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Conserved domains on  [gi|2462632055|ref|XP_054184299|]
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vesicle-associated membrane protein 7 isoform X1 [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 ...
 3-69 8.19e-23

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: 88.85  E-value: 8.19e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462632055   3 YLFHYICQDRIVYLCITDDDFERSRAFNFLNEIKKRFQTTYGSRAQTALPYAMNSEFSSVLAAQLKH 69
Cdd:cd14824    55 YVFHYLVEDGLCYLCITDKEYPKRVAFAFLEEVLDEFLSKYGSSAWTAARPYLFSEFDPELKKLMKK 121
SNARE super family cl22856
SNARE motif; SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) ...
 77-97 2.04e-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: 2.04e-07
                          10        20
                  ....*....|....*....|.
gi 2462632055  77 DKVMETQAQVDELKGIMVRNI 97
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 ...
 3-69 8.19e-23

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: 88.85  E-value: 8.19e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462632055   3 YLFHYICQDRIVYLCITDDDFERSRAFNFLNEIKKRFQTTYGSRAQTALPYAMNSEFSSVLAAQLKH 69
Cdd:cd14824    55 YVFHYLVEDGLCYLCITDKEYPKRVAFAFLEEVLDEFLSKYGSSAWTAARPYLFSEFDPELKKLMKK 121
Longin pfam13774
Regulated-SNARE-like domain; Longin is one of the approximately 26 components required for ...
 3-61 1.71e-21

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: 84.13  E-value: 1.71e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632055   3 YLFHYICQDRIVYLCITDDDFERSRAFNFLNEIKKRFQTTYGSR-AQTALPYAMNSEFSS 61
Cdd:pfam13774  22 YTFHYLIEDGLTYLVIADKSYPRRLAFAFLEEIKDEFLSTYGPWtASALRPYAFNKEFDT 81
R-SNARE_VAMP7 cd15871
SNARE motif of VAMP7; The VAMP-7 (vesicle-associated membrane protein 7, also called ...
 77-97 2.04e-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: 2.04e-07
                          10        20
                  ....*....|....*....|.
gi 2462632055  77 DKVMETQAQVDELKGIMVRNI 97
Cdd:cd15871     1 DKVSKVQGQLDELKGIMVKNI 21
SNC1 COG5143
Synaptobrevin/VAMP-like protein [Intracellular trafficking and secretion];
3-97 6.95e-06

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


Pssm-ID: 227472 [Multi-domain]  Cd Length: 190  Bit Score: 45.11  E-value: 6.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632055   3 YLFHY-ICQDRIVYLCITDDDFERSRAFNFLNEIKKRFQTTYGSRAQT--ALPYAMNsEFSSVLAaqlKHHSENKGLDKV 79
Cdd:COG5143    56 YFFHYlKMSSGIVYVPISDKEYPNKLAYGYLNSIATEFLKSSALEQLIddTVGIMRV-NIDKVIE---KGYRDPSIQDKL 131

                          90
                  ....*....|....*...
gi 2462632055  80 METQAQVDELKGIMVRNI 97
Cdd:COG5143   132 DQLQQELEETKRVLNKNI 149
Synaptobrevin pfam00957
Synaptobrevin;
75-97 1.87e-03

Synaptobrevin;


Pssm-ID: 395764  Cd Length: 89  Bit Score: 36.36  E-value: 1.87e-03
                          10        20
                  ....*....|....*....|...
gi 2462632055  75 GLDKVMETQAQVDELKGIMVRNI 97
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 ...
 3-69 8.19e-23

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: 88.85  E-value: 8.19e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462632055   3 YLFHYICQDRIVYLCITDDDFERSRAFNFLNEIKKRFQTTYGSRAQTALPYAMNSEFSSVLAAQLKH 69
Cdd:cd14824    55 YVFHYLVEDGLCYLCITDKEYPKRVAFAFLEEVLDEFLSKYGSSAWTAARPYLFSEFDPELKKLMKK 121
Longin pfam13774
Regulated-SNARE-like domain; Longin is one of the approximately 26 components required for ...
 3-61 1.71e-21

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: 84.13  E-value: 1.71e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632055   3 YLFHYICQDRIVYLCITDDDFERSRAFNFLNEIKKRFQTTYGSR-AQTALPYAMNSEFSS 61
Cdd:pfam13774  22 YTFHYLIEDGLTYLVIADKSYPRRLAFAFLEEIKDEFLSTYGPWtASALRPYAFNKEFDT 81
longin-like cd14818
Longin-like domains; Longin-like domains are small protein domains present in a variety of ...
 3-66 4.11e-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: 81.80  E-value: 4.11e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462632055   3 YLFHYICQDRIVYLCITDDDFERSRAFNFLNEIKKRFQTTYGSRAQTALPYAMNSEFSSVLAAQ 66
Cdd:cd14818    54 YTFHYYLNKGLYFVVITDEQELRQELFQTLNLLLKEFNSLHGSEVITKNIEDDLEEFESYLDIK 117
R-SNARE_VAMP7 cd15871
SNARE motif of VAMP7; The VAMP-7 (vesicle-associated membrane protein 7, also called ...
 77-97 2.04e-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: 2.04e-07
                          10        20
                  ....*....|....*....|.
gi 2462632055  77 DKVMETQAQVDELKGIMVRNI 97
Cdd:cd15871     1 DKVSKVQGQLDELKGIMVKNI 21
SNC1 COG5143
Synaptobrevin/VAMP-like protein [Intracellular trafficking and secretion];
3-97 6.95e-06

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


Pssm-ID: 227472 [Multi-domain]  Cd Length: 190  Bit Score: 45.11  E-value: 6.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462632055   3 YLFHY-ICQDRIVYLCITDDDFERSRAFNFLNEIKKRFQTTYGSRAQT--ALPYAMNsEFSSVLAaqlKHHSENKGLDKV 79
Cdd:COG5143    56 YFFHYlKMSSGIVYVPISDKEYPNKLAYGYLNSIATEFLKSSALEQLIddTVGIMRV-NIDKVIE---KGYRDPSIQDKL 131

                          90
                  ....*....|....*...
gi 2462632055  80 METQAQVDELKGIMVRNI 97
Cdd:COG5143   132 DQLQQELEETKRVLNKNI 149
R-SNARE cd15843
SNARE motif, subgroup R-SNARE; SNARE (soluble N-ethylmaleimide-sensitive factor attachment ...
 77-97 1.20e-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: 1.20e-03
                          10        20
                  ....*....|....*....|.
gi 2462632055  77 DKVMETQAQVDELKGIMVRNI 97
Cdd:cd15843     1 DKLSKVQEQVDEVKDVMQENI 21
Synaptobrevin pfam00957
Synaptobrevin;
75-97 1.87e-03

Synaptobrevin;


Pssm-ID: 395764  Cd Length: 89  Bit Score: 36.36  E-value: 1.87e-03
                          10        20
                  ....*....|....*....|...
gi 2462632055  75 GLDKVMETQAQVDELKGIMVRNI 97
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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