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Conserved domains on  [gi|1860458958|ref|XP_034940233|]
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syntaxin-binding protein 5 isoform X3 [Chelonus insularis]

Protein Classification

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 1.52e-47

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: 165.06  E-value: 1.52e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860458958  264 VTHPHAkltkdgePEPCKSIQKVEWKLSRSGEAYVIFSGGLAYDTTGRTPSITVIQGKTTTVLEMEHNVVDFITLCESPY 343
Cdd:pfam08366    1 PTTPYG-------PFPCKAITKILWKTTKTGEPFIIFSGGMPRASYGDRHCITVMHGKKHTVFDFTSKVIDFFTLCESPD 73

                           90       100       110
                   ....*....|....*....|....*....|
gi 1860458958  344 TS-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 ...
 1281-1341 3.28e-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: 96.94  E-value: 3.28e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1860458958 1281 NANTEALRERVSTATGDVAMAHQMVMERGEKLSQLEERTARMMNESENFASSAHGLMLKYK 1341
Cdd:cd15873      1 GGGMKALRAKAGSAASAAARARQALNERGEKLSELEDRTAEMEDNAESFASTAKELAKKYK 61
WD40 COG2319
WD40 repeat [General function prediction only];
43-268 1.39e-07

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 55.69  E-value: 1.39e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860458958   43 RHGFPHQPTAVAFDPIQKLLAIGTKTGSLRILG-RPGVDVNIKHEGGAAVIQLEFLINEGALVSVTADDTLHLWNLRQki 121
Cdd:COG2319     74 LLGHTAAVLSVAFSPDGRLLASASADGTVRLWDlATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLAT-- 151

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860458958  122 PQVVQSLKFQRERITSIHLPLQSKWLYVGTERGNIHVLHIET----FVLSGyvinwnkaievsrktHPGAVIHLSDNPlD 197
Cdd:COG2319    152 GKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATgkllRTLTG---------------HTGAVRSVAFSP-D 215

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1860458958  198 lSKMLI-GYESGQISYWDLKTKcaewRCQT-----DEPLRSISWHHEGKQFMCSHTDGSLSTWVLKQPRPVSVTHPH 268
Cdd:COG2319    216 -GKLLAsGSADGTVRLWDLATG----KLLRtltghSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGH 287
Lgl_C super family cl20362
Lethal giant larvae(Lgl) like, C-terminal; The Lethal giant larvae (Lgl) tumour suppressor ...
 1111-1231 1.91e-04

Lethal giant larvae(Lgl) like, C-terminal; The Lethal giant larvae (Lgl) tumour suppressor family is conserved from yeast to mammals. The Lgl family functions in cell polarity, at least in part, by regulating SNARE-mediated membrane delivery events at the cell surface. The N-terminal half of Lgl members contains WD40 repeats (see pfam00400), while the C-terminal half appears specific to the family.


The actual alignment was detected with superfamily member pfam08596:

Pssm-ID: 400768  Cd Length: 393  Bit Score: 45.41  E-value: 1.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860458958 1111 FVVLISEKQARVVALPSQNcayrqqlsETHAVIKAEI----------TTIKDGVCLVCYVSNGHIATYSLPSLRPLVDVD 1180
Cdd:pfam08596  228 FVVATSVSDIRVFKPGKSK--------GTHKSFDYPIlcsgasvvptGQRKHGIVLVALFINGSIKVYSLPSLKEIKKMK 299

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1860458958 1181 -FLPLQDLRISKTICLTNkGHGLYLSSPTEIQKFSL--SSDFCSELPEMMgDLF 1231
Cdd:pfam08596  300 lPFPIDARYLSESSILRN-GDIFIRTGPTEAALISVfgSGSTGALLPPTD-LLY 351
 
Name Accession Description Interval E-value
LLGL pfam08366
LLGL2; This domain is found in lethal giant larvae homolog 2 (LLGL2) proteins and ...
 264-372 1.52e-47

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: 165.06  E-value: 1.52e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860458958  264 VTHPHAkltkdgePEPCKSIQKVEWKLSRSGEAYVIFSGGLAYDTTGRTPSITVIQGKTTTVLEMEHNVVDFITLCESPY 343
Cdd:pfam08366    1 PTTPYG-------PFPCKAITKILWKTTKTGEPFIIFSGGMPRASYGDRHCITVMHGKKHTVFDFTSKVIDFFTLCESPD 73

