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Conserved domains on  [gi|386764312|ref|NP_727628|]
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tomosyn, isoform I [Drosophila melanogaster]

Protein Classification

LLGL and R-SNARE_STXBP5_6 domain-containing protein( domain architecture ID 11456849)

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 ...
268-376 2.43e-42

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: 150.03  E-value: 2.43e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764312   268 QVCPHAkinkdgnAEKCKPIYKVDLKSSATGETFTIFSGGMPSEKGSKSNCITVMVGKATTVLEMEHAVCDFITLCENPW 347
Cdd:pfam08366    1 PTTPYG-------PFPCKAITKILWKTTKTGEPFIIFSGGMPRASYGDRHCITVMHGKKHTVFDFTSKVIDFFTLCESPD 73
                           90       100       110
                   ....*....|....*....|....*....|
gi 386764312   348 PC-ETQEPYAIAVLLQYDLVLIDLLTPGFP 376
Cdd:pfam08366   74 PNaEFDDPYALVVLLEEELVVIDLTTPGWP 103
R-SNARE_STXBP5_6 cd15873
SNARE domain of STXBP5, STXBP6 and related proteins; Syntaxin binding protein 5 (STXBP5, also ...
1403-1463 1.13e-22

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: 92.32  E-value: 1.13e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386764312 1403 GPNLEQLGQRASTAASEISRAHQLAMERGEKLNLLEERAERMANTAQDFSGTAHQLMLKYK 1463
Cdd:cd15873     1 GGGMKALRAKAGSAASAAARARQALNERGEKLSELEDRTAEMEDNAESFASTAKELAKKYK 61
WD40 COG2319
WD40 repeat [General function prediction only];
41-257 5.59e-12

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 69.55  E-value: 5.59e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764312   41 KTFRhGFPYSPTSFAFDPVQKLLAIGDKSGYIRILGRPGVDAHAKHEGESEcAVLFAQFLVNEGALVTVTADDTIHLWSI 120
Cdd:COG2319   198 RTLT-GHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSG-SVRSVAFSPDGRLLASGSADGTVRLWDL 275
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764312  121 RqkTPRIVQSLKFQRERVTCIHL-PVGsKWLYVGTEKGNIHVVHIDTFALSGyiinwnkaievVRTSHPGAVIALCDNPl 199
Cdd:COG2319   276 A--TGELLRTLTGHSGGVNSVAFsPDG-KLLASGSDDGTVRLWDLATGKLLR-----------TLTGHTGAVRSVAFSP- 340
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 386764312  200 DANKLLIAFECGLLVLWDLKAKCAELRWQA-AEAVKSLAWHYEGKYFVSSHTDGSICSW 257
Cdd:COG2319   341 DGKTLASGSDDGTVRLWDLATGELLRTLTGhTGAVTSVAFSPDGRTLASGSADGTVRLW 399
 
Name Accession Description Interval E-value
LLGL pfam08366
LLGL2; This domain is found in lethal giant larvae homolog 2 (LLGL2) proteins and ...
268-376 2.43e-42

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: 150.03  E-value: 2.43e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764312   268 QVCPHAkinkdgnAEKCKPIYKVDLKSSATGETFTIFSGGMPSEKGSKSNCITVMVGKATTVLEMEHAVCDFITLCENPW 347
Cdd:pfam08366    1 PTTPYG-------PFPCKAITKILWKTTKTGEPFIIFSGGMPRASYGDRHCITVMHGKKHTVFDFTSKVIDFFTLCESPD 73
                           90       100       110
                   ....*....|....*....|....*....|
gi 386764312   348 PC-ETQEPYAIAVLLQYDLVLIDLLTPGFP 376
Cdd:pfam08366   74 PNaEFDDPYALVVLLEEELVVIDLTTPGWP 103
R-SNARE_STXBP5_6 cd15873
SNARE domain of STXBP5, STXBP6 and related proteins; Syntaxin binding protein 5 (STXBP5, also ...
1403-1463 1.13e-22

