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Conserved domains on  [gi|299473043|emb|CBN77436|]
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Soluble NSF Attachment Protein (SNAP) Receptor (SNARE), Vesicle-associated membrane protein [Ectocarpus siliculosus]

Protein Classification

longin domain-containing protein( domain architecture ID 13000477)

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 ...
 7-125 4.87e-16

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: 71.52  E-value: 4.87e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473043   7 FLGVIRFTDRVLVAGYSPSEADDS------LIIKELMSNPDTFvEPRKRYSVEGRMFsiHFVADDsNRIYSCVTDKEYPA 80
Cdd:cd14824    2 YALIARGSDGLILAEYTDLSSFSSvkenfkFVAKTILERTPPS-GQRQSVEEGDYVF--HYLVED-GLCYLCITDKEYPK 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 299473043  81 RIAFTLLEEAQTKFLTKVGDKSLTAKEGGLSRTMKSSFSDLCIKY 125
Cdd:cd14824   78 RVAFAFLEEVLDEFLSKYGSSAWTAARPYLFSEFDPELKKLMKKY 122
R-SNARE cd15843
SNARE motif, subgroup R-SNARE; SNARE (soluble N-ethylmaleimide-sensitive factor attachment ...
 147-191 2.64e-11

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: 57.13  E-value: 2.64e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 299473043 147 TMQDNIQQMLANEERLDQISENAENLNEQAKVFQNRSSALRRQMR 191
Cdd:cd15843   16 VMQENIDKVLERGEKLEDLVDKTENLNESANAFKKQARKLKRKMW 60
 
Name Accession Description Interval E-value
Longin cd14824
longin domain; Longin-domain is N-terminal domain of a subgroup of R-SNARE proteins, including ...
 7-125 4.87e-16

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: 71.52  E-value: 4.87e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473043   7 FLGVIRFTDRVLVAGYSPSEADDS------LIIKELMSNPDTFvEPRKRYSVEGRMFsiHFVADDsNRIYSCVTDKEYPA 80
Cdd:cd14824    2 YALIARGSDGLILAEYTDLSSFSSvkenfkFVAKTILERTPPS-GQRQSVEEGDYVF--HYLVED-GLCYLCITDKEYPK 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 299473043  81 RIAFTLLEEAQTKFLTKVGDKSLTAKEGGLSRTMKSSFSDLCIKY 125
Cdd:cd14824   78 RVAFAFLEEVLDEFLSKYGSSAWTAARPYLFSEFDPELKKLMKKY 122
R-SNARE cd15843
SNARE motif, subgroup R-SNARE; SNARE (soluble N-ethylmaleimide-sensitive factor attachment ...
 147-191 2.64e-11

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: 57.13  E-value: 2.64e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 299473043 147 TMQDNIQQMLANEERLDQISENAENLNEQAKVFQNRSSALRRQMR 191
Cdd:cd15843   16 VMQENIDKVLERGEKLEDLVDKTENLNESANAFKKQARKLKRKMW 60
Longin pfam13774
Regulated-SNARE-like domain; Longin is one of the approximately 26 components required for ...
 30-99 6.45e-11

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: 56.78  E-value: 6.45e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473043   30 SLIIKELMSNPdtfveprKRYSVEGRMFSIHFVADDsNRIYSCVTDKEYPARIAFTLLEEAQTKFLTKVG 99
Cdd:pfam13774   2 KTILEKIPQNP-------QRQTYEGDNYTFHYLIED-GLTYLVIADKSYPRRLAFAFLEEIKDEFLSTYG 63
Synaptobrevin pfam00957
Synaptobrevin;
148-209 2.39e-09

Synaptobrevin;


Pssm-ID: 395764  Cd Length: 89  Bit Score: 52.54  E-value: 2.39e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 299473043  148 MQDNIQQMLANEERLDQISENAENLNEQAKVFQNRSSALRRQMRCKAIKMWLLLALVVIILL 209
Cdd:pfam00957  19 MTENIDKVLERGEKLDLLVDKTENLQSSAQQFRRQARKLKRKMWWKNMKLYIILGLVVLILI 80
SNC1 COG5143
Synaptobrevin/VAMP-like protein [Intracellular trafficking and secretion];
31-180 9.40e-09

