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Conserved domains on  [gi|951533812|ref|XP_014470598|]
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PREDICTED: syntaxin-binding protein 5 isoform X4 [Dinoponera quadriceps]

Protein Classification

LLGL and R-SNARE_STXBP5_6 domain-containing protein( domain architecture ID 13236890)

protein containing domains WD40, LLGL, and R-SNARE_STXBP5_6

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 ...
 264-372 4.90e-46

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: 160.43  E-value: 4.90e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951533812   264 VTFPHAkstkdgePESCKPIQKVEWKLSRAGEAYIIFSGGLACDTTGRIPSITVIHGKTTTVLEMEHNVIDFVTLCDSPW 343
Cdd:pfam08366    1 PTTPYG-------PFPCKAITKILWKTTKTGEPFIIFSGGMPRASYGDRHCITVMHGKKHTVFDFTSKVIDFFTLCESPD 73

                           90       100       110
                   ....*....|....*....|....*....|
gi 951533812   344 AS-DFQDPYAVVVLLQNDLVVIDLLTPGFP 372
Cdd:pfam08366   74 PNaEFDDPYALVVLLEEELVVIDLTTPGWP 103
R-SNARE_STXBP5_6 cd15873
SNARE domain of STXBP5, STXBP6 and related proteins; Syntaxin binding protein 5 (STXBP5, also ...
 1150-1210 1.15e-24

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: 98.10  E-value: 1.15e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 951533812 1150 PGPNEALRERVSSATGEVNMAHQMVVERGEKLSHLEERTARMMSEAENFSQTAHGLMLKYK 1210
Cdd:cd15873     1 GGGMKALRAKAGSAASAAARARQALNERGEKLSELEDRTAEMEDNAESFASTAKELAKKYK 61
WD40 super family cl29593
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 37-254 1.58e-08

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


The actual alignment was detected with superfamily member cd00200:

Pssm-ID: 475233 [Multi-domain]  Cd Length: 289  Bit Score: 57.34  E-value: 1.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951533812   37 QVKRTFrHGFPHQPTALAFDPVQRLLAIGTKSGSLRILgrpgvdaHVKHEGCSAVIQ--------LQFLINEGALVSATA 108
Cdd:cd00200    84 ECVRTL-TGHTSYVSSVAFSPDGRILSSSSRDKTIKVW-------DVETGKCLTTLRghtdwvnsVAFSPDGTFVASSSQ 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951533812  109 DDTLHLWNFRQkiPQVVQSLKFQRDRITCIHLPLQSKWLYVGTERGNIHIlhietfvlsgyvinWNKAIEVSRKT---HP 185
Cdd:cd00200   156 DGTIKLWDLRT--GKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKL--------------WDLSTGKCLGTlrgHE 219

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 951533812  186 GAVVHLSDNPldlSKMLI--GYETGQIVFWDLKTKNADYRCQ-TDEPLKSITWHHEGKQFMCCHTDGSLSTW 254
Cdd:cd00200   220 NGVNSVAFSP---DGYLLasGSEDGTIRVWDLRTGECVQTLSgHTNSVTSLAWSPDGKRLASGSADGTIRIW 288
 
Name Accession Description Interval E-value
LLGL pfam08366
LLGL2; This domain is found in lethal giant larvae homolog 2 (LLGL2) proteins and ...
 264-372 4.90e-46

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: 160.43  E-value: 4.90e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951533812   264 VTFPHAkstkdgePESCKPIQKVEWKLSRAGEAYIIFSGGLACDTTGRIPSITVIHGKTTTVLEMEHNVIDFVTLCDSPW 343
Cdd:pfam08366    1 PTTPYG-------PFPCKAITKILWKTTKTGEPFIIFSGGMPRASYGDRHCITVMHGKKHTVFDFTSKVIDFFTLCESPD 73

                           90       100       110
                   ....*....|....*....|....*....|
gi 951533812   344 AS-DFQDPYAVVVLLQNDLVVIDLLTPGFP 372
Cdd:pfam08366   74 PNaEFDDPYALVVLLEEELVVIDLTTPGWP 103
R-SNARE_STXBP5_6 cd15873
SNARE domain of STXBP5, STXBP6 and related proteins; Syntaxin binding protein 5 (STXBP5, also ...
 1150-1210 1.15e-24

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: 98.10  E-value: 1.15e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 951533812 1150 PGPNEALRERVSSATGEVNMAHQMVVERGEKLSHLEERTARMMSEAENFSQTAHGLMLKYK 1210
Cdd:cd15873     1 GGGMKALRAKAGSAASAAARARQALNERGEKLSELEDRTAEMEDNAESFASTAKELAKKYK 61
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 37-254 1.58e-08

