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Conserved domains on  [gi|3172538|gb|AAC27707|]
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syntaxin of plants 41 [Arabidopsis thaliana]

Protein Classification

syntaxin family protein( domain architecture ID 1003635)

syntaxin family protein similar to Arabidopsis thaliana syntaxins, which are involved in neuronal exocytosis, ER-Golgi transport and Golgi-endosome transport

Gene Ontology:  GO:0000149|GO:0005484
PubMed:  11737951

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
COG5325 super family cl34983
t-SNARE complex subunit, syntaxin [Intracellular trafficking and secretion];
73-318 2.69e-31

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


The actual alignment was detected with superfamily member COG5325:

Pssm-ID: 227635 [Multi-domain]  Cd Length: 283  Bit Score: 118.79  E-value: 2.69e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3172538   73 VGLPPAWVDVSEEISVNIQRARTKMAELGKAHAKALMPSFGDGKEDQHNIESLTQEITFLLKKSEKQLQR----LSASGP 148
Cdd:COG5325  30 DALTPTFILSAASVDQELTAVRRSISRLGKVYAKHTEPSFSDKSEKEDEIDELSKKVNQDLQRCEKILKTkyknLQSSFL 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3172538  149 SEDSNVRKNVQRSLATDLQLLSMELRKKQSTYLKRLRQQKEDGMDLEMNLsrnryRPEEDDFGDMLNEHQMSKIKKSE-- 226
Cdd:COG5325 110 QSKLLRDLNTECMEGQRIQQKSAQFRKYQVLQAKFLRNKNNDQHPLEEEE-----DEESLSSLGSQQTLQQQGLSNEEle 184
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3172538  227 ---EVSVEREKEIQQVVESVNDLAQIMKDLSALVIDQGTIVDRIDYNIENVATTVEDGLKQLQKAERTQRHGGMVKCASV 303
Cdd:COG5325 185 yqqILITERDEEIKNLARGIYELNEIFRDLGSLVGEQGELVDRIDFNIENTSDNLKNANKELEKAPAHQRRTKKCRFYLL 264
                       250
                ....*....|....*
gi 3172538  304 LVILCFIMLLLLILK 318
Cdd:COG5325 265 LILLVVLLFVSLIKK 279
 
Name Accession Description Interval E-value
COG5325 COG5325
t-SNARE complex subunit, syntaxin [Intracellular trafficking and secretion];
73-318 2.69e-31

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


Pssm-ID: 227635 [Multi-domain]  Cd Length: 283  Bit Score: 118.79  E-value: 2.69e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3172538   73 VGLPPAWVDVSEEISVNIQRARTKMAELGKAHAKALMPSFGDGKEDQHNIESLTQEITFLLKKSEKQLQR----LSASGP 148
Cdd:COG5325  30 DALTPTFILSAASVDQELTAVRRSISRLGKVYAKHTEPSFSDKSEKEDEIDELSKKVNQDLQRCEKILKTkyknLQSSFL 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3172538  149 SEDSNVRKNVQRSLATDLQLLSMELRKKQSTYLKRLRQQKEDGMDLEMNLsrnryRPEEDDFGDMLNEHQMSKIKKSE-- 226
Cdd:COG5325 110 QSKLLRDLNTECMEGQRIQQKSAQFRKYQVLQAKFLRNKNNDQHPLEEEE-----DEESLSSLGSQQTLQQQGLSNEEle 184
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3172538  227 ---EVSVEREKEIQQVVESVNDLAQIMKDLSALVIDQGTIVDRIDYNIENVATTVEDGLKQLQKAERTQRHGGMVKCASV 303
Cdd:COG5325 185 yqqILITERDEEIKNLARGIYELNEIFRDLGSLVGEQGELVDRIDFNIENTSDNLKNANKELEKAPAHQRRTKKCRFYLL 264
                       250
                ....*....|....*
gi 3172538  304 LVILCFIMLLLLILK 318
Cdd:COG5325 265 LILLVVLLFVSLIKK 279
SNARE_syntaxin16 cd15845
SNARE motif of syntaxin 16; Syntaxin 16 is located in trans-Golgi network (TGN) and regulated ...
231-287 1.62e-27

