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Conserved domains on  [gi|1907132071|ref|XP_036017396|]
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syntaxin-3 isoform X2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Syntaxin super family cl38013
Syntaxin; Syntaxins are the prototype family of SNARE proteins. They usually consist of three ...
 1-129 5.14e-45

Syntaxin; Syntaxins are the prototype family of SNARE proteins. They usually consist of three main regions - a C-terminal transmembrane region, a central SNARE domain which is characteriztic of and conserved in all syntaxins (pfam05739), and an N-terminal domain that is featured in this entry. This domain varies between syntaxin isoforms; in syntaxin 1A it is found as three alpha-helices with a left-handed twist. It may fold back on the SNARE domain to allow the molecule to adopt a 'closed' configuration that prevents formation of the core fusion complex - it thus has an auto-inhibitory role. The function of syntaxins is determined by their localization. They are involved in neuronal exocytosis, ER-Golgi transport and Golgi-endosome transport, for example. They also interact with other proteins as well as those involved in SNARE complexes. These include vesicle coat proteins, Rab GTPases, and tethering factors.


The actual alignment was detected with superfamily member pfam00804:

Pssm-ID: 459942 [Multi-domain]  Cd Length: 203  Bit Score: 148.48  E-value: 5.14e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132071   1 MEKHIEEDEV-----RSSADLRIRKSQHSVLSRKFVEVMTKYNEAQVDFRERSKGRIQRQLEI-TGKKTTDEELEEMLES 74
Cdd:pfam00804  67 LDKSNAENEKkpgcgPGSAVDRIRRSQTAALRKKLKEVMAEYNELRERIREEYKEVIQRQYETvTGKEVSEEEIEEMIET 146

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907132071  75 GNPAIFTSGII--DSQISKQALSEIEGRHKDIVRLESSIKELHDMFMDIAMLVENQG 129
Cdd:pfam00804 147 GSESVFQKAILeqGRGQARSALSEIEERHKELKELESSLKELHQIFLDMAVLVEAQG 203
SNARE super family cl22856
SNARE motif; SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) ...
 97-163 4.33e-11

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 cd15876:

Pssm-ID: 473982 [Multi-domain]  Cd Length: 67  Bit Score: 56.59  E-value: 4.33e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907132071  97 IEGRHKDIVRLESSIKELHDMFMDIAMLVENQGEMLDNIELNVMHTVDHVEKARDETKRAMKYQGQA 163
Cdd:cd15876     1 IKERETAIQQLEADILDVNQIFKDLAMMIHDQGDMIDSIEANVESAEVHVERASEQLQRAAYYQKKS 67
 
Name Accession Description Interval E-value
Syntaxin pfam00804
Syntaxin; Syntaxins are the prototype family of SNARE proteins. They usually consist of three ...
 1-129 5.14e-45

Syntaxin; Syntaxins are the prototype family of SNARE proteins. They usually consist of three main regions - a C-terminal transmembrane region, a central SNARE domain which is characteriztic of and conserved in all syntaxins (pfam05739), and an N-terminal domain that is featured in this entry. This domain varies between syntaxin isoforms; in syntaxin 1A it is found as three alpha-helices with a left-handed twist. It may fold back on the SNARE domain to allow the molecule to adopt a 'closed' configuration that prevents formation of the core fusion complex - it thus has an auto-inhibitory role. The function of syntaxins is determined by their localization. They are involved in neuronal exocytosis, ER-Golgi transport and Golgi-endosome transport, for example. They also interact with other proteins as well as those involved in SNARE complexes. These include vesicle coat proteins, Rab GTPases, and tethering factors.


