NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1297777268|ref|XP_023053736|]
View 

synaptosomal-associated protein 29 [Piliocolobus tephrosceles]

Protein Classification

SNARE domain-containing protein; syntaxin family protein( domain architecture ID 10205263)

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; syntaxin family protein similar to syntaxin 5 (Syn5) that 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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
SNARE_SNAP29N cd15887
N-terminal SNARE motif of SNAP29; N-terminal SNARE motif of SNAP29, a member of the Qb/Qc ...
 47-111 1.33e-33

N-terminal SNARE motif of SNAP29; N-terminal SNARE motif of SNAP29, a member of the Qb/Qc subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins. SNAP29 interacts with STX17 (Qa) 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. Qb/Qc SNAREs consist of 2 coiled-coil helices (called SNARE motifs, one belonging to the Qb subgroup and one belonging to the Qc subgroup), which mediate the interactions with other SNARE proteins, and a transmembrane domain. In general, 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. Other members of the Qb/Qc SNAREs are SNAP23, SNAP25, SNAP47 and SEC9.


:

Pssm-ID: 277240  Cd Length: 65  Bit Score: 117.37  E-value: 1.33e-33
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1297777268  47 QEVLRRAEATAASTSRSLALMYESEKVGVASSEELVRQRGVLERTEKMVDKMDQDLKISQKHINS 111
Cdd:cd15887     1 QEIRRSEQRTLDSTQRSLGLLYESEQIGVATAEELVRQGEQLERTEKNLDKINQDLKTSQRHINS 65
 
Name Accession Description Interval E-value
SNARE_SNAP29N cd15887
N-terminal SNARE motif of SNAP29; N-terminal SNARE motif of SNAP29, a member of the Qb/Qc ...
 47-111 1.33e-33

N-terminal SNARE motif of SNAP29; N-terminal SNARE motif of SNAP29, a member of the Qb/Qc subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins. SNAP29 interacts with STX17 (Qa) 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. Qb/Qc SNAREs consist of 2 coiled-coil helices (called SNARE motifs, one belonging to the Qb subgroup and one belonging to the Qc subgroup), which mediate the interactions with other SNARE proteins, and a transmembrane domain. In general, 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. Other members of the Qb/Qc SNAREs are SNAP23, SNAP25, SNAP47 and SEC9.


Pssm-ID: 277240  Cd Length: 65  Bit Score: 117.37  E-value: 1.33e-33
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1297777268  47 QEVLRRAEATAASTSRSLALMYESEKVGVASSEELVRQRGVLERTEKMVDKMDQDLKISQKHINS 111
Cdd:cd15887     1 QEIRRSEQRTLDSTQRSLGLLYESEQIGVATAEELVRQGEQLERTEKNLDKINQDLKTSQRHINS 65
t_SNARE smart00397
Helical region found in SNAREs; All alpha-helical motifs that form twisted and parallel ...
 47-112 1.40e-07

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: 47.58  E-value: 1.40e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1297777268   47 QEVLRRAEATAASTSRSLALMYESEKVGVASSEELVRQRGVLERTEKMVDKMDQDLKISQKHINSI 112
Cdd:smart00397   1 QQALAREEERDEELEQLEKSIQELKQIFLDMGTELEEQGEQLDRIEDNVDDADVNLKKANKRLKKA 66
V-SNARE_C pfam12352
Snare region anchored in the vesicle membrane C-terminus; Within the SNARE proteins ...
 62-113 5.28e-03

Snare region anchored in the vesicle membrane C-terminus; Within the SNARE proteins interactions in the C-terminal half of the SNARE helix are critical to the driving of membrane fusion; whereas interactions in the N-terminal half of the SNARE domain are important for promoting priming or docking of the vesicle pfam05008.