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: 101.77  E-value: 1.62e-27
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 3172538  231 EREKEIQQVVESVNDLAQIMKDLSALVIDQGTIVDRIDYNIENVATTVEDGLKQLQK 287
Cdd:cd15845   3 ERDREIAKIVESINELAEIFKDLATLVIEQGTILDRIDYNIEQTATRVEKGVKELKK 59
SynN smart00503
Syntaxin N-terminal domain; Three-helix domain that (in Sso1p) slows the rate of its reaction ...
77-185 3.37e-18

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: 78.93  E-value: 3.37e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3172538      77 PAWVDVSEEISVNIQRARTKMAELGKAHAKALMPSFGDGK------EDQHNIESLTQEITFLLKKSEKQLQRLSASGPSE 150
Cdd:smart00503   4 DEFFEKVEEIRANIQKISQNVAELQKLHEELLTPPDADKElrekleRLIDDIKRLAKEIRAKLKELEKENLENRASGSAS 83
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 3172538     151 DSNvRKNVQRSLATDLQLLSMELRKKQSTYLKRLR 185
Cdd:smart00503  84 DRT-RKAQTEKLRKKFKEVMNEFQRLQRKYREREK 117
SNARE pfam05739
SNARE domain; Most if not all vesicular membrane fusion events in eukaryotic cells are ...
262-313 4.00e-11

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: 57.43  E-value: 4.00e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 3172538    262 TIVDRIDYNIENVATTVEDGLKQLQKAERTQRHGGMVKCASVLVILCFIMLL 313
Cdd:pfam05739   1 EMLDRIDTNVENAQSNVERAQKELKKAVKYQKSNRKLKCIILLILVIILLVV 52
 
Name Accession Description Interval E-value
COG5325 COG5325
t-SNARE complex subunit, syntaxin [Intracellular trafficking and secretion];
73-318 2.69e-31

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


Pssm-ID: 227635 [Multi-domain]  Cd Length: 283  Bit Score: 118.79  E-value: 2.69e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3172538   73 VGLPPAWVDVSEEISVNIQRARTKMAELGKAHAKALMPSFGDGKEDQHNIESLTQEITFLLKKSEKQLQR----LSASGP 148
Cdd:COG5325  30 DALTPTFILSAASVDQELTAVRRSISRLGKVYAKHTEPSFSDKSEKEDEIDELSKKVNQDLQRCEKILKTkyknLQSSFL 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3172538  149 SEDSNVRKNVQRSLATDLQLLSMELRKKQSTYLKRLRQQKEDGMDLEMNLsrnryRPEEDDFGDMLNEHQMSKIKKSE-- 226
Cdd:COG5325 110 QSKLLRDLNTECMEGQRIQQKSAQFRKYQVLQAKFLRNKNNDQHPLEEEE-----DEESLSSLGSQQTLQQQGLSNEEle 184
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3172538  227 ---EVSVEREKEIQQVVESVNDLAQIMKDLSALVIDQGTIVDRIDYNIENVATTVEDGLKQLQKAERTQRHGGMVKCASV 303
Cdd:COG5325 185 yqqILITERDEEIKNLARGIYELNEIFRDLGSLVGEQGELVDRIDFNIENTSDNLKNANKELEKAPAHQRRTKKCRFYLL 264
                       250
                ....*....|....*
gi 3172538  304 LVILCFIMLLLLILK 318
Cdd:COG5325 265 LILLVVLLFVSLIKK 279
SNARE_syntaxin16 cd15845
SNARE motif of syntaxin 16; Syntaxin 16 is located in trans-Golgi network (TGN) and regulated ...
231-287 1.62e-27