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 57.34  E-value: 1.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951533812   37 QVKRTFrHGFPHQPTALAFDPVQRLLAIGTKSGSLRILgrpgvdaHVKHEGCSAVIQ--------LQFLINEGALVSATA 108
Cdd:cd00200    84 ECVRTL-TGHTSYVSSVAFSPDGRILSSSSRDKTIKVW-------DVETGKCLTTLRghtdwvnsVAFSPDGTFVASSSQ 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951533812  109 DDTLHLWNFRQkiPQVVQSLKFQRDRITCIHLPLQSKWLYVGTERGNIHIlhietfvlsgyvinWNKAIEVSRKT---HP 185
Cdd:cd00200   156 DGTIKLWDLRT--GKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKL--------------WDLSTGKCLGTlrgHE 219

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 951533812  186 GAVVHLSDNPldlSKMLI--GYETGQIVFWDLKTKNADYRCQ-TDEPLKSITWHHEGKQFMCCHTDGSLSTW 254
Cdd:cd00200   220 NGVNSVAFSP---DGYLLasGSEDGTIRVWDLRTGECVQTLSgHTNSVTSLAWSPDGKRLASGSADGTIRIW 288
WD40 COG2319
WD40 repeat [General function prediction only];
43-257 5.82e-07

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 53.38  E-value: 5.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951533812   43 RHGFPHQPTALAFDPVQRLLAIGTKSGSLRIL---GRPGVDAHVKHEGcsAVIQLQFLINEGALVSATADDTLHLWNFRQ 119
Cdd:COG2319    74 LLGHTAAVLSVAFSPDGRLLASASADGTVRLWdlaTGLLLRTLTGHTG--AVRSVAFSPDGKTLASGSADGTVRLWDLAT 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951533812  120 kiPQVVQSLKFQRDRITCIHLPLQSKWLYVGTERGNIHILHIET----FVLSGyvinwnkaievsrktHPGAVVHLSDNP 195
Cdd:COG2319   152 --GKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATgkllRTLTG---------------HTGAVRSVAFSP 214

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 951533812  196 lDlSKMLI-GYETGQIVFWDLKTKnadyRCQT-----DEPLKSITWHHEGKQFMCCHTDGSLSTWTVR 257
Cdd:COG2319   215 -D-GKLLAsGSADGTVRLWDLATG----KLLRtltghSGSVRSVAFSPDGRLLASGSADGTVRLWDLA 276
Synaptobrevin pfam00957
Synaptobrevin;
1174-1215 4.12e-05

Synaptobrevin;


Pssm-ID: 395764  Cd Length: 89  Bit Score: 43.29  E-value: 4.12e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 951533812  1174 VVERGEKLSHLEERTARMMSEAENFSQTAHGLMLKY--KDKKWY 1215
Cdd:pfam00957   26 VLERGEKLDLLVDKTENLQSSAQQFRRQARKLKRKMwwKNMKLY 69
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 182-462 7.11e-03

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: 40.01  E-value: 7.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951533812  182 KTHPGAVVHLSDNPlDLSKMLIGYETGQIVFWDLKTKNADYRCQT-DEPLKSITWHHEGKQFMCCHTDGSLSTWTVRQLK 260
Cdd:cd00200     6 KGHTGGVTCVAFSP-DGKLLATGSGDGTIKVWDLETGELLRTLKGhTGPVRDVAASADGTYLASGSSDKTIRLWDLETGE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951533812  261 PTNVTFPHAKSTKdgepeSCKPIQKvewklsrageAYIIFSGGLacDTTGRIpsITVIHGKTTTVLEmEHNviDFVTLCD 340
Cdd:cd00200    85 CVRTLTGHTSYVS-----SVAFSPD----------GRILSSSSR--DKTIKV--WDVETGKCLTTLR-GHT--DWVNSVA 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951533812  341 SPWASDFqdpyaVVVLLQNDLV-VIDLLTpgFPCFENpypMDIHESPVTCCAYFAD------CPSDLVPAFYSVGSKSQK 413
Cdd:cd00200   143 FSPDGTF-----VASSSQDGTIkLWDLRT--GKCVAT---LTGHTGEVNSVAFSPDgekllsSSSDGTIKLWDLSTGKCL 212

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 951533812  414 KTGFSEKEWpVSGGEWSSSsssyNEIILTGHADGSIKFWDASAG-TLQVL 462
Cdd:cd00200   213 GTLRGHENG-VNSVAFSPD----GYLLASGSEDGTIRVWDLRTGeCVQTL 257
 