Pssm-ID: 289148  Cd Length: 66  Bit Score: 34.89  E-value: 5.28e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1297777268  62 RSLALMYESEKVGVASSEELVRQRGVLERTEKMVDKMDQDLKISQKHINSIK 113
Cdd:pfam12352  12 NSHRIADETISIGQAILEDLHSQRETLKRARNKLHNTDNRLGKSNSTLRLIN 63
 
Name Accession Description Interval E-value
SNARE_SNAP29N cd15887
N-terminal SNARE motif of SNAP29; N-terminal SNARE motif of SNAP29, a member of the Qb/Qc ...
 47-111 1.33e-33

N-terminal SNARE motif of SNAP29; N-terminal SNARE motif of SNAP29, a member of the Qb/Qc subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins. SNAP29 interacts with STX17 (Qa) 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. Qb/Qc SNAREs consist of 2 coiled-coil helices (called SNARE motifs, one belonging to the Qb subgroup and one belonging to the Qc subgroup), which mediate the interactions with other SNARE proteins, and a transmembrane domain. In general, 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. Other members of the Qb/Qc SNAREs are SNAP23, SNAP25, SNAP47 and SEC9.


Pssm-ID: 277240  Cd Length: 65  Bit Score: 117.37  E-value: 1.33e-33
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1297777268  47 QEVLRRAEATAASTSRSLALMYESEKVGVASSEELVRQRGVLERTEKMVDKMDQDLKISQKHINS 111
Cdd:cd15887     1 QEIRRSEQRTLDSTQRSLGLLYESEQIGVATAEELVRQGEQLERTEKNLDKINQDLKTSQRHINS 65
SNARE_SNAP25N_23N_29N_SEC9N cd15861
N-terminal SNARE motif of SNAP25, SNAP23, SNAP29, and SEC9; N-terminal SNARE motif of members ...
 47-111 2.89e-13

N-terminal SNARE motif of SNAP25, SNAP23, SNAP29, and SEC9; N-terminal SNARE motif of members of the Qb/Qc subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins. Qb/Qc SNAREs consist of 2 coiled-coil helices (called SNARE motifs, one belonging to the Qb subgroup and one belonging to the Qc subgroup), which mediate the interactions with other SNARE proteins, and a transmembrane domain. In general, 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 Qb/Qc SNAREs are SNAP23, SNAP25, SNAP29, SNAP47 and SEC9.


Pssm-ID: 277214  Cd Length: 65  Bit Score: 63.36  E-value: 2.89e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1297777268  47 QEVLRRAEATAASTSRSLALMYESEKVGVASSEELVRQRGVLERTEKMVDKMDQDLKISQKHINS 111
Cdd:cd15861     1 QEADKTQDETTESIRRALRLAEETKEIGADTLEELHRQGEQLERIHNDVDDIDSNLKRAEKLLKE 65
t_SNARE smart00397
Helical region found in SNAREs; All alpha-helical motifs that form twisted and parallel ...
 47-112 1.40e-07

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: 47.58  E-value: 1.40e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1297777268   47 QEVLRRAEATAASTSRSLALMYESEKVGVASSEELVRQRGVLERTEKMVDKMDQDLKISQKHINSI 112
Cdd:smart00397   1 QQALAREEERDEELEQLEKSIQELKQIFLDMGTELEEQGEQLDRIEDNVDDADVNLKKANKRLKKA 66
SNARE_Vti1b cd15890
SNARE motif of Vti1b-like; Vti1b (vesicle transport through interaction with t-SNAREs homolog ...
 54-111 8.55e-06

SNARE motif of Vti1b-like; Vti1b (vesicle transport through interaction with t-SNAREs homolog 1B) belongs to the Qb subgroup of SNAREs (soluble N-ethylmaleimide-sensitive factor attachment protein receptor). Vti1b interacts with syntaxin 7 (Qa), syntaxin 8 (Qc), and the lysosomal R-SNARE VAMP8 or VAMP7 to form the endosomal SNARE core complexes that mediate transport from the early endosomes and the MVBs (multivesicular bodies), and from the MVBs to the lysosomes, respectively. SNARE 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 Qb SNAREs are N-terminal domains of SNAP23 and SNAP25, Vti1, Sec20 and GS27.


