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Conserved domains on  [gi|1496160290|ref|NP_001353830|]
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t-SNARE domain-containing protein 1 isoform d [Homo sapiens]

Protein Classification

SANT/Myb-like DNA-binding domain-containing protein; SNARE domain-containing protein( domain architecture ID 10620650)

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 ...
 265-365 2.61e-28

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


:

Pssm-ID: 464199  Cd Length: 101  Bit Score: 108.12  E-value: 2.61e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496160290 265 SANVFRINSSVTSLERSLQSLGTPSDTQELRDSLHTAQQETNKTIAASASSVKQMAELLRSSCPerlQQERPQLDRLKTQ 344
Cdd:pfam14523   2 SSNLFKINSNVSTLEKLVKQLGTKRDTQELRDKLHKLIEKTNELIKETSELLKKLSSLENLSSD---SQQKLQKEKLSRD 78

                          90       100
                  ....*....|....*....|.
gi 1496160290 345 LSDAIQCYGVVQKKIAEKSRA 365
Cdd:pfam14523  79 FKEALQEFQKLQRQYAEKEKA 99
Myb_DNA-bind_5 pfam13873
Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb/SANT ...
 124-201 5.31e-26

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: 100.82  E-value: 5.31e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1496160290 124 RKPNFCPQETEVLVSKVSKHHQLLFGTGLLKAEPTRRYRVWSRILQAVNALGYCRRDVVDLKHKWRDLRAVVRRKLGD 201
Cdd:pfam13873   1 RKKNFSEEEKEVLVELVEKRKHILEGKKSDAATWKAKNRAWKEIAARVNAIGGVHRTAEELKKKWRDLKRRTKRKLAK 78
SNARE_TSNARE1 cd15877
SNARE motif of TSNARE1; TSNARE1 is member of the Qa subgroup of SNARE (soluble ...
 415-478 5.94e-25

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: 97.79  E-value: 5.94e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1496160290 415 LEAIRLREEAILQMESNLLDVNQIIKDLASMVSEQGEAVDSIEASLEAASSHAEAARQLLAGAS 478
Cdd:cd15877     1 LEAIRQREEAIQQIESDMLDVNQIIKDLASMVSEQGDTIDSIEANIEAASSHVESANQQLAKAS 64
 
Name Accession Description Interval E-value
Syntaxin_2 pfam14523
Syntaxin-like protein; This domain includes syntaxin-like domains including from the Vam3p ...
 265-365 2.61e-28

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


Pssm-ID: 464199  Cd Length: 101  Bit Score: 108.12  E-value: 2.61e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496160290 265 SANVFRINSSVTSLERSLQSLGTPSDTQELRDSLHTAQQETNKTIAASASSVKQMAELLRSSCPerlQQERPQLDRLKTQ 344
Cdd:pfam14523   2 SSNLFKINSNVSTLEKLVKQLGTKRDTQELRDKLHKLIEKTNELIKETSELLKKLSSLENLSSD---SQQKLQKEKLSRD 78

                          90       100
                  ....*....|....*....|.
gi 1496160290 345 LSDAIQCYGVVQKKIAEKSRA 365
Cdd:pfam14523  79 FKEALQEFQKLQRQYAEKEKA 99
Myb_DNA-bind_5 pfam13873
Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb/SANT ...
 124-201 5.31e-26

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: 100.82  E-value: 5.31e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1496160290 124 RKPNFCPQETEVLVSKVSKHHQLLFGTGLLKAEPTRRYRVWSRILQAVNALGYCRRDVVDLKHKWRDLRAVVRRKLGD 201
Cdd:pfam13873   1 RKKNFSEEEKEVLVELVEKRKHILEGKKSDAATWKAKNRAWKEIAARVNAIGGVHRTAEELKKKWRDLKRRTKRKLAK 78
SNARE_TSNARE1 cd15877
SNARE motif of TSNARE1; TSNARE1 is member of the Qa subgroup of SNARE (soluble ...
 415-478 5.94e-25