Name Accession Description Interval E-value
LLGL pfam08366
LLGL2; This domain is found in lethal giant larvae homolog 2 (LLGL2) proteins and ...
 264-372 4.90e-46

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: 160.43  E-value: 4.90e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951533812   264 VTFPHAkstkdgePESCKPIQKVEWKLSRAGEAYIIFSGGLACDTTGRIPSITVIHGKTTTVLEMEHNVIDFVTLCDSPW 343
Cdd:pfam08366    1 PTTPYG-------PFPCKAITKILWKTTKTGEPFIIFSGGMPRASYGDRHCITVMHGKKHTVFDFTSKVIDFFTLCESPD 73

                           90       100       110
                   ....*....|....*....|....*....|
gi 951533812   344 AS-DFQDPYAVVVLLQNDLVVIDLLTPGFP 372
Cdd:pfam08366   74 PNaEFDDPYALVVLLEEELVVIDLTTPGWP 103
R-SNARE_STXBP5_6 cd15873
SNARE domain of STXBP5, STXBP6 and related proteins; Syntaxin binding protein 5 (STXBP5, also ...
 1150-1210 1.15e-24

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: 98.10  E-value: 1.15e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 951533812 1150 PGPNEALRERVSSATGEVNMAHQMVVERGEKLSHLEERTARMMSEAENFSQTAHGLMLKYK 1210
Cdd:cd15873     1 GGGMKALRAKAGSAASAAARARQALNERGEKLSELEDRTAEMEDNAESFASTAKELAKKYK 61
R-SNARE_STXBP5 cd15893
SNARE domain of STXBP5; Syntaxin binding protein 5 (STXBP5, also called Tomosyn), as well as ...
 1150-1210 1.74e-13

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: 66.21  E-value: 1.74e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 951533812 1150 PGPNEALRERVSSATGEVNMAHQMVVERGEKLSHLEERTARMMSEAENFSQTAHGLMLKYK 1210
Cdd:cd15893     1 PGGIEGVKGAASGVVGELARARLALDERGQKLGELEERTAAMLASADSFSKHAHEMMLKYK 61
R-SNARE_STXBP6 cd15892
SNARE domain of STXBP6; Syntaxin binding protein 6 (STXBP6, also called Amisyn), as well as ...
 1151-1210 8.72e-11

SNARE domain of STXBP6; Syntaxin binding protein 6 (STXBP6, also called Amisyn), as well as its relative Syntaxin binding protein 5 (STXBP5, also called Tomosyn), contains a C-terminal R-SNARE-like domain, which allows it to assemble into SNARE complexes, which in turn makes the complexes inactive and inhibits exocytosis. In general, SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins consist of coiled-coil helices (called SNARE motifs) which mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qc-, as well as Qa- and Qb-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle.


Pssm-ID: 277245  Cd Length: 62  Bit Score: 58.62  E-value: 8.72e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 951533812 1151 GPNEALRERVSSATGEVNMAHQMVVERGEKLSHLEERTARMMSEAENFSQTAHGLMLKYK 1210
Cdd:cd15892     2 GGNSILHSAADSVTSAVQKASQALNERGERLGRAEEKTEDMKNSAQQFAETAHKLAMKHK 61
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 37-254 1.58e-08

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 57.34  E-value: 1.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951533812   37 QVKRTFrHGFPHQPTALAFDPVQRLLAIGTKSGSLRILgrpgvdaHVKHEGCSAVIQ--------LQFLINEGALVSATA 108
Cdd:cd00200    84 ECVRTL-TGHTSYVSSVAFSPDGRILSSSSRDKTIKVW-------DVETGKCLTTLRghtdwvnsVAFSPDGTFVASSSQ 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951533812  109 DDTLHLWNFRQkiPQVVQSLKFQRDRITCIHLPLQSKWLYVGTERGNIHIlhietfvlsgyvinWNKAIEVSRKT---HP 185
Cdd:cd00200   156 DGTIKLWDLRT--GKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKL--------------WDLSTGKCLGTlrgHE 219

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 951533812  186 GAVVHLSDNPldlSKMLI--GYETGQIVFWDLKTKNADYRCQ-TDEPLKSITWHHEGKQFMCCHTDGSLSTW 254
Cdd:cd00200   220 NGVNSVAFSP---DGYLLasGSEDGTIRVWDLRTGECVQTLSgHTNSVTSLAWSPDGKRLASGSADGTIRIW 288
WD40 COG2319
WD40 repeat [General function prediction only];
43-257 5.82e-07

