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Conserved domains on  [gi|815930017|ref|NP_001295259|]
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syntaxin-binding protein 5-like isoform 2 [Homo sapiens]

Protein Classification

LLGL and R-SNARE_STXBP5 domain-containing protein( domain architecture ID 11456851)

protein containing domains WD40, LLGL, and R-SNARE_STXBP5

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LLGL pfam08366
LLGL2; This domain is found in lethal giant larvae homolog 2 (LLGL2) proteins and ...
 288-397 3.87e-45

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: 157.74  E-value: 3.87e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815930017   288 TTIPHGksqregrkSESCKPILKVEYKTCKNSEPFIIFSGGLSYDKACRRPSLTIMHGKAITVLEMDHPIVEFLTLCETP 367
Cdd:pfam08366    1 PTTPYG--------PFPCKAITKILWKTTKTGEPFIIFSGGMPRASYGDRHCITVMHGKKHTVFDFTSKVIDFFTLCESP 72

                           90       100       110
                   ....*....|....*....|....*....|.
gi 815930017   368 YPN-EFQEPYAVVVLLEKDLIVVDLTQSNFP 397
Cdd:pfam08366   73 DPNaEFDDPYALVVLLEEELVVIDLTTPGWP 103
R-SNARE_STXBP5 cd15893
SNARE domain of STXBP5; Syntaxin binding protein 5 (STXBP5, also called Tomosyn), as well as ...
 1095-1155 9.67e-32

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: 118.22  E-value: 9.67e-32
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 815930017 1095 PGSIEGMKGAAGGVMGELTRARIALDERGQRLGELEEKTAGMMTSAEAFSKHAHELMLKYK 1155
Cdd:cd15893     1 PGGIEGVKGAASGVVGELARARLALDERGQKLGELEERTAAMLASADSFSKHAHEMMLKYK 61
WD40 COG2319
WD40 repeat [General function prediction only];
37-295 5.33e-14

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 75.33  E-value: 5.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815930017   37 VHPAGTAGVLREEIQETLTSEYFQICKTVRHGFPHQPTALAFDPVQKILAIGTRTGAIRILGRPGVDCYCQHES-GAAVL 115
Cdd:COG2319    45 SPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGhTGAVR 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815930017  116 QLQFLINEGALVSASSDDTLHLWNLRQKRPaiLHSLKFNRERITycHLPF--QSKWLYVGTERGNTHIVNIES----FIL 189
Cdd:COG2319   125 SVAFSPDGKTLASGSADGTVRLWDLATGKL--LRTLTGHSGAVT--SVAFspDGKLLASGSDDGTVRLWDLATgkllRTL 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815930017  190 SGyvimwnkaielstktHPGPVVHLSDSPrdEGKLLI-GYENGTVVFWDLKSKRaELRVY--YDEAIHSIDWHHEGKQFM 266
Cdd:COG2319   201 TG---------------HTGAVRSVAFSP--DGKLLAsGSADGTVRLWDLATGK-LLRTLtgHSGSVRSVAFSPDGRLLA 262

                         250       260
                  ....*....|....*....|....*....
gi 815930017  267 CSHSDGSLTLWNLKSPSRPfqTTIPHGKS 295
Cdd:COG2319   263 SGSADGTVRLWDLATGELL--RTLTGHSG 289
 
Name Accession Description Interval E-value
LLGL pfam08366
LLGL2; This domain is found in lethal giant larvae homolog 2 (LLGL2) proteins and ...
 288-397 3.87e-45

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: 157.74  E-value: 3.87e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815930017   288 TTIPHGksqregrkSESCKPILKVEYKTCKNSEPFIIFSGGLSYDKACRRPSLTIMHGKAITVLEMDHPIVEFLTLCETP 367
Cdd:pfam08366    1 PTTPYG--------PFPCKAITKILWKTTKTGEPFIIFSGGMPRASYGDRHCITVMHGKKHTVFDFTSKVIDFFTLCESP 72