Pssm-ID: 459942 [Multi-domain]  Cd Length: 203  Bit Score: 148.48  E-value: 5.14e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132071   1 MEKHIEEDEV-----RSSADLRIRKSQHSVLSRKFVEVMTKYNEAQVDFRERSKGRIQRQLEI-TGKKTTDEELEEMLES 74
Cdd:pfam00804  67 LDKSNAENEKkpgcgPGSAVDRIRRSQTAALRKKLKEVMAEYNELRERIREEYKEVIQRQYETvTGKEVSEEEIEEMIET 146

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907132071  75 GNPAIFTSGII--DSQISKQALSEIEGRHKDIVRLESSIKELHDMFMDIAMLVENQG 129
Cdd:pfam00804 147 GSESVFQKAILeqGRGQARSALSEIEERHKELKELESSLKELHQIFLDMAVLVEAQG 203
SNARE_syntaxin3 cd15881
SNARE motif of syntaxin 3; Syntaxin 3 (STX3) has been shown to form a complex with VAMP8 ...
 93-160 1.36e-40

SNARE motif of syntaxin 3; Syntaxin 3 (STX3) has been shown to form a complex with VAMP8 (R-SNARE) and SNAP-23 (Qb/c) in mast cells. Mutations have been implicated in human microvillus inclusion disease (MVID), a disorder of the differentiation of intestinal epithelium. Syntaxin 3 is a member of the Qa 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: 277234  Cd Length: 69  Bit Score: 132.84  E-value: 1.36e-40
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907132071  93 ALSEIEGRHKDIVRLESSIKELHDMFMDIAMLVENQGEMLDNIELNVMHTVDHVEKARDETKRAMKYQ 160
Cdd:cd15881     1 ALSEIEGRHKDIVRLESSIKELHDMFVDIAMLVENQGEMLDNIELNVMKTVDHVEKARDETKKAVKYQ 68
COG5074 COG5074
t-SNARE complex subunit, syntaxin [Intracellular trafficking, secretion, and vesicular ...
 16-168 1.22e-20

t-SNARE complex subunit, syntaxin [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 227406 [Multi-domain]  Cd Length: 280  Bit Score: 87.25  E-value: 1.22e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132071  16 LRIRKSQHSVLSRKFVEVMTKYNEAQVDFRERSKGRIQRQLEITGKKTTDEELEEML-ESGNPAIFTSGIIDSQIS---K 91
Cdd:COG5074    95 LANKQAQAENVRQKFLKLIQDYRIIDSNYREEEKEQARRQYIIAQPEATEDEVEAAInDVNGQQVFSQALLNANRRgeaK 174

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907132071  92 QALSEIEGRHKDIVRLESSIKELHDMFMDIAMLVENQGEMLDNIELNVMHTVDHVEKARDETKRAMKYQGQARKNQL 168
Cdd:COG5074   175 TALAEVQARHQEIKKIEKTMAELTQLFNDMEELVIEQQENVDVIDKNVEDAQENVEQGVGHTDKAVKSARAARKKKI 251
t_SNARE smart00397
Helical region found in SNAREs; All alpha-helical motifs that form twisted and parallel ...
 91-156 1.44e-13

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: 62.99  E-value: 1.44e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907132071   91 KQALSEIEGRHKDIVRLESSIKELHDMFMDIAMLVENQGEMLDNIELNVMHTVDHVEKARDETKRA 156
Cdd:smart00397   1 QQALAREEERDEELEQLEKSIQELKQIFLDMGTELEEQGEQLDRIEDNVDDADVNLKKANKRLKKA 66
SNARE_syntaxin12 cd15876
SNARE motif of syntaxin 12; Syntaxin 12 (STX12, also known as STX13 and STX14) forms a complex ...
 97-163 4.33e-11

SNARE motif of syntaxin 12; Syntaxin 12 (STX12, also known as STX13 and STX14) forms a complex with SNAP25 (Qb/Qc) or SNAP29 (Qb/Qc) and VAMP2 or VAMP3 (R-SNARE) and plays a role in plasma membrane to early endosome transport. Syntaxin 12 is a member of the Qa 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: 277229 [Multi-domain]  Cd Length: 67  Bit Score: 56.59  E-value: 4.33e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907132071  97 IEGRHKDIVRLESSIKELHDMFMDIAMLVENQGEMLDNIELNVMHTVDHVEKARDETKRAMKYQGQA 163
Cdd:cd15876     1 IKERETAIQQLEADILDVNQIFKDLAMMIHDQGDMIDSIEANVESAEVHVERASEQLQRAAYYQKKS 67
SNARE pfam05739
SNARE domain; Most if not all vesicular membrane fusion events in eukaryotic cells are ...
 130-165 6.70e-09

