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Conserved domains on  [gi|2217371147|ref|XP_047277444|]
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t-SNARE domain-containing protein 1 isoform X35 [Homo sapiens]

Protein Classification

SANT/Myb-like DNA-binding domain-containing protein; SNARE domain-containing protein( domain architecture ID 10629125)

SANT (SWI3, ADA2, N-CoR and TFIIIB)/Myb-like DNA-binding domain-containing protein binds DNA and may function as a transcription factor; SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) domain-containing protein similar to Arabidopsis thaliana syntaxin-61 which coordinate the trafficking of plasma membrane aquaporin PIP2

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Syntaxin_2 pfam14523
Syntaxin-like protein; This domain includes syntaxin-like domains including from the Vam3p ...
 46-147 7.04e-27

Syntaxin-like protein; This domain includes syntaxin-like domains including from the Vam3p protein.


:

Pssm-ID: 464199  Cd Length: 101  Bit Score: 103.50  E-value: 7.04e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217371147  46 SANVFRINSSVTSLERSLQSLGTPSDTQELRDSLHTAQQETNKTIAASASSVKQMAELLRSSCPqerlQQERPQLDRLKT 125
Cdd:pfam14523   2 SSNLFKINSNVSTLEKLVKQLGTKRDTQELRDKLHKLIEKTNELIKETSELLKKLSSLENLSSD----SQQKLQKEKLSR 77

                          90       100
                  ....*....|....*....|..
gi 2217371147 126 QLSDAIQCYGVVQKKIAEKSRA 147
Cdd:pfam14523  78 DFKEALQEFQKLQRQYAEKEKA 99
Myb_DNA-bind_5 pfam13873
Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb/SANT ...
 280-355 4.44e-22

Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb/SANT like DNA binding domains. This family is greatly expanded in arthropods and higher eukaryotes.


:

Pssm-ID: 433544  Cd Length: 78  Bit Score: 89.65  E-value: 4.44e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217371147 280 RKPNFSPQETEVLVQRVRRHYPLLFG--ALRGTPARKHRVWSRILQAVNALGYCRRDLGDLKHKWRDLRGAVRKKLAE 355
Cdd:pfam13873   1 RKKNFSEEEKEVLVELVEKRKHILEGkkSDAATWKAKNRAWKEIAARVNAIGGVHRTAEELKKKWRDLKRRTKRKLAK 78
SNARE super family cl22856
SNARE motif; SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) ...
 198-238 3.07e-16

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 cd15877:

Pssm-ID: 473982  Cd Length: 64  Bit Score: 72.75  E-value: 3.07e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2217371147 198 LEAIRLREEAILQMESNLLDVNQIIKDLASMVSEQGEAVGS 238
Cdd:cd15877     1 LEAIRQREEAIQQIESDMLDVNQIIKDLASMVSEQGDTIDS 41
 
Name Accession Description Interval E-value
Syntaxin_2 pfam14523
Syntaxin-like protein; This domain includes syntaxin-like domains including from the Vam3p ...
 46-147 7.04e-27

Syntaxin-like protein; This domain includes syntaxin-like domains including from the Vam3p protein.


Pssm-ID: 464199  Cd Length: 101  Bit Score: 103.50  E-value: 7.04e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217371147  46 SANVFRINSSVTSLERSLQSLGTPSDTQELRDSLHTAQQETNKTIAASASSVKQMAELLRSSCPqerlQQERPQLDRLKT 125
Cdd:pfam14523   2 SSNLFKINSNVSTLEKLVKQLGTKRDTQELRDKLHKLIEKTNELIKETSELLKKLSSLENLSSD----SQQKLQKEKLSR 77

                          90       100
                  ....*....|....*....|..
gi 2217371147 126 QLSDAIQCYGVVQKKIAEKSRA 147
Cdd:pfam14523  78 DFKEALQEFQKLQRQYAEKEKA 99
Myb_DNA-bind_5 pfam13873
Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb/SANT ...
 280-355 4.44e-22

Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb/SANT like DNA binding domains. This family is greatly expanded in arthropods and higher eukaryotes.


