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Conserved domains on  [gi|443287677|ref|NP_001259025|]
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syntaxin-4 isoform 2 [Homo sapiens]

Protein Classification

SNARE domain-containing protein; v-SNARE domain-containing protein( domain architecture ID 10075370)

SNARE domain-containing protein such as SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins, which interact to form a SNARE complex that mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation; v-SNARE domain-containing protein similar to Vti1 (vesicle transport through interaction with t-SNAREs homolog 1) which belongs to the Qb subgroup of SNAREs (soluble N-ethylmaleimide-sensitive factor attachment protein receptor)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SynN cd00179
Syntaxin N-terminus domain; syntaxins are nervous system-specific proteins implicated in the ...
42-187 1.55e-42

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: 143.19  E-value: 1.55e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443287677  42 QVRTIRQTIVKLGNKVQELEKQQVTILATPLPEESMKQELQNLRDEIKQLGREIRLQLKAIEPQKEEADENYNSVNTRMR 121
Cdd:cd00179    7 EVEEIRGNIDKISEDVEELQKLHSQLLTAPDADPELKQELESLVQEIKKLAKEIKGKLKELEESNEQNEALNGSSVDRIR 86
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 443287677 122 KTQHGVLSQQFVELINKCNSMQSEYREKNVERIRRQLKITNaGMVSDEELEQMLDSGQSEVFVSNI 187
Cdd:cd00179   87 KTQHSGLSKKFVEVMTEFNKAQRKYRERYKERIQRQLEITG-GEATDEELEDMLESGNSEIFTSQI 151
SNARE_syntaxin4 cd15883
SNARE motif of syntaxin 4; Syntaxin-4 forms a complex with SNAP-23 (Qb/Qc) and R-SNAREs VAMP8, ...
197-259 9.35e-30

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: 107.34  E-value: 9.35e-30
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 443287677 197 ALNEISARHSEIQQLERSIRELHDIFTFLATEVEMQGEMINRIEKNILSSADYVERGQEHVKT 259
Cdd:cd15883    1 ALNEIEARHSEIQKLERSIRELHDMFTYLAMEVEAQGEMIDRIEKNILSSADYVEKAQEHVKT 63
 
Name Accession Description Interval E-value
SynN cd00179
Syntaxin N-terminus domain; syntaxins are nervous system-specific proteins implicated in the ...
42-187 1.55e-42

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: 143.19  E-value: 1.55e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443287677  42 QVRTIRQTIVKLGNKVQELEKQQVTILATPLPEESMKQELQNLRDEIKQLGREIRLQLKAIEPQKEEADENYNSVNTRMR 121
Cdd:cd00179    7 EVEEIRGNIDKISEDVEELQKLHSQLLTAPDADPELKQELESLVQEIKKLAKEIKGKLKELEESNEQNEALNGSSVDRIR 86
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 443287677 122 KTQHGVLSQQFVELINKCNSMQSEYREKNVERIRRQLKITNaGMVSDEELEQMLDSGQSEVFVSNI 187
Cdd:cd00179   87 KTQHSGLSKKFVEVMTEFNKAQRKYRERYKERIQRQLEITG-GEATDEELEDMLESGNSEIFTSQI 151
Syntaxin pfam00804
Syntaxin; Syntaxins are the prototype family of SNARE proteins. They usually consist of three ...
42-233 8.49e-33

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


Pssm-ID: 459942 [Multi-domain]  Cd Length: 203  Bit Score: 119.59  E-value: 8.49e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443287677   42 QVRTIRQTIVKLGNKVQELEKQQV--TILATPLPEESMKQELQNLRDEIKQLGREIRLQLKAIEPQKEEADENY----NS 115
Cdd:pfam00804   5 EVQEIKEEIEKIRLLVKKLQKQNEesKLLTSARRMSVIKRRMNSIARDIKKRAESIKRRLEALDKSNAENEKKPgcgpGS 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443287677  116 VNTRMRKTQHGVLSQQFVELINKCNSMQSEYREKNVERIRRQLKITNAGMVSDEELEQMLDSGQSEVFVSNIL-KDTQVT 194
Cdd:pfam00804  85 AVDRIRRSQTAALRKKLKEVMAEYNELRERIREEYKEVIQRQYETVTGKEVSEEEIEEMIETGSESVFQKAILeQGRGQA 164
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 443287677  195 RQALNEISARHSEIQQLERSIRELHDIFTFLATEVEMQG 233
Cdd:pfam00804 165 RSALSEIEERHKELKELESSLKELHQIFLDMAVLVEAQG 203
SNARE_syntaxin4 cd15883
SNARE motif of syntaxin 4; Syntaxin-4 forms a complex with SNAP-23 (Qb/Qc) and R-SNAREs VAMP8, ...
197-259 9.35e-30

