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Conserved domains on  [gi|4507285|ref|NP_003756|]
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syntaxin-10 isoform 1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SNARE_NTD_STX10 cd21446
N-terminal domain of syntaxin-10; Syntaxin-10 (STX10), also called Syn10, is part of a soluble ...
5-107 3.03e-65

N-terminal domain of syntaxin-10; Syntaxin-10 (STX10), also called Syn10, is part of a soluble NSF attachment protein receptor (SNARE) complex involved in vesicular transport from the late endosomes to the trans-Golgi network, such as the transport of mannose 6-phosphate receptors from endosomes to the Golgi after delivering lysosomal enzymes to the endocytic pathway. This model corresponds to the N-terminal domain of STX10, which is a regulatory domain named Habc.


:

Pssm-ID: 410572 [Multi-domain]  Cd Length: 103  Bit Score: 198.08  E-value: 3.03e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507285    5 DPFFVVRGEVQKAVNTARGLYQRWCELLQESAAVGREELDWTTNELRNGLRSIEWDLEDLEETIGIVEANPGKFKLPAGD 84
Cdd:cd21446   1 DPFFVVKGEVQKAVNTARGLYQRWCELLQESVAVSKEELDWTTNELRNSLRSIEWDLEDLEETIGIVESNPRKFKIDPGE 80
                        90       100
                ....*....|....*....|...
gi 4507285   85 LQERKVFVERMREAVQEMKDHMV 107
Cdd:cd21446  81 LAERRAFVERTRESVKEMKDHMA 103
SNARE_Syntaxin6 cd15851
SNARE motif of syntaxin 6; Syntaxin 6 forms a complex with syntaxin 16 (Qa), Vti1a (Qb) and ...
160-225 8.05e-26

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: 96.02  E-value: 8.05e-26
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4507285  160 MDEQDQQLEMVSGSIQVLKHMSGRVGEELDEQGIMLDAFAQEMDHTQSRMDGVLRKLAKVSHMTSD 225
Cdd:cd15851   1 MREQDEQLDGVGGTVGNLREQAQLIGDELEEQAELLDDLDHEVDRTESRLDRGMKKMAKVIRKNED 66
 
Name Accession Description Interval E-value
SNARE_NTD_STX10 cd21446
N-terminal domain of syntaxin-10; Syntaxin-10 (STX10), also called Syn10, is part of a soluble ...
5-107 3.03e-65

N-terminal domain of syntaxin-10; Syntaxin-10 (STX10), also called Syn10, is part of a soluble NSF attachment protein receptor (SNARE) complex involved in vesicular transport from the late endosomes to the trans-Golgi network, such as the transport of mannose 6-phosphate receptors from endosomes to the Golgi after delivering lysosomal enzymes to the endocytic pathway. This model corresponds to the N-terminal domain of STX10, which is a regulatory domain named Habc.


Pssm-ID: 410572 [Multi-domain]  Cd Length: 103  Bit Score: 198.08  E-value: 3.03e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507285    5 DPFFVVRGEVQKAVNTARGLYQRWCELLQESAAVGREELDWTTNELRNGLRSIEWDLEDLEETIGIVEANPGKFKLPAGD 84
Cdd:cd21446   1 DPFFVVKGEVQKAVNTARGLYQRWCELLQESVAVSKEELDWTTNELRNSLRSIEWDLEDLEETIGIVESNPRKFKIDPGE 80
                        90       100
                ....*....|....*....|...
gi 4507285   85 LQERKVFVERMREAVQEMKDHMV 107
Cdd:cd21446  81 LAERRAFVERTRESVKEMKDHMA 103
Syntaxin-6_N pfam09177
Syntaxin 6, N-terminal; Members of this family, which are found in the amino terminus of ...
5-103 1.58e-39

Syntaxin 6, N-terminal; Members of this family, which are found in the amino terminus of various SNARE proteins, adopt a structure consisting of an antiparallel three-helix bundle. Their exact function has not been determined, though it is known that they regulate the SNARE motif, as well as mediate various protein-protein interactions involved in membrane-transport.


