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Conserved domains on  [gi|1039729672|ref|XP_017177357|]
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syntaxin-6 isoform X2 [Mus musculus]

Protein Classification

SNARE domain-containing protein; syntaxin family protein( domain architecture ID 10205156)

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; syntaxin family protein similar to syntaxin 5 (Syn5) that regulates the transport from the ER to the Golgi, as well as the early/recycling endosomes to the trans-Golgi network and participates in the assembly of transitional ER and the Golgi, lipid droplet fusion, and cytokinesis

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SNARE_Syntaxin6 cd15851
SNARE motif of syntaxin 6; Syntaxin 6 forms a complex with syntaxin 16 (Qa), Vti1a (Qb) and ...
 65-130 1.10e-27

SNARE motif of syntaxin 6; Syntaxin 6 forms a complex with syntaxin 16 (Qa), Vti1a (Qb) and VAMP4 (R-SNARE) and is involved in the regulation of recycling of early endosomes to the trans-Golgi network (TGN). Syntaxin 6 and its yeast homolog TLG1 are members of the Qc subgroup of 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 complexes mediate 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: 277204  Cd Length: 66  Bit Score: 97.56  E-value: 1.10e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039729672  65 VEQQDEQLELVSGSIGVLKNMSQRIGGELEEQAVMLDDFSHELESTQSRLDNVMKKLAKVSHMTSD 130
Cdd:cd15851     1 MREQDEQLDGVGGTVGNLREQAQLIGDELEEQAELLDDLDHEVDRTESRLDRGMKKMAKVIRKNED 66
 
Name Accession Description Interval E-value
SNARE_Syntaxin6 cd15851
SNARE motif of syntaxin 6; Syntaxin 6 forms a complex with syntaxin 16 (Qa), Vti1a (Qb) and ...
 65-130 1.10e-27

SNARE motif of syntaxin 6; Syntaxin 6 forms a complex with syntaxin 16 (Qa), Vti1a (Qb) and VAMP4 (R-SNARE) and is involved in the regulation of recycling of early endosomes to the trans-Golgi network (TGN). Syntaxin 6 and its yeast homolog TLG1 are members of the Qc subgroup of 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 complexes mediate 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: 277204  Cd Length: 66  Bit Score: 97.56  E-value: 1.10e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039729672  65 VEQQDEQLELVSGSIGVLKNMSQRIGGELEEQAVMLDDFSHELESTQSRLDNVMKKLAKVSHMTSD 130
Cdd:cd15851     1 MREQDEQLDGVGGTVGNLREQAQLIGDELEEQAELLDDLDHEVDRTESRLDRGMKKMAKVIRKNED 66
t_SNARE smart00397
Helical region found in SNAREs; All alpha-helical motifs that form twisted and parallel ...
 60-124 3.94e-09

Helical region found in SNAREs; All alpha-helical motifs that form twisted and parallel four-helix bundles in target soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein (SNAP) receptor proteins. This motif found in "Q-SNAREs".


Pssm-ID: 197699 [Multi-domain]  Cd Length: 66  Bit Score: 49.89  E-value: 3.94e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039729672   60 QQQLIVEQQDEQLELVSGSIGVLKNMSQRIGGELEEQAVMLDDFSHELESTQSRLDNVMKKLAKV 124
Cdd:smart00397   2 QALAREEERDEELEQLEKSIQELKQIFLDMGTELEEQGEQLDRIEDNVDDADVNLKKANKRLKKA 66
SNARE pfam05739
SNARE domain; Most if not all vesicular membrane fusion events in eukaryotic cells are ...
 98-138 1.26e-05

SNARE domain; Most if not all vesicular membrane fusion events in eukaryotic cells are believed to be mediated by a conserved fusion machinery, the SNARE [soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein (SNAP) receptors] machinery. The SNARE domain is thought to act as a protein-protein interaction module in the assembly of a SNARE protein complex.


