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Conserved domains on  [gi|2462606049|ref|XP_054210238|]
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syntaxin-binding protein 5 isoform X4 [Homo sapiens]

Protein Classification

LLGL and R-SNARE_STXBP5 domain-containing protein( domain architecture ID 13236891)

protein containing domains WD40, LLGL, and R-SNARE_STXBP5

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LLGL pfam08366
LLGL2; This domain is found in lethal giant larvae homolog 2 (LLGL2) proteins and ...
 71-180 7.12e-48

LLGL2; This domain is found in lethal giant larvae homolog 2 (LLGL2) proteins and syntaxin-binding proteins like tomosyn. It has been identified in eukaryotes and tends to be found together with WD repeats (pfam00400).


:

Pssm-ID: 462446  Cd Length: 103  Bit Score: 165.44  E-value: 7.12e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606049  71 TITPHGkqlkdgkkPEPCKPILKVEFKTTRSGEPFIILSGGLSYDTVGRRPCLTVMHGKSTAVLEMDYSIVDFLTLCETP 150
Cdd:pfam08366   1 PTTPYG--------PFPCKAITKILWKTTKTGEPFIIFSGGMPRASYGDRHCITVMHGKKHTVFDFTSKVIDFFTLCESP 72

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2462606049 151 YPN-DFQEPYAVVVLLEKDLVLIDLAQNGYP 180
Cdd:pfam08366  73 DPNaEFDDPYALVVLLEEELVVIDLTTPGWP 103
R-SNARE_STXBP5 cd15893
SNARE domain of STXBP5; Syntaxin binding protein 5 (STXBP5, also called Tomosyn), as well as ...
 908-968 4.66e-37

SNARE domain of STXBP5; Syntaxin binding protein 5 (STXBP5, also called Tomosyn), as well as its relative Syntaxin binding protein 6 (STXBP6, also called Amisyn) contains a C-terminal R-SNARE-like domain, which allows it to assemble into SNARE complexes, which in turn makes the complexes inactive and inhibits exocytosis. Tomosyn contains an N-terminal WD40 repeat region and has been shown to form complexes with SNAP-25 and syntaxin 1a, as well as SNAP-23 and syntaxin 4. In general, SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins consist of coiled-coil helices (called SNARE motifs) which mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qc-, as well as Qa- and Qb-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle.


:

Pssm-ID: 277246  Cd Length: 61  Bit Score: 133.24  E-value: 4.66e-37
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462606049 908 PGGIEGVKGAASGVVGELARARLALDERGQKLGDLEERTAAMLSSAESFSKHAHEIMLKYK 968
Cdd:cd15893     1 PGGIEGVKGAASGVVGELARARLALDERGQKLGELEERTAAMLASADSFSKHAHEMMLKYK 61
WD40 super family cl29593
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 4-269 3.47e-09

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: 59.27  E-value: 3.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606049   4 GSKLLIGFESGTVVLWDLKSKKADYRYT-YDEAIHSVAWHHEGKQFICSHSDGTLTIWNVRSPaKPVQTITPHgkqlkdg 82
Cdd:cd00200    21 GKLLATGSGDGTIKVWDLETGELLRTLKgHTGPVRDVAASADGTYLASGSSDKTIRLWDLETG-ECVRTLTGH------- 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606049  83 kkpepCKPILKVEFKTTRSgepfiILSGGlSYD------TVGRRPCLTVMHGKSTAVLEMDYSivdfltlcetpyPNDfq 156
Cdd:cd00200    93 -----TSYVSSVAFSPDGR-----ILSSS-SRDktikvwDVETGKCLTTLRGHTDWVNSVAFS------------PDG-- 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606049 157 ePYAVVVLLEKDLVLIDLAqNGYPIfenpYPLSIHESPVTCCEYFADcPVDLIPA-------LYSVGARQKRQGYSKKEW 229
Cdd:cd00200   148 -TFVASSSQDGTIKLWDLR-TGKCV----ATLTGHTGEVNSVAFSPD-GEKLLSSssdgtikLWDLSTGKCLGTLRGHEN 220

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2462606049 230 PINGGNWGLGaqsyPEIIITGHADGSVKFWD-ASAITLQVL 269
Cdd:cd00200   221 GVNSVAFSPD----GYLLASGSEDGTIRVWDlRTGECVQTL 257
 
Name Accession Description Interval E-value
LLGL pfam08366
LLGL2; This domain is found in lethal giant larvae homolog 2 (LLGL2) proteins and ...
 71-180 7.12e-48

LLGL2; This domain is found in lethal giant larvae homolog 2 (LLGL2) proteins and syntaxin-binding proteins like tomosyn. It has been identified in eukaryotes and tends to be found together with WD repeats (pfam00400).