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: 101.77  E-value: 1.62e-27
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 3172538  231 EREKEIQQVVESVNDLAQIMKDLSALVIDQGTIVDRIDYNIENVATTVEDGLKQLQK 287
Cdd:cd15845   3 ERDREIAKIVESINELAEIFKDLATLVIEQGTILDRIDYNIEQTATRVEKGVKELKK 59
SynN smart00503
Syntaxin N-terminal domain; Three-helix domain that (in Sso1p) slows the rate of its reaction ...
77-185 3.37e-18

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: 78.93  E-value: 3.37e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3172538      77 PAWVDVSEEISVNIQRARTKMAELGKAHAKALMPSFGDGK------EDQHNIESLTQEITFLLKKSEKQLQRLSASGPSE 150
Cdd:smart00503   4 DEFFEKVEEIRANIQKISQNVAELQKLHEELLTPPDADKElrekleRLIDDIKRLAKEIRAKLKELEKENLENRASGSAS 83
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 3172538     151 DSNvRKNVQRSLATDLQLLSMELRKKQSTYLKRLR 185
Cdd:smart00503  84 DRT-RKAQTEKLRKKFKEVMNEFQRLQRKYREREK 117
SNARE_Qa cd15840
SNARE motif, subgroup Qa; SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein ...
231-287 2.44e-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: 69.08  E-value: 2.44e-15
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 3172538  231 EREKEIQQVVESVNDLAQIMKDLSALVIDQGTIVDRIDYNIENVATTVEDGLKQLQK 287
Cdd:cd15840   3 EREEEIREIESSIGEVNEIFKDLATLVTEQGEQIDNIENNIEEAAANTEEANKELRK 59
SNARE_syntaxin7_like cd15847
SNARE motif of syntaxin 7, 12 and related sequences; SNARE (soluble N-ethylmaleimide-sensitive ...
231-288 1.39e-13

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: 64.52  E-value: 1.39e-13
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 3172538  231 EREKEIQQVVESVNDLAQIMKDLSALVIDQGTIVDRIDYNIENVATTVEDGLKQLQKA 288
Cdd:cd15847   3 EREERIRQIESDILDVNQIFKDLATLVHEQGETIDSIEANIESAYVNVESGNSQLAKA 60
SNARE_syntaxin7 cd15875
SNARE motif of syntaxin 7; Syntaxin 7 forms a complex with syntaxin 8 (Qc), Vti1b (Qb) and ...
231-288 1.25e-11

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: 58.99  E-value: 1.25e-11
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 3172538  231 EREKEIQQVVESVNDLAQIMKDLSALVIDQGTIVDRIDYNIENVATTVEDGLKQLQKA 288
Cdd:cd15875   3 ERERSIRQLESDIMDVNQIFKDLGMLVHEQGEVIDSIEANVETAAVHVEEANQQLSQA 60
SNARE pfam05739
SNARE domain; Most if not all vesicular membrane fusion events in eukaryotic cells are ...
262-313 4.00e-11

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: 57.43  E-value: 4.00e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 3172538    262 TIVDRIDYNIENVATTVEDGLKQLQKAERTQRHGGMVKCASVLVILCFIMLL 313
Cdd:pfam05739   1 EMLDRIDTNVENAQSNVERAQKELKKAVKYQKSNRKLKCIILLILVIILLVV 52
SNARE_syntaxin12 cd15876
SNARE motif of syntaxin 12; Syntaxin 12 (STX12, also known as STX13 and STX14) forms a complex ...
231-293 9.53e-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: 56.98  E-value: 9.53e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3172538  231 EREKEIQQVVESVNDLAQIMKDLSALVIDQGTIVDRIDYNIENVATTVEDGLKQLQKAERTQR 293
Cdd:cd15876   3 ERETAIQQLEADILDVNQIFKDLAMMIHDQGDMIDSIEANVESAEVHVERASEQLQRAAYYQK 65
SNARE_Sso1 cd15849
SNARE motif of Sso1; Saccharomyces cerevisiae SNARE protein Sso1p forms a complex with ...
231-288 1.36e-10