                           90       100       110
                   ....*....|....*....|....*....|
gi 1860458958  344 TS-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 ...
 1281-1341 3.28e-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: 96.94  E-value: 3.28e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1860458958 1281 NANTEALRERVSTATGDVAMAHQMVMERGEKLSQLEERTARMMNESENFASSAHGLMLKYK 1341
Cdd:cd15873      1 GGGMKALRAKAGSAASAAARARQALNERGEKLSELEDRTAEMEDNAESFASTAKELAKKYK 61
WD40 COG2319
WD40 repeat [General function prediction only];
43-268 1.39e-07

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 55.69  E-value: 1.39e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860458958   43 RHGFPHQPTAVAFDPIQKLLAIGTKTGSLRILG-RPGVDVNIKHEGGAAVIQLEFLINEGALVSVTADDTLHLWNLRQki 121
Cdd:COG2319     74 LLGHTAAVLSVAFSPDGRLLASASADGTVRLWDlATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLAT-- 151

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860458958  122 PQVVQSLKFQRERITSIHLPLQSKWLYVGTERGNIHVLHIET----FVLSGyvinwnkaievsrktHPGAVIHLSDNPlD 197
Cdd:COG2319    152 GKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATgkllRTLTG---------------HTGAVRSVAFSP-D 215

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1860458958  198 lSKMLI-GYESGQISYWDLKTKcaewRCQT-----DEPLRSISWHHEGKQFMCSHTDGSLSTWVLKQPRPVSVTHPH 268
Cdd:COG2319    216 -GKLLAsGSADGTVRLWDLATG----KLLRtltghSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGH 287
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 51-268 1.59e-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: 51.57  E-value: 1.59e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860458958   51 TAVAFDPIQKLLAIGTKTGSLRILGRPGVDVNIK---HEGGAAVIQleFLINEGALVSVTADDTLHLWNLRQkiPQVVQS 127
Cdd:cd00200     13 TCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTlkgHTGPVRDVA--ASADGTYLASGSSDKTIRLWDLET--GECVRT 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860458958  128 LKFQRERITSIHLPLQSKWLYVGTERGNIHVLHIETFVLSgYVInwnkaievsrKTHPGAVIHLSDNPldlSKMLI--GY 205
Cdd:cd00200     89 LTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCL-TTL----------RGHTDWVNSVAFSP---DGTFVasSS 154

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1860458958  206 ESGQISYWDLKTkcaeWRCQT-----DEPLRSISWHHEGKQFMCSHTDGSLSTWVLKQPRPVSVTHPH 268
Cdd:cd00200    155 QDGTIKLWDLRT----GKCVAtltghTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGH 218
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 182-462 2.79e-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: 50.80  E-value: 2.79e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860458958  182 KTHPGAVIHLSDNPlDLSKMLIGYESGQISYWDLKTKCAEWRCQT-DEPLRSISWHHEGKQFMCSHTDGSLSTWVLKQPR 260
Cdd:cd00200      6 KGHTGGVTCVAFSP-DGKLLATGSGDGTIKVWDLETGELLRTLKGhTGPVRDVAASADGTYLASGSSDKTIRLWDLETGE 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860458958  261 PVSVTHPHAKltkdgepePCKSIqkvewKLSRSGEayVIFSGGlaYDTTGR------TPSITVIQGKTTTVlemehNVVD 334
Cdd:cd00200     85 CVRTLTGHTS--------YVSSV-----AFSPDGR--ILSSSS--RDKTIKvwdvetGKCLTTLRGHTDWV-----NSVA 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860458958  335 FitlceSPyTSDFqdpyaVVVLLQNDLV-VIDLLTpgFPCFENpypMDIHESPVTCCAYFAD------CPSDLVPAFYSV 407
Cdd:cd00200    143 F-----SP-DGTF-----VASSSQDGTIkLWDLRT--GKCVAT---LTGHTGEVNSVAFSPDgekllsSSSDGTIKLWDL 206

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1860458958  408 GSKSQKKTGFSEREWpICGGEWSPNSssysEIILTGHADGSIKFWDASAGS-LQVL 462
Cdd:cd00200    207 STGKCLGTLRGHENG-VNSVAFSPDG----YLLASGSEDGTIRVWDLRTGEcVQTL 257
Synaptobrevin pfam00957
Synaptobrevin;
1305-1346 1.30e-05

Synaptobrevin;