Pssm-ID: 433544  Cd Length: 78  Bit Score: 89.65  E-value: 4.44e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217371147 280 RKPNFSPQETEVLVQRVRRHYPLLFG--ALRGTPARKHRVWSRILQAVNALGYCRRDLGDLKHKWRDLRGAVRKKLAE 355
Cdd:pfam13873   1 RKKNFSEEEKEVLVELVEKRKHILEGkkSDAATWKAKNRAWKEIAARVNAIGGVHRTAEELKKKWRDLKRRTKRKLAK 78
SNARE_TSNARE1 cd15877
SNARE motif of TSNARE1; TSNARE1 is member of the Qa subgroup of SNARE (soluble ...
 198-238 3.07e-16

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: 72.75  E-value: 3.07e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2217371147 198 LEAIRLREEAILQMESNLLDVNQIIKDLASMVSEQGEAVGS 238
Cdd:cd15877     1 LEAIRQREEAIQQIESDMLDVNQIIKDLASMVSEQGDTIDS 41
SynN smart00503
Syntaxin N-terminal domain; Three-helix domain that (in Sso1p) slows the rate of its reaction ...
 39-146 2.09e-07

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: 49.27  E-value: 2.09e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217371147   39 QELFQEMSANVFRINSSVTSLERSLQSLGTPSDT-QELRDSLHTAQQETNKTIAASASSVKQMAELL----RSSCPQERL 113
Cdd:smart00503   7 FEKVEEIRANIQKISQNVAELQKLHEELLTPPDAdKELREKLERLIDDIKRLAKEIRAKLKELEKENlenrASGSASDRT 86

                           90       100       110
                   ....*....|....*....|....*....|...
gi 2217371147  114 QQErpQLDRLKTQLSDAIQCYGVVQKKIAEKSR 146
Cdd:smart00503  87 RKA--QTEKLRKKFKEVMNEFQRLQRKYREREK 117
SynN cd00179
Syntaxin N-terminus domain; syntaxins are nervous system-specific proteins implicated in the ...
 38-170 6.45e-07

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: 48.82  E-value: 6.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217371147  38 LQELFQEMSANVFRINSSVTSLERSLQSLGTPSD-TQELRDSLHTAQQETNKTIAASASSVKQMAEL---LRSSCPQERL 113
Cdd:cd00179     4 FFEEVEEIRGNIDKISEDVEELQKLHSQLLTAPDaDPELKQELESLVQEIKKLAKEIKGKLKELEESneqNEALNGSSVD 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2217371147 114 QQERPQLDRLKTQLSDAIQCYGVVQKKIAEKSRAllpMAQRGSKQQSPQAPFAELAD 170
Cdd:cd00179    84 RIRKTQHSGLSKKFVEVMTEFNKAQRKYRERYKE---RIQRQLEITGGEATDEELED 137
COG5325 COG5325
t-SNARE complex subunit, syntaxin [Intracellular trafficking and secretion];
37-236 4.74e-05

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


Pssm-ID: 227635 [Multi-domain]  Cd Length: 283  Bit Score: 44.83  E-value: 4.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217371147  37 NLQELFQEMSANvfrINSSVTSLERSLQSLGTPSDTQELR---DSLHTAQQETNKTIAASaSSVKQMAELLRSSCPQERL 113
Cdd:COG5325    31 ALTPTFILSAAS---VDQELTAVRRSISRLGKVYAKHTEPsfsDKSEKEDEIDELSKKVN-QDLQRCEKILKTKYKNLQS 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217371147 114 QQERPQLDR-LKTQLSDAiqcYGVVQKKIAEKSRALLpmAQRGSKQQSPQAPFAELADDEKVFNGSDNMWQGQEQALLPD 192
Cdd:COG5325   107 SFLQSKLLRdLNTECMEG---QRIQQKSAQFRKYQVL--QAKFLRNKNNDQHPLEEEEDEESLSSLGSQQTLQQQGLSNE 181

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2217371147 193 ITEEDLEAIRLREEAILQMESNLLDVNQIIKDLASMVSEQGEAV 236
Cdd:COG5325   182 ELEYQQILITERDEEIKNLARGIYELNEIFRDLGSLVGEQGELV 225
t_SNARE smart00397
Helical region found in SNAREs; All alpha-helical motifs that form twisted and parallel ...
 204-234 3.66e-03

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: 35.64  E-value: 3.66e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 2217371147  204 REEAILQMESNLLDVNQIIKDLASMVSEQGE 234
Cdd:smart00397  10 RDEELEQLEKSIQELKQIFLDMGTELEEQGE 40
 
Name Accession Description Interval E-value
Syntaxin_2 pfam14523
Syntaxin-like protein; This domain includes syntaxin-like domains including from the Vam3p ...
 46-147 7.04e-27

Syntaxin-like protein; This domain includes syntaxin-like domains including from the Vam3p protein.