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: 107.34  E-value: 9.35e-30
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 443287677 197 ALNEISARHSEIQQLERSIRELHDIFTFLATEVEMQGEMINRIEKNILSSADYVERGQEHVKT 259
Cdd:cd15883    1 ALNEIEARHSEIQKLERSIRELHDMFTYLAMEVEAQGEMIDRIEKNILSSADYVEKAQEHVKT 63
COG5074 COG5074
t-SNARE complex subunit, syntaxin [Intracellular trafficking, secretion, and vesicular ...
46-291 1.46e-25

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


Pssm-ID: 227406 [Multi-domain]  Cd Length: 280  Bit Score: 102.66  E-value: 1.46e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443287677  46 IRQTIVKLGNKVQELEKQQVTILATPLPEESM--KQELQNLRDEIKQLGREIRLQLKAIEPQKeeadenynsVNTRMRKT 123
Cdd:COG5074   30 INKNLSVYEKEINQIDNLHKDLLTEVFEEQSRklRRSLDNFSSQTTDLQRNLKKDIKSAERDG---------IHLANKQA 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443287677 124 QHGVLSQQFVELINKCNSMQSEYREKNVERIRRQLKITNAGMVSDEELEQMLDSGQSEVFVSNILKDTQV--TRQALNEI 201
Cdd:COG5074  101 QAENVRQKFLKLIQDYRIIDSNYREEEKEQARRQYIIAQPEATEDEVEAAINDVNGQQVFSQALLNANRRgeAKTALAEV 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443287677 202 SARHSEIQQLERSIRELHDIFTFLATEVEMQGEMINRIEKNILSSADYVERGQEHVKTALENQKKARKKKVLI-AICVSI 280
Cdd:COG5074  181 QARHQEIKKIEKTMAELTQLFNDMEELVIEQQENVDVIDKNVEDAQENVEQGVGHTDKAVKSARAARKKKIRCyGICFII 260
                        250
                 ....*....|.
gi 443287677 281 TVVLLAVIIGV 291
Cdd:COG5074  261 IIVIVVVVFKV 271
SynN smart00503
Syntaxin N-terminal domain; Three-helix domain that (in Sso1p) slows the rate of its reaction ...
42-149 7.33e-25

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: 96.26  E-value: 7.33e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443287677    42 QVRTIRQTIVKLGNKVQELEKQQVTILATPLPEESMKQELQNLRDEIKQLGREIRLQLKAIEPQKEEADENyNSVNTRMR 121
Cdd:smart00503   9 KVEEIRANIQKISQNVAELQKLHEELLTPPDADKELREKLERLIDDIKRLAKEIRAKLKELEKENLENRAS-GSASDRTR 87
                           90       100
                   ....*....|....*....|....*...
gi 443287677   122 KTQHGVLSQQFVELINKCNSMQSEYREK 149
Cdd:smart00503  88 KAQTEKLRKKFKEVMNEFQRLQRKYRER 115
t_SNARE smart00397
Helical region found in SNAREs; All alpha-helical motifs that form twisted and parallel ...
195-260 1.90e-13

Helical region found in SNAREs; All alpha-helical motifs that form twisted and parallel four-helix bundles in target soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein (SNAP) receptor proteins. This motif found in "Q-SNAREs".


