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Conserved domains on  [gi|9755337|ref|NP_013194|]
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Nyv1p [Saccharomyces cerevisiae S288C]

Protein Classification

synaptobrevin family protein( domain architecture ID 12100077)

synaptobrevin family protein may be involved in targeting and fusion of synaptic vesicles with the presynaptic membrane as well as in neurotransmitter release; similar to Drosophila melanogaster synaptobrevin involved in the targeting and/or fusion of transport vesicles to their target membrane

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Nyv1_longin pfam09426
Vacuolar R-SNARE Nyv1, longin domain; This domain corresponds to the N terminal longin domain ...
 6-144 1.55e-70

Vacuolar R-SNARE Nyv1, longin domain; This domain corresponds to the N terminal longin domain of vacuolar R-SNARE Nyv1 which contains YXXomega-like sorting motif (Y31GTI34), responsible for the AP3-dependent vacuolar localization of Nyv1.


:

Pssm-ID: 401399  Cd Length: 138  Bit Score: 212.91  E-value: 1.55e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755337      6 VSYVEVIKNGETISSCFQPFQKNE-NYGTITSANEQITPVIFHNLIMDMVLPKVVPIKGNKVTKMSMNLIDGFDCFYSTD 84
Cdd:pfam09426   1 VSYVEVIKNGETISSCFNDNDNGSsSYGSISNRDSAATPDVFHKLIHDMVLPKVVPVEGNKVTKVSMDLIDGYDCYYTTA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755337     85 DHDpkTVYVCFTLVDMPKILPIRILSGLQEYESNATNELLSSHVGQILDSFHEELVEYRN 144
Cdd:pfam09426  81 DDG--KVLVCFTREDVPKILPIRLLSELKEALNNDTDEELSANIGNILDEFHEELLSYRN 138
Synaptobrevin pfam00957
Synaptobrevin;
165-250 1.30e-25

Synaptobrevin;


:

Pssm-ID: 395764  Cd Length: 89  Bit Score: 96.07  E-value: 1.30e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755337    165 SDIGDATEDQIKDVIQIMNDNIDKFLERQERVSLLVDKTSQLNSSSNKFRRKAVNIKEIMWWQKVKNITLLTFTIILFVS 244
Cdd:pfam00957   2 NDKLAKIQAEVDEVKDIMTENIDKVLERGEKLDLLVDKTENLQSSAQQFRRQARKLKRKMWWKNMKLYIILGLVVLILIL 81


                  ....*.
gi 9755337    245 AAFMFF 250
Cdd:pfam00957  82 IIIIFI 87
 
Name Accession Description Interval E-value
Nyv1_longin pfam09426
Vacuolar R-SNARE Nyv1, longin domain; This domain corresponds to the N terminal longin domain ...
 6-144 1.55e-70

Vacuolar R-SNARE Nyv1, longin domain; This domain corresponds to the N terminal longin domain of vacuolar R-SNARE Nyv1 which contains YXXomega-like sorting motif (Y31GTI34), responsible for the AP3-dependent vacuolar localization of Nyv1.


Pssm-ID: 401399  Cd Length: 138  Bit Score: 212.91  E-value: 1.55e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755337      6 VSYVEVIKNGETISSCFQPFQKNE-NYGTITSANEQITPVIFHNLIMDMVLPKVVPIKGNKVTKMSMNLIDGFDCFYSTD 84
Cdd:pfam09426   1 VSYVEVIKNGETISSCFNDNDNGSsSYGSISNRDSAATPDVFHKLIHDMVLPKVVPVEGNKVTKVSMDLIDGYDCYYTTA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755337     85 DHDpkTVYVCFTLVDMPKILPIRILSGLQEYESNATNELLSSHVGQILDSFHEELVEYRN 144
Cdd:pfam09426  81 DDG--KVLVCFTREDVPKILPIRLLSELKEALNNDTDEELSANIGNILDEFHEELLSYRN 138
SNC1 COG5143
Synaptobrevin/VAMP-like protein [Intracellular trafficking and secretion];
18-227 3.71e-64

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


Pssm-ID: 227472 [Multi-domain]  Cd Length: 190  Bit Score: 198.42  E-value: 3.71e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755337   18 ISSCFQPFQKNENYGTITSANEQITPVIFHNLIMDMVLPKVVPIKGNkvtkmsMNLIDGFDCFYSTDDHDPKTVYVCFTL 97
Cdd:COG5143   1 IASISLFRVKGEPLRTLSDAESLSSFSFFHRSKVKEVLRFLSKTSAS------RASIESGDYFFHYLKMSSGIVYVPISD 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755337   98 VDMPKILPIrilsglQEYESNATNELLSSHVGQILDSFHEElveYRNQTLNSSgngqsSNGNGQNTISDIGDATEDQIKD 177
Cdd:COG5143  75 KEYPNKLAY------GYLNSIATEFLKSSALEQLIDDTVGI---MRVNIDKVI-----EKGYRDPSIQDKLDQLQQELEE 140