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: 50.11  E-value: 6.70e-09
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1907132071 130 EMLDNIELNVMHTVDHVEKARDETKRAMKYQGQARK 165
Cdd:pfam05739   1 EMLDRIDTNVENAQSNVERAQKELKKAVKYQKSNRK 36
 
Name Accession Description Interval E-value
Syntaxin pfam00804
Syntaxin; Syntaxins are the prototype family of SNARE proteins. They usually consist of three ...
 1-129 5.14e-45

Syntaxin; Syntaxins are the prototype family of SNARE proteins. They usually consist of three main regions - a C-terminal transmembrane region, a central SNARE domain which is characteriztic of and conserved in all syntaxins (pfam05739), and an N-terminal domain that is featured in this entry. This domain varies between syntaxin isoforms; in syntaxin 1A it is found as three alpha-helices with a left-handed twist. It may fold back on the SNARE domain to allow the molecule to adopt a 'closed' configuration that prevents formation of the core fusion complex - it thus has an auto-inhibitory role. The function of syntaxins is determined by their localization. They are involved in neuronal exocytosis, ER-Golgi transport and Golgi-endosome transport, for example. They also interact with other proteins as well as those involved in SNARE complexes. These include vesicle coat proteins, Rab GTPases, and tethering factors.


Pssm-ID: 459942 [Multi-domain]  Cd Length: 203  Bit Score: 148.48  E-value: 5.14e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132071   1 MEKHIEEDEV-----RSSADLRIRKSQHSVLSRKFVEVMTKYNEAQVDFRERSKGRIQRQLEI-TGKKTTDEELEEMLES 74
Cdd:pfam00804  67 LDKSNAENEKkpgcgPGSAVDRIRRSQTAALRKKLKEVMAEYNELRERIREEYKEVIQRQYETvTGKEVSEEEIEEMIET 146

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907132071  75 GNPAIFTSGII--DSQISKQALSEIEGRHKDIVRLESSIKELHDMFMDIAMLVENQG 129
Cdd:pfam00804 147 GSESVFQKAILeqGRGQARSALSEIEERHKELKELESSLKELHQIFLDMAVLVEAQG 203
SNARE_syntaxin3 cd15881
SNARE motif of syntaxin 3; Syntaxin 3 (STX3) has been shown to form a complex with VAMP8 ...
 93-160 1.36e-40

SNARE motif of syntaxin 3; Syntaxin 3 (STX3) has been shown to form a complex with VAMP8 (R-SNARE) and SNAP-23 (Qb/c) in mast cells. Mutations have been implicated in human microvillus inclusion disease (MVID), a disorder of the differentiation of intestinal epithelium. Syntaxin 3 is a member of the Qa 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: 277234  Cd Length: 69  Bit Score: 132.84  E-value: 1.36e-40
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907132071  93 ALSEIEGRHKDIVRLESSIKELHDMFMDIAMLVENQGEMLDNIELNVMHTVDHVEKARDETKRAMKYQ 160
Cdd:cd15881     1 ALSEIEGRHKDIVRLESSIKELHDMFVDIAMLVENQGEMLDNIELNVMKTVDHVEKARDETKKAVKYQ 68
SynN cd00179
Syntaxin N-terminus domain; syntaxins are nervous system-specific proteins implicated in the ...
 1-84 4.31e-30

Syntaxin N-terminus domain; syntaxins are nervous system-specific proteins implicated in the docking of synaptic vesicles with the presynaptic plasma membrane; they are a family of receptors for intracellular transport vesicles; each target membrane may be identified by a specific member of the syntaxin family; syntaxins contain a moderately well conserved amino-terminal domain, called Habc, whose structure is an antiparallel three-helix bundle; a linker of about 30 amino acids connects this to the carboxy-terminal region, designated H3 (t_SNARE), of the syntaxin cytoplasmic domain; the highly conserved H3 region forms a single, long alpha-helix when it is part of the core SNARE complex and anchors the protein on the cytoplasmic surface of cellular membranes; H3 is not included in defining this domain


