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Conserved domains on  [gi|24648015|ref|NP_650739|]
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golgi SNARE, 28 kDa [Drosophila melanogaster]

Protein Classification

SNARE domain-containing protein( domain architecture ID 366304)

SNARE domain-containing protein such as SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins, which interact to form a SNARE complex that mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SNARE super family cl22856
SNARE motif; SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) ...
 142-207 5.88e-22

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 cd15864:

Pssm-ID: 473982  Cd Length: 66  Bit Score: 85.57  E-value: 5.88e-22
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24648015 142 REMYLKESGHLNSASHLVNDQINIAIETRDHLHAQRQAFKRLQTRFNDISNRFPLISSLIQRINIK 207
Cdd:cd15864   1 TELYLKEHEHLRNSDRLIDEQISIAMATKENLTSQRGMLKSITSRMNTLANRFPAINSLIQKINLR 66
 
Name Accession Description Interval E-value
SNARE_GS28 cd15864
SNARE motif of GS28; GS28 (also known as golgi SNAP receptor complex member 1 or GOSR1) forms ...
 142-207 5.88e-22

SNARE motif of GS28; GS28 (also known as golgi SNAP receptor complex member 1 or GOSR1) forms complexes with syntaxin-5 (Qa), Ykt6 (R-SNARE) and either Bet1 (Qc) or GS15 (Qc). These complexes regulate 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. GS28 is a member of the Qb 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: 277217  Cd Length: 66  Bit Score: 85.57  E-value: 5.88e-22
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24648015 142 REMYLKESGHLNSASHLVNDQINIAIETRDHLHAQRQAFKRLQTRFNDISNRFPLISSLIQRINIK 207
Cdd:cd15864   1 TELYLKEHEHLRNSDRLIDEQISIAMATKENLTSQRGMLKSITSRMNTLANRFPAINSLIQKINLR 66
V-SNARE_C pfam12352
Snare region anchored in the vesicle membrane C-terminus; Within the SNARE proteins ...
 143-208 1.37e-15

Snare region anchored in the vesicle membrane C-terminus; Within the SNARE proteins interactions in the C-terminal half of the SNARE helix are critical to the driving of membrane fusion; whereas interactions in the N-terminal half of the SNARE domain are important for promoting priming or docking of the vesicle pfam05008.


Pssm-ID: 289148  Cd Length: 66  Bit Score: 68.79  E-value: 1.37e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24648015   143 EMYLKESGHLNSASHLVNDQINIAIETRDHLHAQRQAFKRLQTRFNDISNRFPLISSLIQRINIKK 208
Cdd:pfam12352   1 ERLLREHDRLKNSHRIADETISIGQAILEDLHSQRETLKRARNKLHNTDNRLGKSNSTLRLINRRR 66
 
Name Accession Description Interval E-value
SNARE_GS28 cd15864
SNARE motif of GS28; GS28 (also known as golgi SNAP receptor complex member 1 or GOSR1) forms ...
 142-207 5.88e-22

SNARE motif of GS28; GS28 (also known as golgi SNAP receptor complex member 1 or GOSR1) forms complexes with syntaxin-5 (Qa), Ykt6 (R-SNARE) and either Bet1 (Qc) or GS15 (Qc). These complexes regulate 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. GS28 is a member of the Qb 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: 277217  Cd Length: 66  Bit Score: 85.57  E-value: 5.88e-22
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24648015 142 REMYLKESGHLNSASHLVNDQINIAIETRDHLHAQRQAFKRLQTRFNDISNRFPLISSLIQRINIK 207
Cdd:cd15864   1 TELYLKEHEHLRNSDRLIDEQISIAMATKENLTSQRGMLKSITSRMNTLANRFPAINSLIQKINLR 66
V-SNARE_C pfam12352
Snare region anchored in the vesicle membrane C-terminus; Within the SNARE proteins ...
 143-208 1.37e-15

Snare region anchored in the vesicle membrane C-terminus; Within the SNARE proteins interactions in the C-terminal half of the SNARE helix are critical to the driving of membrane fusion; whereas interactions in the N-terminal half of the SNARE domain are important for promoting priming or docking of the vesicle pfam05008.


Pssm-ID: 289148  Cd Length: 66  Bit Score: 68.79  E-value: 1.37e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24648015   143 EMYLKESGHLNSASHLVNDQINIAIETRDHLHAQRQAFKRLQTRFNDISNRFPLISSLIQRINIKK 208
Cdd:pfam12352   1 ERLLREHDRLKNSHRIADETISIGQAILEDLHSQRETLKRARNKLHNTDNRLGKSNSTLRLINRRR 66
 
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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