                           90       100       110
                   ....*....|....*....|....*....|.
gi 815930017   368 YPN-EFQEPYAVVVLLEKDLIVVDLTQSNFP 397
Cdd:pfam08366   73 DPNaEFDDPYALVVLLEEELVVIDLTTPGWP 103
R-SNARE_STXBP5 cd15893
SNARE domain of STXBP5; Syntaxin binding protein 5 (STXBP5, also called Tomosyn), as well as ...
 1095-1155 9.67e-32

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: 118.22  E-value: 9.67e-32
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 815930017 1095 PGSIEGMKGAAGGVMGELTRARIALDERGQRLGELEEKTAGMMTSAEAFSKHAHELMLKYK 1155
Cdd:cd15893     1 PGGIEGVKGAASGVVGELARARLALDERGQKLGELEERTAAMLASADSFSKHAHEMMLKYK 61
WD40 COG2319
WD40 repeat [General function prediction only];
37-295 5.33e-14

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 75.33  E-value: 5.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815930017   37 VHPAGTAGVLREEIQETLTSEYFQICKTVRHGFPHQPTALAFDPVQKILAIGTRTGAIRILGRPGVDCYCQHES-GAAVL 115
Cdd:COG2319    45 SPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGhTGAVR 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815930017  116 QLQFLINEGALVSASSDDTLHLWNLRQKRPaiLHSLKFNRERITycHLPF--QSKWLYVGTERGNTHIVNIES----FIL 189
Cdd:COG2319   125 SVAFSPDGKTLASGSADGTVRLWDLATGKL--LRTLTGHSGAVT--SVAFspDGKLLASGSDDGTVRLWDLATgkllRTL 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815930017  190 SGyvimwnkaielstktHPGPVVHLSDSPrdEGKLLI-GYENGTVVFWDLKSKRaELRVY--YDEAIHSIDWHHEGKQFM 266
Cdd:COG2319   201 TG---------------HTGAVRSVAFSP--DGKLLAsGSADGTVRLWDLATGK-LLRTLtgHSGSVRSVAFSPDGRLLA 262

                         250       260
                  ....*....|....*....|....*....
gi 815930017  267 CSHSDGSLTLWNLKSPSRPfqTTIPHGKS 295
Cdd:COG2319   263 SGSADGTVRLWDLATGELL--RTLTGHSG 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 74-281 1.58e-13

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 72.37  E-value: 1.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815930017   74 TALAFDPVQKILAIGTRTGAIRILGRPGVDC---YCQHESGaaVLQLQFLINEGALVSASSDDTLHLWNLRQKRPaiLHS 150
Cdd:cd00200    13 TCVAFSPDGKLLATGSGDGTIKVWDLETGELlrtLKGHTGP--VRDVAASADGTYLASGSSDKTIRLWDLETGEC--VRT 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815930017  151 LKFNRERITYCHlpfqskwlyvgtergnthIVNIESFILSGY----VIMWN---KAIELSTKTHPGPVVHLSDSPrDEGK 223
Cdd:cd00200    89 LTGHTSYVSSVA------------------FSPDGRILSSSSrdktIKVWDvetGKCLTTLRGHTDWVNSVAFSP-DGTF 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 815930017  224 LLIGYENGTVVFWDLKSKRaELRVYY--DEAIHSIDWHHEGKQFMCSHSDGSLTLWNLKS 281
Cdd:cd00200   150 VASSSQDGTIKLWDLRTGK-CVATLTghTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLST 208
Synaptobrevin pfam00957
Synaptobrevin;
1121-1160 5.83e-04

Synaptobrevin;


Pssm-ID: 395764  Cd Length: 89  Bit Score: 39.83  E-value: 5.83e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 815930017  1121 ERGQRLGELEEKTAGMMTSAEAFSKHAHELMLKY--KDKKWY 1160
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 ...
 288-397 3.87e-45

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: 157.74  E-value: 3.87e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815930017   288 TTIPHGksqregrkSESCKPILKVEYKTCKNSEPFIIFSGGLSYDKACRRPSLTIMHGKAITVLEMDHPIVEFLTLCETP 367
Cdd:pfam08366    1 PTTPYG--------PFPCKAITKILWKTTKTGEPFIIFSGGMPRASYGDRHCITVMHGKKHTVFDFTSKVIDFFTLCESP 72

