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Conserved domains on  [gi|17549917|ref|NP_509586|]
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Golgi SNAP receptor complex member 2 homolog memb-1 [Caenorhabditis elegans]

Protein Classification

golgi SNAP receptor complex member 2 family protein( domain architecture ID 10205203)

golgi SNAP receptor complex member 2 (GOSR2) family protein similar to human GOSR2 which is involved in ER-to-Golgi trafficking; belongs to the Qb-SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) family of vesicle docking proteins

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SNARE_GS27 cd15863
SNARE motif of GS27; GS27 (also known as Bos1, EPM6, golgi SNAP receptor complex member 2 or ...
 121-185 2.95e-23

SNARE motif of GS27; GS27 (also known as Bos1, EPM6, golgi SNAP receptor complex member 2 or GOSR2) is a member of the Qb subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins. GS27 forms a complex together with Bet1 (Qc), syntaxin-5 (Qa) and Sec22B (R-SNARE). This complex regulates the early secretory pathway of eukaryotic cells at the level of the transport from endoplasmic reticulum (ER) to the ER-Golgi intermediate compartment (ERGIC). 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 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.


:

Pssm-ID: 277216  Cd Length: 66  Bit Score: 88.35  E-value: 2.95e-23
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17549917 121 DHELLLNDRLQSSHTHLDDLISQGSAVLENLKSQHLNLRGVGRKMHEIGQALGLSNSTLQVIDRR 185
Cdd:cd15863   2 DGLLQENSSLQNSHRQLDDLLESGSAILENLRDQRSTLKGAQRKLLDIANTLGLSNTVMRLIERR 66
 
Name Accession Description Interval E-value
SNARE_GS27 cd15863
SNARE motif of GS27; GS27 (also known as Bos1, EPM6, golgi SNAP receptor complex member 2 or ...
 121-185 2.95e-23

SNARE motif of GS27; GS27 (also known as Bos1, EPM6, golgi SNAP receptor complex member 2 or GOSR2) is a member of the Qb subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins. GS27 forms a complex together with Bet1 (Qc), syntaxin-5 (Qa) and Sec22B (R-SNARE). This complex regulates the early secretory pathway of eukaryotic cells at the level of the transport from endoplasmic reticulum (ER) to the ER-Golgi intermediate compartment (ERGIC). 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 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.


Pssm-ID: 277216  Cd Length: 66  Bit Score: 88.35  E-value: 2.95e-23
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17549917 121 DHELLLNDRLQSSHTHLDDLISQGSAVLENLKSQHLNLRGVGRKMHEIGQALGLSNSTLQVIDRR 185
Cdd:cd15863   2 DGLLQENSSLQNSHRQLDDLLESGSAILENLRDQRSTLKGAQRKLLDIANTLGLSNTVMRLIERR 66
V-SNARE_C pfam12352
Snare region anchored in the vesicle membrane C-terminus; Within the SNARE proteins ...
 121-186 2.17e-18

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: 75.72  E-value: 2.17e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17549917   121 DHELLLNDRLQSSHTHLDDLISQGSAVLENLKSQHLNLRGVGRKMHEIGQALGLSNSTLQVIDRRV 186
Cdd:pfam12352   1 ERLLREHDRLKNSHRIADETISIGQAILEDLHSQRETLKRARNKLHNTDNRLGKSNSTLRLINRRR 66
 
Name Accession Description Interval E-value
SNARE_GS27 cd15863
SNARE motif of GS27; GS27 (also known as Bos1, EPM6, golgi SNAP receptor complex member 2 or ...
 121-185 2.95e-23

SNARE motif of GS27; GS27 (also known as Bos1, EPM6, golgi SNAP receptor complex member 2 or GOSR2) is a member of the Qb subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins. GS27 forms a complex together with Bet1 (Qc), syntaxin-5 (Qa) and Sec22B (R-SNARE). This complex regulates the early secretory pathway of eukaryotic cells at the level of the transport from endoplasmic reticulum (ER) to the ER-Golgi intermediate compartment (ERGIC). 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 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.


Pssm-ID: 277216  Cd Length: 66  Bit Score: 88.35  E-value: 2.95e-23
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17549917 121 DHELLLNDRLQSSHTHLDDLISQGSAVLENLKSQHLNLRGVGRKMHEIGQALGLSNSTLQVIDRR 185
Cdd:cd15863   2 DGLLQENSSLQNSHRQLDDLLESGSAILENLRDQRSTLKGAQRKLLDIANTLGLSNTVMRLIERR 66
V-SNARE_C pfam12352
Snare region anchored in the vesicle membrane C-terminus; Within the SNARE proteins ...
 121-186 2.17e-18

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: 75.72  E-value: 2.17e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17549917   121 DHELLLNDRLQSSHTHLDDLISQGSAVLENLKSQHLNLRGVGRKMHEIGQALGLSNSTLQVIDRRV 186
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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