Pssm-ID: 462446  Cd Length: 103  Bit Score: 165.44  E-value: 7.12e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606049  71 TITPHGkqlkdgkkPEPCKPILKVEFKTTRSGEPFIILSGGLSYDTVGRRPCLTVMHGKSTAVLEMDYSIVDFLTLCETP 150
Cdd:pfam08366   1 PTTPYG--------PFPCKAITKILWKTTKTGEPFIIFSGGMPRASYGDRHCITVMHGKKHTVFDFTSKVIDFFTLCESP 72

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2462606049 151 YPN-DFQEPYAVVVLLEKDLVLIDLAQNGYP 180
Cdd:pfam08366  73 DPNaEFDDPYALVVLLEEELVVIDLTTPGWP 103
R-SNARE_STXBP5 cd15893
SNARE domain of STXBP5; Syntaxin binding protein 5 (STXBP5, also called Tomosyn), as well as ...
 908-968 4.66e-37

SNARE domain of STXBP5; Syntaxin binding protein 5 (STXBP5, also called Tomosyn), as well as its relative Syntaxin binding protein 6 (STXBP6, also called Amisyn) contains a C-terminal R-SNARE-like domain, which allows it to assemble into SNARE complexes, which in turn makes the complexes inactive and inhibits exocytosis. Tomosyn contains an N-terminal WD40 repeat region and has been shown to form complexes with SNAP-25 and syntaxin 1a, as well as SNAP-23 and syntaxin 4. In general, SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins consist of coiled-coil helices (called SNARE motifs) which mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qc-, as well as Qa- and Qb-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle.


Pssm-ID: 277246  Cd Length: 61  Bit Score: 133.24  E-value: 4.66e-37
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462606049 908 PGGIEGVKGAASGVVGELARARLALDERGQKLGDLEERTAAMLSSAESFSKHAHEIMLKYK 968
Cdd:cd15893     1 PGGIEGVKGAASGVVGELARARLALDERGQKLGELEERTAAMLASADSFSKHAHEMMLKYK 61
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 4-269 3.47e-09

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: 59.27  E-value: 3.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606049   4 GSKLLIGFESGTVVLWDLKSKKADYRYT-YDEAIHSVAWHHEGKQFICSHSDGTLTIWNVRSPaKPVQTITPHgkqlkdg 82
Cdd:cd00200    21 GKLLATGSGDGTIKVWDLETGELLRTLKgHTGPVRDVAASADGTYLASGSSDKTIRLWDLETG-ECVRTLTGH------- 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606049  83 kkpepCKPILKVEFKTTRSgepfiILSGGlSYD------TVGRRPCLTVMHGKSTAVLEMDYSivdfltlcetpyPNDfq 156
Cdd:cd00200    93 -----TSYVSSVAFSPDGR-----ILSSS-SRDktikvwDVETGKCLTTLRGHTDWVNSVAFS------------PDG-- 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606049 157 ePYAVVVLLEKDLVLIDLAqNGYPIfenpYPLSIHESPVTCCEYFADcPVDLIPA-------LYSVGARQKRQGYSKKEW 229
Cdd:cd00200   148 -TFVASSSQDGTIKLWDLR-TGKCV----ATLTGHTGEVNSVAFSPD-GEKLLSSssdgtikLWDLSTGKCLGTLRGHEN 220

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2462606049 230 PINGGNWGLGaqsyPEIIITGHADGSVKFWD-ASAITLQVL 269
Cdd:cd00200   221 GVNSVAFSPD----GYLLASGSEDGTIRVWDlRTGECVQTL 257
WD40 COG2319
WD40 repeat [General function prediction only];
4-76 4.32e-09