Pssm-ID: 464199  Cd Length: 101  Bit Score: 103.50  E-value: 7.04e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217371147  46 SANVFRINSSVTSLERSLQSLGTPSDTQELRDSLHTAQQETNKTIAASASSVKQMAELLRSSCPqerlQQERPQLDRLKT 125
Cdd:pfam14523   2 SSNLFKINSNVSTLEKLVKQLGTKRDTQELRDKLHKLIEKTNELIKETSELLKKLSSLENLSSD----SQQKLQKEKLSR 77

                          90       100
                  ....*....|....*....|..
gi 2217371147 126 QLSDAIQCYGVVQKKIAEKSRA 147
Cdd:pfam14523  78 DFKEALQEFQKLQRQYAEKEKA 99
Myb_DNA-bind_5 pfam13873
Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb/SANT ...
 280-355 4.44e-22

Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb/SANT like DNA binding domains. This family is greatly expanded in arthropods and higher eukaryotes.


Pssm-ID: 433544  Cd Length: 78  Bit Score: 89.65  E-value: 4.44e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217371147 280 RKPNFSPQETEVLVQRVRRHYPLLFG--ALRGTPARKHRVWSRILQAVNALGYCRRDLGDLKHKWRDLRGAVRKKLAE 355
Cdd:pfam13873   1 RKKNFSEEEKEVLVELVEKRKHILEGkkSDAATWKAKNRAWKEIAARVNAIGGVHRTAEELKKKWRDLKRRTKRKLAK 78
SNARE_TSNARE1 cd15877
SNARE motif of TSNARE1; TSNARE1 is member of the Qa subgroup of SNARE (soluble ...
 198-238 3.07e-16

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: 72.75  E-value: 3.07e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2217371147 198 LEAIRLREEAILQMESNLLDVNQIIKDLASMVSEQGEAVGS 238
Cdd:cd15877     1 LEAIRQREEAIQQIESDMLDVNQIIKDLASMVSEQGDTIDS 41
SNARE_syntaxin7_like cd15847
SNARE motif of syntaxin 7, 12 and related sequences; SNARE (soluble N-ethylmaleimide-sensitive ...
 204-238 3.03e-10

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: 55.66  E-value: 3.03e-10
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2217371147 204 REEAILQMESNLLDVNQIIKDLASMVSEQGEAVGS 238
Cdd:cd15847     4 REERIRQIESDILDVNQIFKDLATLVHEQGETIDS 38
SNARE_syntaxin7 cd15875
SNARE motif of syntaxin 7; Syntaxin 7 forms a complex with syntaxin 8 (Qc), Vti1b (Qb) and ...
 201-238 3.55e-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: 55.52  E-value: 3.55e-10
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2217371147 201 IRLREEAILQMESNLLDVNQIIKDLASMVSEQGEAVGS 238
Cdd:cd15875     1 LEERERSIRQLESDIMDVNQIFKDLGMLVHEQGEVIDS 38
SNARE_syntaxin12 cd15876
SNARE motif of syntaxin 12; Syntaxin 12 (STX12, also known as STX13 and STX14) forms a complex ...
 201-238 1.08e-09

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: 54.28  E-value: 1.08e-09
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2217371147 201 IRLREEAILQMESNLLDVNQIIKDLASMVSEQGEAVGS 238
Cdd:cd15876     1 IKERETAIQQLEADILDVNQIFKDLAMMIHDQGDMIDS 38
SNARE_Qa cd15840
SNARE motif, subgroup Qa; SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein ...
 201-236 4.36e-08

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: 49.43  E-value: 4.36e-08
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2217371147 201 IRLREEAILQMESNLLDVNQIIKDLASMVSEQGEAV 236
Cdd:cd15840     1 IEEREEEIREIESSIGEVNEIFKDLATLVTEQGEQI 36
SynN smart00503
Syntaxin N-terminal domain; Three-helix domain that (in Sso1p) slows the rate of its reaction ...
 39-146 2.09e-07

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: 49.27  E-value: 2.09e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217371147   39 QELFQEMSANVFRINSSVTSLERSLQSLGTPSDT-QELRDSLHTAQQETNKTIAASASSVKQMAELL----RSSCPQERL 113
Cdd:smart00503   7 FEKVEEIRANIQKISQNVAELQKLHEELLTPPDAdKELREKLERLIDDIKRLAKEIRAKLKELEKENlenrASGSASDRT 86

                           90       100       110
                   ....*....|....*....|....*....|...
gi 2217371147  114 QQErpQLDRLKTQLSDAIQCYGVVQKKIAEKSR 146
Cdd:smart00503  87 RKA--QTEKLRKKFKEVMNEFQRLQRKYREREK 117
SynN cd00179
Syntaxin N-terminus domain; syntaxins are nervous system-specific proteins implicated in the ...
 38-170 6.45e-07