Pssm-ID: 462706 [Multi-domain]  Cd Length: 99  Bit Score: 132.30  E-value: 1.58e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507285      5 DPFFVVRGEVQKAVNTARGLYQRWCELLQESAAVGREELDWTTNELRNGLRSIEWDLEDLEETIGIVEANPGKFKLPAGD 84
Cdd:pfam09177   1 DPFFEVKEEVQESLDKLESLYRSWLRLLSLTSSSSSPELDELRRELRTALESLEWDLEDLEEAVRIVESNPSKFGLDEAE 80
                          90
                  ....*....|....*....
gi 4507285     85 LQERKVFVERMREAVQEMK 103
Cdd:pfam09177  81 LSRRRQFVEAIRNEISDMK 99
SNARE_Syntaxin6 cd15851
SNARE motif of syntaxin 6; Syntaxin 6 forms a complex with syntaxin 16 (Qa), Vti1a (Qb) and ...
160-225 8.05e-26

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: 96.02  E-value: 8.05e-26
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4507285  160 MDEQDQQLEMVSGSIQVLKHMSGRVGEELDEQGIMLDAFAQEMDHTQSRMDGVLRKLAKVSHMTSD 225
Cdd:cd15851   1 MREQDEQLDGVGGTVGNLREQAQLIGDELEEQAELLDDLDHEVDRTESRLDRGMKKMAKVIRKNED 66
t_SNARE smart00397
Helical region found in SNAREs; All alpha-helical motifs that form twisted and parallel ...
155-219 2.45e-10

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: 54.90  E-value: 2.45e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4507285     155 TQQLIMDEQDQQLEMVSGSIQVLKHMSGRVGEELDEQGIMLDAFAQEMDHTQSRMDGVLRKLAKV 219
Cdd:smart00397   2 QALAREEERDEELEQLEKSIQELKQIFLDMGTELEEQGEQLDRIEDNVDDADVNLKKANKRLKKA 66
SNARE pfam05739
SNARE domain; Most if not all vesicular membrane fusion events in eukaryotic cells are ...
194-233 1.08e-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: 41.64  E-value: 1.08e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 4507285    194 MLDAFAQEMDHTQSRMDGVLRKLAKVSHMTSDRRQWCAIA 233
Cdd:pfam05739   2 MLDRIDTNVENAQSNVERAQKELKKAVKYQKSNRKLKCII 41
 
Name Accession Description Interval E-value
SNARE_NTD_STX10 cd21446
N-terminal domain of syntaxin-10; Syntaxin-10 (STX10), also called Syn10, is part of a soluble ...
5-107 3.03e-65

N-terminal domain of syntaxin-10; Syntaxin-10 (STX10), also called Syn10, is part of a soluble NSF attachment protein receptor (SNARE) complex involved in vesicular transport from the late endosomes to the trans-Golgi network, such as the transport of mannose 6-phosphate receptors from endosomes to the Golgi after delivering lysosomal enzymes to the endocytic pathway. This model corresponds to the N-terminal domain of STX10, which is a regulatory domain named Habc.


Pssm-ID: 410572 [Multi-domain]  Cd Length: 103  Bit Score: 198.08  E-value: 3.03e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507285    5 DPFFVVRGEVQKAVNTARGLYQRWCELLQESAAVGREELDWTTNELRNGLRSIEWDLEDLEETIGIVEANPGKFKLPAGD 84
Cdd:cd21446   1 DPFFVVKGEVQKAVNTARGLYQRWCELLQESVAVSKEELDWTTNELRNSLRSIEWDLEDLEETIGIVESNPRKFKIDPGE 80
                        90       100
                ....*....|....*....|...
gi 4507285   85 LQERKVFVERMREAVQEMKDHMV 107
Cdd:cd21446  81 LAERRAFVERTRESVKEMKDHMA 103
SNARE_NTD_STX6_STX10 cd21443
N-terminal domain of syntaxin-6, syntaxin-10, and similar proteins; This subfamily includes ...
5-106 4.43e-58

N-terminal domain of syntaxin-6, syntaxin-10, and similar proteins; This subfamily includes two soluble NSF attachment protein receptor (SNARE) proteins, syntaxin-6 (STX6) and syntaxin-10 (STX10). STX6 is involved in intracellular vesicle trafficking. STX10, also called Syn10, is involved in vesicular transport from the late endosomes to the trans-Golgi network. This model corresponds to the N-terminal domain of STX6 and STX10, which is a regulatory domain named Habc.