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 53.38  E-value: 5.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951533812   43 RHGFPHQPTALAFDPVQRLLAIGTKSGSLRIL---GRPGVDAHVKHEGcsAVIQLQFLINEGALVSATADDTLHLWNFRQ 119
Cdd:COG2319    74 LLGHTAAVLSVAFSPDGRLLASASADGTVRLWdlaTGLLLRTLTGHTG--AVRSVAFSPDGKTLASGSADGTVRLWDLAT 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951533812  120 kiPQVVQSLKFQRDRITCIHLPLQSKWLYVGTERGNIHILHIET----FVLSGyvinwnkaievsrktHPGAVVHLSDNP 195
Cdd:COG2319   152 --GKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATgkllRTLTG---------------HTGAVRSVAFSP 214

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 951533812  196 lDlSKMLI-GYETGQIVFWDLKTKnadyRCQT-----DEPLKSITWHHEGKQFMCCHTDGSLSTWTVR 257
Cdd:COG2319   215 -D-GKLLAsGSADGTVRLWDLATG----KLLRtltghSGSVRSVAFSPDGRLLASGSADGTVRLWDLA 276
WD40 COG2319
WD40 repeat [General function prediction only];
40-268 1.21e-06

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 52.22  E-value: 1.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951533812   40 RTFRhGFPHQPTALAFDPVQRLLAIGTKSGSLRI--LGRPGVDAHVK-HEGcsAVIQLQFLINEGALVSATADDTLHLWN 116
Cdd:COG2319   156 RTLT-GHSGAVTSVAFSPDGKLLASGSDDGTVRLwdLATGKLLRTLTgHTG--AVRSVAFSPDGKLLASGSADGTVRLWD 232

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951533812  117 FRQkiPQVVQSLKFQRDRITCIHLPLQSKWLYVGTERGNIHILHIETfvlsgyvinwnKAIEVSRKTHPGAVVHLSDNPl 196
Cdd:COG2319   233 LAT--GKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLAT-----------GELLRTLTGHSGGVNSVAFSP- 298

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 951533812  197 DLSKMLIGYETGQIVFWDLKTKnadyRCQT-----DEPLKSITWHHEGKQFMCCHTDGSLSTWTVRQLKPTNVTFPH 268
Cdd:COG2319   299 DGKLLASGSDDGTVRLWDLATG----KLLRtltghTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGH 371
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 39-260 3.19e-06

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: 50.41  E-value: 3.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951533812   39 KRTFRhGFPHQPTALAFDPVQRLLAIGTKSGSLRI--LGRPGVDAHVK-HEGCsaVIQLQFLINEGALVSATADDTLHLW 115
Cdd:cd00200     2 RRTLK-GHTGGVTCVAFSPDGKLLATGSGDGTIKVwdLETGELLRTLKgHTGP--VRDVAASADGTYLASGSSDKTIRLW 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951533812  116 NFRQkiPQVVQSLKFQRDRITCIHLPLQSKWLYVGTERGNIHILHIETFVLSgYVInwnkaievsrKTHPGAVVHLSDNP 195
Cdd:cd00200    79 DLET--GECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCL-TTL----------RGHTDWVNSVAFSP 145

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 951533812  196 ldlSKMLI--GYETGQIVFWDLKTKNADYRCQT-DEPLKSITWHHEGKQFMCCHTDGSLSTWTVRQLK 260
Cdd:cd00200   146 ---DGTFVasSSQDGTIKLWDLRTGKCVATLTGhTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGK 210
R-SNARE cd15843
SNARE motif, subgroup R-SNARE; SNARE (soluble N-ethylmaleimide-sensitive factor attachment ...
 1172-1210 1.34e-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: 43.64  E-value: 1.34e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 951533812 1172 QMVVERGEKLSHLEERTARMMSEAENFSQTAHGLMLKYK 1210
Cdd:cd15843    22 DKVLERGEKLEDLVDKTENLNESANAFKKQARKLKRKMW 60
Synaptobrevin pfam00957
Synaptobrevin;
1174-1215 4.12e-05

Synaptobrevin;


Pssm-ID: 395764  Cd Length: 89  Bit Score: 43.29  E-value: 4.12e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 951533812  1174 VVERGEKLSHLEERTARMMSEAENFSQTAHGLMLKY--KDKKWY 1215
Cdd:pfam00957   26 VLERGEKLDLLVDKTENLQSSAQQFRRQARKLKRKMwwKNMKLY 69
WD40 COG2319
WD40 repeat [General function prediction only];
37-163 4.71e-05