Pssm-ID: 277243  Cd Length: 62  Bit Score: 42.56  E-value: 8.55e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1297777268  54 EATAASTSRSLALMYESEKVGVASSEELVRQRGVLERTEKMVDKMDQDLKISQKHINS 111
Cdd:cd15890     5 NRTSDSLARSQRIAAETEQIGTEIIEELGEQREQLLRTRDRLEETDANLSRARRILRS 62
SNARE_Vti1 cd15862
SNARE motif of Vti1; Vti1 (vesicle transport through interaction with t-SNAREs homolog 1) ...
 61-111 5.61e-05

SNARE motif of Vti1; Vti1 (vesicle transport through interaction with t-SNAREs homolog 1) belongs to the Qb subgroup of SNAREs (soluble N-ethylmaleimide-sensitive factor attachment protein receptor). Vti1b interacts with syntaxin 7 (Qa), syntaxin 8 (Qc), and the lysosomal R-SNARE VAMP8 or VAMP7 to form the endosomal SNARE core complex that mediates transport from the early endosomes and the MVBs (multivesicular bodies), and from the MVBs to the lysosomes, respectively. Vti1a interacts with syntaxin 16 (Qa), syntaxin 6 (Qc), and the lysosomal R-SNARE VAMP4 to form an endosomal SNARE core complex that mediates transport from the early endosomes to the TGN (trans-Golgi network). SNARE 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 Qb SNAREs are N-terminal domains of SNAP23 and SNAP25, Vti1, Sec20 and GS27.


Pssm-ID: 277215  Cd Length: 62  Bit Score: 40.20  E-value: 5.61e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1297777268  61 SRSLALmyESEKVGVASSEELVRQRGVLERTEKMVDKMDQDLKISQKHINS 111
Cdd:cd15862    14 SRRIAA--ETEEVGANILEDLGRQRETLLRARDRLRETDGNLDRSRRILKS 62
SNARE_SNAP25N cd15894
N-terminal SNARE motif of SNAP25; N-terminal SNARE motifs of SNAP25, a member of the Qb/Qc ...
 47-112 1.46e-04

N-terminal SNARE motif of SNAP25; N-terminal SNARE motifs of SNAP25, a member of the Qb/Qc subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins. SNAP25 interacts with Syntaxin-1 (Qa) and the R-SNARE VAMP2 (also called synaptobrevin-2). The complex plays a role in transport of secretory granule from trans-Golgi network to the plasma membrane. Qb/Qc SNAREs consist of 2 coiled-coil helices (called SNARE motifs, one belonging to the Qb subgroup and one belonging to the Qc subgroup), which mediate the interactions with other SNARE proteins, and a transmembrane domain. In general, 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. Other members of the Qb/Qc SNAREs are SNAP23, SNAP29, SNAP47 and SEC9.


Pssm-ID: 277247  Cd Length: 73  Bit Score: 39.60  E-value: 1.46e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1297777268  47 QEVLRRAEATA----ASTSRSLALMYESEKVGVASSEELVRQRGVLERTEKMVDKMDQDLKISQKHINSI 112
Cdd:cd15894     3 EEMQRRADQLAdeslESTRRMLQLVEESKDAGIRTLVMLDEQGEQLDRVEEGMNHINQDMKEAEKNLKDL 72
SNARE_Qb cd15842
SNARE motif, subgroup Qb; SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein ...
 57-111 5.27e-04

SNARE motif, subgroup Qb; 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 Qb SNAREs are N-terminal domains of SNAP23 and SNAP25, Vti1, Sec20 and GS27.


