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Conserved domains on  [gi|1720367240|ref|XP_030102114|]
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synaptosomal-associated protein 47 isoform X1 [Mus musculus]

Protein Classification

SNARE_SNAP47N and SNARE domain-containing protein( domain architecture ID 10351658)

protein containing domains PH-like, SNARE_SNAP47N, and SNARE

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SNARE_SNAP47N cd15888
N-terminal SNARE motif of SNAP47; N-terminal SNARE motif of SNAP47, a member of the Qb/Qc ...
 106-170 5.94e-31

N-terminal SNARE motif of SNAP47; N-terminal SNARE motif of SNAP47, a member of the Qb/Qc subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins. The exact funtion of SNAP47 is unknown. 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, SNAP29 and SEC9.


:

Pssm-ID: 277241  Cd Length: 65  Bit Score: 112.85  E-value: 5.94e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720367240 106 PGTAANIPSHVTRGQELIGLMANSQKRMEDTAKDLQQQSEQLDSVLKGLEKMESDLDVADRLLTE 170
Cdd:cd15888     1 PYGAHEASEPTTRGKELLGLAAGSQRRLEDTAKVLHHQGEQLDSVMKGLDKMESDLDVADRLLTE 65
SNARE super family cl22856
SNARE motif; SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) ...
 353-411 3.08e-23

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


The actual alignment was detected with superfamily member cd15854:

Pssm-ID: 473982  Cd Length: 59  Bit Score: 91.85  E-value: 3.08e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720367240 353 PLFSEGEAQELTQILSKMKGLALDTEAELERQDAALDGITVAVDRATLNVDKQNRRMRK 411
Cdd:cd15854     1 PIVSEAETQELKQILRKLKSLALEAETELERQDEALDVLSDSVDRATLNIDKHNRRMKK 59
PH-like super family cl17171
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
 2-98 3.44e-07

Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like and IRS-like PTB domains, the ran-binding domain, the EVH1 domain, a domain in neurobeachin and the third domain of FERM. All of these domains have a PH fold, but lack significant sequence similarity. They are generally involved in targeting to protein to the appropriate cellular location or interacting with a binding partner. This domain family possesses multiple functions including the ability to bind inositol phosphates and to other proteins.


The actual alignment was detected with superfamily member cd13220:

Pssm-ID: 473070  Cd Length: 94  Bit Score: 47.89  E-value: 3.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367240   2 SSDMRVHSWSCSYYLDLEKQwvsGKLTLTPHSL----KFIVEKTEEVLvglPLSSIIEIRKESSLFIF-GAITVLEKGQt 76
Cdd:cd13220     1 EDERLIDDFSCALQRDILLQ---GRLYISENHLcfysNIFGWETKLVI---PFKDITSIEKKKTALIFpNAIEITTKGE- 73

                          90       100
                  ....*....|....*....|..
gi 1720367240  77 KHWFSSLQpSRNVVFNVIEHFW 98
Cdd:cd13220    74 KYFFTSFL-SRDSAYKLLTRVW 94
 
Name Accession Description Interval E-value
SNARE_SNAP47N cd15888
N-terminal SNARE motif of SNAP47; N-terminal SNARE motif of SNAP47, a member of the Qb/Qc ...
 106-170 5.94e-31

N-terminal SNARE motif of SNAP47; N-terminal SNARE motif of SNAP47, a member of the Qb/Qc subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins. The exact funtion of SNAP47 is unknown. 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, SNAP29 and SEC9.


Pssm-ID: 277241  Cd Length: 65  Bit Score: 112.85  E-value: 5.94e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720367240 106 PGTAANIPSHVTRGQELIGLMANSQKRMEDTAKDLQQQSEQLDSVLKGLEKMESDLDVADRLLTE 170
Cdd:cd15888     1 PYGAHEASEPTTRGKELLGLAAGSQRRLEDTAKVLHHQGEQLDSVMKGLDKMESDLDVADRLLTE 65
SNARE_SNAP47C cd15854
C-terminal SNARE motif of SNAP47; C-terminal SNARE motif of SNAP47, a member of the Qb/Qc ...
 353-411 3.08e-23

C-terminal SNARE motif of SNAP47; C-terminal SNARE motif of SNAP47, a member of the Qb/Qc subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins. The exact funtion of SNAP47 is unknown. 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, SNAP29 and SEC9.


Pssm-ID: 277207  Cd Length: 59  Bit Score: 91.85  E-value: 3.08e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720367240 353 PLFSEGEAQELTQILSKMKGLALDTEAELERQDAALDGITVAVDRATLNVDKQNRRMRK 411
Cdd:cd15854     1 PIVSEAETQELKQILRKLKSLALEAETELERQDEALDVLSDSVDRATLNIDKHNRRMKK 59
PH-GRAM_GRAMDC cd13220
GRAM domain-containing protein (GRAMDC) Pleckstrin Homology-Glucosyltransferases, Rab-like ...
 2-98 3.44e-07

GRAM domain-containing protein (GRAMDC) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; The GRAMDC proteins are membrane proteins. Nothing is known about its function. Members include: GRAMDC1A, GRAMDC1B, GRAMDC1C, GRAMDC2, GRAMDC3, GRAMDC4, and GRAMDC-like proteins. All of the members, except for GRAMDC4 are included in this hierarchy. Each contains a single PH-GRAM domain at their N-terminus. The GRAM domain is found in glucosyltransferases, myotubularins and other putative membrane-associated proteins. The GRAM domain is part of a larger motif with a pleckstrin homology (PH) domain fold.