Pssm-ID: 410569 [Multi-domain]  Cd Length: 103  Bit Score: 179.72  E-value: 4.43e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507285    5 DPFFVVRGEVQKAVNTARGLYQRWCELLQESAAVGREELDWTTNELRNGLRSIEWDLEDLEETIGIVEANPGKFKLPAGD 84
Cdd:cd21443   1 DPFFVVKDEVEKALNKAQELYERWRELQDEDSTSSNEELEWTTNELRNSLRSIEWDLEDLEETIGIVEKNPSKFKLDAEE 80
                        90       100
                ....*....|....*....|..
gi 4507285   85 LQERKVFVERMREAVQEMKDHM 106
Cdd:cd21443  81 IQARRQFIEETRQEVKEIKDEL 102
SNARE_NTD_STX6 cd21447
N-terminal domain of syntaxin-6; Syntaxin-6 (STX6) is a component of a soluble NSF attachment ...
5-106 4.56e-52

N-terminal domain of syntaxin-6; Syntaxin-6 (STX6) is a component of a soluble NSF attachment protein receptor (SNARE) complex involved in intracellular vesicle trafficking and in the fusion of retrograde transport carriers with the trans-Golgi network (TGN). This model corresponds to N-terminal domain of STX6, which is a regulatory domain named Habc.


Pssm-ID: 410573 [Multi-domain]  Cd Length: 103  Bit Score: 164.33  E-value: 4.56e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507285    5 DPFFVVRGEVQKAVNTARGLYQRWCELLQESAAVGREELDWTTNELRNGLRSIEWDLEDLEETIGIVEANPGKFKLPAGD 84
Cdd:cd21447   1 DPFFVVKGEVQKAVNTAQGLFQRWTELLQDPSSATKEEIDWTTNELRNSLRSIEWDLEDLDETISIVEANPRKFNLDPTE 80
                        90       100
                ....*....|....*....|..
gi 4507285   85 LQERKVFVERMREAVQEMKDHM 106
Cdd:cd21447  81 LSIRKAFITSTRQVVREMKDQM 102
Syntaxin-6_N pfam09177
Syntaxin 6, N-terminal; Members of this family, which are found in the amino terminus of ...
5-103 1.58e-39

Syntaxin 6, N-terminal; Members of this family, which are found in the amino terminus of various SNARE proteins, adopt a structure consisting of an antiparallel three-helix bundle. Their exact function has not been determined, though it is known that they regulate the SNARE motif, as well as mediate various protein-protein interactions involved in membrane-transport.


Pssm-ID: 462706 [Multi-domain]  Cd Length: 99  Bit Score: 132.30  E-value: 1.58e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507285      5 DPFFVVRGEVQKAVNTARGLYQRWCELLQESAAVGREELDWTTNELRNGLRSIEWDLEDLEETIGIVEANPGKFKLPAGD 84
Cdd:pfam09177   1 DPFFEVKEEVQESLDKLESLYRSWLRLLSLTSSSSSPELDELRRELRTALESLEWDLEDLEEAVRIVESNPSKFGLDEAE 80
                          90
                  ....*....|....*....
gi 4507285     85 LQERKVFVERMREAVQEMK 103
Cdd:pfam09177  81 LSRRRQFVEAIRNEISDMK 99
SNARE_NTD_STX6-like cd21442
N-terminal domain of syntaxin-6 and similar proteins; The family includes soluble NSF ...
5-106 1.19e-34