Pssm-ID: 461727 [Multi-domain]  Cd Length: 52  Bit Score: 40.48  E-value: 1.26e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1039729672  98 VMLDDFSHELESTQSRLDNVMKKLAKVSHMTSDRRQWCAIA 138
Cdd:pfam05739   1 EMLDRIDTNVENAQSNVERAQKELKKAVKYQKSNRKLKCII 41
 
Name Accession Description Interval E-value
SNARE_Syntaxin6 cd15851
SNARE motif of syntaxin 6; Syntaxin 6 forms a complex with syntaxin 16 (Qa), Vti1a (Qb) and ...
 65-130 1.10e-27

SNARE motif of syntaxin 6; Syntaxin 6 forms a complex with syntaxin 16 (Qa), Vti1a (Qb) and VAMP4 (R-SNARE) and is involved in the regulation of recycling of early endosomes to the trans-Golgi network (TGN). Syntaxin 6 and its yeast homolog TLG1 are members of the Qc subgroup of 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 complexes mediate 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: 277204  Cd Length: 66  Bit Score: 97.56  E-value: 1.10e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039729672  65 VEQQDEQLELVSGSIGVLKNMSQRIGGELEEQAVMLDDFSHELESTQSRLDNVMKKLAKVSHMTSD 130
Cdd:cd15851     1 MREQDEQLDGVGGTVGNLREQAQLIGDELEEQAELLDDLDHEVDRTESRLDRGMKKMAKVIRKNED 66
SNARE_Qc cd15841
SNARE motif, subgroup Qc; SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein ...
 66-123 4.39e-13

SNARE motif, subgroup Qc; 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). Qc-, as well as Qa- and Qb-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 Qc SNAREs are C-terminal domains of SNAP23 and SNAP25, syntaxin 8, syntaxin 6, and Bet1.


Pssm-ID: 277194 [Multi-domain]  Cd Length: 59  Bit Score: 60.26  E-value: 4.39e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039729672  66 EQQDEQLELVSGSIGVLKNMSQRIGGELEEQAVMLDDFSHELESTQSRLDNVMKKLAK 123
Cdd:cd15841     2 KEQDEQLDELSGSVGRLKNIALAINEELDLQNRLLDDLDEDVDKTQSRLKKVNKKLKK 59
SNARE_SYN8 cd15859
SNARE motif of SYN8; Fungal SYN8 is a member of the Qc subfamily of SNARE (soluble ...
 66-130 2.58e-10

SNARE motif of SYN8; Fungal SYN8 is a member of the Qc subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) protein family presetn in the endosomes. 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). Qc-, as well as Qa- and Qb-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: 277212  Cd Length: 68  Bit Score: 53.31  E-value: 2.58e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039729672  66 EQQDEQLELVSGSIGVLKNMSQRIGGELEEQAVMLDDFSHELESTQSRLDNVMKKLAKVSHMTSD 130
Cdd:cd15859     2 LEQDEHLDHLSASIRRQHELSLQINDELDEQNELLDDLENGVDRTGRRLNRARRRLDKFRRKARE 66
SNARE cd00193
SNARE motif; SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) ...
 70-123 4.39e-10

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.


Pssm-ID: 277192  Cd Length: 54  Bit Score: 52.39  E-value: 4.39e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039729672  70 EQLELVSGSIGVLKNMSQRIGGELEEQAVMLDDFSHELESTQSRLDNVMKKLAK 123
Cdd:cd00193     1 ESLEQLEASIGELKDIGRDMAMELEEQGEQLDRIEERAESTQARVSRAEKSLAK 54
t_SNARE smart00397
Helical region found in SNAREs; All alpha-helical motifs that form twisted and parallel ...
 60-124 3.94e-09

Helical region found in SNAREs; All alpha-helical motifs that form twisted and parallel four-helix bundles in target soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein (SNAP) receptor proteins. This motif found in "Q-SNAREs".


Pssm-ID: 197699 [Multi-domain]  Cd Length: 66  Bit Score: 49.89  E-value: 3.94e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039729672   60 QQQLIVEQQDEQLELVSGSIGVLKNMSQRIGGELEEQAVMLDDFSHELESTQSRLDNVMKKLAKV 124
Cdd:smart00397   2 QALAREEERDEELEQLEKSIQELKQIFLDMGTELEEQGEQLDRIEDNVDDADVNLKKANKRLKKA 66
SNARE_Syntaxin8 cd15852
SNARE motif of syntaxin 8; Syntaxin 8 forms a complex with syntaxin 7 (Qa), Vti1b (Qb) and ...
 66-116 2.26e-06