Pssm-ID: 238105 [Multi-domain]  Cd Length: 151  Bit Score: 108.53  E-value: 4.31e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132071   1 MEKHIEEDEVR-SSADLRIRKSQHSVLSRKFVEVMTKYNEAQVDFRERSKGRIQRQLEITGKKTTDEELEEMLESGNPAI 79
Cdd:cd00179    67 LEESNEQNEALnGSSVDRIRKTQHSGLSKKFVEVMTEFNKAQRKYRERYKERIQRQLEITGGEATDEELEDMLESGNSEI 146


                  ....*
gi 1907132071  80 FTSGI 84
Cdd:cd00179   147 FTSQI 151
SNARE_syntaxin2 cd15882
SNARE motif of syntaxin 2; Syntaxin 2 (STX2), also known as epimorphin (EPM or EPIM), may ...
 93-160 1.29e-29

SNARE motif of syntaxin 2; Syntaxin 2 (STX2), also known as epimorphin (EPM or EPIM), may interact with SNAP-23 (Qb/c) and genetic varioations are associated with type 1 von Willebrand disease (VWD). Syntaxin 2 is a member of the Qa 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: 277235  Cd Length: 69  Bit Score: 105.13  E-value: 1.29e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907132071  93 ALSEIEGRHKDIVRLESSIKELHDMFMDIAMLVENQGEMLDNIELNVMHTVDHVEKARDETKRAMKYQ 160
Cdd:cd15882     1 ALNEIESRHKDIMKLESSIRELHDMFVDMAMLVETQGEMINNIEKNVHNAVEYVEHAKEETKKAVKYQ 68
SNARE_syntaxin1-like cd15848
SNARE motif of syntaxin 1 and related proteins; SNARE (soluble N-ethylmaleimide-sensitive ...
 93-155 1.90e-29

SNARE motif of syntaxin 1 and related proteins; 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-, 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. This subgroup of the Qa SNAREs includes syntaxin 1, syntaxin 11, syntaxin 19, syntaxin 2, syntaxin 3, syntaxin 4 and related proteins.


Pssm-ID: 277201  Cd Length: 63  Bit Score: 104.15  E-value: 1.90e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907132071  93 ALSEIEGRHKDIVRLESSIKELHDMFMDIAMLVENQGEMLDNIELNVMHTVDHVEKARDETKR 155
Cdd:cd15848     1 ALADIEERHQDILKLEKSIRELHQMFLDMAVLVESQGELIDNIEYNVEKAKDYVEKGNEELKK 63
SNARE_syntaxin1 cd15880
SNARE motif of syntaxin 1; Syntaxin-1 belongs to the Qa subgroup of SNAREs and interacts with ...
 93-160 8.79e-29

SNARE motif of syntaxin 1; Syntaxin-1 belongs to the Qa subgroup of SNAREs and interacts with SNAP-25 (Qb/Qc) and the R-SNARE VAMP2 (also called synaptobrevin-2). The complex plays a role in exocytosis of synaptic vesicles. 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: 277233  Cd Length: 69  Bit Score: 102.97  E-value: 8.79e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907132071  93 ALSEIEGRHKDIVRLESSIKELHDMFMDIAMLVENQGEMLDNIELNVMHTVDHVEKARDETKRAMKYQ 160
Cdd:cd15880     1 ALSEIEARHNDIIKLENSIRELHDMFMDMAMLVESQGEMIDRIEYNVEHAVDYVERAVSDTKKAVKYQ 68
COG5074 COG5074
t-SNARE complex subunit, syntaxin [Intracellular trafficking, secretion, and vesicular ...
 16-168 1.22e-20

t-SNARE complex subunit, syntaxin [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 227406 [Multi-domain]  Cd Length: 280  Bit Score: 87.25  E-value: 1.22e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132071  16 LRIRKSQHSVLSRKFVEVMTKYNEAQVDFRERSKGRIQRQLEITGKKTTDEELEEML-ESGNPAIFTSGIIDSQIS---K 91
Cdd:COG5074    95 LANKQAQAENVRQKFLKLIQDYRIIDSNYREEEKEQARRQYIIAQPEATEDEVEAAInDVNGQQVFSQALLNANRRgeaK 174