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 9755337  178 VIQIMNDNIDKFLERQERVSLLVDKTSQLNSSSNKFRRKAVNIKEIMWWQ 227
Cdd:COG5143 141 TKRVLNKNIEKVLYRDEKLDLLVDLSSILLLSSKMFPKSAKKSNLCCLIN 190
Synaptobrevin pfam00957
Synaptobrevin;
165-250 1.30e-25

Synaptobrevin;


Pssm-ID: 395764  Cd Length: 89  Bit Score: 96.07  E-value: 1.30e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755337    165 SDIGDATEDQIKDVIQIMNDNIDKFLERQERVSLLVDKTSQLNSSSNKFRRKAVNIKEIMWWQKVKNITLLTFTIILFVS 244
Cdd:pfam00957   2 NDKLAKIQAEVDEVKDIMTENIDKVLERGEKLDLLVDKTENLQSSAQQFRRQARKLKRKMWWKNMKLYIILGLVVLILIL 81


                  ....*.
gi 9755337    245 AAFMFF 250
Cdd:pfam00957  82 IIIIFI 87
R-SNARE cd15843
SNARE motif, subgroup R-SNARE; SNARE (soluble N-ethylmaleimide-sensitive factor attachment ...
 169-225 2.45e-18

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: 76.39  E-value: 2.45e-18
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 9755337  169 DATEDQIKDVIQIMNDNIDKFLERQERVSLLVDKTSQLNSSSNKFRRKAVNIKEIMW 225
Cdd:cd15843   4 SKVQEQVDEVKDVMQENIDKVLERGEKLEDLVDKTENLNESANAFKKQARKLKRKMW 60
 
Name Accession Description Interval E-value
Nyv1_longin pfam09426
Vacuolar R-SNARE Nyv1, longin domain; This domain corresponds to the N terminal longin domain ...
 6-144 1.55e-70

Vacuolar R-SNARE Nyv1, longin domain; This domain corresponds to the N terminal longin domain of vacuolar R-SNARE Nyv1 which contains YXXomega-like sorting motif (Y31GTI34), responsible for the AP3-dependent vacuolar localization of Nyv1.


Pssm-ID: 401399  Cd Length: 138  Bit Score: 212.91  E-value: 1.55e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755337      6 VSYVEVIKNGETISSCFQPFQKNE-NYGTITSANEQITPVIFHNLIMDMVLPKVVPIKGNKVTKMSMNLIDGFDCFYSTD 84
Cdd:pfam09426   1 VSYVEVIKNGETISSCFNDNDNGSsSYGSISNRDSAATPDVFHKLIHDMVLPKVVPVEGNKVTKVSMDLIDGYDCYYTTA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755337     85 DHDpkTVYVCFTLVDMPKILPIRILSGLQEYESNATNELLSSHVGQILDSFHEELVEYRN 144
Cdd:pfam09426  81 DDG--KVLVCFTREDVPKILPIRLLSELKEALNNDTDEELSANIGNILDEFHEELLSYRN 138
SNC1 COG5143
Synaptobrevin/VAMP-like protein [Intracellular trafficking and secretion];
18-227 3.71e-64

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


Pssm-ID: 227472 [Multi-domain]  Cd Length: 190  Bit Score: 198.42  E-value: 3.71e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755337   18 ISSCFQPFQKNENYGTITSANEQITPVIFHNLIMDMVLPKVVPIKGNkvtkmsMNLIDGFDCFYSTDDHDPKTVYVCFTL 97
Cdd:COG5143   1 IASISLFRVKGEPLRTLSDAESLSSFSFFHRSKVKEVLRFLSKTSAS------RASIESGDYFFHYLKMSSGIVYVPISD 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755337   98 VDMPKILPIrilsglQEYESNATNELLSSHVGQILDSFHEElveYRNQTLNSSgngqsSNGNGQNTISDIGDATEDQIKD 177
Cdd:COG5143  75 KEYPNKLAY------GYLNSIATEFLKSSALEQLIDDTVGI---MRVNIDKVI-----EKGYRDPSIQDKLDQLQQELEE 140

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 9755337  178 VIQIMNDNIDKFLERQERVSLLVDKTSQLNSSSNKFRRKAVNIKEIMWWQ 227
Cdd:COG5143 141 TKRVLNKNIEKVLYRDEKLDLLVDLSSILLLSSKMFPKSAKKSNLCCLIN 190
Synaptobrevin pfam00957
Synaptobrevin;
165-250 1.30e-25

Synaptobrevin;


Pssm-ID: 395764  Cd Length: 89  Bit Score: 96.07  E-value: 1.30e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755337    165 SDIGDATEDQIKDVIQIMNDNIDKFLERQERVSLLVDKTSQLNSSSNKFRRKAVNIKEIMWWQKVKNITLLTFTIILFVS 244
Cdd:pfam00957   2 NDKLAKIQAEVDEVKDIMTENIDKVLERGEKLDLLVDKTENLQSSAQQFRRQARKLKRKMWWKNMKLYIILGLVVLILIL 81