SNARE motif of syntaxin 8; Syntaxin 8 forms a complex with syntaxin 7 (Qa), Vti1b (Qb) and either VAMP7 or VAMP8 (R-SNARE) and is involved in the transport from early endosomes to the lysosome. Syntaxin 8 is a member of the Qc subgroup of 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 complexes mediate 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: 277205 [Multi-domain]  Cd Length: 59  Bit Score: 42.60  E-value: 2.26e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039729672  66 EQQDEQLELVSGSIGVLKNMSQRIGGELEEQAVMLDDFSHELESTQSRLDN 116
Cdd:cd15852     2 QEQDQGLDALSSIISRQKQIGQAIGDEVDDQNEIIDDLADGMDRTDARLRR 52
SNARE_VAM7 cd15858
SNARE motif of VAM7; Fungal VAM7 (vacuolar morphogenesis protein 7) is a member of the Qc ...
 65-123 3.31e-06

SNARE motif of VAM7; Fungal VAM7 (vacuolar morphogenesis protein 7) is a member of the Qc subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) protein family involved in vacuolar protein transport and membrane fusion. 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). Qc-, as well as Qa- and Qb-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: 277211 [Multi-domain]  Cd Length: 59  Bit Score: 42.10  E-value: 3.31e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039729672  65 VEQQDEQLELVSGSIGVLKNMSQRIGGELEEQAVMLDDFSHELESTQSRLDNVMKKLAK 123
Cdd:cd15858     1 MQEQDQQLEQLRKIVQRQKELGLAINQELEEQNELLDELDEDVDRTGGKLRVANKRAKR 59
SNARE_Bet1 cd15853
SNARE motif of Bet1; Bet1 forms a complexes with GS27 (Qb), syntaxin-5 (Qa) and Sec22B ...
 66-121 3.83e-06

SNARE motif of Bet1; Bet1 forms a complexes with GS27 (Qb), syntaxin-5 (Qa) and Sec22B (R-SNARE) or GS28 (Qb), syntaxin-5 (Qa) and Ykt6 (R-SNARE). These complexes 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) and from ERGIC to the cis-Golgi, respectively. Bet1 is a member of the Qc subgroup of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins, which consist of coiled-coil helices (called SNARE motifs) which mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complexes mediate 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: 277206  Cd Length: 59  Bit Score: 42.10  E-value: 3.83e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039729672  66 EQQDEQLELVSGSIGVLKNMSQRIGGELEEQAVMLDDFSHELESTQSRLDNVMKKL 121
Cdd:cd15853     2 SQNDRRLDELSSKVSALKSLTIDIGDEVRDQNKLLDGMGDDFDSTGGLLGGTMKRL 57
SNARE pfam05739
SNARE domain; Most if not all vesicular membrane fusion events in eukaryotic cells are ...
 98-138 1.26e-05

SNARE domain; Most if not all vesicular membrane fusion events in eukaryotic cells are believed to be mediated by a conserved fusion machinery, the SNARE [soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein (SNAP) receptors] machinery. The SNARE domain is thought to act as a protein-protein interaction module in the assembly of a SNARE protein complex.


Pssm-ID: 461727 [Multi-domain]  Cd Length: 52  Bit Score: 40.48  E-value: 1.26e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1039729672  98 VMLDDFSHELESTQSRLDNVMKKLAKVSHMTSDRRQWCAIA 138
Cdd:pfam05739   1 EMLDRIDTNVENAQSNVERAQKELKKAVKYQKSNRKLKCII 41
SNARE_SNAP23C cd15884
C-terminal SNARE motif of SNAP23; C-terminal SNARE motifs of SNAP23, a member of the Qb/Qc ...
 66-115 3.16e-03

C-terminal SNARE motif of SNAP23; C-terminal SNARE motifs of SNAP23, a member of the Qb/Qc subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins. SNAP23 interacts with Syntaxin-4 (Qa) and the R-SNARE VAMP8. The complex plays a role in exocytosis of secretory granule. Qb/Qc SNAREs consist of 2 coiled-coil helices (called SNARE motifs, one belonging to the Qb subgroup and one belonging to the Qc subgroup), which mediate the interactions with other SNARE proteins, and a transmembrane domain. In general, 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. Other members of the Qb/Qc SNAREs are SNAP25, SNAP29, SNAP47 and SEC9.


Pssm-ID: 277237  Cd Length: 59  Bit Score: 34.36  E-value: 3.16e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039729672  66 EQQDEQLELVSGSIGVLKNMSQRIGGELEEQAVMLDDFSHELESTQSRLD 115
Cdd:cd15884     2 DEMDENLTQVGSILGNLKSMALDMGNELDKQNKQIGRINEKADMNSDRID 51
 
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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