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: 56.38  E-value: 1.36e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 3172538  231 EREKEIQQVVESVNDLAQIMKDLSALVIDQGTIVDRIDYNIENVATTVEDGLKQLQKA 288
Cdd:cd15849   6 ARHNEIQRIEQTLTELAQLFNDMATLVEQQDEVIQQIEQNAEEVETDLEKGNVHLEKA 63
t_SNARE smart00397
Helical region found in SNAREs; All alpha-helical motifs that form twisted and parallel ...
231-288 1.43e-08

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: 50.66  E-value: 1.43e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 3172538     231 EREKEIQQVVESVNDLAQIMKDLSALVIDQGTIVDRIDYNIENVATTVEDGLKQLQKA 288
Cdd:smart00397   9 ERDEELEQLEKSIQELKQIFLDMGTELEEQGEQLDRIEDNVDDADVNLKKANKRLKKA 66
SNARE_syntaxin5 cd15844
SNARE motif of syntaxin 5; Syntaxin 5 (Syn5) regulates the transport from the ER to the Golgi, ...
231-287 1.44e-08

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: 51.36  E-value: 1.44e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 3172538  231 EREKEIQQVVESVNDLAQIMKDLSALVIDQGTIVDRIDYNIENVATTVEDGLKQLQK 287
Cdd:cd15844   3 SRADAVQNIESTIVELGQIFQQLATMVAEQGEMVQRIDENVEDALANVEAAHSELLK 59
SNARE_syntaxin1-like cd15848
SNARE motif of syntaxin 1 and related proteins; SNARE (soluble N-ethylmaleimide-sensitive ...
231-287 1.01e-07

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: 48.30  E-value: 1.01e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 3172538  231 EREKEIQQVVESVNDLAQIMKDLSALVIDQGTIVDRIDYNIENVATTVEDGLKQLQK 287
Cdd:cd15848   7 ERHQDILKLEKSIRELHQMFLDMAVLVESQGELIDNIEYNVEKAKDYVEKGNEELKK 63
COG5074 COG5074
t-SNARE complex subunit, syntaxin [Intracellular trafficking, secretion, and vesicular ...
119-314 1.22e-07

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


Pssm-ID: 227406 [Multi-domain]  Cd Length: 280  Bit Score: 52.20  E-value: 1.22e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3172538  119 QHNIESLTQEITFLLKKSEKQLQRLSASGpSEDSNVRKNVQRSLATDLQLLSmELRKKQSTYlkrlRQQKEDGMDLEMNL 198
Cdd:COG5074  64 RRSLDNFSSQTTDLQRNLKKDIKSAERDG-IHLANKQAQAENVRQKFLKLIQ-DYRIIDSNY----REEEKEQARRQYII 137
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3172538  199 SRNRYRPEE------DDFGD------MLNEHQMSKIKKSEEVSVEREKEIQQVVESVNDLAQIMKDLSALVIDQGTIVDR 266
Cdd:COG5074 138 AQPEATEDEveaainDVNGQqvfsqaLLNANRRGEAKTALAEVQARHQEIKKIEKTMAELTQLFNDMEELVIEQQENVDV 217
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 3172538  267 IDYNIENVATTVEDGLKQLQKAERTQRHGGMVK--CASVL-VILCFIMLLL 314
Cdd:COG5074 218 IDKNVEDAQENVEQGVGHTDKAVKSARAARKKKirCYGICfIIIIVIVVVV 268
SNARE_TSNARE1 cd15877
SNARE motif of TSNARE1; TSNARE1 is member of the Qa subgroup of SNARE (soluble ...
227-288 2.15e-07