Pssm-ID: 197699 [Multi-domain]  Cd Length: 66  Bit Score: 64.14  E-value: 1.90e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 443287677   195 RQALNEISARHSEIQQLERSIRELHDIFTFLATEVEMQGEMINRIEKNILSSADYVERGQEHVKTA 260
Cdd:smart00397   1 QQALAREEERDEELEQLEKSIQELKQIFLDMGTELEEQGEQLDRIEDNVDDADVNLKKANKRLKKA 66
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
78-269 1.26e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.43  E-value: 1.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443287677    78 KQELQNLRDEIKQLGREIRLQLKAIEpQKEEADENYNSVNTRMRKTQHGvLSQQFVELINKCNSMQSEyREKNVERIRRQ 157
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALA-ELRKELEELEEELEQLRKELEE-LSRQISALRKDLARLEAE-VEQLEERIAQL 752
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443287677   158 LKITNAGMVSDEELEQMLDSGQSEvfvsniLKDTQVTRQALNEISARHS-EIQQLERSIRELHDIFTFLATEVEMQGEMI 236
Cdd:TIGR02168  753 SKELTELEAEIEELEERLEEAEEE------LAEAEAEIEELEAQIEQLKeELKALREALDELRAELTLLNEEAANLRERL 826
                          170       180       190
                   ....*....|....*....|....*....|...
gi 443287677   237 NRIEKNILSSADYVERGQEHVKTALENQKKARK 269
Cdd:TIGR02168  827 ESLERRIAATERRLEDLEEQIEELSEDIESLAA 859
 
Name Accession Description Interval E-value
SynN cd00179
Syntaxin N-terminus domain; syntaxins are nervous system-specific proteins implicated in the ...
42-187 1.55e-42

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: 143.19  E-value: 1.55e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443287677  42 QVRTIRQTIVKLGNKVQELEKQQVTILATPLPEESMKQELQNLRDEIKQLGREIRLQLKAIEPQKEEADENYNSVNTRMR 121
Cdd:cd00179    7 EVEEIRGNIDKISEDVEELQKLHSQLLTAPDADPELKQELESLVQEIKKLAKEIKGKLKELEESNEQNEALNGSSVDRIR 86
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 443287677 122 KTQHGVLSQQFVELINKCNSMQSEYREKNVERIRRQLKITNaGMVSDEELEQMLDSGQSEVFVSNI 187
Cdd:cd00179   87 KTQHSGLSKKFVEVMTEFNKAQRKYRERYKERIQRQLEITG-GEATDEELEDMLESGNSEIFTSQI 151
Syntaxin pfam00804
Syntaxin; Syntaxins are the prototype family of SNARE proteins. They usually consist of three ...
42-233 8.49e-33

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


Pssm-ID: 459942 [Multi-domain]  Cd Length: 203  Bit Score: 119.59  E-value: 8.49e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443287677   42 QVRTIRQTIVKLGNKVQELEKQQV--TILATPLPEESMKQELQNLRDEIKQLGREIRLQLKAIEPQKEEADENY----NS 115
Cdd:pfam00804   5 EVQEIKEEIEKIRLLVKKLQKQNEesKLLTSARRMSVIKRRMNSIARDIKKRAESIKRRLEALDKSNAENEKKPgcgpGS 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443287677  116 VNTRMRKTQHGVLSQQFVELINKCNSMQSEYREKNVERIRRQLKITNAGMVSDEELEQMLDSGQSEVFVSNIL-KDTQVT 194
Cdd:pfam00804  85 AVDRIRRSQTAALRKKLKEVMAEYNELRERIREEYKEVIQRQYETVTGKEVSEEEIEEMIETGSESVFQKAILeQGRGQA 164
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 443287677  195 RQALNEISARHSEIQQLERSIRELHDIFTFLATEVEMQG 233
Cdd:pfam00804 165 RSALSEIEERHKELKELESSLKELHQIFLDMAVLVEAQG 203
SNARE_syntaxin4 cd15883
SNARE motif of syntaxin 4; Syntaxin-4 forms a complex with SNAP-23 (Qb/Qc) and R-SNAREs VAMP8, ...
197-259 9.35e-30

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: 107.34  E-value: 9.35e-30
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 443287677 197 ALNEISARHSEIQQLERSIRELHDIFTFLATEVEMQGEMINRIEKNILSSADYVERGQEHVKT 259
Cdd:cd15883    1 ALNEIEARHSEIQKLERSIRELHDMFTYLAMEVEAQGEMIDRIEKNILSSADYVEKAQEHVKT 63
COG5074 COG5074
t-SNARE complex subunit, syntaxin [Intracellular trafficking, secretion, and vesicular ...
46-291 1.46e-25