Pssm-ID: 275406  Cd Length: 94  Bit Score: 47.89  E-value: 3.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367240   2 SSDMRVHSWSCSYYLDLEKQwvsGKLTLTPHSL----KFIVEKTEEVLvglPLSSIIEIRKESSLFIF-GAITVLEKGQt 76
Cdd:cd13220     1 EDERLIDDFSCALQRDILLQ---GRLYISENHLcfysNIFGWETKLVI---PFKDITSIEKKKTALIFpNAIEITTKGE- 73

                          90       100
                  ....*....|....*....|..
gi 1720367240  77 KHWFSSLQpSRNVVFNVIEHFW 98
Cdd:cd13220    74 KYFFTSFL-SRDSAYKLLTRVW 94
GRAM pfam02893
GRAM domain; The GRAM domain is found in in glucosyltransferases, myotubularins and other ...
 11-99 7.07e-04

GRAM domain; The GRAM domain is found in in glucosyltransferases, myotubularins and other putative membrane-associated proteins. Note the alignment is lacking the last two beta strands and alpha helix.


Pssm-ID: 397160  Cd Length: 112  Bit Score: 38.89  E-value: 7.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367240  11 SCSYYLDLEKQWVSGKLTLTPH-----SLKFIVEKTeevlVGLPLSSIIEIRKESSL--FIFGAITVLEKGQTKHWFSSL 83
Cdd:pfam02893  18 SYSCYLNRDGGPVQGRLYLTNYrlcfrSLPKGWSTK----VVIPLVDIEEIEKLKGGanLFPNGIQVETGSNDKFSFAGF 93

                          90
                  ....*....|....*.
gi 1720367240  84 QpSRNVVFNVIEHFWR 99
Cdd:pfam02893  94 V-TRDEAIEFILALLK 108
t_SNARE smart00397
Helical region found in SNAREs; All alpha-helical motifs that form twisted and parallel ...
 356-412 3.31e-03

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


Pssm-ID: 197699 [Multi-domain]  Cd Length: 66  Bit Score: 36.02  E-value: 3.31e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720367240  356 SEGEAQELTQILSKMKGLALDTEAELERQDAALDGITVAVDRATLNVDKQNRRMRKL 412
Cdd:smart00397  10 RDEELEQLEKSIQELKQIFLDMGTELEEQGEQLDRIEDNVDDADVNLKKANKRLKKA 66
 
Name Accession Description Interval E-value
SNARE_SNAP47N cd15888
N-terminal SNARE motif of SNAP47; N-terminal SNARE motif of SNAP47, a member of the Qb/Qc ...
 106-170 5.94e-31

N-terminal SNARE motif of SNAP47; N-terminal SNARE motif of SNAP47, a member of the Qb/Qc subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins. The exact funtion of SNAP47 is unknown. 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, SNAP29 and SEC9.


Pssm-ID: 277241  Cd Length: 65  Bit Score: 112.85  E-value: 5.94e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720367240 106 PGTAANIPSHVTRGQELIGLMANSQKRMEDTAKDLQQQSEQLDSVLKGLEKMESDLDVADRLLTE 170
Cdd:cd15888     1 PYGAHEASEPTTRGKELLGLAAGSQRRLEDTAKVLHHQGEQLDSVMKGLDKMESDLDVADRLLTE 65
SNARE_SNAP47C cd15854
C-terminal SNARE motif of SNAP47; C-terminal SNARE motif of SNAP47, a member of the Qb/Qc ...
 353-411 3.08e-23

C-terminal SNARE motif of SNAP47; C-terminal SNARE motif of SNAP47, a member of the Qb/Qc subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins. The exact funtion of SNAP47 is unknown. 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, SNAP29 and SEC9.


Pssm-ID: 277207  Cd Length: 59  Bit Score: 91.85  E-value: 3.08e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720367240 353 PLFSEGEAQELTQILSKMKGLALDTEAELERQDAALDGITVAVDRATLNVDKQNRRMRK 411
Cdd:cd15854     1 PIVSEAETQELKQILRKLKSLALEAETELERQDEALDVLSDSVDRATLNIDKHNRRMKK 59
SNARE_SNAP29C cd15856
C-terminal SNARE motif of SNAP29; C-terminal SNARE motif of SNAP29, a member of the Qb/Qc ...
 347-411 6.17e-11