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 47.21  E-value: 4.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951533812   37 QVKRTFRHGfPHQPTALAFDPVQRLLAIGTKSGSLRIL----GRPgVDAHVKHEGcsAVIQLQFLINEGALVSATADDTL 112
Cdd:COG2319   279 ELLRTLTGH-SGGVNSVAFSPDGKLLASGSDDGTVRLWdlatGKL-LRTLTGHTG--AVRSVAFSPDGKTLASGSDDGTV 354

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 951533812  113 HLWNFRQKipQVVQSLKFQRDRITCIHLPLQSKWLYVGTERGNIHILHIET 163
Cdd:COG2319   355 RLWDLATG--ELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
R-SNARE_VAMP5 cd15872
SNARE motif of VAMP5; The VAMP-5 (vesicle-associated membrane protein 5) protein belongs to ...
 1174-1214 2.96e-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: 37.39  E-value: 2.96e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 951533812 1174 VVERGEKLSHLEERTARMMSEAENFSQTAHGLMLKYKDKKW 1214
Cdd:cd15872    25 ALEREGKLSDLEDRADELLNMSKAFEKTTQTVAQKKRWENI 65
R-SNARE_VAMP2 cd15870
SNARE motif of VAMP2; The VAMP-2 (vesicle-associated membrane protein 2, also called ...
 1174-1216 4.38e-03

SNARE motif of VAMP2; The VAMP-2 (vesicle-associated membrane protein 2, also called synaptobrevin-2) protein belongs to the R-SNARE subgroup of SNAREs and interacts with Syntaxin-1 (Qa) and SNAP-25(Qb/Qc), as well as syntaxin 12 (Qa) and SNAP23 (Qb/Qc). The complexes play a role in transport of secretory granule from trans-Golgi network to the plasma membrane, and in the transport from early endosomes to and from the plasma membrane, respectively. 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: 277223 [Multi-domain]  Cd Length: 63  Bit Score: 36.98  E-value: 4.38e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 951533812 1174 VVERGEKLSHLEERTARMMSEAENFSQTAHGLMLKYkdkkWYQ 1216
Cdd:cd15870    24 VLERDQKLSELDDRADALQAGASQFETSAGKLKRKY----WWK 62
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 182-462 7.11e-03

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: 40.01  E-value: 7.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951533812  182 KTHPGAVVHLSDNPlDLSKMLIGYETGQIVFWDLKTKNADYRCQT-DEPLKSITWHHEGKQFMCCHTDGSLSTWTVRQLK 260
Cdd:cd00200     6 KGHTGGVTCVAFSP-DGKLLATGSGDGTIKVWDLETGELLRTLKGhTGPVRDVAASADGTYLASGSSDKTIRLWDLETGE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951533812  261 PTNVTFPHAKSTKdgepeSCKPIQKvewklsrageAYIIFSGGLacDTTGRIpsITVIHGKTTTVLEmEHNviDFVTLCD 340
Cdd:cd00200    85 CVRTLTGHTSYVS-----SVAFSPD----------GRILSSSSR--DKTIKV--WDVETGKCLTTLR-GHT--DWVNSVA 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951533812  341 SPWASDFqdpyaVVVLLQNDLV-VIDLLTpgFPCFENpypMDIHESPVTCCAYFAD------CPSDLVPAFYSVGSKSQK 413
Cdd:cd00200   143 FSPDGTF-----VASSSQDGTIkLWDLRT--GKCVAT---LTGHTGEVNSVAFSPDgekllsSSSDGTIKLWDLSTGKCL 212

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 951533812  414 KTGFSEKEWpVSGGEWSSSsssyNEIILTGHADGSIKFWDASAG-TLQVL 462
Cdd:cd00200   213 GTLRGHENG-VNSVAFSPD----GYLLASGSEDGTIRVWDLRTGeCVQTL 257
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 125-274 8.63e-03

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: 39.63  E-value: 8.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951533812  125 VQSLKFQRDRITCIHLPLQSKWLYVGTERGNIHILHIETFVLsgyvinwnkaiEVSRKTHPGAVVHLSDNPlDLSKMLIG 204
Cdd:cd00200     2 RRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGEL-----------LRTLKGHTGPVRDVAASA-DGTYLASG 69

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 951533812  205 YETGQIVFWDLKTKN--ADYRCQTDEpLKSITWHHEGKQFMCCHTDGSLSTWTVRQLKPTNVTFPHAKSTKD 274
Cdd:cd00200    70 SSDKTIRLWDLETGEcvRTLTGHTSY-VSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNS 140
 
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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