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Conserved domains on  [gi|297747292|ref|NP_001172112|]
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vesicle-associated membrane protein 7 isoform 3 [Homo sapiens]

Protein Classification

longin domain-containing protein( domain architecture ID 13000503)

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 ...
4-116 5.54e-37

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: 126.99  E-value: 5.54e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297747292   4 LFAVVARG--TTILAKHAWCG------GNFLEVTEQILAKIPSENNKLTYSHGNYLFHYICQDRIVYLCITDDDFERSRA 75
Cdd:cd14824    1 LYALIARGsdGLILAEYTDLSsfssvkENFKFVAKTILERTPPSGQRQSVEEGDYVFHYLVEDGLCYLCITDKEYPKRVA 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 297747292  76 FNFLNEIKKRFQTTYGSRAQTALPYAMNSEFSSVLAAQLKH 116
Cdd:cd14824   81 FAFLEEVLDEFLSKYGSSAWTAARPYLFSEFDPELKKLMKK 121
SNARE super family cl22856
SNARE motif; SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) ...
124-144 3.00e-07

SNARE motif; 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). Qa-, 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.


The actual alignment was detected with superfamily member cd15871:

Pssm-ID: 473982 [Multi-domain]  Cd Length: 65  Bit Score: 46.64  E-value: 3.00e-07
                         10        20
                 ....*....|....*....|.
gi 297747292 124 DKVMETQAQVDELKGIMVRNI 144
Cdd:cd15871    1 DKVSKVQGQLDELKGIMVKNI 21
 
Name Accession Description Interval E-value
Longin cd14824
longin domain; Longin-domain is N-terminal domain of a subgroup of R-SNARE proteins, including ...
4-116 5.54e-37

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: 126.99  E-value: 5.54e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297747292   4 LFAVVARG--TTILAKHAWCG------GNFLEVTEQILAKIPSENNKLTYSHGNYLFHYICQDRIVYLCITDDDFERSRA 75
Cdd:cd14824    1 LYALIARGsdGLILAEYTDLSsfssvkENFKFVAKTILERTPPSGQRQSVEEGDYVFHYLVEDGLCYLCITDKEYPKRVA 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 297747292  76 FNFLNEIKKRFQTTYGSRAQTALPYAMNSEFSSVLAAQLKH 116
Cdd:cd14824   81 FAFLEEVLDEFLSKYGSSAWTAARPYLFSEFDPELKKLMKK 121
Longin pfam13774
Regulated-SNARE-like domain; Longin is one of the approximately 26 components required for ...
29-108 3.06e-31

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: 110.71  E-value: 3.06e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297747292   29 TEQILAKIPSENNKLTYSHGNYLFHYICQDRIVYLCITDDDFERSRAFNFLNEIKKRFQTTYGSR-AQTALPYAMNSEFS 107
Cdd:pfam13774   1 AKTILEKIPQNPQRQTYEGDNYTFHYLIEDGLTYLVIADKSYPRRLAFAFLEEIKDEFLSTYGPWtASALRPYAFNKEFD 80

                  .
gi 297747292  108 S 108
Cdd:pfam13774  81 T 81
SNC1 COG5143
Synaptobrevin/VAMP-like protein [Intracellular trafficking and secretion];
36-144 1.37e-07

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


Pssm-ID: 227472 [Multi-domain]  Cd Length: 190  Bit Score: 50.50  E-value: 1.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297747292  36 IPSENNKLTYSHGNYLFHY-ICQDRIVYLCITDDDFERSRAFNFLNEIKKRFQTTYGSRAQT--ALPYAMNsEFSSVLAa 112
Cdd:COG5143   42 SKTSASRASIESGDYFFHYlKMSSGIVYVPISDKEYPNKLAYGYLNSIATEFLKSSALEQLIddTVGIMRV-NIDKVIE- 119
                         90       100       110
                 ....*....|....*....|....*....|..
gi 297747292 113 qlKHHSENKGLDKVMETQAQVDELKGIMVRNI 144
Cdd:COG5143  120 --KGYRDPSIQDKLDQLQQELEETKRVLNKNI 149
R-SNARE_VAMP7 cd15871
SNARE motif of VAMP7; The VAMP-7 (vesicle-associated membrane protein 7, also called ...
124-144 3.00e-07

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: 46.64  E-value: 3.00e-07
                         10        20
                 ....*....|....*....|.
gi 297747292 124 DKVMETQAQVDELKGIMVRNI 144
Cdd:cd15871    1 DKVSKVQGQLDELKGIMVKNI 21
Synaptobrevin pfam00957
Synaptobrevin;
122-144 2.87e-03

Synaptobrevin;


Pssm-ID: 395764  Cd Length: 89  Bit Score: 35.98  E-value: 2.87e-03
                          10        20
                  ....*....|....*....|...
gi 297747292  122 GLDKVMETQAQVDELKGIMVRNI 144
Cdd:pfam00957   1 SNDKLAKIQAEVDEVKDIMTENI 23
 