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907132071  92 QALSEIEGRHKDIVRLESSIKELHDMFMDIAMLVENQGEMLDNIELNVMHTVDHVEKARDETKRAMKYQGQARKNQL 168
Cdd:COG5074   175 TALAEVQARHQEIKKIEKTMAELTQLFNDMEELVIEQQENVDVIDKNVEDAQENVEQGVGHTDKAVKSARAARKKKI 251
SNARE_syntaxin4 cd15883
SNARE motif of syntaxin 4; Syntaxin-4 forms a complex with SNAP-23 (Qb/Qc) and R-SNAREs VAMP8, ...
 93-154 1.83e-18

SNARE motif of syntaxin 4; Syntaxin-4 forms a complex with SNAP-23 (Qb/Qc) and R-SNAREs VAMP8, VAMP2 and VAMP7 which plays a role in exocytosis of secetory granule. Syntaxin 4 is member of the Qa 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: 277236  Cd Length: 63  Bit Score: 76.14  E-value: 1.83e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907132071  93 ALSEIEGRHKDIVRLESSIKELHDMFMDIAMLVENQGEMLDNIELNVMHTVDHVEKARDETK 154
Cdd:cd15883     1 ALNEIEARHSEIQKLERSIRELHDMFTYLAMEVEAQGEMIDRIEKNILSSADYVEKAQEHVK 62
SNARE_syntaxin11 cd15878
SNARE motif of syntaxin 11; Syntaxin 11 (also known as STX11, FHL4, HLH4, HPLH4) is present on ...
 93-155 1.66e-17

SNARE motif of syntaxin 11; Syntaxin 11 (also known as STX11, FHL4, HLH4, HPLH4) is present on endosomal membranes, including late endosomes and lysosomes in macrophages, and has been shown to bind Vti1b and regulate the availability of Vti1b to form other SNARE-complexes. Mutations in human STX11 has been linked to familial hemophagocytic lymphohistiocytosis type-4 (FHL-4), an autosomal recessive disorder of immune dysregulation. Syntaxin 11 is a member of the Qa 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: 277231  Cd Length: 63  Bit Score: 73.34  E-value: 1.66e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907132071  93 ALSEIEGRHKDIVRLESSIKELHDMFMDIAMLVENQGEMLDNIELNVMHTVDHVEKARDETKR 155
Cdd:cd15878     1 ALNEIETRHKELLELESRIREVHELFLQMALLVEEQADTLNNIELNVEKTQDYVGKAKAQVKK 63
SNARE_Qa cd15840
SNARE motif, subgroup Qa; SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein ...
 97-155 1.41e-15

SNARE motif, subgroup Qa; 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-, 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 Qa SNAREs are syntaxin 18, syntaxin 5, syntaxin 16, and syntaxin 1.


Pssm-ID: 277193 [Multi-domain]  Cd Length: 59  Bit Score: 68.31  E-value: 1.41e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907132071  97 IEGRHKDIVRLESSIKELHDMFMDIAMLVENQGEMLDNIELNVMHTVDHVEKARDETKR 155
Cdd:cd15840     1 IEEREEEIREIESSIGEVNEIFKDLATLVTEQGEQIDNIENNIEEAAANTEEANKELRK 59
SNARE_Sso1 cd15849
SNARE motif of Sso1; Saccharomyces cerevisiae SNARE protein Sso1p forms a complex with ...
 94-156 3.20e-14

SNARE motif of Sso1; Saccharomyces cerevisiae SNARE protein Sso1p forms a complex with synaptobrevin homolog Snc1p (R-SNARE) and the SNAP-25 homolog Sec9p (Qb/c) which is involved in exocytosis. Sso1 is member of the Qa 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: 277202  Cd Length: 64  Bit Score: 64.86  E-value: 3.20e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907132071  94 LSEIEGRHKDIVRLESSIKELHDMFMDIAMLVENQGEMLDNIELNVMHTVDHVEKARDETKRA 156
Cdd:cd15849     1 LGEVQARHNEIQRIEQTLTELAQLFNDMATLVEQQDEVIQQIEQNAEEVETDLEKGNVHLEKA 63
SNARE_syntaxin19 cd15879
SNARE motif of syntaxin 19; Syntaxin 19 has been shown to have the potential to form SNARE ...
 94-154 3.92e-14

SNARE motif of syntaxin 19; Syntaxin 19 has been shown to have the potential to form SNARE complexes with SNAP-23, 25 and 29 (Qb/Qc) and VAMP3 and VAMP8 (R-SNARE), indicating a role in post-Golgi trafficking or plasma membrane fusion. Syntaxin 19 is member of the Qa 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: 277232  Cd Length: 63  Bit Score: 64.47  E-value: 3.92e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907132071  94 LSEIEGRHKDIVRLESSIKELHDMFMDIAMLVENQGEMLDNIELNVMHTVDHVEKARDETK 154
Cdd:cd15879     2 LSEIEQRHKELVSLENQIKDLKDLFIQISLLVEEQGEMINNIEISVNNTQEYVQASKEKFG 62
t_SNARE smart00397
Helical region found in SNAREs; All alpha-helical motifs that form twisted and parallel ...
 91-156 1.44e-13

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: 62.99  E-value: 1.44e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907132071   91 KQALSEIEGRHKDIVRLESSIKELHDMFMDIAMLVENQGEMLDNIELNVMHTVDHVEKARDETKRA 156
Cdd:smart00397   1 QQALAREEERDEELEQLEKSIQELKQIFLDMGTELEEQGEQLDRIEDNVDDADVNLKKANKRLKKA 66
SNARE_syntaxin12 cd15876
SNARE motif of syntaxin 12; Syntaxin 12 (STX12, also known as STX13 and STX14) forms a complex ...
 97-163 4.33e-11

SNARE motif of syntaxin 12; Syntaxin 12 (STX12, also known as STX13 and STX14) forms a complex with SNAP25 (Qb/Qc) or SNAP29 (Qb/Qc) and VAMP2 or VAMP3 (R-SNARE) and plays a role in plasma membrane to early endosome transport. Syntaxin 12 is a member of the Qa 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: 277229 [Multi-domain]  Cd Length: 67  Bit Score: 56.59  E-value: 4.33e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907132071  97 IEGRHKDIVRLESSIKELHDMFMDIAMLVENQGEMLDNIELNVMHTVDHVEKARDETKRAMKYQGQA 163
Cdd:cd15876     1 IKERETAIQQLEADILDVNQIFKDLAMMIHDQGDMIDSIEANVESAEVHVERASEQLQRAAYYQKKS 67
SNARE_syntaxin16 cd15845
SNARE motif of syntaxin 16; Syntaxin 16 is located in trans-Golgi network (TGN) and regulated ...
 97-155 1.21e-10

SNARE motif of syntaxin 16; Syntaxin 16 is located in trans-Golgi network (TGN) and regulated by the SM protein Vps45p. It forms a complex with syntaxin 6 (Qc), Vti1a (Qb) and VAMP4 (R-SNARE) and is involved in the regulation of recycling of early endosomes to the trans-Golgi network (TGN). Syntaxin 16 is a member of the Qa 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: 277198  Cd Length: 59  Bit Score: 55.16  E-value: 1.21e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907132071  97 IEGRHKDIVRLESSIKELHDMFMDIAMLVENQGEMLDNIELNVMHTVDHVEKARDETKR 155
Cdd:cd15845     1 IQERDREIAKIVESINELAEIFKDLATLVIEQGTILDRIDYNIEQTATRVEKGVKELKK 59
COG5325 COG5325
t-SNARE complex subunit, syntaxin [Intracellular trafficking and secretion];
50-165 2.12e-10

t-SNARE complex subunit, syntaxin [Intracellular trafficking and secretion];


Pssm-ID: 227635 [Multi-domain]  Cd Length: 283  Bit Score: 58.70  E-value: 2.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132071  50 GRIQRQLEITGKKTTDEELEEMLESGNPAIFTSGIIDSQISKQALSE----IEGRHKDIVRLESSIKELHDMFMDIAMLV 125
Cdd:COG5325   139 VLQAKFLRNKNNDQHPLEEEEDEESLSSLGSQQTLQQQGLSNEELEYqqilITERDEEIKNLARGIYELNEIFRDLGSLV 218

