPaKPVQTITP 278
Cdd:COG2319   254 FSPD----GRLLAsGSADGTVRLWDLATGELLRTLTgHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATG-KLLRTLTG 328


                  ..
gi 189217897  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 1.24e-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 189217897   61 SALAFDPVQKILAVGTQTGALRLFGRPGVEC---YCQHDSgaAVIQLQFLINEGALVSALADDTLHLWNLRQKRPaiLHS 137
Cdd:cd00200    55 RDVAASADGTYLASGSSDKTIRLWDLETGECvrtLTGHTS--YVSSVAFSPDGRILSSSSRDKTIKVWDVETGKC--LTT 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189217897  138 LKFCRERVTFCHLPFQSKWLYVGTERGNIHIVNVESF----TLSGyvimwnkaielssksHPGPVVHISDNPmDEGKLLI 213
Cdd:cd00200   131 LRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGkcvaTLTG---------------HTGEVNSVAFSP-DGEKLLS 194

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 189217897  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 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 189217897    237 DEAIHSVAWHHEGKQFICSHSDGTLTIWN 265
Cdd:smart00320   12 TGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
Synaptobrevin pfam00957
Synaptobrevin;
1074-1113 1.37e-03

Synaptobrevin;


Pssm-ID: 395764  Cd Length: 89  Bit Score: 39.06  E-value: 1.37e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 189217897  1074 ERGQKLGDLEERTAAMLSSAESFSKHAHEIMLKY--KDKKWY 1113
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 7.89e-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: 165.44  E-value: 7.89e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189217897   275 TITPHGkqlkdgkkPEPCKPILKVEFKTTRSGEPFIILSGGLSYDTVGRRPCLTVMHGKSTAVLEMDYSIVDFLTLCETP 354
Cdd:pfam08366    1 PTTPYG--------PFPCKAITKILWKTTKTGEPFIIFSGGMPRASYGDRHCITVMHGKKHTVFDFTSKVIDFFTLCESP 72

                           90       100       110
                   ....*....|....*....|....*....|.
gi 189217897   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 ...
 1048-1108 5.33e-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: 5.33e-37
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 189217897 1048 PGGIEGVKGAASGVVGELARARLALDERGQKLGDLEERTAAMLSSAESFSKHAHEIMLKYK 1108
Cdd:cd15893     1 PGGIEGVKGAASGVVGELARARLALDERGQKLGELEERTAAMLASADSFSKHAHEMMLKYK 61
R-SNARE_STXBP5_6 cd15873
SNARE domain of STXBP5, STXBP6 and related proteins; Syntaxin binding protein 5 (STXBP5, also ...
 1048-1108 5.76e-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: 5.76e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 189217897 1048 PGGIEGVKGAASGVVGELARARLALDERGQKLGDLEERTAAMLSSAESFSKHAHEIMLKYK 1108
Cdd:cd15873     1 GGGMKALRAKAGSAASAAARARQALNERGEKLSELEDRTAEMEDNAESFASTAKELAKKYK 61
WD40 COG2319
WD40 repeat [General function prediction only];
48-280 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 189217897   48 LCKTVRHGFPYQPSALAFDPVQKILAVGTQTGALRLFGRPGVECYCQ-HDSGAAVIQLQFLINEGALVSALADDTLHLWN 126
Cdd:COG2319   111 LLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTlTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWD 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189217897  127 LRQKRPaiLHSLKFCRERVTFCHLPFQSKWLYVGTERGNIHIVNVES----FTLSGyvimwnkaielssksHPGPV--VH 200
Cdd:COG2319   191 LATGKL--LRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATgkllRTLTG---------------HSGSVrsVA 253

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189217897  201 ISDNpmdeGKLLI-GFESGTVVLWDLKSKKADYRYT-YDEAIHSVAWHHEGKQFICSHSDGTLTIWNVRSPaKPVQTITP 278
Cdd:COG2319   254 FSPD----GRLLAsGSADGTVRLWDLATGELLRTLTgHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATG-KLLRTLTG 328