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 59.92  E-value: 4.32e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462606049   4 GSKLLIGFESGTVVLWDLKSKKADYRYT-YDEAIHSVAWHHEGKQFICSHSDGTLTIWNVRSPaKPVQTITPHG 76
Cdd:COG2319   258 GRLLASGSADGTVRLWDLATGELLRTLTgHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATG-KLLRTLTGHT 330
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 33-61 8.59e-04

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 37.68  E-value: 8.59e-04
                           10        20
                   ....*....|....*....|....*....
gi 2462606049   33 DEAIHSVAWHHEGKQFICSHSDGTLTIWN 61
Cdd:smart00320  12 TGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
Synaptobrevin pfam00957
Synaptobrevin;
934-973 1.19e-03

Synaptobrevin;


Pssm-ID: 395764  Cd Length: 89  Bit Score: 39.06  E-value: 1.19e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2462606049 934 ERGQKLGDLEERTAAMLSSAESFSKHAHEIMLKY--KDKKWY 973
Cdd:pfam00957  28 ERGEKLDLLVDKTENLQSSAQQFRRQARKLKRKMwwKNMKLY 69
 
Name Accession Description Interval E-value
LLGL pfam08366
LLGL2; This domain is found in lethal giant larvae homolog 2 (LLGL2) proteins and ...
 71-180 7.12e-48

LLGL2; This domain is found in lethal giant larvae homolog 2 (LLGL2) proteins and syntaxin-binding proteins like tomosyn. It has been identified in eukaryotes and tends to be found together with WD repeats (pfam00400).


Pssm-ID: 462446  Cd Length: 103  Bit Score: 165.44  E-value: 7.12e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606049  71 TITPHGkqlkdgkkPEPCKPILKVEFKTTRSGEPFIILSGGLSYDTVGRRPCLTVMHGKSTAVLEMDYSIVDFLTLCETP 150
Cdd:pfam08366   1 PTTPYG--------PFPCKAITKILWKTTKTGEPFIIFSGGMPRASYGDRHCITVMHGKKHTVFDFTSKVIDFFTLCESP 72

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2462606049 151 YPN-DFQEPYAVVVLLEKDLVLIDLAQNGYP 180
Cdd:pfam08366  73 DPNaEFDDPYALVVLLEEELVVIDLTTPGWP 103
R-SNARE_STXBP5 cd15893
SNARE domain of STXBP5; Syntaxin binding protein 5 (STXBP5, also called Tomosyn), as well as ...
 908-968 4.66e-37

SNARE domain of STXBP5; Syntaxin binding protein 5 (STXBP5, also called Tomosyn), as well as its relative Syntaxin binding protein 6 (STXBP6, also called Amisyn) contains a C-terminal R-SNARE-like domain, which allows it to assemble into SNARE complexes, which in turn makes the complexes inactive and inhibits exocytosis. Tomosyn contains an N-terminal WD40 repeat region and has been shown to form complexes with SNAP-25 and syntaxin 1a, as well as SNAP-23 and syntaxin 4. In general, SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins consist of coiled-coil helices (called SNARE motifs) which mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qc-, as well as Qa- and Qb-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle.


Pssm-ID: 277246  Cd Length: 61  Bit Score: 133.24  E-value: 4.66e-37
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462606049 908 PGGIEGVKGAASGVVGELARARLALDERGQKLGDLEERTAAMLSSAESFSKHAHEIMLKYK 968
Cdd:cd15893     1 PGGIEGVKGAASGVVGELARARLALDERGQKLGELEERTAAMLASADSFSKHAHEMMLKYK 61
R-SNARE_STXBP5_6 cd15873
SNARE domain of STXBP5, STXBP6 and related proteins; Syntaxin binding protein 5 (STXBP5, also ...
 908-968 5.03e-23

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


Pssm-ID: 277226  Cd Length: 61  Bit Score: 93.09  E-value: 5.03e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462606049 908 PGGIEGVKGAASGVVGELARARLALDERGQKLGDLEERTAAMLSSAESFSKHAHEIMLKYK 968
Cdd:cd15873     1 GGGMKALRAKAGSAASAAARARQALNERGEKLSELEDRTAEMEDNAESFASTAKELAKKYK 61
R-SNARE_STXBP6 cd15892
SNARE domain of STXBP6; Syntaxin binding protein 6 (STXBP6, also called Amisyn), as well as ...
 909-968 3.60e-10

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


Pssm-ID: 277245  Cd Length: 62  Bit Score: 56.70  E-value: 3.60e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606049 909 GGIEGVKGAASGVVGELARARLALDERGQKLGDLEERTAAMLSSAESFSKHAHEIMLKYK 968
Cdd:cd15892     2 GGNSILHSAADSVTSAVQKASQALNERGERLGRAEEKTEDMKNSAQQFAETAHKLAMKHK 61
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 4-269 3.47e-09

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: 59.27  E-value: 3.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606049   4 GSKLLIGFESGTVVLWDLKSKKADYRYT-YDEAIHSVAWHHEGKQFICSHSDGTLTIWNVRSPaKPVQTITPHgkqlkdg 82
Cdd:cd00200    21 GKLLATGSGDGTIKVWDLETGELLRTLKgHTGPVRDVAASADGTYLASGSSDKTIRLWDLETG-ECVRTLTGH------- 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606049  83 kkpepCKPILKVEFKTTRSgepfiILSGGlSYD------TVGRRPCLTVMHGKSTAVLEMDYSivdfltlcetpyPNDfq 156
Cdd:cd00200    93 -----TSYVSSVAFSPDGR-----ILSSS-SRDktikvwDVETGKCLTTLRGHTDWVNSVAFS------------PDG-- 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462606049 157 ePYAVVVLLEKDLVLIDLAqNGYPIfenpYPLSIHESPVTCCEYFADcPVDLIPA-------LYSVGARQKRQGYSKKEW 229
Cdd:cd00200   148 -TFVASSSQDGTIKLWDLR-TGKCV----ATLTGHTGEVNSVAFSPD-GEKLLSSssdgtikLWDLSTGKCLGTLRGHEN 220

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2462606049 230 PINGGNWGLGaqsyPEIIITGHADGSVKFWD-ASAITLQVL 269
Cdd:cd00200   221 GVNSVAFSPD----GYLLASGSEDGTIRVWDlRTGECVQTL 257
WD40 COG2319
WD40 repeat [General function prediction only];
4-76 4.32e-09

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 59.92  E-value: 4.32e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462606049   4 GSKLLIGFESGTVVLWDLKSKKADYRYT-YDEAIHSVAWHHEGKQFICSHSDGTLTIWNVRSPaKPVQTITPHG 76
Cdd:COG2319   258 GRLLASGSADGTVRLWDLATGELLRTLTgHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATG-KLLRTLTGHT 330
WD40 COG2319
WD40 repeat [General function prediction only];
4-76 7.06e-09

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 59.15  E-value: 7.06e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462606049   4 GSKLLIGFESGTVVLWDLKSKKADYRYT-YDEAIHSVAWHHEGKQFICSHSDGTLTIWNVRSPaKPVQTITPHG 76
Cdd:COG2319   174 GKLLASGSDDGTVRLWDLATGKLLRTLTgHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATG-KLLRTLTGHS 246
WD40 COG2319
WD40 repeat [General function prediction only];
4-76 2.79e-08

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 57.23  E-value: 2.79e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462606049   4 GSKLLIGFESGTVVLWDLKSKKADYRYT-YDEAIHSVAWHHEGKQFICSHSDGTLTIWNVRSPaKPVQTITPHG 76
Cdd:COG2319   132 GKTLASGSADGTVRLWDLATGKLLRTLTgHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATG-KLLRTLTGHT 204
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 3-75 5.27e-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: 55.42  E-value: 5.27e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462606049   3 KGSKLLIGFESGTVVLWDLKSKKADYRYTY-DEAIHSVAWHHEGKQFICSHSDGTLTIWNVRSPaKPVQTITPH 75
Cdd:cd00200   188 DGEKLLSSSSDGTIKLWDLSTGKCLGTLRGhENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTG-ECVQTLSGH 260
WD40 COG2319
WD40 repeat [General function prediction only];
4-76 7.97e-08