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


Pssm-ID: 227406 [Multi-domain]  Cd Length: 280  Bit Score: 102.66  E-value: 1.46e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443287677  46 IRQTIVKLGNKVQELEKQQVTILATPLPEESM--KQELQNLRDEIKQLGREIRLQLKAIEPQKeeadenynsVNTRMRKT 123
Cdd:COG5074   30 INKNLSVYEKEINQIDNLHKDLLTEVFEEQSRklRRSLDNFSSQTTDLQRNLKKDIKSAERDG---------IHLANKQA 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443287677 124 QHGVLSQQFVELINKCNSMQSEYREKNVERIRRQLKITNAGMVSDEELEQMLDSGQSEVFVSNILKDTQV--TRQALNEI 201
Cdd:COG5074  101 QAENVRQKFLKLIQDYRIIDSNYREEEKEQARRQYIIAQPEATEDEVEAAINDVNGQQVFSQALLNANRRgeAKTALAEV 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443287677 202 SARHSEIQQLERSIRELHDIFTFLATEVEMQGEMINRIEKNILSSADYVERGQEHVKTALENQKKARKKKVLI-AICVSI 280
Cdd:COG5074  181 QARHQEIKKIEKTMAELTQLFNDMEELVIEQQENVDVIDKNVEDAQENVEQGVGHTDKAVKSARAARKKKIRCyGICFII 260
                        250
                 ....*....|.
gi 443287677 281 TVVLLAVIIGV 291
Cdd:COG5074  261 IIVIVVVVFKV 271
SynN smart00503
Syntaxin N-terminal domain; Three-helix domain that (in Sso1p) slows the rate of its reaction ...
42-149 7.33e-25

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: 96.26  E-value: 7.33e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443287677    42 QVRTIRQTIVKLGNKVQELEKQQVTILATPLPEESMKQELQNLRDEIKQLGREIRLQLKAIEPQKEEADENyNSVNTRMR 121
Cdd:smart00503   9 KVEEIRANIQKISQNVAELQKLHEELLTPPDADKELREKLERLIDDIKRLAKEIRAKLKELEKENLENRAS-GSASDRTR 87
                           90       100
                   ....*....|....*....|....*...
gi 443287677   122 KTQHGVLSQQFVELINKCNSMQSEYREK 149
Cdd:smart00503  88 KAQTEKLRKKFKEVMNEFQRLQRKYRER 115
SNARE_syntaxin1-like cd15848
SNARE motif of syntaxin 1 and related proteins; SNARE (soluble N-ethylmaleimide-sensitive ...
197-259 7.67e-24

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: 91.83  E-value: 7.67e-24
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 443287677 197 ALNEISARHSEIQQLERSIRELHDIFTFLATEVEMQGEMINRIEKNILSSADYVERGQEHVKT 259
Cdd:cd15848    1 ALADIEERHQDILKLEKSIRELHQMFLDMAVLVESQGELIDNIEYNVEKAKDYVEKGNEELKK 63
SNARE_syntaxin2 cd15882
SNARE motif of syntaxin 2; Syntaxin 2 (STX2), also known as epimorphin (EPM or EPIM), may ...
197-264 1.05e-19

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: 81.24  E-value: 1.05e-19
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 443287677 197 ALNEISARHSEIQQLERSIRELHDIFTFLATEVEMQGEMINRIEKNILSSADYVERGQEHVKTALENQ 264
Cdd:cd15882    1 ALNEIESRHKDIMKLESSIRELHDMFVDMAMLVETQGEMINNIEKNVHNAVEYVEHAKEETKKAVKYQ 68
SNARE_syntaxin1 cd15880
SNARE motif of syntaxin 1; Syntaxin-1 belongs to the Qa subgroup of SNAREs and interacts with ...
197-264 2.96e-17

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: 74.47  E-value: 2.96e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 443287677 197 ALNEISARHSEIQQLERSIRELHDIFTFLATEVEMQGEMINRIEKNILSSADYVERGQEHVKTALENQ 264
Cdd:cd15880    1 ALSEIEARHNDIIKLENSIRELHDMFMDMAMLVESQGEMIDRIEYNVEHAVDYVERAVSDTKKAVKYQ 68
SNARE_syntaxin3 cd15881
SNARE motif of syntaxin 3; Syntaxin 3 (STX3) has been shown to form a complex with VAMP8 ...
197-265 7.15e-16