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: 48.82  E-value: 6.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217371147  38 LQELFQEMSANVFRINSSVTSLERSLQSLGTPSD-TQELRDSLHTAQQETNKTIAASASSVKQMAEL---LRSSCPQERL 113
Cdd:cd00179     4 FFEEVEEIRGNIDKISEDVEELQKLHSQLLTAPDaDPELKQELESLVQEIKKLAKEIKGKLKELEESneqNEALNGSSVD 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2217371147 114 QQERPQLDRLKTQLSDAIQCYGVVQKKIAEKSRAllpMAQRGSKQQSPQAPFAELAD 170
Cdd:cd00179    84 RIRKTQHSGLSKKFVEVMTEFNKAQRKYRERYKE---RIQRQLEITGGEATDEELED 137
COG5325 COG5325
t-SNARE complex subunit, syntaxin [Intracellular trafficking and secretion];
37-236 4.74e-05

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


Pssm-ID: 227635 [Multi-domain]  Cd Length: 283  Bit Score: 44.83  E-value: 4.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217371147  37 NLQELFQEMSANvfrINSSVTSLERSLQSLGTPSDTQELR---DSLHTAQQETNKTIAASaSSVKQMAELLRSSCPQERL 113
Cdd:COG5325    31 ALTPTFILSAAS---VDQELTAVRRSISRLGKVYAKHTEPsfsDKSEKEDEIDELSKKVN-QDLQRCEKILKTKYKNLQS 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217371147 114 QQERPQLDR-LKTQLSDAiqcYGVVQKKIAEKSRALLpmAQRGSKQQSPQAPFAELADDEKVFNGSDNMWQGQEQALLPD 192
Cdd:COG5325   107 SFLQSKLLRdLNTECMEG---QRIQQKSAQFRKYQVL--QAKFLRNKNNDQHPLEEEEDEESLSSLGSQQTLQQQGLSNE 181

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2217371147 193 ITEEDLEAIRLREEAILQMESNLLDVNQIIKDLASMVSEQGEAV 236
Cdd:COG5325   182 ELEYQQILITERDEEIKNLARGIYELNEIFRDLGSLVGEQGELV 225
Myb_DNA-bind_4 pfam13837
Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb ...
 281-346 2.81e-04

Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb/SANT-like DNA binding domains. In particular pfam10545 seems most related. This family is greatly expanded in plants and appears in several proteins annotated as transposon proteins.


Pssm-ID: 463994  Cd Length: 84  Bit Score: 39.56  E-value: 2.81e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217371147 281 KPNFSPQETEVLVQRVRRHYPLLFGALRGtpaRKHRVWSRILQAVNALGYcRRDLGDLKHKWRDLR 346
Cdd:pfam13837   1 RNKWTEEETLALIEIWGERLELRFQESKK---RNKKLWEEIAEKMAELGY-NRSPEQCKEKWENLK 62
SNARE_syntaxin16 cd15845
SNARE motif of syntaxin 16; Syntaxin 16 is located in trans-Golgi network (TGN) and regulated ...
 201-233 4.26e-04

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: 38.21  E-value: 4.26e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2217371147 201 IRLREEAILQMESNLLDVNQIIKDLASMVSEQG 233
Cdd:cd15845     1 IQERDREIAKIVESINELAEIFKDLATLVIEQG 33
SNARE_syntaxin5 cd15844
SNARE motif of syntaxin 5; Syntaxin 5 (Syn5) regulates the transport from the ER to the Golgi, ...
 201-236 5.02e-04

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: 38.65  E-value: 5.02e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2217371147 201 IRLREEAILQMESNLLDVNQIIKDLASMVSEQGEAV 236
Cdd:cd15844     1 LQSRADAVQNIESTIVELGQIFQQLATMVAEQGEMV 36
SNARE_syntaxin1-like cd15848
SNARE motif of syntaxin 1 and related proteins; SNARE (soluble N-ethylmaleimide-sensitive ...
 198-234 5.36e-04

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: 37.90  E-value: 5.36e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2217371147 198 LEAIRLREEAILQMESNLLDVNQIIKDLASMVSEQGE 234
Cdd:cd15848     2 LADIEERHQDILKLEKSIRELHQMFLDMAVLVESQGE 38
t_SNARE smart00397
Helical region found in SNAREs; All alpha-helical motifs that form twisted and parallel ...
 204-234 3.66e-03

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: 35.64  E-value: 3.66e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 2217371147  204 REEAILQMESNLLDVNQIIKDLASMVSEQGE 234
Cdd:smart00397  10 RDEELEQLEKSIQELKQIFLDMGTELEEQGE 40
 
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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