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: 92.32  E-value: 1.13e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386764312 1403 GPNLEQLGQRASTAASEISRAHQLAMERGEKLNLLEERAERMANTAQDFSGTAHQLMLKYK 1463
Cdd:cd15873     1 GGGMKALRAKAGSAASAAARARQALNERGEKLSELEDRTAEMEDNAESFASTAKELAKKYK 61
WD40 COG2319
WD40 repeat [General function prediction only];
41-257 5.59e-12

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 69.55  E-value: 5.59e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764312   41 KTFRhGFPYSPTSFAFDPVQKLLAIGDKSGYIRILGRPGVDAHAKHEGESEcAVLFAQFLVNEGALVTVTADDTIHLWSI 120
Cdd:COG2319   198 RTLT-GHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSG-SVRSVAFSPDGRLLASGSADGTVRLWDL 275
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764312  121 RqkTPRIVQSLKFQRERVTCIHL-PVGsKWLYVGTEKGNIHVVHIDTFALSGyiinwnkaievVRTSHPGAVIALCDNPl 199
Cdd:COG2319   276 A--TGELLRTLTGHSGGVNSVAFsPDG-KLLASGSDDGTVRLWDLATGKLLR-----------TLTGHTGAVRSVAFSP- 340
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 386764312  200 DANKLLIAFECGLLVLWDLKAKCAELRWQA-AEAVKSLAWHYEGKYFVSSHTDGSICSW 257
Cdd:COG2319   341 DGKTLASGSDDGTVRLWDLATGELLRTLTGhTGAVTSVAFSPDGRTLASGSADGTVRLW 399
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
52-257 1.41e-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: 57.73  E-value: 1.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764312   52 TSFAFDPVQKLLAIGDKSGYIRILGRPGVDAHAKHEGESECaVLFAQFLVNEGALVTVTADDTIHLWSIrqKTPRIVQSL 131
Cdd:cd00200    13 TCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGP-VRDVAASADGTYLASGSSDKTIRLWDL--ETGECVRTL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764312  132 KFQRERVTCIHLPVGSKWLYVGTEKGNI----------------H---VVHI-----DTFALSG----YIINWN-KAIEV 182
Cdd:cd00200    90 TGHTSYVSSVAFSPDGRILSSSSRDKTIkvwdvetgkclttlrgHtdwVNSVafspdGTFVASSsqdgTIKLWDlRTGKC 169
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386764312  183 VRT--SHPGAVIALCDNPlDANKLLIAFECGLLVLWDLKA-KCAELRWQAAEAVKSLAWHYEGKYFVSSHTDGSICSW 257
Cdd:cd00200   170 VATltGHTGEVNSVAFSP-DGEKLLSSSSDGTIKLWDLSTgKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVW 246
Synaptobrevin pfam00957
Synaptobrevin;
1425-1468 1.42e-05

Synaptobrevin;


Pssm-ID: 395764  Cd Length: 89  Bit Score: 44.84  E-value: 1.42e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 386764312  1425 QLAMERGEKLNLLEERAERMANTAQDFSGTAHQLMLKY--KDKKWY 1468
Cdd:pfam00957   24 DKVLERGEKLDLLVDKTENLQSSAQQFRRQARKLKRKMwwKNMKLY 69
 
Name Accession Description Interval E-value
LLGL pfam08366
LLGL2; This domain is found in lethal giant larvae homolog 2 (LLGL2) proteins and ...
268-376 2.43e-42

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: 150.03  E-value: 2.43e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764312   268 QVCPHAkinkdgnAEKCKPIYKVDLKSSATGETFTIFSGGMPSEKGSKSNCITVMVGKATTVLEMEHAVCDFITLCENPW 347
Cdd:pfam08366    1 PTTPYG-------PFPCKAITKILWKTTKTGEPFIIFSGGMPRASYGDRHCITVMHGKKHTVFDFTSKVIDFFTLCESPD 73
                           90       100       110
                   ....*....|....*....|....*....|
gi 386764312   348 PC-ETQEPYAIAVLLQYDLVLIDLLTPGFP 376
Cdd:pfam08366   74 PNaEFDDPYALVVLLEEELVVIDLTTPGWP 103
R-SNARE_STXBP5_6 cd15873
SNARE domain of STXBP5, STXBP6 and related proteins; Syntaxin binding protein 5 (STXBP5, also ...
1403-1463 1.13e-22