                  ....*.
gi 9755337    245 AAFMFF 250
Cdd:pfam00957  82 IIIIFI 87
R-SNARE cd15843
SNARE motif, subgroup R-SNARE; SNARE (soluble N-ethylmaleimide-sensitive factor attachment ...
 169-225 2.45e-18

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: 76.39  E-value: 2.45e-18
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 9755337  169 DATEDQIKDVIQIMNDNIDKFLERQERVSLLVDKTSQLNSSSNKFRRKAVNIKEIMW 225
Cdd:cd15843   4 SKVQEQVDEVKDVMQENIDKVLERGEKLEDLVDKTENLNESANAFKKQARKLKRKMW 60
R-SNARE_VAMP8 cd15868
SNARE motif of VAMP8; The lysosomal VAMP8 (vesicle-associated membrane protein 8, also called ...
 169-232 3.40e-12

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: 60.02  E-value: 3.40e-12
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9755337  169 DATEDQIKDVIQIMNDNIDKFLERQERVSLLVDKTSQLNSSSNKFRRKAVNIKEIMWWQKVKNI 232
Cdd:cd15868   5 SALQSQVDEVKNIMTQNIDKILARGERLDDLMDKTEDLEATSKTFQKTSQKVARKYWWKNTKMI 68
R-SNARE_VAMP7 cd15871
SNARE motif of VAMP7; The VAMP-7 (vesicle-associated membrane protein 7, also called ...
 169-230 7.28e-12

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: 59.35  E-value: 7.28e-12
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9755337  169 DATEDQIKDVIQIMNDNIDKFLERQERVSLLVDKTSQLNSSSNKFRRKAVNIKEIMWWQKVK 230
Cdd:cd15871   4 SKVQGQLDELKGIMVKNIDSIAQRGEKLELLVDKTEDLSSSSVTFKKTSRNLARAMCMKNIK 65
R-SNARE_VAMP4 cd15869
SNARE motif of VAMP4; The VAMP-4 (vesicle-associated membrane protein 4) protein belongs to ...
 174-230 9.86e-12

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: 58.94  E-value: 9.86e-12
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 9755337  174 QIKDVIQIMNDNIDKFLERQERVSLLVDKTSQLNSSSNKFRRKAVNIKEIMWWQKVK 230
Cdd:cd15869  10 QVDEVVDVMQDNITKVIDRGEKLEDLQDKSESLSDNASAFRSRSKQLRRKMWWQNCK 66
R-SNARE_VAMP2 cd15870
SNARE motif of VAMP2; The VAMP-2 (vesicle-associated membrane protein 2, also called ...
 171-227 7.39e-11

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: 56.24  E-value: 7.39e-11
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 9755337  171 TEDQIKDVIQIMNDNIDKFLERQERVSLLVDKTSQLNSSSNKFRRKAVNIKEIMWWQ 227
Cdd:cd15870   6 TQAQVDEVVDIMRVNVDKVLERDQKLSELDDRADALQAGASQFETSAGKLKRKYWWK 62
R-SNARE_Snc1 cd15874
SNARE motif of Snc1; Saccharomyces cerevisiae SNARE protein Snc1p forms a complex with ...
 174-225 5.36e-10

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: 53.91  E-value: 5.36e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 9755337  174 QIKDVIQIMNDNIDKFLERQERVSLLVDKTSQLNSSSNKFRRKAVNIKEIMW 225
Cdd:cd15874   9 EIDGAVGIMRHNIEKVAQRGERLDSLQDKTDNLAVSAQGFRRGANRVRKQMW 60
R-SNARE_VAMP5 cd15872
SNARE motif of VAMP5; The VAMP-5 (vesicle-associated membrane protein 5) protein belongs to ...
 171-230 1.63e-07

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: 47.40  E-value: 1.63e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 9755337  171 TEDQIKDVIQIMNDNIDKFLERQERVSLLVDKTSQLNSSSNKFRRKAVNIKEIMWWQKVK 230
Cdd:cd15872   7 CQREAEEVKVIMLDNLNKALEREGKLSDLEDRADELLNMSKAFEKTTQTVAQKKRWENIK 66
R-SNARE_SEC22 cd15866
SNARE motif of SEC22; SEC22 forms complexes with syntaxin 18 (Qa), Sec20 (Qb) and USE1 (Qc), ...
 173-220 1.05e-06

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: 44.82  E-value: 1.05e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 9755337  173 DQIKDVIQIMNDNIDKFLERQERVSLLVDKTSQLNSSSNKFRRKAVNI 220
Cdd:cd15866   9 DELQDVQRIMTKNIDDVLGRGEKLDDLSDKSSNLSSESKKYKKDAKKL 56
 
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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