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: 70.82  E-value: 7.15e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 443287677 197 ALNEISARHSEIQQLERSIRELHDIFTFLATEVEMQGEMINRIEKNILSSADYVERGQEHVKTALENQK 265
Cdd:cd15881    1 ALSEIEGRHKDIVRLESSIKELHDMFVDIAMLVENQGEMLDNIELNVMKTVDHVEKARDETKKAVKYQS 69
t_SNARE smart00397
Helical region found in SNAREs; All alpha-helical motifs that form twisted and parallel ...
195-260 1.90e-13

Helical region found in SNAREs; All alpha-helical motifs that form twisted and parallel four-helix bundles in target soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein (SNAP) receptor proteins. This motif found in "Q-SNAREs".


Pssm-ID: 197699 [Multi-domain]  Cd Length: 66  Bit Score: 64.14  E-value: 1.90e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 443287677   195 RQALNEISARHSEIQQLERSIRELHDIFTFLATEVEMQGEMINRIEKNILSSADYVERGQEHVKTA 260
Cdd:smart00397   1 QQALAREEERDEELEQLEKSIQELKQIFLDMGTELEEQGEQLDRIEDNVDDADVNLKKANKRLKKA 66
SNARE_Qa cd15840
SNARE motif, subgroup Qa; SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein ...
201-258 1.58e-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: 1.58e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 443287677 201 ISARHSEIQQLERSIRELHDIFTFLATEVEMQGEMINRIEKNILSSADYVERGQEHVK 258
Cdd:cd15840    1 IEEREEEIREIESSIGEVNEIFKDLATLVTEQGEQIDNIENNIEEAAANTEEANKELR 58
COG5325 COG5325
t-SNARE complex subunit, syntaxin [Intracellular trafficking and secretion];
42-288 1.70e-12

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


Pssm-ID: 227635 [Multi-domain]  Cd Length: 283  Bit Score: 66.40  E-value: 1.70e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443287677  42 QVRTIRQTIVKLGNKVQELEKQQVtILATPLPEESMKQElqnlrDEIKQLGREIRLQLKAIEPQKEEADENYNSvNTRMR 121
Cdd:COG5325   39 SAASVDQELTAVRRSISRLGKVYA-KHTEPSFSDKSEKE-----DEIDELSKKVNQDLQRCEKILKTKYKNLQS-SFLQS 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443287677 122 KtqhgvLSQQFVELINKCNSMQSEYREKNVERIRRQ----LKITNAGMVSDEELEQMLDSGQSEVFVSNILKDTQVTRQA 197
Cdd:COG5325  112 K-----LLRDLNTECMEGQRIQQKSAQFRKYQVLQAkflrNKNNDQHPLEEEEDEESLSSLGSQQTLQQQGLSNEELEYQ 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443287677 198 LNEISARHSEIQQLERSIRELHDIFTFLATEVEMQGEMINRIEKNILSSADYVERGQEHVKTALENQKKARKKKV--LIA 275
Cdd:COG5325  187 QILITERDEEIKNLARGIYELNEIFRDLGSLVGEQGELVDRIDFNIENTSDNLKNANKELEKAPAHQRRTKKCRFylLLI 266
                        250
                 ....*....|...
gi 443287677 276 ICVSITVVLLAVI 288
Cdd:COG5325  267 LLVVLLFVSLIKK 279
SNARE_Sso1 cd15849
SNARE motif of Sso1; Saccharomyces cerevisiae SNARE protein Sso1p forms a complex with ...
198-260 3.24e-11

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: 57.92  E-value: 3.24e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 443287677 198 LNEISARHSEIQQLERSIRELHDIFTFLATEVEMQGEMINRIEKNILSSADYVERGQEHVKTA 260
Cdd:cd15849    1 LGEVQARHNEIQRIEQTLTELAQLFNDMATLVEQQDEVIQQIEQNAEEVETDLEKGNVHLEKA 63
SNARE_syntaxin11 cd15878
SNARE motif of syntaxin 11; Syntaxin 11 (also known as STX11, FHL4, HLH4, HPLH4) is present on ...
197-258 4.47e-11

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: 57.55  E-value: 4.47e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 443287677 197 ALNEISARHSEIQQLERSIRELHDIFTFLATEVEMQGEMINRIEKNILSSADYVERGQEHVK 258
Cdd:cd15878    1 ALNEIETRHKELLELESRIREVHELFLQMALLVEEQADTLNNIELNVEKTQDYVGKAKAQVK 62
SNARE_syntaxin12 cd15876
SNARE motif of syntaxin 12; Syntaxin 12 (STX12, also known as STX13 and STX14) forms a complex ...
201-267 3.53e-10

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: 55.05  E-value: 3.53e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 443287677 201 ISARHSEIQQLERSIRELHDIFTFLATEVEMQGEMINRIEKNILSSADYVERGQEHVKTALENQKKA 267
Cdd:cd15876    1 IKERETAIQQLEADILDVNQIFKDLAMMIHDQGDMIDSIEANVESAEVHVERASEQLQRAAYYQKKS 67
SNARE pfam05739
SNARE domain; Most if not all vesicular membrane fusion events in eukaryotic cells are ...
234-285 1.10e-09

SNARE domain; Most if not all vesicular membrane fusion events in eukaryotic cells are believed to be mediated by a conserved fusion machinery, the SNARE [soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein (SNAP) receptors] machinery. The SNARE domain is thought to act as a protein-protein interaction module in the assembly of a SNARE protein complex.


Pssm-ID: 461727 [Multi-domain]  Cd Length: 52  Bit Score: 53.19  E-value: 1.10e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 443287677  234 EMINRIEKNILSSADYVERGQEHVKTALENQKKARKKKVLIAICVSITVVLL 285
Cdd:pfam05739   1 EMLDRIDTNVENAQSNVERAQKELKKAVKYQKSNRKLKCIILLILVIILLVV 52
SNARE_syntaxin5 cd15844
SNARE motif of syntaxin 5; Syntaxin 5 (Syn5) regulates the transport from the ER to the Golgi, ...
201-282 1.95e-09

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: 53.67  E-value: 1.95e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443287677 201 ISARHSEIQQLERSIRELHDIFTFLATEVEMQGEMINRIEKNILSSADYVERGQEHVKTALENQKKARK--KKVLIAICV 278
Cdd:cd15844    1 LQSRADAVQNIESTIVELGQIFQQLATMVAEQGEMVQRIDENVEDALANVEAAHSELLKYYRSISSNRWliLKIFGVLIV 80

                 ....
gi 443287677 279 SITV 282
Cdd:cd15844   81 FIVI 84
SNARE_syntaxin19 cd15879
SNARE motif of syntaxin 19; Syntaxin 19 has been shown to have the potential to form SNARE ...
198-258 7.32e-08

SNARE motif of syntaxin 19; Syntaxin 19 has been shown to have the potential to form SNARE complexes with SNAP-23, 25 and 29 (Qb/Qc) and VAMP3 and VAMP8 (R-SNARE), indicating a role in post-Golgi trafficking or plasma membrane fusion. Syntaxin 19 is member of the Qa subgroup of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins, which consist of coiled-coil helices (called SNARE motifs) that mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complexes mediate membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle.


Pssm-ID: 277232  Cd Length: 63  Bit Score: 48.29  E-value: 7.32e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 443287677 198 LNEISARHSEIQQLERSIRELHDIFTFLATEVEMQGEMINRIEKNILSSADYVERGQEHVK 258
Cdd:cd15879    2 LSEIEQRHKELVSLENQIKDLKDLFIQISLLVEEQGEMINNIEISVNNTQEYVQASKEKFG 62
SNARE_syntaxin7_like cd15847
SNARE motif of syntaxin 7, 12 and related sequences; SNARE (soluble N-ethylmaleimide-sensitive ...
204-260 1.22e-07

SNARE motif of syntaxin 7, 12 and related sequences; SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins consist of coiled-coil helices (called SNARE motifs) which mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles. This subgroup of the Qa SNAREs includes syntaxin 7, syntaxin 12, TSNARE1 and related proteins.