Pssm-ID: 395764  Cd Length: 89  Bit Score: 44.84  E-value: 1.30e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1860458958 1305 VMERGEKLSQLEERTARMMNESENFASSAHGLMLKY--KDKKWY 1346
Cdd:pfam00957   26 VLERGEKLDLLVDKTENLQSSAQQFRRQARKLKRKMwwKNMKLY 69
Lgl_C pfam08596
Lethal giant larvae(Lgl) like, C-terminal; The Lethal giant larvae (Lgl) tumour suppressor ...
 1111-1231 1.91e-04

Lethal giant larvae(Lgl) like, C-terminal; The Lethal giant larvae (Lgl) tumour suppressor family is conserved from yeast to mammals. The Lgl family functions in cell polarity, at least in part, by regulating SNARE-mediated membrane delivery events at the cell surface. The N-terminal half of Lgl members contains WD40 repeats (see pfam00400), while the C-terminal half appears specific to the family.


Pssm-ID: 400768  Cd Length: 393  Bit Score: 45.41  E-value: 1.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860458958 1111 FVVLISEKQARVVALPSQNcayrqqlsETHAVIKAEI----------TTIKDGVCLVCYVSNGHIATYSLPSLRPLVDVD 1180
Cdd:pfam08596  228 FVVATSVSDIRVFKPGKSK--------GTHKSFDYPIlcsgasvvptGQRKHGIVLVALFINGSIKVYSLPSLKEIKKMK 299

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1860458958 1181 -FLPLQDLRISKTICLTNkGHGLYLSSPTEIQKFSL--SSDFCSELPEMMgDLF 1231
Cdd:pfam08596  300 lPFPIDARYLSESSILRN-GDIFIRTGPTEAALISVfgSGSTGALLPPTD-LLY 351
 
Name Accession Description Interval E-value
LLGL pfam08366
LLGL2; This domain is found in lethal giant larvae homolog 2 (LLGL2) proteins and ...
 264-372 1.52e-47

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: 165.06  E-value: 1.52e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860458958  264 VTHPHAkltkdgePEPCKSIQKVEWKLSRSGEAYVIFSGGLAYDTTGRTPSITVIQGKTTTVLEMEHNVVDFITLCESPY 343
Cdd:pfam08366    1 PTTPYG-------PFPCKAITKILWKTTKTGEPFIIFSGGMPRASYGDRHCITVMHGKKHTVFDFTSKVIDFFTLCESPD 73

                           90       100       110
                   ....*....|....*....|....*....|
gi 1860458958  344 TS-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 ...
 1281-1341 3.28e-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: 96.94  E-value: 3.28e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1860458958 1281 NANTEALRERVSTATGDVAMAHQMVMERGEKLSQLEERTARMMNESENFASSAHGLMLKYK 1341
Cdd:cd15873      1 GGGMKALRAKAGSAASAAARARQALNERGEKLSELEDRTAEMEDNAESFASTAKELAKKYK 61
R-SNARE_STXBP5 cd15893
SNARE domain of STXBP5; Syntaxin binding protein 5 (STXBP5, also called Tomosyn), as well as ...
 1285-1341 1.67e-11

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: 60.82  E-value: 1.67e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1860458958 1285 EALRERVSTATGDVAMAHQMVMERGEKLSQLEERTARMMNESENFASSAHGLMLKYK 1341
Cdd:cd15893      5 EGVKGAASGVVGELARARLALDERGQKLGELEERTAAMLASADSFSKHAHEMMLKYK 61
R-SNARE_STXBP6 cd15892
SNARE domain of STXBP6; Syntaxin binding protein 6 (STXBP6, also called Amisyn), as well as ...
 1287-1341 2.94e-09

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


Pssm-ID: 277245  Cd Length: 62  Bit Score: 54.39  E-value: 2.94e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1860458958 1287 LRERVSTATGDVAMAHQMVMERGEKLSQLEERTARMMNESENFASSAHGLMLKYK 1341
Cdd:cd15892      7 LHSAADSVTSAVQKASQALNERGERLGRAEEKTEDMKNSAQQFAETAHKLAMKHK 61
WD40 COG2319
WD40 repeat [General function prediction only];
43-268 1.39e-07

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 55.69  E-value: 1.39e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860458958   43 RHGFPHQPTAVAFDPIQKLLAIGTKTGSLRILG-RPGVDVNIKHEGGAAVIQLEFLINEGALVSVTADDTLHLWNLRQki 121
Cdd:COG2319     74 LLGHTAAVLSVAFSPDGRLLASASADGTVRLWDlATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLAT-- 151

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860458958  122 PQVVQSLKFQRERITSIHLPLQSKWLYVGTERGNIHVLHIET----FVLSGyvinwnkaievsrktHPGAVIHLSDNPlD 197
Cdd:COG2319    152 GKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATgkllRTLTG---------------HTGAVRSVAFSP-D 215

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1860458958  198 lSKMLI-GYESGQISYWDLKTKcaewRCQT-----DEPLRSISWHHEGKQFMCSHTDGSLSTWVLKQPRPVSVTHPH 268
Cdd:COG2319    216 -GKLLAsGSADGTVRLWDLATG----KLLRtltghSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGH 287
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 51-268 1.59e-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: 51.57  E-value: 1.59e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860458958   51 TAVAFDPIQKLLAIGTKTGSLRILGRPGVDVNIK---HEGGAAVIQleFLINEGALVSVTADDTLHLWNLRQkiPQVVQS 127
Cdd:cd00200     13 TCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTlkgHTGPVRDVA--ASADGTYLASGSSDKTIRLWDLET--GECVRT 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860458958  128 LKFQRERITSIHLPLQSKWLYVGTERGNIHVLHIETFVLSgYVInwnkaievsrKTHPGAVIHLSDNPldlSKMLI--GY 205
Cdd:cd00200     89 LTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCL-TTL----------RGHTDWVNSVAFSP---DGTFVasSS 154

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1860458958  206 ESGQISYWDLKTkcaeWRCQT-----DEPLRSISWHHEGKQFMCSHTDGSLSTWVLKQPRPVSVTHPH 268
Cdd:cd00200    155 QDGTIKLWDLRT----GKCVAtltghTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGH 218
WD40 COG2319
WD40 repeat [General function prediction only];
44-268 1.77e-06

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 51.84  E-value: 1.77e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860458958   44 HGFPHQPTAVAFDPIQKLLAIGTKTGSLRILG-RPGVDVNIKHEGGAAVIQLEFLINEGALVSVTADDTLHLWNLRQkiP 122
Cdd:COG2319    117 TGHTGAVRSVAFSPDGKTLASGSADGTVRLWDlATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLAT--G 194

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860458958  123 QVVQSLKFQRERITSIHLPLQSKWLYVGTERGNIHVLHIETfvlsgyvinwnKAIEVSRKTHPGAVIHLSDNPlDlSKML 202
Cdd:COG2319    195 KLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLAT-----------GKLLRTLTGHSGSVRSVAFSP-D-GRLL 261

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1860458958  203 I-GYESGQISYWDLKT-KCAEWRCQTDEPLRSISWHHEGKQFMCSHTDGSLSTWVLKQPRPVSVTHPH 268
Cdd:COG2319    262 AsGSADGTVRLWDLATgELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGH 329
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 182-462 2.79e-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: 50.80  E-value: 2.79e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860458958  182 KTHPGAVIHLSDNPlDLSKMLIGYESGQISYWDLKTKCAEWRCQT-DEPLRSISWHHEGKQFMCSHTDGSLSTWVLKQPR 260
Cdd:cd00200      6 KGHTGGVTCVAFSP-DGKLLATGSGDGTIKVWDLETGELLRTLKGhTGPVRDVAASADGTYLASGSSDKTIRLWDLETGE 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860458958  261 PVSVTHPHAKltkdgepePCKSIqkvewKLSRSGEayVIFSGGlaYDTTGR------TPSITVIQGKTTTVlemehNVVD 334
Cdd:cd00200     85 CVRTLTGHTS--------YVSSV-----AFSPDGR--ILSSSS--RDKTIKvwdvetGKCLTTLRGHTDWV-----NSVA 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860458958  335 FitlceSPyTSDFqdpyaVVVLLQNDLV-VIDLLTpgFPCFENpypMDIHESPVTCCAYFAD------CPSDLVPAFYSV 407
Cdd:cd00200    143 F-----SP-DGTF-----VASSSQDGTIkLWDLRT--GKCVAT---LTGHTGEVNSVAFSPDgekllsSSSDGTIKLWDL 206

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1860458958  408 GSKSQKKTGFSEREWpICGGEWSPNSssysEIILTGHADGSIKFWDASAGS-LQVL 462
Cdd:cd00200    207 STGKCLGTLRGHENG-VNSVAFSPDG----YLLASGSEDGTIRVWDLRTGEcVQTL 257
R-SNARE cd15843
SNARE motif, subgroup R-SNARE; SNARE (soluble N-ethylmaleimide-sensitive factor attachment ...
 1303-1341 4.75e-06