Pssm-ID: 277195  Cd Length: 62  Bit Score: 37.47  E-value: 5.27e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1297777268  57 AASTSRSLALMYESEKVGVASSEELVRQRGVLERTEKMVDKMDQDLKISQKHINS 111
Cdd:cd15842     8 TESLRRSHRGMEELKQAGIETLEMLDEQREQLERTEERINSINGDIKLSRKILRK 62
SNARE_SNAP25N_23N cd15889
N-terminal SNARE motif of SNAP25 and SNAP23; N-terminal SNARE motifs of SNAP25 and SNAP23, ...
 58-108 6.94e-04

N-terminal SNARE motif of SNAP25 and SNAP23; N-terminal SNARE motifs of SNAP25 and SNAP23, members of the Qb/Qc subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins. SNAP23 interacts with STX4 (Qa) and the lysosomal R-SNARE VAMP8. The complex plays a role in transport of secretory granule from trans-Golgi network to the plasma membrane. SNAP25 interacts with Syntaxin-1 (Qa) and the R-SNARE VAMP2 (also called synaptobrevin-2). The complex plays a role in transport of secretory granule from trans-Golgi network to the plasma membrane. Qb/Qc SNAREs consist of 2 coiled-coil helices (called SNARE motifs, one belonging to the Qb subgroup and one belonging to the Qc subgroup), which mediate the interactions with other SNARE proteins, and a transmembrane domain. In general, 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. Other members of the Qb/Qc SNAREs are SNAP29, SNAP47 and SEC9.


Pssm-ID: 277242  Cd Length: 65  Bit Score: 37.23  E-value: 6.94e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1297777268  58 ASTSRSLALMYESEKVGVASSEELVRQRGVLERTEKMVDKMDQDLKISQKH 108
Cdd:cd15889    12 ESTRRMLQLCEESQDAGIKTLVMLDEQGEQLDRIEEGMDQINADMKEAEKN 62
V-SNARE_C pfam12352
Snare region anchored in the vesicle membrane C-terminus; Within the SNARE proteins ...
 62-113 5.28e-03

Snare region anchored in the vesicle membrane C-terminus; Within the SNARE proteins interactions in the C-terminal half of the SNARE helix are critical to the driving of membrane fusion; whereas interactions in the N-terminal half of the SNARE domain are important for promoting priming or docking of the vesicle pfam05008.


Pssm-ID: 289148  Cd Length: 66  Bit Score: 34.89  E-value: 5.28e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1297777268  62 RSLALMYESEKVGVASSEELVRQRGVLERTEKMVDKMDQDLKISQKHINSIK 113
Cdd:pfam12352  12 NSHRIADETISIGQAILEDLHSQRETLKRARNKLHNTDNRLGKSNSTLRLIN 63
SNARE_SNAP23N cd15895
N-terminal SNARE motif of SNAP23; N-terminal SNARE motifs of SNAP23, a member of the Qb/Qc ...
 53-109 6.12e-03

N-terminal SNARE motif of SNAP23; N-terminal SNARE motifs of SNAP23, a member of the Qb/Qc subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins. SNAP23 interacts with Syntaxin-4 (Qa) and the R-SNARE VAMP8. The complex plays a role in exocytosis of secretory granule. Qb/Qc SNAREs consist of 2 coiled-coil helices (called SNARE motifs, one belonging to the Qb subgroup and one belonging to the Qc subgroup), which mediate the interactions with other SNARE proteins, and a transmembrane domain. In general, 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. Other members of the Qb/Qc SNAREs are SNAP25, SNAP29, SNAP47 and SEC9.


Pssm-ID: 277248  Cd Length: 67  Bit Score: 34.64  E-value: 6.12e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1297777268  53 AEATAASTSRSLALMYESEKVGVASSEELVRQRGVLERTEKMVDKMDQDLKISQKHI 109
Cdd:cd15895     9 TDESLESTRRILGLAIESQDAGIKTITMLDEQGEQLNRIEEGMDQINKDMREAEKTL 65
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH