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Conserved domains on  [gi|335892854|ref|NP_001229456|]
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vesicle-associated membrane protein 7 [Apis mellifera]

Protein Classification

longin domain-containing protein( domain architecture ID 13000496)

longin domain-containing protein similar to R-SNARE subgroup proteins, including VAMP7, Ykt6, and Sec22 which is required for transporting proteins from the ER to the plasma membrane, via the Golgi apparatus

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Longin cd14824
longin domain; Longin-domain is N-terminal domain of a subgroup of R-SNARE proteins, including ...
 4-117 4.12e-36

longin domain; Longin-domain is N-terminal domain of a subgroup of R-SNARE proteins, including VAMP7, Ykt6, and Sec22. Longin is one of the approximately 26 components required for transporting proteins from the ER to the plasma membrane, via the Golgi apparatus. It is necessary for the steps of the transfer from the ER to the Golgi complex. Longins are the only R-SNAREs that are common to all eukaryotes, and they are characterized by a conserved N-terminal domain with a profilin-like fold called a longin domain.


:

Pssm-ID: 341428  Cd Length: 122  Bit Score: 123.52  E-value: 4.12e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335892854   4 LYSVVARG--TTILAKYASCT------GNFDEVTENILTKIPPQNDKLTYSQGQYLFHYICENNIIYMCTTDADFQRSRA 75
Cdd:cd14824    1 LYALIARGsdGLILAEYTDLSsfssvkENFKFVAKTILERTPPSGQRQSVEEGDYVFHYLVEDGLCYLCITDKEYPKRVA 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 335892854  76 FLYLAEMKGRFLAAYGQDAQTAVPYAMNTDFARTLASTMKHY 117
Cdd:cd14824   81 FAFLEEVLDEFLSKYGSSAWTAARPYLFSEFDPELKKLMKKY 122
R-SNARE_VAMP7 cd15871
SNARE motif of VAMP7; The VAMP-7 (vesicle-associated membrane protein 7, also called ...
 125-189 7.63e-35

SNARE motif of VAMP7; The VAMP-7 (vesicle-associated membrane protein 7, also called synaptobrevin-like protein 1) protein belongs to the R-SNARE subgroup of SNAREs and interacts with syntaxin 7(Qa), syntaxin 8 (Qc) and Vti1b (Qb). The complex is involved in the transport from early endosomes to the lysosome via regulating the transport from multivesicular bodies to the lysosomes. 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: 277224 [Multi-domain]  Cd Length: 65  Bit Score: 118.28  E-value: 7.63e-35
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 335892854 125 DVLANALGDLDELKDIMSKNIDNVAMRGERLELLVNKTENLTANSVTFRKTSRNLARSLFWKNVK 189
Cdd:cd15871    1 DKVSKVQGQLDELKGIMVKNIDSIAQRGEKLELLVDKTEDLSSSSVTFKKTSRNLARAMCMKNIK 65
 
Name Accession Description Interval E-value
Longin cd14824
longin domain; Longin-domain is N-terminal domain of a subgroup of R-SNARE proteins, including ...
 4-117 4.12e-36

longin domain; Longin-domain is N-terminal domain of a subgroup of R-SNARE proteins, including VAMP7, Ykt6, and Sec22. Longin is one of the approximately 26 components required for transporting proteins from the ER to the plasma membrane, via the Golgi apparatus. It is necessary for the steps of the transfer from the ER to the Golgi complex. Longins are the only R-SNAREs that are common to all eukaryotes, and they are characterized by a conserved N-terminal domain with a profilin-like fold called a longin domain.


Pssm-ID: 341428  Cd Length: 122  Bit Score: 123.52  E-value: 4.12e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335892854   4 LYSVVARG--TTILAKYASCT------GNFDEVTENILTKIPPQNDKLTYSQGQYLFHYICENNIIYMCTTDADFQRSRA 75
Cdd:cd14824    1 LYALIARGsdGLILAEYTDLSsfssvkENFKFVAKTILERTPPSGQRQSVEEGDYVFHYLVEDGLCYLCITDKEYPKRVA 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 335892854  76 FLYLAEMKGRFLAAYGQDAQTAVPYAMNTDFARTLASTMKHY 117
Cdd:cd14824   81 FAFLEEVLDEFLSKYGSSAWTAARPYLFSEFDPELKKLMKKY 122
R-SNARE_VAMP7 cd15871
SNARE motif of VAMP7; The VAMP-7 (vesicle-associated membrane protein 7, also called ...
 125-189 7.63e-35

SNARE motif of VAMP7; The VAMP-7 (vesicle-associated membrane protein 7, also called synaptobrevin-like protein 1) protein belongs to the R-SNARE subgroup of SNAREs and interacts with syntaxin 7(Qa), syntaxin 8 (Qc) and Vti1b (Qb). The complex is involved in the transport from early endosomes to the lysosome via regulating the transport from multivesicular bodies to the lysosomes. 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: 277224 [Multi-domain]  Cd Length: 65  Bit Score: 118.28  E-value: 7.63e-35
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 335892854 125 DVLANALGDLDELKDIMSKNIDNVAMRGERLELLVNKTENLTANSVTFRKTSRNLARSLFWKNVK 189
Cdd:cd15871    1 DKVSKVQGQLDELKGIMVKNIDSIAQRGEKLELLVDKTEDLSSSSVTFKKTSRNLARAMCMKNIK 65
Longin pfam13774
Regulated-SNARE-like domain; Longin is one of the approximately 26 components required for ...
 29-108 6.00e-27

Regulated-SNARE-like domain; Longin is one of the approximately 26 components required for transporting proteins from the ER to the plasma membrane, via the Golgi apparatus. It is necessary for the steps of the transfer from the ER to the Golgi complex. Longins are the only R-SNAREs that are common to all eukaryotes, and they are characterized by a conserved N-terminal domain with a profilin-like fold called a longin domain.


Pssm-ID: 463978  Cd Length: 81  Bit Score: 98.38  E-value: 6.00e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335892854   29 TENILTKIPPQNDKLTYSQGQYLFHYICENNIIYMCTTDADFQRSRAFLYLAEMKGRFLAAYG-QDAQTAVPYAMNTDFA 107
Cdd:pfam13774   1 AKTILEKIPQNPQRQTYEGDNYTFHYLIEDGLTYLVIADKSYPRRLAFAFLEEIKDEFLSTYGpWTASALRPYAFNKEFD 80


                  .
gi 335892854  108 R 108
Cdd:pfam13774  81 T 81
Synaptobrevin pfam00957
Synaptobrevin;
123-196 6.96e-26

Synaptobrevin;


Pssm-ID: 395764  Cd Length: 89  Bit Score: 96.07  E-value: 6.96e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 335892854  123 EIDVLANALGDLDELKDIMSKNIDNVAMRGERLELLVNKTENLTANSVTFRKTSRNLARSLFWKNVKIYVIVAA 196
Cdd:pfam00957   1 SNDKLAKIQAEVDEVKDIMTENIDKVLERGEKLDLLVDKTENLQSSAQQFRRQARKLKRKMWWKNMKLYIILGL 74
SNC1 COG5143
Synaptobrevin/VAMP-like protein [Intracellular trafficking and secretion];
32-185 4.13e-15

Synaptobrevin/VAMP-like protein [Intracellular trafficking and secretion];


Pssm-ID: 227472 [Multi-domain]  Cd Length: 190  Bit Score: 70.54  E-value: 4.13e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335892854  32 ILTKIPPQNDKLTY-SQGQYLFHYICENN-IIYMCTTDADFQRSRAFLYLAEMKGRFL--AAYGQDAQTAVPYAMNTdfa 107
Cdd:COG5143   37 VLRFLSKTSASRASiESGDYFFHYLKMSSgIVYVPISDKEYPNKLAYGYLNSIATEFLksSALEQLIDDTVGIMRVN--- 113

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 335892854 108 rTLASTMKHYNESNQEiDVLANALGDLDELKDIMSKNIDNVAMRGERLELLVNKTENLTANSVTFRKTSRNLARSLFW 185
Cdd:COG5143  114 -IDKVIEKGYRDPSIQ-DKLDQLQQELEETKRVLNKNIEKVLYRDEKLDLLVDLSSILLLSSKMFPKSAKKSNLCCLI 189
 
Name Accession Description Interval E-value
Longin cd14824
longin domain; Longin-domain is N-terminal domain of a subgroup of R-SNARE proteins, including ...
 4-117 4.12e-36

longin domain; Longin-domain is N-terminal domain of a subgroup of R-SNARE proteins, including VAMP7, Ykt6, and Sec22. Longin is one of the approximately 26 components required for transporting proteins from the ER to the plasma membrane, via the Golgi apparatus. It is necessary for the steps of the transfer from the ER to the Golgi complex. Longins are the only R-SNAREs that are common to all eukaryotes, and they are characterized by a conserved N-terminal domain with a profilin-like fold called a longin domain.


Pssm-ID: 341428  Cd Length: 122  Bit Score: 123.52  E-value: 4.12e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335892854   4 LYSVVARG--TTILAKYASCT------GNFDEVTENILTKIPPQNDKLTYSQGQYLFHYICENNIIYMCTTDADFQRSRA 75
Cdd:cd14824    1 LYALIARGsdGLILAEYTDLSsfssvkENFKFVAKTILERTPPSGQRQSVEEGDYVFHYLVEDGLCYLCITDKEYPKRVA 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 335892854  76 FLYLAEMKGRFLAAYGQDAQTAVPYAMNTDFARTLASTMKHY 117
Cdd:cd14824   81 FAFLEEVLDEFLSKYGSSAWTAARPYLFSEFDPELKKLMKKY 122
R-SNARE_VAMP7 cd15871
SNARE motif of VAMP7; The VAMP-7 (vesicle-associated membrane protein 7, also called ...
 125-189 7.63e-35

SNARE motif of VAMP7; The VAMP-7 (vesicle-associated membrane protein 7, also called synaptobrevin-like protein 1) protein belongs to the R-SNARE subgroup of SNAREs and interacts with syntaxin 7(Qa), syntaxin 8 (Qc) and Vti1b (Qb). The complex is involved in the transport from early endosomes to the lysosome via regulating the transport from multivesicular bodies to the lysosomes. 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: 277224 [Multi-domain]  Cd Length: 65  Bit Score: 118.28  E-value: 7.63e-35
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 335892854 125 DVLANALGDLDELKDIMSKNIDNVAMRGERLELLVNKTENLTANSVTFRKTSRNLARSLFWKNVK 189
Cdd:cd15871    1 DKVSKVQGQLDELKGIMVKNIDSIAQRGEKLELLVDKTEDLSSSSVTFKKTSRNLARAMCMKNIK 65
Longin pfam13774
Regulated-SNARE-like domain; Longin is one of the approximately 26 components required for ...
 29-108 6.00e-27

Regulated-SNARE-like domain; Longin is one of the approximately 26 components required for transporting proteins from the ER to the plasma membrane, via the Golgi apparatus. It is necessary for the steps of the transfer from the ER to the Golgi complex. Longins are the only R-SNAREs that are common to all eukaryotes, and they are characterized by a conserved N-terminal domain with a profilin-like fold called a longin domain.


Pssm-ID: 463978  Cd Length: 81  Bit Score: 98.38  E-value: 6.00e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335892854   29 TENILTKIPPQNDKLTYSQGQYLFHYICENNIIYMCTTDADFQRSRAFLYLAEMKGRFLAAYG-QDAQTAVPYAMNTDFA 107
Cdd:pfam13774   1 AKTILEKIPQNPQRQTYEGDNYTFHYLIEDGLTYLVIADKSYPRRLAFAFLEEIKDEFLSTYGpWTASALRPYAFNKEFD 80


                  .
gi 335892854  108 R 108
Cdd:pfam13774  81 T 81
Synaptobrevin pfam00957
Synaptobrevin;
123-196 6.96e-26

Synaptobrevin;


Pssm-ID: 395764  Cd Length: 89  Bit Score: 96.07  E-value: 6.96e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 335892854  123 EIDVLANALGDLDELKDIMSKNIDNVAMRGERLELLVNKTENLTANSVTFRKTSRNLARSLFWKNVKIYVIVAA 196
Cdd:pfam00957   1 SNDKLAKIQAEVDEVKDIMTENIDKVLERGEKLDLLVDKTENLQSSAQQFRRQARKLKRKMWWKNMKLYIILGL 74
R-SNARE_VAMP8 cd15868
SNARE motif of VAMP8; The lysosomal VAMP8 (vesicle-associated membrane protein 8, also called ...
 135-190 1.48e-20

SNARE motif of VAMP8; The lysosomal VAMP8 (vesicle-associated membrane protein 8, also called endobrevin) protein belongs to the R-SNARE subgroup of SNAREs and interacts with STX17 (Qa) and SNAP29 (Qb/Qc). The complex plays a role in autophagosome-lysosome fusion via regulating the transport from early endosomes to multivesicular bodies. Autophagosome transports cytoplasmic materials including cytoplasmic proteins, glycogen, lipids, organelles, and invading bacteria to the lysosome for degradation. 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: 277221 [Multi-domain]  Cd Length: 68  Bit Score: 81.59  E-value: 1.48e-20
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 335892854 135 DELKDIMSKNIDNVAMRGERLELLVNKTENLTANSVTFRKTSRNLARSLFWKNVKI 190
Cdd:cd15868   12 DEVKNIMTQNIDKILARGERLDDLMDKTEDLEATSKTFQKTSQKVARKYWWKNTKM 67
longin-like cd14818
Longin-like domains; Longin-like domains are small protein domains present in a variety of ...
 4-113 7.75e-20

Longin-like domains; Longin-like domains are small protein domains present in a variety of proteins and members of protein complexes involved in or required for different steps during the transport of proteins from the ribosome to the ER to the plasma membrane, via the Golgi apparatus. Examples are mu and sigma subunits of the heterotetrameric adaptor protein (AP) complex, zeta and delta subunits of the heterotetrameric F-COPI complex, a subgroup of R-SNARE proteins, a subfamily of the transport protein particle (TRAPP), and the signal recognition particle receptor subunit alpha (SR-alpha).


