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Conserved domains on  [gi|569007509|ref|XP_006527259|]
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vesicle transport through interaction with t-SNAREs homolog 1A isoform X13 [Mus musculus]

Protein Classification

v-SNARE domain-containing protein( domain architecture ID 10523371)

v-SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) domain-containing protein is part of various SNARE complexes involved in multiple transport pathways

CATH:  1.20.58.400
Gene Ontology:  GO:0005484|GO:0006906|GO:0015031
SCOP:  4000986
TCDB:  1.F.1

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
V-SNARE pfam05008
Vesicle transport v-SNARE protein N-terminus; V-SNARE proteins are required for protein ...
12-90 1.80e-23

Vesicle transport v-SNARE protein N-terminus; V-SNARE proteins are required for protein traffic between eukaryotic organelles. The v-SNAREs on transport vesicles interact with t-SNAREs on target membranes in order to facilitate this. This domain is the N-terminal half of the V-Snare proteins.


:

Pssm-ID: 461516  Cd Length: 79  Bit Score: 87.28  E-value: 1.80e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569007509   12 FAVLTAEITSKIARVPRLPPDEKKQMVANVEKQLEEARELLEQMDLEVREIPPQSRGMYSNRMRSYKQEMGKLETDFKR 90
Cdd:pfam05008   1 FKELLAEITRKLARLSSLPGEERKAALREIERKLDEAEELLDQMELEVRNLPSSERSKYKAKLREYKSDLKKLKKELKR 79
SNARE super family cl22856
SNARE motif; SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) ...
129-149 3.64e-05

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 cd15891:

Pssm-ID: 473982  Cd Length: 62  Bit Score: 39.59  E-value: 3.64e-05
                         10        20
                 ....*....|....*....|.
gi 569007509 129 TERLERSSRRLEAGYQIAVET 149
Cdd:cd15891    1 TERLERSSRRLEDGYRIAVET 21
 
Name Accession Description Interval E-value
V-SNARE pfam05008
Vesicle transport v-SNARE protein N-terminus; V-SNARE proteins are required for protein ...
12-90 1.80e-23

Vesicle transport v-SNARE protein N-terminus; V-SNARE proteins are required for protein traffic between eukaryotic organelles. The v-SNAREs on transport vesicles interact with t-SNAREs on target membranes in order to facilitate this. This domain is the N-terminal half of the V-Snare proteins.


Pssm-ID: 461516  Cd Length: 79  Bit Score: 87.28  E-value: 1.80e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569007509   12 FAVLTAEITSKIARVPRLPPDEKKQMVANVEKQLEEARELLEQMDLEVREIPPQSRGMYSNRMRSYKQEMGKLETDFKR 90
Cdd:pfam05008   1 FKELLAEITRKLARLSSLPGEERKAALREIERKLDEAEELLDQMELEVRNLPSSERSKYKAKLREYKSDLKKLKKELKR 79
SNARE_Vti1a cd15891
SNARE motif of Vti1b-like; Vti1a (vesicle transport through interaction with t-SNAREs homolog ...
129-149 3.64e-05

SNARE motif of Vti1b-like; Vti1a (vesicle transport through interaction with t-SNAREs homolog 1A) belongs to the Qb subgroup of SNAREs (soluble N-ethylmaleimide-sensitive factor attachment protein receptor). Vti1a interacts with syntaxin 16 (Qa), syntaxin 6 (Qc), and the lysosomal R-SNARE VAMP4 to form an endosomal SNARE core complex that mediates transport from the early endosomes to the TGN (trans-Golgi network). SNARE 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-, 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. Examples for members of the Qb SNAREs are N-terminal domains of SNAP23 and SNAP25, Vti1, Sec20 and GS27.


Pssm-ID: 277244  Cd Length: 62  Bit Score: 39.59  E-value: 3.64e-05
                         10        20
                 ....*....|....*....|.
gi 569007509 129 TERLERSSRRLEAGYQIAVET 149
Cdd:cd15891    1 TERLERSSRRLEDGYRIAVET 21
 
Name Accession Description Interval E-value
V-SNARE pfam05008
Vesicle transport v-SNARE protein N-terminus; V-SNARE proteins are required for protein ...
12-90 1.80e-23

Vesicle transport v-SNARE protein N-terminus; V-SNARE proteins are required for protein traffic between eukaryotic organelles. The v-SNAREs on transport vesicles interact with t-SNAREs on target membranes in order to facilitate this. This domain is the N-terminal half of the V-Snare proteins.


Pssm-ID: 461516  Cd Length: 79  Bit Score: 87.28  E-value: 1.80e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569007509   12 FAVLTAEITSKIARVPRLPPDEKKQMVANVEKQLEEARELLEQMDLEVREIPPQSRGMYSNRMRSYKQEMGKLETDFKR 90
Cdd:pfam05008   1 FKELLAEITRKLARLSSLPGEERKAALREIERKLDEAEELLDQMELEVRNLPSSERSKYKAKLREYKSDLKKLKKELKR 79
SNARE_Vti1a cd15891
SNARE motif of Vti1b-like; Vti1a (vesicle transport through interaction with t-SNAREs homolog ...
129-149 3.64e-05

SNARE motif of Vti1b-like; Vti1a (vesicle transport through interaction with t-SNAREs homolog 1A) belongs to the Qb subgroup of SNAREs (soluble N-ethylmaleimide-sensitive factor attachment protein receptor). Vti1a interacts with syntaxin 16 (Qa), syntaxin 6 (Qc), and the lysosomal R-SNARE VAMP4 to form an endosomal SNARE core complex that mediates transport from the early endosomes to the TGN (trans-Golgi network). SNARE 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-, 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. Examples for members of the Qb SNAREs are N-terminal domains of SNAP23 and SNAP25, Vti1, Sec20 and GS27.


Pssm-ID: 277244  Cd Length: 62  Bit Score: 39.59  E-value: 3.64e-05
                         10        20
                 ....*....|....*....|.
gi 569007509 129 TERLERSSRRLEAGYQIAVET 149
Cdd:cd15891    1 TERLERSSRRLEDGYRIAVET 21
 
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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