N-terminal domain of syntaxin-6 and similar proteins; The family includes soluble NSF attachment protein receptor (SNARE) proteins, syntaxin-6 (STX6) and syntaxin-10 (STX10), and their homologs found in fungi and plants, such as Tlg1p, AtSYP61, and similar proteins. STX6 is involved in intracellular vesicle trafficking. STX10, also called Syn10, is involved in vesicular transport from the late endosomes to the trans-Golgi network. Tlg1p, also called syntaxin TLG1, is a SNARE protein (of Qc type) involved in membrane fusion probably in retrograde traffic of cytosolic double-membrane vesicles derived from both, early and possibly late endosomes/PVC (prevacuolar compartment) back to the trans-Golgi network (TGN or late Golgi). It has been reported to function both as a (target membrane) t-SNARE and as a (vesicle) v-SNARE. AtSYP61, also called osmotic stress-sensitive mutant 1 (OSM1), is a vesicle trafficking syntaxin protein that functions in the secretory pathway. It is involved in osmotic stress tolerance and in abscisic acid (ABA) regulation of stomatal responses in Arabidopsis.


Pssm-ID: 410568 [Multi-domain]  Cd Length: 103  Bit Score: 119.72  E-value: 1.19e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507285    5 DPFFVVRGEVQKAVNTARGLYQRWCELLQESAAVGREELDWTTNELRNGLRSIEWDLEDLEETIGIVEANPGKFKLPAGD 84
Cdd:cd21442   1 DPFFEAKEEVQASLDRAESLYRSWLRIRKTAQSGSSEELSDARNELKTTLGTLEWDLEDLEESVRVVEADGKRFGISEDE 80
                        90       100
                ....*....|....*....|..
gi 4507285   85 LQERKVFVERMREAVQEMKDHM 106
Cdd:cd21442  81 VSRRRQFVRRIRQQIEAMKKDV 102
SNARE_Syntaxin6 cd15851
SNARE motif of syntaxin 6; Syntaxin 6 forms a complex with syntaxin 16 (Qa), Vti1a (Qb) and ...
160-225 8.05e-26

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: 96.02  E-value: 8.05e-26
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4507285  160 MDEQDQQLEMVSGSIQVLKHMSGRVGEELDEQGIMLDAFAQEMDHTQSRMDGVLRKLAKVSHMTSD 225
Cdd:cd15851   1 MREQDEQLDGVGGTVGNLREQAQLIGDELEEQAELLDDLDHEVDRTESRLDRGMKKMAKVIRKNED 66
SNARE_NTD_AtSYP61-like cd21445
N-terminal domain of Arabidopsis thaliana syntaxin-61 and similar proteins; Arabidopsis ...
5-104 8.52e-16

N-terminal domain of Arabidopsis thaliana syntaxin-61 and similar proteins; Arabidopsis thaliana syntaxin-61 (AtSYP61), also called osmotic stress-sensitive mutant 1 (OSM1), is a vesicle trafficking syntaxin protein that functions in the secretory pathway. It is involved in osmotic stress tolerance and in abscisic acid (ABA) regulation of stomatal responses in Arabidopsis. This model corresponds to the N-terminal domain of AtSYP61, which shows high sequence similarity with the N-terminal domain of yeast Tlg1p, a soluble NSF attachment protein receptor (SNARE) protein (of Qc type) involved in membrane fusion.


Pssm-ID: 410571 [Multi-domain]  Cd Length: 99  Bit Score: 70.74  E-value: 8.52e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507285    5 DPFFVVRGEVQKAVNTARGLYQRWcELLQESAAvgreELDWTTNELRNGLRSIEWDLEDLEETIGIVEANPGKFKLPAGD 84
Cdd:cd21445   2 DPFYLVRDEIQESVDKLQQSFRRW-EGLPAGSA----ERARLARELESDCESLEWQVDELDRAVDVAERDPARFGLSAAE 76
                        90       100
                ....*....|....*....|
gi 4507285   85 LQERKVFVERMREAVQEMKD 104
Cdd:cd21445  77 LESRRRWTSATRDQVSGIKE 96
SNARE_Qc cd15841
SNARE motif, subgroup Qc; SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein ...
160-218 1.32e-14

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: 66.43  E-value: 1.32e-14
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 4507285  160 MDEQDQQLEMVSGSIQVLKHMSGRVGEELDEQGIMLDAFAQEMDHTQSRMDGVLRKLAK 218
Cdd:cd15841   1 MKEQDEQLDELSGSVGRLKNIALAINEELDLQNRLLDDLDEDVDKTQSRLKKVNKKLKK 59
SNARE_SYN8 cd15859
SNARE motif of SYN8; Fungal SYN8 is a member of the Qc subfamily of SNARE (soluble ...
160-225 1.02e-11