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: 92.32  E-value: 1.13e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386764312 1403 GPNLEQLGQRASTAASEISRAHQLAMERGEKLNLLEERAERMANTAQDFSGTAHQLMLKYK 1463
Cdd:cd15873     1 GGGMKALRAKAGSAASAAARARQALNERGEKLSELEDRTAEMEDNAESFASTAKELAKKYK 61
WD40 COG2319
WD40 repeat [General function prediction only];
41-257 5.59e-12

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 69.55  E-value: 5.59e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764312   41 KTFRhGFPYSPTSFAFDPVQKLLAIGDKSGYIRILGRPGVDAHAKHEGESEcAVLFAQFLVNEGALVTVTADDTIHLWSI 120
Cdd:COG2319   198 RTLT-GHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSG-SVRSVAFSPDGRLLASGSADGTVRLWDL 275
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764312  121 RqkTPRIVQSLKFQRERVTCIHL-PVGsKWLYVGTEKGNIHVVHIDTFALSGyiinwnkaievVRTSHPGAVIALCDNPl 199
Cdd:COG2319   276 A--TGELLRTLTGHSGGVNSVAFsPDG-KLLASGSDDGTVRLWDLATGKLLR-----------TLTGHTGAVRSVAFSP- 340
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 386764312  200 DANKLLIAFECGLLVLWDLKAKCAELRWQA-AEAVKSLAWHYEGKYFVSSHTDGSICSW 257
Cdd:COG2319   341 DGKTLASGSDDGTVRLWDLATGELLRTLTGhTGAVTSVAFSPDGRTLASGSADGTVRLW 399
R-SNARE_STXBP5 cd15893
SNARE domain of STXBP5; Syntaxin binding protein 5 (STXBP5, also called Tomosyn), as well as ...
1402-1463 7.11e-09

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: 53.50  E-value: 7.11e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386764312 1402 PGpNLEQLGQRASTAASEISRAHQLAMERGEKLNLLEERAERMANTAQDFSGTAHQLMLKYK 1463
Cdd:cd15893     1 PG-GIEGVKGAASGVVGELARARLALDERGQKLGELEERTAAMLASADSFSKHAHEMMLKYK 61
R-SNARE_STXBP6 cd15892
SNARE domain of STXBP6; Syntaxin binding protein 6 (STXBP6, also called Amisyn), as well as ...
1413-1463 8.29e-09

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


Pssm-ID: 277245  Cd Length: 62  Bit Score: 53.23  E-value: 8.29e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 386764312 1413 ASTAASEISRAHQLAMERGEKLNLLEERAERMANTAQDFSGTAHQLMLKYK 1463
Cdd:cd15892    11 ADSVTSAVQKASQALNERGERLGRAEEKTEDMKNSAQQFAETAHKLAMKHK 61
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
52-257 1.41e-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: 57.73  E-value: 1.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764312   52 TSFAFDPVQKLLAIGDKSGYIRILGRPGVDAHAKHEGESECaVLFAQFLVNEGALVTVTADDTIHLWSIrqKTPRIVQSL 131
Cdd:cd00200    13 TCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGP-VRDVAASADGTYLASGSSDKTIRLWDL--ETGECVRTL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764312  132 KFQRERVTCIHLPVGSKWLYVGTEKGNI----------------H---VVHI-----DTFALSG----YIINWN-KAIEV 182
Cdd:cd00200    90 TGHTSYVSSVAFSPDGRILSSSSRDKTIkvwdvetgkclttlrgHtdwVNSVafspdGTFVASSsqdgTIKLWDlRTGKC 169
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386764312  183 VRT--SHPGAVIALCDNPlDANKLLIAFECGLLVLWDLKA-KCAELRWQAAEAVKSLAWHYEGKYFVSSHTDGSICSW 257
Cdd:cd00200   170 VATltGHTGEVNSVAFSP-DGEKLLSSSSDGTIKLWDLSTgKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVW 246
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
91-254 2.88e-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: 56.96  E-value: 2.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764312   91 ECAVLFAQFLVNEGALVTVTADDTIHLWSIRqkTPRIVQSLKFQRERVTCIHL-PVGSKwLYVGTEKGNIHVVHIDTFAL 169
Cdd:cd00200   135 TDWVNSVAFSPDGTFVASSSQDGTIKLWDLR--TGKCVATLTGHTGEVNSVAFsPDGEK-LLSSSSDGTIKLWDLSTGKC 211
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764312  170 SGYIinwnkaievvrTSHPGAVIALCDNPldaNKLLI--AFECGLLVLWDLKAK--CAELRwQAAEAVKSLAWHYEGKYF 245
Cdd:cd00200   212 LGTL-----------RGHENGVNSVAFSP---DGYLLasGSEDGTIRVWDLRTGecVQTLS-GHTNSVTSLAWSPDGKRL 276