                           90       100       110
                   ....*....|....*....|....*....|.
gi 815930017   368 YPN-EFQEPYAVVVLLEKDLIVVDLTQSNFP 397
Cdd:pfam08366   73 DPNaEFDDPYALVVLLEEELVVIDLTTPGWP 103
R-SNARE_STXBP5 cd15893
SNARE domain of STXBP5; Syntaxin binding protein 5 (STXBP5, also called Tomosyn), as well as ...
 1095-1155 9.67e-32

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: 118.22  E-value: 9.67e-32
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 815930017 1095 PGSIEGMKGAAGGVMGELTRARIALDERGQRLGELEEKTAGMMTSAEAFSKHAHELMLKYK 1155
Cdd:cd15893     1 PGGIEGVKGAASGVVGELARARLALDERGQKLGELEERTAAMLASADSFSKHAHEMMLKYK 61
R-SNARE_STXBP5_6 cd15873
SNARE domain of STXBP5, STXBP6 and related proteins; Syntaxin binding protein 5 (STXBP5, also ...
 1095-1155 2.18e-21

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: 88.47  E-value: 2.18e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 815930017 1095 PGSIEGMKGAAGGVMGELTRARIALDERGQRLGELEEKTAGMMTSAEAFSKHAHELMLKYK 1155
Cdd:cd15873     1 GGGMKALRAKAGSAASAAARARQALNERGEKLSELEDRTAEMEDNAESFASTAKELAKKYK 61
WD40 COG2319
WD40 repeat [General function prediction only];
37-295 5.33e-14

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 75.33  E-value: 5.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815930017   37 VHPAGTAGVLREEIQETLTSEYFQICKTVRHGFPHQPTALAFDPVQKILAIGTRTGAIRILGRPGVDCYCQHES-GAAVL 115
Cdd:COG2319    45 SPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGhTGAVR 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815930017  116 QLQFLINEGALVSASSDDTLHLWNLRQKRPaiLHSLKFNRERITycHLPF--QSKWLYVGTERGNTHIVNIES----FIL 189
Cdd:COG2319   125 SVAFSPDGKTLASGSADGTVRLWDLATGKL--LRTLTGHSGAVT--SVAFspDGKLLASGSDDGTVRLWDLATgkllRTL 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815930017  190 SGyvimwnkaielstktHPGPVVHLSDSPrdEGKLLI-GYENGTVVFWDLKSKRaELRVY--YDEAIHSIDWHHEGKQFM 266
Cdd:COG2319   201 TG---------------HTGAVRSVAFSP--DGKLLAsGSADGTVRLWDLATGK-LLRTLtgHSGSVRSVAFSPDGRLLA 262

                         250       260
                  ....*....|....*....|....*....
gi 815930017  267 CSHSDGSLTLWNLKSPSRPfqTTIPHGKS 295
Cdd:COG2319   263 SGSADGTVRLWDLATGELL--RTLTGHSG 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 74-281 1.58e-13

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 72.37  E-value: 1.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815930017   74 TALAFDPVQKILAIGTRTGAIRILGRPGVDC---YCQHESGaaVLQLQFLINEGALVSASSDDTLHLWNLRQKRPaiLHS 150
Cdd:cd00200    13 TCVAFSPDGKLLATGSGDGTIKVWDLETGELlrtLKGHTGP--VRDVAASADGTYLASGSSDKTIRLWDLETGEC--VRT 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815930017  151 LKFNRERITYCHlpfqskwlyvgtergnthIVNIESFILSGY----VIMWN---KAIELSTKTHPGPVVHLSDSPrDEGK 223
Cdd:cd00200    89 LTGHTSYVSSVA------------------FSPDGRILSSSSrdktIKVWDvetGKCLTTLRGHTDWVNSVAFSP-DGTF 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 815930017  224 LLIGYENGTVVFWDLKSKRaELRVYY--DEAIHSIDWHHEGKQFMCSHSDGSLTLWNLKS 281
Cdd:cd00200   150 VASSSQDGTIKLWDLRTGK-CVATLTghTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLST 208
WD40 COG2319
WD40 repeat [General function prediction only];
74-281 4.72e-13