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: 58.70  E-value: 1.02e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4507285  160 MDEQDQQLEMVSGSIQVLKHMSGRVGEELDEQGIMLDAFAQEMDHTQSRMDGVLRKLAKVSHMTSD 225
Cdd:cd15859   1 LLEQDEHLDHLSASIRRQHELSLQINDELDEQNELLDDLENGVDRTGRRLNRARRRLDKFRRKARE 66
t_SNARE smart00397
Helical region found in SNAREs; All alpha-helical motifs that form twisted and parallel ...
155-219 2.45e-10

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: 54.90  E-value: 2.45e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4507285     155 TQQLIMDEQDQQLEMVSGSIQVLKHMSGRVGEELDEQGIMLDAFAQEMDHTQSRMDGVLRKLAKV 219
Cdd:smart00397   2 QALAREEERDEELEQLEKSIQELKQIFLDMGTELEEQGEQLDRIEDNVDDADVNLKKANKRLKKA 66
SNARE_NTD_Tlg1p-like cd21444
N-terminal domain of t-SNARE affecting a late Golgi compartment protein 1 and similar proteins; ...
5-106 1.28e-09

N-terminal domain of t-SNARE affecting a late Golgi compartment protein 1 and similar proteins; t-SNARE affecting a late Golgi compartment protein 1 (Tlg1p), also called syntaxin TLG1, is a soluble NSF attachment protein receptor (SNARE) protein (of Qc type) involved in membrane fusion, probably in retrograde traffic of cytosolic double-membrane vesicles derived from both, early and possibly late endosomes/PVC (prevacuolar compartment) back to the trans-Golgi network (TGN or late Golgi). It has been reported to function both as a (target membrane) t-SNARE and as a (vesicle) v-SNARE. The model corresponds to the N-terminal domain of Tlg1p, which consists of a three-helix bundle.


Pssm-ID: 410570 [Multi-domain]  Cd Length: 93  Bit Score: 53.74  E-value: 1.28e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507285    5 DPFFVVRGEVQKAVNTARGLYQRWcellqesaavGREELDWTTNELRNGLRSIEWDLEDLEETIGIVEANPGKFKLPAGD 84
Cdd:cd21444   1 DPFNQVQEDAWSQLERLRQLLTSY----------LRIPTNEAKSDFENNIQELEETIEDLKQSVEISEADPERFGLDEEE 70
                        90       100
                ....*....|....*....|..
gi 4507285   85 LQERKVFVERMREAVQEMKDHM 106
Cdd:cd21444  71 ISERERIVAELESQLDDLKEEW 92
SNARE_VAM7 cd15858
SNARE motif of VAM7; Fungal VAM7 (vacuolar morphogenesis protein 7) is a member of the Qc ...
160-218 2.06e-08

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: 49.42  E-value: 2.06e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 4507285  160 MDEQDQQLEMVSGSIQVLKHMSGRVGEELDEQGIMLDAFAQEMDHTQSRMDGVLRKLAK 218
Cdd:cd15858   1 MQEQDQQLEQLRKIVQRQKELGLAINQELEEQNELLDELDEDVDRTGGKLRVANKRAKR 59
SNARE_Syntaxin8 cd15852
SNARE motif of syntaxin 8; Syntaxin 8 forms a complex with syntaxin 7 (Qa), Vti1b (Qb) and ...
160-209 4.71e-08

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: 48.38  E-value: 4.71e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 4507285  160 MDEQDQQLEMVSGSIQVLKHMSGRVGEELDEQGIMLDAFAQEMDHTQSRM 209
Cdd:cd15852   1 IQEQDQGLDALSSIISRQKQIGQAIGDEVDDQNEIIDDLADGMDRTDARL 50
SNARE cd00193
SNARE motif; SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) ...
165-218 2.09e-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.