                  ....*....
gi 386764312  246 VSSHTDGSI 254
Cdd:cd00200   277 ASGSADGTI 285
WD40 COG2319
WD40 repeat [General function prediction only];
45-257 1.38e-07

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 55.69  E-value: 1.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764312   45 HGFPYSPTSFAFDPVQKLLAIGDKSGYIRILGRPGVDAHAKHEGESEcAVLFAQFLVNEGALVTVTADDTIHLWSIRqkT 124
Cdd:COG2319   117 TGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSG-AVTSVAFSPDGKLLASGSDDGTVRLWDLA--T 193
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764312  125 PRIVQSLKFQRERVTCIHLPVGSKWLYVGTEKGNIHVVHIDTfalsgyiinwnKAIEVVRTSHPGAVIALCDNPlDANKL 204
Cdd:COG2319   194 GKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLAT-----------GKLLRTLTGHSGSVRSVAFSP-DGRLL 261
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 386764312  205 LIAFECGLLVLWDLKAKcAELRWQAAE--AVKSLAWHYEGKYFVSSHTDGSICSW 257
Cdd:COG2319   262 ASGSADGTVRLWDLATG-ELLRTLTGHsgGVNSVAFSPDGKLLASGSDDGTVRLW 315
Synaptobrevin pfam00957
Synaptobrevin;
1425-1468 1.42e-05

Synaptobrevin;


Pssm-ID: 395764  Cd Length: 89  Bit Score: 44.84  E-value: 1.42e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 386764312  1425 QLAMERGEKLNLLEERAERMANTAQDFSGTAHQLMLKY--KDKKWY 1468
Cdd:pfam00957   24 DKVLERGEKLDLLVDKTENLQSSAQQFRRQARKLKRKMwwKNMKLY 69
R-SNARE cd15843
SNARE motif, subgroup R-SNARE; SNARE (soluble N-ethylmaleimide-sensitive factor attachment ...
1428-1463 1.51e-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: 44.03  E-value: 1.51e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 386764312 1428 MERGEKLNLLEERAERMANTAQDFSGTAHQLMLKYK 1463
Cdd:cd15843    25 LERGEKLEDLVDKTENLNESANAFKKQARKLKRKMW 60
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
128-257 3.28e-04

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: 44.25  E-value: 3.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764312  128 VQSLKFQRERVTCIHLPVGSKWLYVGTEKGNIHVVHIDTFALsgyiinwnkaiEVVRTSHPGAV--IALCDnplDANKLL 205
Cdd:cd00200     2 RRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGEL-----------LRTLKGHTGPVrdVAASA---DGTYLA 67
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 386764312  206 IAFECGLLVLWDLK--AKCAELRwQAAEAVKSLAWHYEGKYFVSSHTDGSICSW 257
Cdd:cd00200    68 SGSSDKTIRLWDLEtgECVRTLT-GHTSYVSSVAFSPDGRILSSSSRDKTIKVW 120
R-SNARE_VAMP2 cd15870
SNARE motif of VAMP2; The VAMP-2 (vesicle-associated membrane protein 2, also called ...
1427-1469 2.63e-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: 37.75  E-value: 2.63e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 386764312 1427 AMERGEKLNLLEERAERMANTAQDFSGTAHQLMLKYkdkkWYQ 1469
Cdd:cd15870    24 VLERDQKLSELDDRADALQAGASQFETSAGKLKRKY----WWK 62
WD40 COG2319
WD40 repeat [General function prediction only];
55-257 2.71e-03