Pssm-ID: 277200 [Multi-domain]  Cd Length: 60  Bit Score: 47.57  E-value: 1.22e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 443287677 204 RHSEIQQLERSIRELHDIFTFLATEVEMQGEMINRIEKNILSSADYVERGQEHVKTA 260
Cdd:cd15847    4 REERIRQIESDILDVNQIFKDLATLVHEQGETIDSIEANIESAYVNVESGNSQLAKA 60
SNARE_syntaxin16 cd15845
SNARE motif of syntaxin 16; Syntaxin 16 is located in trans-Golgi network (TGN) and regulated ...
201-258 2.74e-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: 43.99  E-value: 2.74e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 443287677 201 ISARHSEIQQLERSIRELHDIFTFLATEVEMQGEMINRIEKNILSSADYVERGQEHVK 258
Cdd:cd15845    1 IQERDREIAKIVESINELAEIFKDLATLVIEQGTILDRIDYNIEQTATRVEKGVKELK 58
SNARE_syntaxin7 cd15875
SNARE motif of syntaxin 7; Syntaxin 7 forms a complex with syntaxin 8 (Qc), Vti1b (Qb) and ...
201-260 3.29e-06

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: 43.58  E-value: 3.29e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 443287677 201 ISARHSEIQQLERSIRELHDIFTFLATEVEMQGEMINRIEKNILSSADYVERGQEHVKTA 260
Cdd:cd15875    1 LEERERSIRQLESDIMDVNQIFKDLGMLVHEQGEVIDSIEANVETAAVHVEEANQQLSQA 60
SNARE cd00193
SNARE motif; SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) ...
206-252 4.61e-06

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: 43.14  E-value: 4.61e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 443287677 206 SEIQQLERSIRELHDIFTFLATEVEMQGEMINRIEKNILSSADYVER 252
Cdd:cd00193    1 ESLEQLEASIGELKDIGRDMAMELEEQGEQLDRIEERAESTQARVSR 47
SNARE_syntaxin17 cd15846
SNARE motif of syntaxin 17; Synthaxin 17 (STX17) belongs to the Qa subgroup of SNAREs and ...
207-256 1.71e-05

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: 41.89  E-value: 1.71e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 443287677 207 EIQQLERSIRELHDIFTFLATEVEMQGEMINRIEKNILSSADYVERGQEH 256
Cdd:cd15846   10 SWETLQQDLEDLHGLFTDFHQLVHDQGEQVDTIEDNVEEALENVQEGTKN 59
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
57-264 1.03e-03