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 72.64  E-value: 4.72e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815930017   74 TALAFDPVQKILAIGTRTGAIRILGRPGVDC-YCQHESGAAVLQLQFLINEGALVSASSDDTLHLWNLRQKRPaiLHSLK 152
Cdd:COG2319   208 RSVAFSPDGKLLASGSADGTVRLWDLATGKLlRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGEL--LRTLT 285

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815930017  153 FNRERITYCHLPFQSKWLYVGTERGNTHIVNIES----FILSGyvimwnkaielstktHPGPVVHLSDSPrDEGKLLIGY 228
Cdd:COG2319   286 GHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATgkllRTLTG---------------HTGAVRSVAFSP-DGKTLASGS 349

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 815930017  229 ENGTVVFWDLKSKRaELRVY--YDEAIHSIDWHHEGKQFMCSHSDGSLTLWNLKS 281
Cdd:COG2319   350 DDGTVRLWDLATGE-LLRTLtgHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 67-278 5.46e-12

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: 67.75  E-value: 5.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815930017   67 HGFPHQPTALAFDPVQKILAIGTRTGAIRIL-GRPGVDCYCQHESGAAVLQLQFLINEGALVSASSDDTLHLWNLRQKRP 145
Cdd:cd00200    90 TGHTSYVSSVAFSPDGRILSSSSRDKTIKVWdVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKC 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815930017  146 aiLHSLKFNRERITycHLPF--QSKWLYVGTERGNthivniesfilsgyVIMWNKAIELSTKT---HPGPVVHLSDSPrd 220
Cdd:cd00200   170 --VATLTGHTGEVN--SVAFspDGEKLLSSSSDGT--------------IKLWDLSTGKCLGTlrgHENGVNSVAFSP-- 229

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 815930017  221 EGKLLIGY-ENGTVVFWDLKSKRaELRVY--YDEAIHSIDWHHEGKQFMCSHSDGSLTLWN 278
Cdd:cd00200   230 DGYLLASGsEDGTIRVWDLRTGE-CVQTLsgHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
R-SNARE_STXBP6 cd15892
SNARE domain of STXBP6; Syntaxin binding protein 6 (STXBP6, also called Amisyn), as well as ...
 1094-1155 3.66e-11

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


Pssm-ID: 277245  Cd Length: 62  Bit Score: 59.78  E-value: 3.66e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 815930017 1094 GPGSIegMKGAAGGVMGELTRARIALDERGQRLGELEEKTAGMMTSAEAFSKHAHELMLKYK 1155
Cdd:cd15892     2 GGNSI--LHSAADSVTSAVQKASQALNERGERLGRAEEKTEDMKNSAQQFAETAHKLAMKHK 61
R-SNARE cd15843
SNARE motif, subgroup R-SNARE; SNARE (soluble N-ethylmaleimide-sensitive factor attachment ...
 1121-1155 3.62e-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: 42.49  E-value: 3.62e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 815930017 1121 ERGQRLGELEEKTAGMMTSAEAFSKHAHELMLKYK 1155
Cdd:cd15843    26 ERGEKLEDLVDKTENLNESANAFKKQARKLKRKMW 60
Synaptobrevin pfam00957
Synaptobrevin;
1121-1160 5.83e-04

Synaptobrevin;


Pssm-ID: 395764  Cd Length: 89  Bit Score: 39.83  E-value: 5.83e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 815930017  1121 ERGQRLGELEEKTAGMMTSAEAFSKHAHELMLKY--KDKKWY 1160
Cdd:pfam00957   28 ERGEKLDLLVDKTENLQSSAQQFRRQARKLKRKMwwKNMKLY 69
WD40 COG2319
WD40 repeat [General function prediction only];
68-141 1.09e-03

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 42.98  E-value: 1.09e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 815930017   68 GFPHQPTALAFDPVQKILAIGTRTGAIRILGRPGVDCYC---QHEsgAAVLQLQFLINEGALVSASSDDTLHLWNLR 141
Cdd:COG2319   328 GHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRtltGHT--GAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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