Name Accession Description Interval E-value
Longin cd14824
longin domain; Longin-domain is N-terminal domain of a subgroup of R-SNARE proteins, including ...
4-116 5.54e-37

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: 126.99  E-value: 5.54e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297747292   4 LFAVVARG--TTILAKHAWCG------GNFLEVTEQILAKIPSENNKLTYSHGNYLFHYICQDRIVYLCITDDDFERSRA 75
Cdd:cd14824    1 LYALIARGsdGLILAEYTDLSsfssvkENFKFVAKTILERTPPSGQRQSVEEGDYVFHYLVEDGLCYLCITDKEYPKRVA 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 297747292  76 FNFLNEIKKRFQTTYGSRAQTALPYAMNSEFSSVLAAQLKH 116
Cdd:cd14824   81 FAFLEEVLDEFLSKYGSSAWTAARPYLFSEFDPELKKLMKK 121
longin-like cd14818
Longin-like domains; Longin-like domains are small protein domains present in a variety of ...
4-113 8.46e-35

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: 121.09  E-value: 8.46e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297747292   4 LFAVVARG-TTILAKHAWCGG-----NFLEVTEQILAKI-PSENNKLTYSHGNYLFHYICQDRIVYLCITDDDFERSRAF 76
Cdd:cd14818    1 LQLAVFDPqGQVLAASNWLGKkpsvkFSLIQIKSFFSKLiTSGFDFLTLTIGSYTFHYYLNKGLYFVVITDEQELRQELF 80
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 297747292  77 NFLNEIKKRFQTTYGSRAQTALPYAMNSEFSSVLAAQ 113
Cdd:cd14818   81 QTLNLLLKEFNSLHGSEVITKNIEDDLEEFESYLDIK 117
Longin pfam13774
Regulated-SNARE-like domain; Longin is one of the approximately 26 components required for ...
29-108 3.06e-31

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: 110.71  E-value: 3.06e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297747292   29 TEQILAKIPSENNKLTYSHGNYLFHYICQDRIVYLCITDDDFERSRAFNFLNEIKKRFQTTYGSR-AQTALPYAMNSEFS 107
Cdd:pfam13774   1 AKTILEKIPQNPQRQTYEGDNYTFHYLIEDGLTYLVIADKSYPRRLAFAFLEEIKDEFLSTYGPWtASALRPYAFNKEFD 80

                  .
gi 297747292  108 S 108
Cdd:pfam13774  81 T 81
SNC1 COG5143
Synaptobrevin/VAMP-like protein [Intracellular trafficking and secretion];
36-144 1.37e-07

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


Pssm-ID: 227472 [Multi-domain]  Cd Length: 190  Bit Score: 50.50  E-value: 1.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297747292  36 IPSENNKLTYSHGNYLFHY-ICQDRIVYLCITDDDFERSRAFNFLNEIKKRFQTTYGSRAQT--ALPYAMNsEFSSVLAa 112
Cdd:COG5143   42 SKTSASRASIESGDYFFHYlKMSSGIVYVPISDKEYPNKLAYGYLNSIATEFLKSSALEQLIddTVGIMRV-NIDKVIE- 119
                         90       100       110
                 ....*....|....*....|....*....|..
gi 297747292 113 qlKHHSENKGLDKVMETQAQVDELKGIMVRNI 144
Cdd:COG5143  120 --KGYRDPSIQDKLDQLQQELEETKRVLNKNI 149
R-SNARE_VAMP7 cd15871
SNARE motif of VAMP7; The VAMP-7 (vesicle-associated membrane protein 7, also called ...
124-144 3.00e-07

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: 46.64  E-value: 3.00e-07
                         10        20
                 ....*....|....*....|.
gi 297747292 124 DKVMETQAQVDELKGIMVRNI 144
Cdd:cd15871    1 DKVSKVQGQLDELKGIMVKNI 21
R-SNARE cd15843
SNARE motif, subgroup R-SNARE; SNARE (soluble N-ethylmaleimide-sensitive factor attachment ...
124-144 1.53e-03

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: 35.94  E-value: 1.53e-03
                         10        20
                 ....*....|....*....|.
gi 297747292 124 DKVMETQAQVDELKGIMVRNI 144
Cdd:cd15843    1 DKLSKVQEQVDEVKDVMQENI 21
Synaptobrevin pfam00957
Synaptobrevin;
122-144 2.87e-03

Synaptobrevin;


Pssm-ID: 395764  Cd Length: 89  Bit Score: 35.98  E-value: 2.87e-03
                          10        20
                  ....*....|....*....|...
gi 297747292  122 GLDKVMETQAQVDELKGIMVRNI 144
Cdd:pfam00957   1 SNDKLAKIQAEVDEVKDIMTENI 23
 
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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