                  ..
gi 189217897  279 HG 280
Cdd:COG2319   329 HT 330
WD40 COG2319
WD40 repeat [General function prediction only];
61-268 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 189217897   61 SALAFDPVQKILAVGTQTGALRLFGRPGVEC-YCQHDSGAAVIQLQFLINEGALVSALADDTLHLWNLRQKRPaiLHSLK 139
Cdd:COG2319   208 RSVAFSPDGKLLASGSADGTVRLWDLATGKLlRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGEL--LRTLT 285

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189217897  140 FCRERVTFCHLPFQSKWLYVGTERGNIHIVNVES----FTLSGyvimwnkaielssksHPGPVVHISDNPmDEGKLLIGF 215
Cdd:COG2319   286 GHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATgkllRTLTG---------------HTGAVRSVAFSP-DGKTLASGS 349

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 189217897  216 ESGTVVLWDLKSKKADYRYT-YDEAIHSVAWHHEGKQFICSHSDGTLTIWNVRS 268
Cdd:COG2319   350 DDGTVRLWDLATGELLRTLTgHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
WD40 COG2319
WD40 repeat [General function prediction only];
47-280 3.38e-16

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 82.27  E-value: 3.38e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189217897   47 QLCKTVRHGFPYQPSALAFDPVQKILAVGTQTGALRLFGRPGVECYCQ-HDSGAAVIQLQFLINEGALVSALADDTLHLW 125
Cdd:COG2319    68 GALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTlTGHTGAVRSVAFSPDGKTLASGSADGTVRLW 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189217897  126 NLRQKRPaiLHSLKFCRERVTfcHLPF--QSKWLYVGTERGNIHIVNVES----FTLSGyvimwnkaielssksHPGPVV 199
Cdd:COG2319   148 DLATGKL--LRTLTGHSGAVT--SVAFspDGKLLASGSDDGTVRLWDLATgkllRTLTG---------------HTGAVR 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189217897  200 HISDNPmdEGKLLI-GFESGTVVLWDLKSKKADYRYT-YDEAIHSVAWHHEGKQFICSHSDGTLTIWNVRSPaKPVQTIT 277
Cdd:COG2319   209 SVAFSP--DGKLLAsGSADGTVRLWDLATGKLLRTLTgHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATG-ELLRTLT 285


                  ...
gi 189217897  278 PHG 280
Cdd:COG2319   286 GHS 288
WD40 COG2319
WD40 repeat [General function prediction only];
51-280 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 189217897   51 TVRHGFPYQPSALAFDPVQKILAVGTQTGALRLFGRPGVECYCQHDSGAAVIQLQFLINEGALVSALADDTLHLWNLRQK 130
Cdd:COG2319    31 LLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATG 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189217897  131 RPaiLHSLKFCRERVTFCHLPFQSKWLYVGTERGNIHIVNVES----FTLSGyvimwnkaielssksHPGPV--VHISDN 204
Cdd:COG2319   111 LL--LRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATgkllRTLTG---------------HSGAVtsVAFSPD 173

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 189217897  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 1.24e-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 189217897   61 SALAFDPVQKILAVGTQTGALRLFGRPGVEC---YCQHDSgaAVIQLQFLINEGALVSALADDTLHLWNLRQKRPaiLHS 137
Cdd:cd00200    55 RDVAASADGTYLASGSSDKTIRLWDLETGECvrtLTGHTS--YVSSVAFSPDGRILSSSSRDKTIKVWDVETGKC--LTT 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189217897  138 LKFCRERVTFCHLPFQSKWLYVGTERGNIHIVNVESF----TLSGyvimwnkaielssksHPGPVVHISDNPmDEGKLLI 213
Cdd:cd00200   131 LRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGkcvaTLTG---------------HTGEVNSVAFSP-DGEKLLS 194