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: 45.19  E-value: 4.75e-06
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1860458958 1303 QMVMERGEKLSQLEERTARMMNESENFASSAHGLMLKYK 1341
Cdd:cd15843     22 DKVLERGEKLEDLVDKTENLNESANAFKKQARKLKRKMW 60
Synaptobrevin pfam00957
Synaptobrevin;
1305-1346 1.30e-05

Synaptobrevin;


Pssm-ID: 395764  Cd Length: 89  Bit Score: 44.84  E-value: 1.30e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1860458958 1305 VMERGEKLSQLEERTARMMNESENFASSAHGLMLKY--KDKKWY 1346
Cdd:pfam00957   26 VLERGEKLDLLVDKTENLQSSAQQFRRQARKLKRKMwwKNMKLY 69
R-SNARE_VAMP2 cd15870
SNARE motif of VAMP2; The VAMP-2 (vesicle-associated membrane protein 2, also called ...
 1305-1347 1.23e-04

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: 41.22  E-value: 1.23e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1860458958 1305 VMERGEKLSQLEERTARMMNESENFASSAHGLMLKYkdkkWYQ 1347
Cdd:cd15870     24 VLERDQKLSELDDRADALQAGASQFETSAGKLKRKY----WWK 62
Lgl_C pfam08596
Lethal giant larvae(Lgl) like, C-terminal; The Lethal giant larvae (Lgl) tumour suppressor ...
 1111-1231 1.91e-04

Lethal giant larvae(Lgl) like, C-terminal; The Lethal giant larvae (Lgl) tumour suppressor family is conserved from yeast to mammals. The Lgl family functions in cell polarity, at least in part, by regulating SNARE-mediated membrane delivery events at the cell surface. The N-terminal half of Lgl members contains WD40 repeats (see pfam00400), while the C-terminal half appears specific to the family.


Pssm-ID: 400768  Cd Length: 393  Bit Score: 45.41  E-value: 1.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860458958 1111 FVVLISEKQARVVALPSQNcayrqqlsETHAVIKAEI----------TTIKDGVCLVCYVSNGHIATYSLPSLRPLVDVD 1180
Cdd:pfam08596  228 FVVATSVSDIRVFKPGKSK--------GTHKSFDYPIlcsgasvvptGQRKHGIVLVALFINGSIKVYSLPSLKEIKKMK 299

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1860458958 1181 -FLPLQDLRISKTICLTNkGHGLYLSSPTEIQKFSL--SSDFCSELPEMMgDLF 1231
Cdd:pfam08596  300 lPFPIDARYLSESSILRN-GDIFIRTGPTEAALISVfgSGSTGALLPPTD-LLY 351
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 44-254 3.37e-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: 3.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860458958   44 HGFPHQPTAVAFDPIQKLLAIGTKTGSLRILgrpgvDVNIK--------HEGgaAVIQLEFLINEGALVSVTADDTLHLW 115
Cdd:cd00200     90 TGHTSYVSSVAFSPDGRILSSSSRDKTIKVW-----DVETGkclttlrgHTD--WVNSVAFSPDGTFVASSSQDGTIKLW 162

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860458958  116 NLRQkiPQVVQSLKFQRERITSIHLPLQSKWLYVGTERGNIHVlhietfvlsgyvinWNKAIEVSRKT---HPGAVIHLS 192
Cdd:cd00200    163 DLRT--GKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKL--------------WDLSTGKCLGTlrgHENGVNSVA 226

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1860458958  193 DNPldlSKMLI--GYESGQISYWDLKTkcaeWRCQ-----TDEPLRSISWHHEGKQFMCSHTDGSLSTW 254
Cdd:cd00200    227 FSP---DGYLLasGSEDGTIRVWDLRT----GECVqtlsgHTNSVTSLAWSPDGKRLASGSADGTIRIW 288
WD40 COG2319
WD40 repeat [General function prediction only];
37-163 4.65e-04

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 44.13  E-value: 4.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860458958   37 QVKKTFRHGfPHQPTAVAFDPIQKLLAIGTKTGSLRIL-GRPGVDVNIKHEGGAAVIQLEFLINEGALVSVTADDTLHLW 115
Cdd:COG2319    279 ELLRTLTGH-SGGVNSVAFSPDGKLLASGSDDGTVRLWdLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLW 357

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1860458958  116 NLRQKipQVVQSLKFQRERITSIHLPLQSKWLYVGTERGNIHVLHIET 163
Cdd:COG2319    358 DLATG--ELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
 
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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