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: 47.33  E-value: 2.15e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3172538  227 EVSVEREKEIQQVVESVNDLAQIMKDLSALVIDQGTIVDRIDYNIENVATTVEDGLKQLQKA 288
Cdd:cd15877   2 EAIRQREEAIQQIESDMLDVNQIIKDLASMVSEQGDTIDSIEANIEAASSHVESANQQLAKA 63
SNARE_syntaxin17 cd15846
SNARE motif of syntaxin 17; Synthaxin 17 (STX17) belongs to the Qa subgroup of SNAREs and ...
234-287 3.72e-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: 43.82  E-value: 3.72e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 3172538  234 KEIQQVVESVNDLAQIMKDLSALVIDQGTIVDRIDYNIENVATTVEDGLKQLQK 287
Cdd:cd15846   9 ESWETLQQDLEDLHGLFTDFHQLVHDQGEQVDTIEDNVEEALENVQEGTKNLRK 62
SNARE_syntaxin1 cd15880
SNARE motif of syntaxin 1; Syntaxin-1 belongs to the Qa subgroup of SNAREs and interacts with ...
232-292 9.64e-05

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: 39.80  E-value: 9.64e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3172538  232 REKEIQQVVESVNDLAQIMKDLSALVIDQGTIVDRIDYNIENVATTVEDGLKQLQKAERTQ 292
Cdd:cd15880   8 RHNDIIKLENSIRELHDMFMDMAMLVESQGEMIDRIEYNVEHAVDYVERAVSDTKKAVKYQ 68
SNARE_syntaxin2 cd15882
SNARE motif of syntaxin 2; Syntaxin 2 (STX2), also known as epimorphin (EPM or EPIM), may ...
232-292 1.83e-04

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: 39.26  E-value: 1.83e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3172538  232 REKEIQQVVESVNDLAQIMKDLSALVIDQGTIVDRIDYNIENVATTVEDGLKQLQKAERTQ 292
Cdd:cd15882   8 RHKDIMKLESSIRELHDMFVDMAMLVETQGEMINNIEKNVHNAVEYVEHAKEETKKAVKYQ 68
SNARE cd00193
SNARE motif; SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) ...
235-287 7.22e-04

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: 36.98  E-value: 7.22e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 3172538  235 EIQQVVESVNDLAQIMKDLSALVIDQGTIVDRIDYNIENVATTVEDGLKQLQK 287
Cdd:cd00193   2 SLEQLEASIGELKDIGRDMAMELEEQGEQLDRIEERAESTQARVSRAEKSLAK 54
SNARE_syntaxin3 cd15881
SNARE motif of syntaxin 3; Syntaxin 3 (STX3) has been shown to form a complex with VAMP8 ...
232-293 4.70e-03

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: 35.39  E-value: 4.70e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3172538  232 REKEIQQVVESVNDLAQIMKDLSALVIDQGTIVDRIDYNIENVATTVEDGLKQLQKAERTQR 293
Cdd:cd15881   8 RHKDIVRLESSIKELHDMFVDIAMLVENQGEMLDNIELNVMKTVDHVEKARDETKKAVKYQS 69
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
150-268 7.36e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 36.41  E-value: 7.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3172538     150 EDSNVRKNVQRSLATDLQLLSMELRKKQstylKRLRQQKEDGMDLEMNLSRNRYRPEEDDFGDMLNEHQMSKIKKSEEVS 229
Cdd:smart00935  11 QESPAGKAAQKQLEKEFKKRQAELEKLE----KELQKLKEKLQKDAATLSEAAREKKEKELQKKVQEFQRKQQKLQQDLQ 86
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 3172538     230 VEREKEIQQVVESVND-LAQIMKDLS-ALVIDQGTIV---DRID 268
Cdd:smart00935  87 KRQQEELQKILDKINKaIKEVAKKKGyDLVLDRNAVLyadPSID 130
 
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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