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 41.82  E-value: 2.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764312   55 AFDPVQKLLAIGDKSGYIRILGRPGVDAHAKHEGESECAVLFAQFLVNEGALVTVTADDTIHLWSIrqkTPRIVQSLKFQ 134
Cdd:COG2319     1 ALSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAA---AGALLATLLGH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386764312  135 RERVTCIHLPVGSKWLYVGTEKGNIHVVHIDTfalsgyiinwnKAIEVVRTSHPGAVIALCDNPlDANKLLIAFECGLLV 214
Cdd:COG2319    78 TAAVLSVAFSPDGRLLASASADGTVRLWDLAT-----------GLLLRTLTGHTGAVRSVAFSP-DGKTLASGSADGTVR 145
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 386764312  215 LWDLK-AKC-AELRWQAaEAVKSLAWHYEGKYFVSSHTDGSICSW 257
Cdd:COG2319   146 LWDLAtGKLlRTLTGHS-GAVTSVAFSPDGKLLASGSDDGTVRLW 189
R-SNARE_VAMP4 cd15869
SNARE motif of VAMP4; The VAMP-4 (vesicle-associated membrane protein 4) protein belongs to ...
1428-1469 4.59e-03

SNARE motif of VAMP4; The VAMP-4 (vesicle-associated membrane protein 4) protein belongs to the R-SNARE subgroup of SNAREs and interacts with syntaxin 16 (Qa), Vti1a (Qb) and syntaxin 6 (Qc). This complex plays a role in maintenance of Golgi ribbon structure and normal retrograde trafficking from the early endosome to the trans-Golgi network (TGN). 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: 277222 [Multi-domain]  Cd Length: 67  Bit Score: 36.98  E-value: 4.59e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 386764312 1428 MERGEKLNLLEERAERMANTAQDFSGTAHQLmlkyKDKKWYQ 1469
Cdd:cd15869    26 IDRGEKLEDLQDKSESLSDNASAFRSRSKQL----RRKMWWQ 63
R-SNARE_Snc1 cd15874
SNARE motif of Snc1; Saccharomyces cerevisiae SNARE protein Snc1p forms a complex with ...
1428-1457 5.02e-03

SNARE motif of Snc1; Saccharomyces cerevisiae SNARE protein Snc1p forms a complex with synaptobrevin homolog Sso1p (Qa) and the SNAP-25 homolog Sec9p (Qb/c) which is involved in exocytosis. Snc1 is a member of the R-SNARE subgroup of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins, which consist of coiled-coil helices (called SNARE motifs) that mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complexes mediate 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.


Pssm-ID: 277227 [Multi-domain]  Cd Length: 60  Bit Score: 36.96  E-value: 5.02e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 386764312 1428 MERGEKLNLLEERAERMANTAQDFSGTAHQ 1457
Cdd:cd15874    25 AQRGERLDSLQDKTDNLAVSAQGFRRGANR 54
R-SNARE_VAMP5 cd15872
SNARE motif of VAMP5; The VAMP-5 (vesicle-associated membrane protein 5) protein belongs to ...
1405-1467 5.59e-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: 37.00  E-value: 5.59e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386764312 1405 NLEQLgQRASTAASEISRAH-QLAMERGEKLNLLEERAERMANTAQDFSGTAHQLMLKYKDKKW 1467
Cdd:cd15872     3 RLERC-QREAEEVKVIMLDNlNKALEREGKLSDLEDRADELLNMSKAFEKTTQTVAQKKRWENI 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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