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1907132071 126 ENQGEMLDNIELNVMHTVDHVEKARDETKRAMKYQGQARK 165
Cdd:COG5325   219 GEQGELVDRIDFNIENTSDNLKNANKELEKAPAHQRRTKK 258
SynN smart00503
Syntaxin N-terminal domain; Three-helix domain that (in Sso1p) slows the rate of its reaction ...
 1-49 2.86e-10

Syntaxin N-terminal domain; Three-helix domain that (in Sso1p) slows the rate of its reaction with the SNAP-25 homologue Sec9p


Pssm-ID: 214699 [Multi-domain]  Cd Length: 117  Bit Score: 55.81  E-value: 2.86e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1907132071    1 MEKHIEEDEVRSSADLRIRKSQHSVLSRKFVEVMTKYNEAQVDFRERSK 49
Cdd:smart00503  69 LEKENLENRASGSASDRTRKAQTEKLRKKFKEVMNEFQRLQRKYREREK 117
SNARE_syntaxin7 cd15875
SNARE motif of syntaxin 7; Syntaxin 7 forms a complex with syntaxin 8 (Qc), Vti1b (Qb) and ...
 97-156 8.29e-10

SNARE motif of syntaxin 7; Syntaxin 7 forms a complex with syntaxin 8 (Qc), Vti1b (Qb) and either VAMP7 or VAMP8 (R-SNARE) and is involved in the transport from early endosomes to the lysosome. Syntaxin 7 is member of the Qa 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: 277228 [Multi-domain]  Cd Length: 60  Bit Score: 52.83  E-value: 8.29e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132071  97 IEGRHKDIVRLESSIKELHDMFMDIAMLVENQGEMLDNIELNVMHTVDHVEKARDETKRA 156
Cdd:cd15875     1 LEERERSIRQLESDIMDVNQIFKDLGMLVHEQGEVIDSIEANVETAAVHVEEANQQLSQA 60
SNARE pfam05739
SNARE domain; Most if not all vesicular membrane fusion events in eukaryotic cells are ...
 130-165 6.70e-09

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: 50.11  E-value: 6.70e-09
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1907132071 130 EMLDNIELNVMHTVDHVEKARDETKRAMKYQGQARK 165
Cdd:pfam05739   1 EMLDRIDTNVENAQSNVERAQKELKKAVKYQKSNRK 36
SNARE cd00193
SNARE motif; SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) ...
 104-155 7.03e-09

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: 50.46  E-value: 7.03e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907132071 104 IVRLESSIKELHDMFMDIAMLVENQGEMLDNIELNVMHTVDHVEKARDETKR 155
Cdd:cd00193     3 LEQLEASIGELKDIGRDMAMELEEQGEQLDRIEERAESTQARVSRAEKSLAK 54
SNARE_syntaxin7_like cd15847
SNARE motif of syntaxin 7, 12 and related sequences; SNARE (soluble N-ethylmaleimide-sensitive ...
 100-156 1.75e-07

SNARE motif of syntaxin 7, 12 and related sequences; 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-, 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. This subgroup of the Qa SNAREs includes syntaxin 7, syntaxin 12, TSNARE1 and related proteins.


Pssm-ID: 277200 [Multi-domain]  Cd Length: 60  Bit Score: 46.80  E-value: 1.75e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907132071 100 RHKDIVRLESSIKELHDMFMDIAMLVENQGEMLDNIELNVMHTVDHVEKARDETKRA 156
Cdd:cd15847     4 REERIRQIESDILDVNQIFKDLATLVHEQGETIDSIEANIESAYVNVESGNSQLAKA 60
SNARE_syntaxin5 cd15844
SNARE motif of syntaxin 5; Syntaxin 5 (Syn5) regulates the transport from the ER to the Golgi, ...
 97-166 2.87e-07