Pssm-ID: 341426  Cd Length: 117  Bit Score: 81.42  E-value: 7.75e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335892854   4 LYSVVARG-TTILAKYASCTG-----NFDEVTENILTKIPPQ-NDKLTYSQGQYLFHYICENNIIYMCTTDADFQRSRAF 76
Cdd:cd14818    1 LQLAVFDPqGQVLAASNWLGKkpsvkFSLIQIKSFFSKLITSgFDFLTLTIGSYTFHYYLNKGLYFVVITDEQELRQELF 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 335892854  77 LYLAEMKGRFLAAYGQDAQTAVPYAMNTDFARTLAST 113
Cdd:cd14818   81 QTLNLLLKEFNSLHGSEVITKNIEDDLEEFESYLDIK 117
R-SNARE cd15843
SNARE motif, subgroup R-SNARE; SNARE (soluble N-ethylmaleimide-sensitive factor attachment ...
 125-184 1.35e-17

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: 73.69  E-value: 1.35e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 335892854 125 DVLANALGDLDELKDIMSKNIDNVAMRGERLELLVNKTENLTANSVTFRKTSRNLARSLF 184
Cdd:cd15843    1 DKLSKVQEQVDEVKDVMQENIDKVLERGEKLEDLVDKTENLNESANAFKKQARKLKRKMW 60
SNC1 COG5143
Synaptobrevin/VAMP-like protein [Intracellular trafficking and secretion];
32-185 4.13e-15

Synaptobrevin/VAMP-like protein [Intracellular trafficking and secretion];


Pssm-ID: 227472 [Multi-domain]  Cd Length: 190  Bit Score: 70.54  E-value: 4.13e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335892854  32 ILTKIPPQNDKLTY-SQGQYLFHYICENN-IIYMCTTDADFQRSRAFLYLAEMKGRFL--AAYGQDAQTAVPYAMNTdfa 107
Cdd:COG5143   37 VLRFLSKTSASRASiESGDYFFHYLKMSSgIVYVPISDKEYPNKLAYGYLNSIATEFLksSALEQLIDDTVGIMRVN--- 113

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 335892854 108 rTLASTMKHYNESNQEiDVLANALGDLDELKDIMSKNIDNVAMRGERLELLVNKTENLTANSVTFRKTSRNLARSLFW 185
Cdd:COG5143  114 -IDKVIEKGYRDPSIQ-DKLDQLQQELEETKRVLNKNIEKVLYRDEKLDLLVDLSSILLLSSKMFPKSAKKSNLCCLI 189
R-SNARE_VAMP4 cd15869
SNARE motif of VAMP4; The VAMP-4 (vesicle-associated membrane protein 4) protein belongs to ...
 132-190 1.35e-13

SNARE motif of VAMP4; The VAMP-4 (vesicle-associated membrane protein 4) protein belongs to the R-SNARE subgroup of SNAREs and interacts with syntaxin 16 (Qa), Vti1a (Qb) and syntaxin 6 (Qc). This complex plays a role in maintenance of Golgi ribbon structure and normal retrograde trafficking from the early endosome to the trans-Golgi network (TGN). SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins contain coiled-coil helices (called SNARE motifs) which mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles.


Pssm-ID: 277222 [Multi-domain]  Cd Length: 67  Bit Score: 63.17  E-value: 1.35e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 335892854 132 GDLDELKDIMSKNIDNVAMRGERLELLVNKTENLTANSVTFRKTSRNLARSLFWKNVKI 190
Cdd:cd15869    9 NQVDEVVDVMQDNITKVIDRGEKLEDLQDKSESLSDNASAFRSRSKQLRRKMWWQNCKM 67
R-SNARE_SEC22 cd15866
SNARE motif of SEC22; SEC22 forms complexes with syntaxin 18 (Qa), Sec20 (Qb) and USE1 (Qc), ...
 133-186 1.43e-11