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 189217897  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 2.77e-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: 2.77e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189217897   61 SALAFDPVQKILAVGTQTGALRLFGRPGVEC---YCQHDSGaaVIQLQFLINEGALVSALADDTLHLWNLRQKRPaiLHS 137
Cdd:cd00200    13 TCVAFSPDGKLLATGSGDGTIKVWDLETGELlrtLKGHTGP--VRDVAASADGTYLASGSSDKTIRLWDLETGEC--VRT 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189217897  138 LKFCRERVTFCHLPFQSKWLYVGTERGNIHIVNVESFTLSgYVImwnkaielssKSHPGPVVHISDNPmdEGKLLIGFES 217
Cdd:cd00200    89 LTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCL-TTL----------RGHTDWVNSVAFSP--DGTFVASSSQ 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 189217897  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 5.69e-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: 5.69e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189217897   61 SALAFDPVQKILAVGTQTGALRLF-GRPGVECYCQHDSGAAVIQLQFLINEGALVSALADDTLHLWNLRQKRPaiLHSLK 139
Cdd:cd00200    97 SSVAFSPDGRILSSSSRDKTIKVWdVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKC--VATLT 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189217897  140 FCRERVTFCHLPFQSKWLYVGTERGNIHIVNVESFTLSGYVImwnkaielsskSHPGPVVHISDNPmdEGKLLI-GFESG 218
Cdd:cd00200   175 GHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLR-----------GHENGVNSVAFSP--DGYLLAsGSEDG 241

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 189217897  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 3.23e-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: 3.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189217897   95 HDSGaaVIQLQFLINEGALVSALADDTLHLWNLRQKRPAI---LHSLKfcrerVTFCHLPFQSKWLYVGTERGNIHIVNV 171
Cdd:cd00200     8 HTGG--VTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRtlkGHTGP-----VRDVAASADGTYLASGSSDKTIRLWDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189217897  172 ESFTLSGYVimwnkaielssKSHPGPV--VHISDNpmdeGKLLIG-FESGTVVLWDLKSKKADYRYTY-DEAIHSVAWHH 247
Cdd:cd00200    81 ETGECVRTL-----------TGHTSYVssVAFSPD----GRILSSsSRDKTIKVWDVETGKCLTTLRGhTDWVNSVAFSP 145

                         170       180       190
                  ....*....|....*....|....*....|..
gi 189217897  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 ...
 1049-1108 4.13e-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: 4.13e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 189217897 1049 GGIEGVKGAASGVVGELARARLALDERGQKLGDLEERTAAMLSSAESFSKHAHEIMLKYK 1108
Cdd:cd15892     2 GGNSILHSAADSVTSAVQKASQALNERGERLGRAEEKTEDMKNSAQQFAETAHKLAMKHK 61
R-SNARE cd15843
SNARE motif, subgroup R-SNARE; SNARE (soluble N-ethylmaleimide-sensitive factor attachment ...
 1074-1108 5.60e-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: 5.60e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 189217897 1074 ERGQKLGDLEERTAAMLSSAESFSKHAHEIMLKYK 1108
Cdd:cd15843    26 ERGEKLEDLVDKTENLNESANAFKKQARKLKRKMW 60
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 237-265 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 189217897    237 DEAIHSVAWHHEGKQFICSHSDGTLTIWN 265
Cdd:smart00320   12 TGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
Synaptobrevin pfam00957
Synaptobrevin;
1074-1113 1.37e-03

Synaptobrevin;


Pssm-ID: 395764  Cd Length: 89  Bit Score: 39.06  E-value: 1.37e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 189217897  1074 ERGQKLGDLEERTAAMLSSAESFSKHAHEIMLKY--KDKKWY 1113
Cdd:pfam00957   28 ERGEKLDLLVDKTENLQSSAQQFRRQARKLKRKMwwKNMKLY 69
R-SNARE_VAMP5 cd15872
SNARE motif of VAMP5; The VAMP-5 (vesicle-associated membrane protein 5) protein belongs to ...
 1073-1112 5.14e-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: 5.14e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 189217897 1073 DERGQKLGDLEERTAAMLSSAESFSKHAHEIMLKYKDKKW 1112
Cdd:cd15872    26 LEREGKLSDLEDRADELLNMSKAFEKTTQTVAQKKRWENI 65
WD40 COG2319
WD40 repeat [General function prediction only];
55-128 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 189217897   55 GFPYQPSALAFDPVQKILAVGTQTGALRLFGRPGVECYC---QHDsgAAVIQLQFLINEGALVSALADDTLHLWNLR 128
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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