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


Pssm-ID: 227472 [Multi-domain]  Cd Length: 190  Bit Score: 53.20  E-value: 9.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473043  31 LIIKELMsnPDTFVEPRKRYSVEGRMFSIHFVADDSNRIYSCVTDKEYPARIAFTLLEEAQTKFLTKVGDKSLTAKEGGL 110
Cdd:COG5143   32 SKVKEVL--RFLSKTSASRASIESGDYFFHYLKMSSGIVYVPISDKEYPNKLAYGYLNSIATEFLKSSALEQLIDDTVGI 109

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473043 111 SRTMKSSFSDLciKYDDIRNVDRMAAVQDKVDVVKVTMQDNIQQMLANEERLDQISENAENLNEQAKVFQ 180
Cdd:COG5143  110 MRVNIDKVIEK--GYRDPSIQDKLDQLQQELEETKRVLNKNIEKVLYRDEKLDLLVDLSSILLLSSKMFP 177
 
Name Accession Description Interval E-value
Longin cd14824
longin domain; Longin-domain is N-terminal domain of a subgroup of R-SNARE proteins, including ...
 7-125 4.87e-16

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: 71.52  E-value: 4.87e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473043   7 FLGVIRFTDRVLVAGYSPSEADDS------LIIKELMSNPDTFvEPRKRYSVEGRMFsiHFVADDsNRIYSCVTDKEYPA 80
Cdd:cd14824    2 YALIARGSDGLILAEYTDLSSFSSvkenfkFVAKTILERTPPS-GQRQSVEEGDYVF--HYLVED-GLCYLCITDKEYPK 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 299473043  81 RIAFTLLEEAQTKFLTKVGDKSLTAKEGGLSRTMKSSFSDLCIKY 125
Cdd:cd14824   78 RVAFAFLEEVLDEFLSKYGSSAWTAARPYLFSEFDPELKKLMKKY 122
R-SNARE cd15843
SNARE motif, subgroup R-SNARE; SNARE (soluble N-ethylmaleimide-sensitive factor attachment ...
 147-191 2.64e-11

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: 57.13  E-value: 2.64e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 299473043 147 TMQDNIQQMLANEERLDQISENAENLNEQAKVFQNRSSALRRQMR 191
Cdd:cd15843   16 VMQENIDKVLERGEKLEDLVDKTENLNESANAFKKQARKLKRKMW 60
Longin pfam13774
Regulated-SNARE-like domain; Longin is one of the approximately 26 components required for ...
 30-99 6.45e-11

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: 56.78  E-value: 6.45e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473043   30 SLIIKELMSNPdtfveprKRYSVEGRMFSIHFVADDsNRIYSCVTDKEYPARIAFTLLEEAQTKFLTKVG 99
Cdd:pfam13774   2 KTILEKIPQNP-------QRQTYEGDNYTFHYLIED-GLTYLVIADKSYPRRLAFAFLEEIKDEFLSTYG 63
Synaptobrevin pfam00957
Synaptobrevin;
148-209 2.39e-09

Synaptobrevin;


Pssm-ID: 395764  Cd Length: 89  Bit Score: 52.54  E-value: 2.39e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 299473043  148 MQDNIQQMLANEERLDQISENAENLNEQAKVFQNRSSALRRQMRCKAIKMWLLLALVVIILL 209
Cdd:pfam00957  19 MTENIDKVLERGEKLDLLVDKTENLQSSAQQFRRQARKLKRKMWWKNMKLYIILGLVVLILI 80
SNC1 COG5143
Synaptobrevin/VAMP-like protein [Intracellular trafficking and secretion];
31-180 9.40e-09

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


Pssm-ID: 227472 [Multi-domain]  Cd Length: 190  Bit Score: 53.20  E-value: 9.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473043  31 LIIKELMsnPDTFVEPRKRYSVEGRMFSIHFVADDSNRIYSCVTDKEYPARIAFTLLEEAQTKFLTKVGDKSLTAKEGGL 110
Cdd:COG5143   32 SKVKEVL--RFLSKTSASRASIESGDYFFHYLKMSSGIVYVPISDKEYPNKLAYGYLNSIATEFLKSSALEQLIDDTVGI 109

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473043 111 SRTMKSSFSDLciKYDDIRNVDRMAAVQDKVDVVKVTMQDNIQQMLANEERLDQISENAENLNEQAKVFQ 180
Cdd:COG5143  110 MRVNIDKVIEK--GYRDPSIQDKLDQLQQELEETKRVLNKNIEKVLYRDEKLDLLVDLSSILLLSSKMFP 177
R-SNARE_VAMP4 cd15869
SNARE motif of VAMP4; The VAMP-4 (vesicle-associated membrane protein 4) protein belongs to ...
 147-197 8.32e-07

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: 45.07  E-value: 8.32e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 299473043 147 TMQDNIQQMLANEERLDQISENAENLNEQAKVFQNRSSALRRQMRCKAIKM 197
Cdd:cd15869   17 VMQDNITKVIDRGEKLEDLQDKSESLSDNASAFRSRSKQLRRKMWWQNCKM 67
R-SNARE_VAMP8 cd15868
SNARE motif of VAMP8; The lysosomal VAMP8 (vesicle-associated membrane protein 8, also called ...
 148-197 6.79e-06

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: 42.69  E-value: 6.79e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 299473043 148 MQDNIQQMLANEERLDQISENAENLNEQAKVFQNRSSALRRQMRCKAIKM 197
Cdd:cd15868   18 MTQNIDKILARGERLDDLMDKTEDLEATSKTFQKTSQKVARKYWWKNTKM 67
R-SNARE_Snc1 cd15874
SNARE motif of Snc1; Saccharomyces cerevisiae SNARE protein Snc1p forms a complex with ...
 147-190 1.91e-04

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: 38.50  E-value: 1.91e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 299473043 147 TMQDNIQQMLANEERLDQISENAENLNEQAKVFQNRSSALRRQM 190
Cdd:cd15874   16 IMRHNIEKVAQRGERLDSLQDKTDNLAVSAQGFRRGANRVRKQM 59
R-SNARE_VAMP5 cd15872
SNARE motif of VAMP5; The VAMP-5 (vesicle-associated membrane protein 5) protein belongs to ...
 148-196 4.11e-04

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: 37.77  E-value: 4.11e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 299473043 148 MQDNIQQMLANEERLDQISENAENLNEQAKVFQNRSSALRRQMRCKAIK 196
Cdd:cd15872   18 MLDNLNKALEREGKLSDLEDRADELLNMSKAFEKTTQTVAQKKRWENIK 66
R-SNARE_VAMP2 cd15870
SNARE motif of VAMP2; The VAMP-2 (vesicle-associated membrane protein 2, also called ...
 148-190 6.00e-04

SNARE motif of VAMP2; The VAMP-2 (vesicle-associated membrane protein 2, also called synaptobrevin-2) protein belongs to the R-SNARE subgroup of SNAREs and interacts with Syntaxin-1 (Qa) and SNAP-25(Qb/Qc), as well as syntaxin 12 (Qa) and SNAP23 (Qb/Qc). The complexes play a role in transport of secretory granule from trans-Golgi network to the plasma membrane, and in the transport from early endosomes to and from the plasma membrane, respectively. SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins contain coiled-coil helices (called SNARE motifs) which mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles.


Pssm-ID: 277223 [Multi-domain]  Cd Length: 63  Bit Score: 36.98  E-value: 6.00e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 299473043 148 MQDNIQQMLANEERLDQISENAENLNEQAKVFQNRSSALRRQM 190
Cdd:cd15870   17 MRVNVDKVLERDQKLSELDDRADALQAGASQFETSAGKLKRKY 59
R-SNARE_VAMP7 cd15871
SNARE motif of VAMP7; The VAMP-7 (vesicle-associated membrane protein 7, also called ...
 148-196 6.29e-04

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: 37.01  E-value: 6.29e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 299473043 148 MQDNIQQMLANEERLDQISENAENLNEQAKVFQNRSSALRRQMRCKAIK 196
Cdd:cd15871   17 MVKNIDSIAQRGEKLELLVDKTEDLSSSSVTFKKTSRNLARAMCMKNIK 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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