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 55.69  E-value: 7.97e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462606049   4 GSKLLIGFESGTVVLWDLKSKKADYRYT-YDEAIHSVAWHHEGKQFICSHSDGTLTIWNVRSPaKPVQTITPHG 76
Cdd:COG2319   216 GKLLASGSADGTVRLWDLATGKLLRTLTgHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATG-ELLRTLTGHS 288
WD40 COG2319
WD40 repeat [General function prediction only];
4-75 1.84e-07

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 54.53  E-value: 1.84e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462606049   4 GSKLLIGFESGTVVLWDLKSKKADYRYT-YDEAIHSVAWHHEGKQFICSHSDGTLTIWNVRSPaKPVQTITPH 75
Cdd:COG2319    90 GRLLASASADGTVRLWDLATGLLLRTLTgHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATG-KLLRTLTGH 161
WD40 COG2319
WD40 repeat [General function prediction only];
4-64 4.94e-07

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 53.38  E-value: 4.94e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462606049   4 GSKLLIGFESGTVVLWDLKSKKADYRYT-YDEAIHSVAWHHEGKQFICSHSDGTLTIWNVRS 64
Cdd:COG2319   342 GKTLASGSDDGTVRLWDLATGELLRTLTgHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
WD40 COG2319
WD40 repeat [General function prediction only];
4-76 8.55e-07

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 52.61  E-value: 8.55e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462606049   4 GSKLLIGFESGTVVLWDLKSKKADYRYT-YDEAIHSVAWHHEGKQFICSHSDGTLTIWNVRSPaKPVQTITPHG 76
Cdd:COG2319   300 GKLLASGSDDGTVRLWDLATGKLLRTLTgHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATG-ELLRTLTGHT 372
R-SNARE cd15843
SNARE motif, subgroup R-SNARE; SNARE (soluble N-ethylmaleimide-sensitive factor attachment ...
 934-968 4.89e-04

SNARE motif, subgroup R-SNARE; SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins consist of coiled-coil helices (called SNARE motifs) which mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). In contrast to Qa-, Qb- and Qc-SNAREs that are localized to target organelle membranes, R-SNAREs are localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles. Examples for members of the Qa SNAREs are syntaxin 18, syntaxin 5, syntaxin 16, and syntaxin 1.


Pssm-ID: 277196 [Multi-domain]  Cd Length: 60  Bit Score: 39.02  E-value: 4.89e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2462606049 934 ERGQKLGDLEERTAAMLSSAESFSKHAHEIMLKYK 968
Cdd:cd15843    26 ERGEKLEDLVDKTENLNESANAFKKQARKLKRKMW 60
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 5-61 7.58e-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: 42.71  E-value: 7.58e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462606049   5 SKLLI-GFESGTVVLWDLKSKKADYRYT-YDEAIHSVAWHHEGKQFICSHSDGTLTIWN 61
Cdd:cd00200   231 GYLLAsGSEDGTIRVWDLRTGECVQTLSgHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 33-61 8.59e-04

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 37.68  E-value: 8.59e-04
                           10        20
                   ....*....|....*....|....*....
gi 2462606049   33 DEAIHSVAWHHEGKQFICSHSDGTLTIWN 61
Cdd:smart00320  12 TGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
Synaptobrevin pfam00957
Synaptobrevin;
934-973 1.19e-03

Synaptobrevin;


Pssm-ID: 395764  Cd Length: 89  Bit Score: 39.06  E-value: 1.19e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2462606049 934 ERGQKLGDLEERTAAMLSSAESFSKHAHEIMLKY--KDKKWY 973
Cdd:pfam00957  28 ERGEKLDLLVDKTENLQSSAQQFRRQARKLKRKMwwKNMKLY 69
R-SNARE_VAMP5 cd15872
SNARE motif of VAMP5; The VAMP-5 (vesicle-associated membrane protein 5) protein belongs to ...
 933-972 4.48e-03

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


Pssm-ID: 277225 [Multi-domain]  Cd Length: 68  Bit Score: 36.62  E-value: 4.48e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2462606049 933 DERGQKLGDLEERTAAMLSSAESFSKHAHEIMLKYKDKKW 972
Cdd:cd15872    26 LEREGKLSDLEDRADELLNMSKAFEKTTQTVAQKKRWENI 65
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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