Pssm-ID: 277192  Cd Length: 54  Bit Score: 46.61  E-value: 2.09e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 4507285  165 QQLEMVSGSIQVLKHMSGRVGEELDEQGIMLDAFAQEMDHTQSRMDGVLRKLAK 218
Cdd:cd00193   1 ESLEQLEASIGELKDIGRDMAMELEEQGEQLDRIEERAESTQARVSRAEKSLAK 54
SNARE pfam05739
SNARE domain; Most if not all vesicular membrane fusion events in eukaryotic cells are ...
194-233 1.08e-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: 41.64  E-value: 1.08e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 4507285    194 MLDAFAQEMDHTQSRMDGVLRKLAKVSHMTSDRRQWCAIA 233
Cdd:pfam05739   2 MLDRIDTNVENAQSNVERAQKELKKAVKYQKSNRKLKCII 41
SNARE_SNAP25C_23C cd15855
C-terminal SNARE motif of SNAP25 and SNAP23; C-terminal SNARE motifs of SNAP25 and SNAP23, ...
161-218 2.51e-04

C-terminal SNARE motif of SNAP25 and SNAP23; C-terminal SNARE motifs of SNAP25 and SNAP23, members of the Qb/Qc subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins. SNAP23 interacts with STX4 (Qa) and the lysosomal R-SNARE VAMP8. The complex plays a role in transport of secretory granule from trans-Golgi network to the plasma membrane. SNAP25 interacts with Syntaxin-1 (Qa) and the R-SNARE VAMP2 (also called synaptobrevin-2). The complex plays a role in transport of secretory granule from trans-Golgi network to the plasma membrane. 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 SNAP29, SNAP47 and SEC9.


Pssm-ID: 277208  Cd Length: 59  Bit Score: 38.26  E-value: 2.51e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 4507285  161 DEQDQQLEMVSGSIQVLKHMSGRVGEELDEQGIMLDAFAQEMDHTQSRMDGVLRKLAK 218
Cdd:cd15855   2 DEMDENLQQVSGILGNLRHMALDMGNEIDTQNRQLDRIDEKADSNKTRIEAANDRATK 59
SNARE_Bet1 cd15853
SNARE motif of Bet1; Bet1 forms a complexes with GS27 (Qb), syntaxin-5 (Qa) and Sec22B ...
161-216 3.85e-03

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: 34.79  E-value: 3.85e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 4507285  161 DEQDQQLEMVSGSIQVLKHMSGRVGEELDEQGIMLDAFAQEMDHTQSRMDGVLRKL 216
Cdd:cd15853   2 SQNDRRLDELSSKVSALKSLTIDIGDEVRDQNKLLDGMGDDFDSTGGLLGGTMKRL 57
SNARE_SNAP23C cd15884
C-terminal SNARE motif of SNAP23; C-terminal SNARE motifs of SNAP23, a member of the Qb/Qc ...
161-211 4.05e-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: 34.74  E-value: 4.05e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 4507285  161 DEQDQQLEMVSGSIQVLKHMSGRVGEELDEQGIMLDAFAQEMDHTQSRMDG 211
Cdd:cd15884   2 DEMDENLTQVGSILGNLKSMALDMGNELDKQNKQIGRINEKADMNSDRIDE 52
SNARE_SNAP25C cd15885
C-terminal SNARE motif of SNAP25; C-terminal SNARE motifs of SNAP25, a member of the Qb/Qc ...
161-210 9.62e-03

C-terminal SNARE motif of SNAP25; C-terminal SNARE motifs of SNAP25, a member of the Qb/Qc subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins. SNAP25 interacts with Syntaxin-1 (Qa) and the R-SNARE VAMP2 (also called synaptobrevin-2). The complex plays a role in transport of secretory granule from trans-Golgi network to the plasma membrane. 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 SNAP23, SNAP29, SNAP47 and SEC9.


Pssm-ID: 277238  Cd Length: 59  Bit Score: 33.86  E-value: 9.62e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 4507285  161 DEQDQQLEMVSGSIQVLKHMSGRVGEELDEQGIMLDAFAQEMDHTQSRMD 210
Cdd:cd15885   2 DEMEENLGQVSGMIGNLRNMAIDMGSEIESQNRQIDRINEKAESNETRID 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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