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 40.48  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443287677   57 VQELEKQQVTILATPLPEESMKQELQNL-------RDEIKQLGREIRLQLKAIEPQKEEADENYNSVNTRMRKTQhgvls 129
Cdd:pfam05483 512 TLELKKHQEDIINCKKQEERMLKQIENLeekemnlRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKE----- 586
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443287677  130 QQFVELINKCNSM--QSEYREKNVERIRRQLK-ITNAGMVSDEELEQMldsgqsEVFVSNILKDTQVTRQALNEISARHS 206
Cdd:pfam05483 587 KQMKILENKCNNLkkQIENKNKNIEELHQENKaLKKKGSAENKQLNAY------EIKVNKLELELASAKQKFEEIIDNYQ 660
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 443287677  207 ---EIQQL--ERSIRELHDIFTFLATEVEMQGEMINRIEKNILSSADYVERGQEHVKTALENQ 264
Cdd:pfam05483 661 keiEDKKIseEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEER 723
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
78-269 1.26e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.43  E-value: 1.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443287677    78 KQELQNLRDEIKQLGREIRLQLKAIEpQKEEADENYNSVNTRMRKTQHGvLSQQFVELINKCNSMQSEyREKNVERIRRQ 157
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALA-ELRKELEELEEELEQLRKELEE-LSRQISALRKDLARLEAE-VEQLEERIAQL 752
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443287677   158 LKITNAGMVSDEELEQMLDSGQSEvfvsniLKDTQVTRQALNEISARHS-EIQQLERSIRELHDIFTFLATEVEMQGEMI 236
Cdd:TIGR02168  753 SKELTELEAEIEELEERLEEAEEE------LAEAEAEIEELEAQIEQLKeELKALREALDELRAELTLLNEEAANLRERL 826
                          170       180       190
                   ....*....|....*....|....*....|...
gi 443287677   237 NRIEKNILSSADYVERGQEHVKTALENQKKARK 269
Cdd:TIGR02168  827 ESLERRIAATERRLEDLEEQIEELSEDIESLAA 859
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
42-241 2.18e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 39.67  E-value: 2.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443287677    42 QVRTIRQTIVKLGNKVQELEKQQVTILATPLPEESMKQELQNLRDEIKQLGREIRLQLKAIEPQKEEADENYNSVNTRMR 121
Cdd:TIGR02169  799 ELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALR 878
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443287677   122 K--TQHGVLSQQFVELINKCNSMQSEYREKN--VERIRRQLKITNA--GMVSDE--ELEQMLDSGQSEVFVSNILKDTQV 193
Cdd:TIGR02169  879 DleSRLGDLKKERDELEAQLRELERKIEELEaqIEKKRKRLSELKAklEALEEElsEIEDPKGEDEEIPEEELSLEDVQA 958
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 443287677   194 TRQALN-EISARHS----EIQQLERSIRELHDIFTFLATEVEMQGEMINRIEK 241
Cdd:TIGR02169  959 ELQRVEeEIRALEPvnmlAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEE 1011
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
42-272 4.79e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.38  E-value: 4.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443287677  42 QVRTIRQTIVKLGNKVQELEKQQVTILATplpEESMKQELQNLRDEIKQLGREIRLQLKAIEpqKEEADENYNSVNTRMR 121
Cdd:COG1196  240 ELEELEAELEELEAELEELEAELAELEAE---LEELRLELEELELELEEAQAEEYELLAELA--RLEQDIARLEERRREL 314
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443287677 122 KTQHGVLSQQFVELINKCNSMQSEYREKNVERIRRQLKITNAGMVSDEELEQMLDsgQSEVFVSNILKDTQVTRQALNEI 201
Cdd:COG1196  315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE--AEAELAEAEEELEELAEELLEAL 392
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 443287677 202 SARHSEIQQLERSIRELHDiftfLATEVEMQGEMINRIEKNILSSADYVERGQEHVKTALENQKKARKKKV 272
Cdd:COG1196  393 RAAAELAAQLEELEEAEEA----LLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459
PilO COG3167
Type IV pilus assembly protein PilO [Cell motility, Extracellular structures];
42-121 5.22e-03

Type IV pilus assembly protein PilO [Cell motility, Extracellular structures];


Pssm-ID: 442400 [Multi-domain]  Cd Length: 202  Bit Score: 37.23  E-value: 5.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443287677  42 QVRTIRQTIVKLGNKVQELE--KQQVTILATPLPEesmKQELQNLRDEIKQLGREIRLQLKAIEPQKEEADENYNSVNTR 119
Cdd:COG3167   61 ELEKKQAKAANLPALKAQLEelEQQLGELLKQLPS---KAEVPALLDDISQAALGSGLEFELFKPGPEVPKEFYAELPIS 137

                 ..
gi 443287677 120 MR 121
Cdd:COG3167  138 IR 139
SNARE_TSNARE1 cd15877
SNARE motif of TSNARE1; TSNARE1 is member of the Qa subgroup of SNARE (soluble ...
198-260 6.49e-03

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: 34.62  E-value: 6.49e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 443287677 198 LNEISARHSEIQQLERSIRELHDIFTFLATEVEMQGEMINRIEKNILSSADYVERGQEHVKTA 260
Cdd:cd15877    1 LEAIRQREEAIQQIESDMLDVNQIIKDLASMVSEQGDTIDSIEANIEAASSHVESANQQLAKA 63
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
75-221 9.60e-03

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 37.04  E-value: 9.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443287677   75 ESMKQELQNLRDEIKQLGREIRLQLKAIEPQKEEADENYNSVNTRMRKTQHGVLSQQFV------ELINKCNSMQSEY-- 146
Cdd:pfam09787  64 QKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQLATERSARREAEAELERLQEElryleeELRRSKATLQSRIkd 143
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 443287677  147 REKNVERIRRQLKITNAGMVSDEELEQMLDSgqsevfvsniLKDTQVTRQALNEI--SARHSEIQQLERSIRELHDI 221
Cdd:pfam09787 144 REAEIEKLRNQLTSKSQSSSSQSELENRLHQ----------LTETLIQKQTMLEAlsTEKNSLVLQLERMEQQIKEL 210
 
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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