SNARE motif of syntaxin 5; Syntaxin 5 (Syn5) 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. Syn5 exists in 2 isoforms, long (42 kDa) and short (35 kDa). The short form is localized in the Golgi complex, whereas the long form is additionally found in the endoplasmic reticulum (ER). The syntaxin-5 SNARE complexes, which also contain Bet1 (Qc) and either GS27 (Qb) and Sec22B (R-SNARE) or GS28 (Qb) and Ykt6 (R-SNARE), regulate the early secretory pathway of eukaryotic cells at the level of endoplasmic reticulum (ER) to Golgi transport. The syntaxin-5 SNARE complex, which also contains GS15 (Qc), GS28 (Qb) and Ykt6 (R-SNAREs) is involved in the transport from the trans-Golgi network to the cis-Golgi. Syn5 is member of the Qa 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 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: 277197  Cd Length: 86  Bit Score: 46.74  E-value: 2.87e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907132071  97 IEGRHKDIVRLESSIKELHDMFMDIAMLVENQGEMLDNIELNVMHTVDHVEKARDETkraMKYQGQARKN 166
Cdd:cd15844     1 LQSRADAVQNIESTIVELGQIFQQLATMVAEQGEMVQRIDENVEDALANVEAAHSEL---LKYYRSISSN 67
SNARE_syntaxin17 cd15846
SNARE motif of syntaxin 17; Synthaxin 17 (STX17) belongs to the Qa subgroup of SNAREs and ...
 106-147 3.49e-06

SNARE motif of syntaxin 17; Synthaxin 17 (STX17) belongs to the Qa subgroup of SNAREs and interacts with SNAP29 (Qb/Qc) and the lysosomal R-SNARE VAMP8. The complex plays a role in autophagosome-lysosome fusion. Autophagosome transports cytoplasmic materials, including cytoplasmic proteins, glycogen, lipids, organelles, and invading bacteria to the lysosome for degradation. 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 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: 277199 [Multi-domain]  Cd Length: 62  Bit Score: 43.05  E-value: 3.49e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1907132071 106 RLESSIKELHDMFMDIAMLVENQGEMLDNIELNVMHTVDHVE 147
Cdd:cd15846    13 TLQQDLEDLHGLFTDFHQLVHDQGEQVDTIEDNVEEALENVQ 54
SNARE_TSNARE1 cd15877
SNARE motif of TSNARE1; TSNARE1 is member of the Qa subgroup of SNARE (soluble ...
 94-156 6.32e-04

SNARE motif of TSNARE1; TSNARE1 is member of the Qa 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. Its function is unknown, but polymorphisms in human TSNARE1 have been associated with schizophrenia susceptibility. 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. TSNARE1 is part of a subgroup of the Qa SNAREs that also includes syntaxin 7, syntaxin 12 and related proteins.


Pssm-ID: 277230  Cd Length: 64  Bit Score: 36.93  E-value: 6.32e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907132071  94 LSEIEGRHKDIVRLESSIKELHDMFMDIAMLVENQGEMLDNIELNVMHTVDHVEKARDETKRA 156
Cdd:cd15877     1 LEAIRQREEAIQQIESDMLDVNQIIKDLASMVSEQGDTIDSIEANIEAASSHVESANQQLAKA 63
Branch pfam02485
Core-2/I-Branching enzyme; This is a family of two different beta-1, ...
 1-46 7.06e-03

Core-2/I-Branching enzyme; This is a family of two different beta-1,6-N-acetylglucosaminyltransferase enzymes, I-branching enzyme and core-2 branching enzyme. I-branching enzyme is responsible for the production of the blood group I-antigen during embryonic development. Core-2 branching enzyme forms crucial side-chain branches in O-glycans. This is a fmmily of glycosyl-transferases that are Type II membrane proteins that are found in the endoplasmic reticulum (ER) and Golgi apparatus.


Pssm-ID: 426795  Cd Length: 250  Bit Score: 36.49  E-value: 7.06e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1907132071   1 MEKHIEEDEVRSSADLRIRK-SQHSVLSRKFVEVMTKYNEAQVDFRE 46
Cdd:pfam02485 144 MLPEIKKSKLFLPTAFKWRKgSQWFVLSRAFAEYVVWDNLYYPLFKY 190
 
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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