SNARE motif of SEC22; SEC22 forms complexes with syntaxin 18 (Qa), Sec20 (Qb) and USE1 (Qc), and with syntaxin 5 (Qa), GS27 (Qb) and Bet1 (Qc). These complexes are involved in the transport from cis-Golgi to the endoplasmic reticulum (ER) and in the transport from endoplasmic reticulum (ER) to the ER-Golgi intermediate compartment (ERGIC), respectively. SEC22 is a member of the R-SNARE subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins which contain coiled-coil helices (called SNARE motifs) that 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: 277219 [Multi-domain]  Cd Length: 64  Bit Score: 57.91  E-value: 1.43e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 335892854 133 DLDELKDIMSKNIDNVAMRGERLELLVNKTENLTANSVTFRKTSRNLARSLFWK 186
Cdd:cd15866   10 ELQDVQRIMTKNIDDVLGRGEKLDDLSDKSSNLSSESKKYKKDAKKLNLQALYR 63
R-SNARE_Snc1 cd15874
SNARE motif of Snc1; Saccharomyces cerevisiae SNARE protein Snc1p forms a complex with ...
 125-185 2.27e-09

SNARE motif of Snc1; Saccharomyces cerevisiae SNARE protein Snc1p forms a complex with synaptobrevin homolog Sso1p (Qa) and the SNAP-25 homolog Sec9p (Qb/c) which is involved in exocytosis. Snc1 is a member of the R-SNARE subgroup of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins, which consist of coiled-coil helices (called SNARE motifs) that mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complexes mediate membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle.


Pssm-ID: 277227 [Multi-domain]  Cd Length: 60  Bit Score: 51.98  E-value: 2.27e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 335892854 125 DVLANALGDLDELKDIMSKNIDNVAMRGERLELLVNKTENLTANSVTFRkTSRNLARSLFW 185
Cdd:cd15874    1 SRTEALQKEIDGAVGIMRHNIEKVAQRGERLDSLQDKTDNLAVSAQGFR-RGANRVRKQMW 60
R-SNARE_VAMP2 cd15870
SNARE motif of VAMP2; The VAMP-2 (vesicle-associated membrane protein 2, also called ...
 135-187 2.21e-08

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: 49.31  E-value: 2.21e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 335892854 135 DELKDIMSKNIDNVAMRGERLELLVNKTENLTANSVTFRKTSRNLARSLFWKN 187
Cdd:cd15870   11 DEVVDIMRVNVDKVLERDQKLSELDDRADALQAGASQFETSAGKLKRKYWWKN 63
R-SNARE_YKT6 cd15867
SNARE motif of YKT6; Ykt6 forms complexes with syntaxin-5 (Qa), GS28 (Qb) and either Bet1 (Qc) ...
 133-177 4.22e-07

SNARE motif of YKT6; Ykt6 forms complexes with syntaxin-5 (Qa), GS28 (Qb) and either Bet1 (Qc) or GS15 (Qc). This complex regulates the early secretory pathway of eukaryotic cells at the level of the transport from the ER-Golgi intermediate compartment (ERGIC) to the cis-Golgi and transport from the trans-Golgi network to the cis-Golgi, respectively. Ykt6 is a member of the R-SNARE subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins which contain coiled-coil helices (called SNARE motifs) that 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: 277220  Cd Length: 61  Bit Score: 45.82  E-value: 4.22e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 335892854 133 DLDELKDIMSKNIDNVAMRGERLELLVNKTENLTANSVTFRKTSR 177
Cdd:cd15867   10 ELDETKIILHKTIESVLERGEKLDDLVEKSEDLSDQSKMFYKTAK 54
R-SNARE_VAMP5 cd15872
SNARE motif of VAMP5; The VAMP-5 (vesicle-associated membrane protein 5) protein belongs to ...
 127-189 1.04e-06

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: 44.70  E-value: 1.04e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 335892854 127 LANALGDLDELKDIMSKNIDNVAMRGERLELLVNKTENLTANSVTFRKTSRNLARSLFWKNVK 189
Cdd:cd15872    4 LERCQREAEEVKVIMLDNLNKALEREGKLSDLEDRADELLNMSKAFEKTTQTVAQKKRWENIK 66
R-SNARE_STXBP5_6 cd15873
SNARE domain of STXBP5, STXBP6 and related proteins; Syntaxin binding protein 5 (STXBP5, also ...
 135-181 4.04e-03

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: 34.54  E-value: 4.04e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 335892854 135 DELKDIMSKNIDNVAMRGERLELLVNKTENLTANSVTFRKTSRNLAR 181
Cdd:cd15873   12 GSAASAAARARQALNERGEKLSELEDRTAEMEDNAESFASTAKELAK 58
 
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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