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: 97.79  E-value: 5.94e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1496160290 415 LEAIRLREEAILQMESNLLDVNQIIKDLASMVSEQGEAVDSIEASLEAASSHAEAARQLLAGAS 478
Cdd:cd15877     1 LEAIRQREEAIQQIESDMLDVNQIIKDLASMVSEQGDTIDSIEANIEAASSHVESANQQLAKAS 64
COG5325 COG5325
t-SNARE complex subunit, syntaxin [Intracellular trafficking and secretion];
242-501 3.95e-11

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


Pssm-ID: 227635 [Multi-domain]  Cd Length: 283  Bit Score: 63.71  E-value: 3.95e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496160290 242 FSLEPPRATQVDPCNLQELFQEMSANvfrINSSVTSLERSLQSLGtpsDTQE------LRDSLHTAQQETNKTIAASaSS 315
Cdd:COG5325    17 FTDEYKNQHRKEDDALTPTFILSAAS---VDQELTAVRRSISRLG---KVYAkhtepsFSDKSEKEDEIDELSKKVN-QD 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496160290 316 VKQMAELLRsscpERLQQERPQLDRLKTQLSDAIQC---YGVVQKKIAEKSRALLPMAQRGSKQSPQAPFAElADDEKVF 392
Cdd:COG5325    90 LQRCEKILK----TKYKNLQSSFLQSKLLRDLNTECmegQRIQQKSAQFRKYQVLQAKFLRNKNNDQHPLEE-EEDEESL 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496160290 393 NGSDNMWQGQEQALLPDITEEDLEAIRLREEAILQMESNLLDVNQIIKDLASMVSEQGEAVDSIEASLEAASSHAEAARQ 472
Cdd:COG5325   165 SSLGSQQTLQQQGLSNEELEYQQILITERDEEIKNLARGIYELNEIFRDLGSLVGEQGELVDRIDFNIENTSDNLKNANK 244

                         250       260       270
                  ....*....|....*....|....*....|
gi 1496160290 473 LLAGASRHQLQRHK-IKCCFLSAGVTALLV 501
Cdd:COG5325   245 ELEKAPAHQRRTKKcRFYLLLILLVVLLFV 274
SynN smart00503
Syntaxin N-terminal domain; Three-helix domain that (in Sso1p) slows the rate of its reaction ...
 258-364 2.75e-08

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: 51.96  E-value: 2.75e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496160290  258 QELFQEMSANVFRINSSVTSLERSLQSLGTPSDT-QELRDSLHTAQQETNKTIAASASSVKQMAEL---LRSSCPERLQQ 333
Cdd:smart00503   7 FEKVEEIRANIQKISQNVAELQKLHEELLTPPDAdKELREKLERLIDDIKRLAKEIRAKLKELEKEnleNRASGSASDRT 86

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1496160290  334 ERPQLDRLKTQLSDAIQCYGVVQKKIAEKSR 364
Cdd:smart00503  87 RKAQTEKLRKKFKEVMNEFQRLQRKYREREK 117
SynN cd00179
Syntaxin N-terminus domain; syntaxins are nervous system-specific proteins implicated in the ...
 257-364 2.01e-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: 50.36  E-value: 2.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496160290 257 LQELFQEMSANVFRINSSVTSLERSLQSLGTPSD-TQELRDSLHTAQQETNKTIAASASSVKQM------AELLRSSCPE 329
Cdd:cd00179     4 FFEEVEEIRGNIDKISEDVEELQKLHSQLLTAPDaDPELKQELESLVQEIKKLAKEIKGKLKELeesneqNEALNGSSVD 83

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1496160290 330 RLQQErpQLDRLKTQLSDAIQCYGVVQKKIAEKSR 364
Cdd:cd00179    84 RIRKT--QHSGLSKKFVEVMTEFNKAQRKYRERYK 116
t_SNARE smart00397
Helical region found in SNAREs; All alpha-helical motifs that form twisted and parallel ...
 421-460 3.69e-06

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: 44.50  E-value: 3.69e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1496160290  421 REEAILQMESNLLDVNQIIKDLASMVSEQGEAVDSIEASL 460
Cdd:smart00397  10 RDEELEQLEKSIQELKQIFLDMGTELEEQGEQLDRIEDNV 49
 
Name Accession Description Interval E-value
Syntaxin_2 pfam14523
Syntaxin-like protein; This domain includes syntaxin-like domains including from the Vam3p ...
 265-365 2.61e-28

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


Pssm-ID: 464199  Cd Length: 101  Bit Score: 108.12  E-value: 2.61e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496160290 265 SANVFRINSSVTSLERSLQSLGTPSDTQELRDSLHTAQQETNKTIAASASSVKQMAELLRSSCPerlQQERPQLDRLKTQ 344
Cdd:pfam14523   2 SSNLFKINSNVSTLEKLVKQLGTKRDTQELRDKLHKLIEKTNELIKETSELLKKLSSLENLSSD---SQQKLQKEKLSRD 78

                          90       100
                  ....*....|....*....|.
gi 1496160290 345 LSDAIQCYGVVQKKIAEKSRA 365
Cdd:pfam14523  79 FKEALQEFQKLQRQYAEKEKA 99
Myb_DNA-bind_5 pfam13873
Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb/SANT ...
 124-201 5.31e-26

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: 100.82  E-value: 5.31e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1496160290 124 RKPNFCPQETEVLVSKVSKHHQLLFGTGLLKAEPTRRYRVWSRILQAVNALGYCRRDVVDLKHKWRDLRAVVRRKLGD 201
Cdd:pfam13873   1 RKKNFSEEEKEVLVELVEKRKHILEGKKSDAATWKAKNRAWKEIAARVNAIGGVHRTAEELKKKWRDLKRRTKRKLAK 78
SNARE_TSNARE1 cd15877
SNARE motif of TSNARE1; TSNARE1 is member of the Qa subgroup of SNARE (soluble ...
 415-478 5.94e-25

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: 97.79  E-value: 5.94e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1496160290 415 LEAIRLREEAILQMESNLLDVNQIIKDLASMVSEQGEAVDSIEASLEAASSHAEAARQLLAGAS 478
Cdd:cd15877     1 LEAIRQREEAIQQIESDMLDVNQIIKDLASMVSEQGDTIDSIEANIEAASSHVESANQQLAKAS 64
SNARE_syntaxin7_like cd15847
SNARE motif of syntaxin 7, 12 and related sequences; SNARE (soluble N-ethylmaleimide-sensitive ...
 421-459 8.38e-15

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: 68.76  E-value: 8.38e-15
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1496160290 421 REEAILQMESNLLDVNQIIKDLASMVSEQGEAVDSIEAS 459
Cdd:cd15847     4 REERIRQIESDILDVNQIFKDLATLVHEQGETIDSIEAN 42
SNARE_syntaxin7 cd15875
SNARE motif of syntaxin 7; Syntaxin 7 forms a complex with syntaxin 8 (Qc), Vti1b (Qb) and ...
 418-477 1.66e-14

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: 67.85  E-value: 1.66e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496160290 418 IRLREEAILQMESNLLDVNQIIKDLASMVSEQGEAVDSIEASLEAASSHAEAARQLLAGA 477
Cdd:cd15875     1 LEERERSIRQLESDIMDVNQIFKDLGMLVHEQGEVIDSIEANVETAAVHVEEANQQLSQA 60
SNARE_syntaxin12 cd15876
SNARE motif of syntaxin 12; Syntaxin 12 (STX12, also known as STX13 and STX14) forms a complex ...
 418-481 1.13e-13

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: 65.84  E-value: 1.13e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1496160290 418 IRLREEAILQMESNLLDVNQIIKDLASMVSEQGEAVDSIEASLEAASSHAEAARQLLAGASRHQ 481
Cdd:cd15876     1 IKERETAIQQLEADILDVNQIFKDLAMMIHDQGDMIDSIEANVESAEVHVERASEQLQRAAYYQ 64
SNARE_Qa cd15840
SNARE motif, subgroup Qa; SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein ...
 418-460 3.74e-12

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: 61.38  E-value: 3.74e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1496160290 418 IRLREEAILQMESNLLDVNQIIKDLASMVSEQGEAVDSIEASL 460
Cdd:cd15840     1 IEEREEEIREIESSIGEVNEIFKDLATLVTEQGEQIDNIENNI 43
COG5325 COG5325
t-SNARE complex subunit, syntaxin [Intracellular trafficking and secretion];
242-501 3.95e-11

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


Pssm-ID: 227635 [Multi-domain]  Cd Length: 283  Bit Score: 63.71  E-value: 3.95e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496160290 242 FSLEPPRATQVDPCNLQELFQEMSANvfrINSSVTSLERSLQSLGtpsDTQE------LRDSLHTAQQETNKTIAASaSS 315
Cdd:COG5325    17 FTDEYKNQHRKEDDALTPTFILSAAS---VDQELTAVRRSISRLG---KVYAkhtepsFSDKSEKEDEIDELSKKVN-QD 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496160290 316 VKQMAELLRsscpERLQQERPQLDRLKTQLSDAIQC---YGVVQKKIAEKSRALLPMAQRGSKQSPQAPFAElADDEKVF 392
Cdd:COG5325    90 LQRCEKILK----TKYKNLQSSFLQSKLLRDLNTECmegQRIQQKSAQFRKYQVLQAKFLRNKNNDQHPLEE-EEDEESL 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496160290 393 NGSDNMWQGQEQALLPDITEEDLEAIRLREEAILQMESNLLDVNQIIKDLASMVSEQGEAVDSIEASLEAASSHAEAARQ 472
Cdd:COG5325   165 SSLGSQQTLQQQGLSNEELEYQQILITERDEEIKNLARGIYELNEIFRDLGSLVGEQGELVDRIDFNIENTSDNLKNANK 244

                         250       260       270
                  ....*....|....*....|....*....|
gi 1496160290 473 LLAGASRHQLQRHK-IKCCFLSAGVTALLV 501
Cdd:COG5325   245 ELEKAPAHQRRTKKcRFYLLLILLVVLLFV 274
SynN smart00503
Syntaxin N-terminal domain; Three-helix domain that (in Sso1p) slows the rate of its reaction ...
 258-364 2.75e-08

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: 51.96  E-value: 2.75e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496160290  258 QELFQEMSANVFRINSSVTSLERSLQSLGTPSDT-QELRDSLHTAQQETNKTIAASASSVKQMAEL---LRSSCPERLQQ 333
Cdd:smart00503   7 FEKVEEIRANIQKISQNVAELQKLHEELLTPPDAdKELREKLERLIDDIKRLAKEIRAKLKELEKEnleNRASGSASDRT 86

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1496160290  334 ERPQLDRLKTQLSDAIQCYGVVQKKIAEKSR 364
Cdd:smart00503  87 RKAQTEKLRKKFKEVMNEFQRLQRKYREREK 117
SynN cd00179
Syntaxin N-terminus domain; syntaxins are nervous system-specific proteins implicated in the ...
 257-364 2.01e-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: 50.36  E-value: 2.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496160290 257 LQELFQEMSANVFRINSSVTSLERSLQSLGTPSD-TQELRDSLHTAQQETNKTIAASASSVKQM------AELLRSSCPE 329
Cdd:cd00179     4 FFEEVEEIRGNIDKISEDVEELQKLHSQLLTAPDaDPELKQELESLVQEIKKLAKEIKGKLKELeesneqNEALNGSSVD 83

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1496160290 330 RLQQErpQLDRLKTQLSDAIQCYGVVQKKIAEKSR 364
Cdd:cd00179    84 RIRKT--QHSGLSKKFVEVMTEFNKAQRKYRERYK 116
SNARE_syntaxin1-like cd15848
SNARE motif of syntaxin 1 and related proteins; SNARE (soluble N-ethylmaleimide-sensitive ...
 415-457 1.85e-06

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: 45.22  E-value: 1.85e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1496160290 415 LEAIRLREEAILQMESNLLDVNQIIKDLASMVSEQGEAVDSIE 457
Cdd:cd15848     2 LADIEERHQDILKLEKSIRELHQMFLDMAVLVESQGELIDNIE 44
SNARE_syntaxin17 cd15846
SNARE motif of syntaxin 17; Synthaxin 17 (STX17) belongs to the Qa subgroup of SNAREs and ...
 418-458 3.52e-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: 44.59  E-value: 3.52e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1496160290 418 IRLREEAILQMES---NLLDVNQIIKDLASMVSEQGEAVDSIEA 458
Cdd:cd15846     1 LPQRQACLESWETlqqDLEDLHGLFTDFHQLVHDQGEQVDTIED 44
t_SNARE smart00397
Helical region found in SNAREs; All alpha-helical motifs that form twisted and parallel ...
 421-460 3.69e-06

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: 44.50  E-value: 3.69e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1496160290  421 REEAILQMESNLLDVNQIIKDLASMVSEQGEAVDSIEASL 460
Cdd:smart00397  10 RDEELEQLEKSIQELKQIFLDMGTELEEQGEQLDRIEDNV 49
SNARE_syntaxin16 cd15845
SNARE motif of syntaxin 16; Syntaxin 16 is located in trans-Golgi network (TGN) and regulated ...
 418-457 9.09e-06

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: 43.22  E-value: 9.09e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1496160290 418 IRLREEAILQMESNLLDVNQIIKDLASMVSEQGEAVDSIE 457
Cdd:cd15845     1 IQERDREIAKIVESINELAEIFKDLATLVIEQGTILDRID 40
SNARE_syntaxin5 cd15844
SNARE motif of syntaxin 5; Syntaxin 5 (Syn5) regulates the transport from the ER to the Golgi, ...
 418-458 2.27e-05

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: 42.88  E-value: 2.27e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1496160290 418 IRLREEAILQMESNLLDVNQIIKDLASMVSEQGEAVDSIEA 458
Cdd:cd15844     1 LQSRADAVQNIESTIVELGQIFQQLATMVAEQGEMVQRIDE 41
Myb_DNA-bind_4 pfam13837
Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb ...
 125-193 2.97e-05

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: 42.64  E-value: 2.97e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1496160290 125 KPNFCPQETEVLVSKVSKHHQLLFGTGLLKAEptrryRVWSRILQAVNALGYcRRDVVDLKHKWRDLRA 193
Cdd:pfam13837   1 RNKWTEEETLALIEIWGERLELRFQESKKRNK-----KLWEEIAEKMAELGY-NRSPEQCKEKWENLKK 63
COG5074 COG5074
t-SNARE complex subunit, syntaxin [Intracellular trafficking, secretion, and vesicular ...
 289-460 1.61e-04

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


Pssm-ID: 227406 [Multi-domain]  Cd Length: 280  Bit Score: 43.72  E-value: 1.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496160290 289 SDTQELRDSLHT-AQQETNKTIAASASS-----VKQMAELLRSSCPERLQQER---------PQLDRLKTQLSDAIQCYG 353
Cdd:COG5074    38 EKEINQIDNLHKdLLTEVFEEQSRKLRRsldnfSSQTTDLQRNLKKDIKSAERdgihlankqAQAENVRQKFLKLIQDYR 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1496160290 354 VVQKKIAEKSRallpmaQRGSKQSPQAPFAELADDEKVFNGSDNMWQGQEQALL----PDITEEDLEAIRLREEAILQME 429
Cdd:COG5074   118 IIDSNYREEEK------EQARRQYIIAQPEATEDEVEAAINDVNGQQVFSQALLnanrRGEAKTALAEVQARHQEIKKIE 191

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1496160290 430 SNLLDVNQIIKDLASMVSEQGEAVDSIEASL 460
Cdd:COG5074   192 KTMAELTQLFNDMEELVIEQQENVDVIDKNV 222
SNARE_Sso1 cd15849
SNARE motif of Sso1; Saccharomyces cerevisiae SNARE protein Sso1p forms a complex with ...
 415-457 2.93e-04

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: 39.05  E-value: 2.93e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1496160290 415 LEAIRLREEAILQMESNLLDVNQIIKDLASMVSEQGEAVDSIE 457
Cdd:cd15849     1 LGEVQARHNEIQRIEQTLTELAQLFNDMATLVEQQDEVIQQIE 43
SNARE_syntaxin2 cd15882
SNARE motif of syntaxin 2; Syntaxin 2 (STX2), also known as epimorphin (EPM or EPIM), may ...
 415-457 6.89e-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: 38.10  E-value: 6.89e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1496160290 415 LEAIRLREEAILQMESNLLDVNQIIKDLASMVSEQGEAVDSIE 457
Cdd:cd15882     2 LNEIESRHKDIMKLESSIRELHDMFVDMAMLVETQGEMINNIE 44
SNARE_syntaxin3 cd15881
SNARE motif of syntaxin 3; Syntaxin 3 (STX3) has been shown to form a complex with VAMP8 ...
 415-481 8.92e-04

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: 38.08  E-value: 8.92e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1496160290 415 LEAIRLREEAILQMESNLLDVNQIIKDLASMVSEQGEAVDSIEASLEAASSHAEAARQLLAGASRHQ 481
Cdd:cd15881     2 LSEIEGRHKDIVRLESSIKELHDMFVDIAMLVENQGEMLDNIELNVMKTVDHVEKARDETKKAVKYQ 68
SNARE cd00193
SNARE motif; SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) ...
 423-460 1.37e-03

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: 1.37e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1496160290 423 EAILQMESNLLDVNQIIKDLASMVSEQGEAVDSIEASL 460
Cdd:cd00193     1 ESLEQLEASIGELKDIGRDMAMELEEQGEQLDRIEERA 38
SNARE_syntaxin1 cd15880
SNARE motif of syntaxin 1; Syntaxin-1 belongs to the Qa subgroup of SNAREs and interacts with ...
 414-457 1.38e-03

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: 37.49  E-value: 1.38e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1496160290 414 DLEAirlREEAILQMESNLLDVNQIIKDLASMVSEQGEAVDSIE 457
Cdd:cd15880     4 EIEA---RHNDIIKLENSIRELHDMFMDMAMLVESQGEMIDRIE 44
SNARE_syntaxin11 cd15878
SNARE motif of syntaxin 11; Syntaxin 11 (also known as STX11, FHL4, HLH4, HPLH4) is present on ...
 415-460 5.50e-03

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: 35.59  E-value: 5.50e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1496160290 415 LEAIRLREEAILQMESNLLDVNQIIKDLASMVSEQGEAVDSIEASL 460
Cdd:cd15878     2 LNEIETRHKELLELESRIREVHELFLQMALLVEEQADTLNNIELNV 47
SNARE_syntaxin4 cd15883
SNARE motif of syntaxin 4; Syntaxin-4 forms a complex with SNAP-23 (Qb/Qc) and R-SNAREs VAMP8, ...
 415-460 9.17e-03

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: 34.92  E-value: 9.17e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1496160290 415 LEAIRLREEAILQMESNLLDVNQIIKDLASMVSEQGEAVDSIEASL 460
Cdd:cd15883     2 LNEIEARHSEIQKLERSIRELHDMFTYLAMEVEAQGEMIDRIEKNI 47
 
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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