C-terminal SNARE motif of SNAP29; C-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: 277209  Cd Length: 59  Bit Score: 57.57  E-value: 6.17e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720367240 347 QLQKNLPLFSEGeaqeltqiLSKMKGLALDTEAELERQDAALDGITVAVDRATLNVDKQNRRMRK 411
Cdd:cd15856     3 QLDENLDEMSSG--------LSRLKGLALGLGTEIDSQNDLLDRITDKADKADIKIKKQNKQMNK 59
SNARE_SNAP25N_23N_29N_SEC9N cd15861
N-terminal SNARE motif of SNAP25, SNAP23, SNAP29, and SEC9; N-terminal SNARE motif of members ...
 120-170 1.27e-07

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: 48.34  E-value: 1.27e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1720367240 120 QELIGLMANSQKRMEDTAKDLQQQSEQLDSVLKGLEKMESDLDVADRLLTE 170
Cdd:cd15861    15 RRALRLAEETKEIGADTLEELHRQGEQLERIHNDVDDIDSNLKRAEKLLKE 65
PH-GRAM_GRAMDC cd13220
GRAM domain-containing protein (GRAMDC) Pleckstrin Homology-Glucosyltransferases, Rab-like ...
 2-98 3.44e-07

GRAM domain-containing protein (GRAMDC) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; The GRAMDC proteins are membrane proteins. Nothing is known about its function. Members include: GRAMDC1A, GRAMDC1B, GRAMDC1C, GRAMDC2, GRAMDC3, GRAMDC4, and GRAMDC-like proteins. All of the members, except for GRAMDC4 are included in this hierarchy. Each contains a single PH-GRAM domain at their N-terminus. The GRAM domain is found in glucosyltransferases, myotubularins and other putative membrane-associated proteins. The GRAM domain is part of a larger motif with a pleckstrin homology (PH) domain fold.


Pssm-ID: 275406  Cd Length: 94  Bit Score: 47.89  E-value: 3.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367240   2 SSDMRVHSWSCSYYLDLEKQwvsGKLTLTPHSL----KFIVEKTEEVLvglPLSSIIEIRKESSLFIF-GAITVLEKGQt 76
Cdd:cd13220     1 EDERLIDDFSCALQRDILLQ---GRLYISENHLcfysNIFGWETKLVI---PFKDITSIEKKKTALIFpNAIEITTKGE- 73

                          90       100
                  ....*....|....*....|..
gi 1720367240  77 KHWFSSLQpSRNVVFNVIEHFW 98
Cdd:cd13220    74 KYFFTSFL-SRDSAYKLLTRVW 94
SNARE_Qc cd15841
SNARE motif, subgroup Qc; SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein ...
 362-411 6.10e-06

SNARE motif, subgroup Qc; 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). Qc-, as well as Qa- and Qb-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 Qc SNAREs are C-terminal domains of SNAP23 and SNAP25, syntaxin 8, syntaxin 6, and Bet1.


Pssm-ID: 277194 [Multi-domain]  Cd Length: 59  Bit Score: 43.32  E-value: 6.10e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720367240 362 ELTQILSKMKGLALDTEAELERQDAALDGITVAVDRATLNVDKQNRRMRK 411
Cdd:cd15841    10 ELSGSVGRLKNIALAINEELDLQNRLLDDLDEDVDKTQSRLKKVNKKLKK 59
SNARE_SNAP29N cd15887
N-terminal SNARE motif of SNAP29; N-terminal SNARE motif of SNAP29, a member of the Qb/Qc ...
 124-169 1.57e-05

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: 42.26  E-value: 1.57e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1720367240 124 GLMANSQKRMEDTAKDLQQQSEQLDSVLKGLEKMESDLDVADRLLT 169
Cdd:cd15887    19 GLLYESEQIGVATAEELVRQGEQLERTEKNLDKINQDLKTSQRHIN 64
GRAM pfam02893
GRAM domain; The GRAM domain is found in in glucosyltransferases, myotubularins and other ...
 11-99 7.07e-04

GRAM domain; The GRAM domain is found in in glucosyltransferases, myotubularins and other putative membrane-associated proteins. Note the alignment is lacking the last two beta strands and alpha helix.


Pssm-ID: 397160  Cd Length: 112  Bit Score: 38.89  E-value: 7.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720367240  11 SCSYYLDLEKQWVSGKLTLTPH-----SLKFIVEKTeevlVGLPLSSIIEIRKESSL--FIFGAITVLEKGQTKHWFSSL 83
Cdd:pfam02893  18 SYSCYLNRDGGPVQGRLYLTNYrlcfrSLPKGWSTK----VVIPLVDIEEIEKLKGGanLFPNGIQVETGSNDKFSFAGF 93

                          90
                  ....*....|....*.
gi 1720367240  84 QpSRNVVFNVIEHFWR 99
Cdd:pfam02893  94 V-TRDEAIEFILALLK 108
SNARE_SNAP23C cd15884
C-terminal SNARE motif of SNAP23; C-terminal SNARE motifs of SNAP23, a member of the Qb/Qc ...
 361-411 7.16e-04

C-terminal SNARE motif of SNAP23; C-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: 277237  Cd Length: 59  Bit Score: 37.44  E-value: 7.16e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720367240 361 QELTQ---ILSKMKGLALDTEAELERQDAALDGITVAVDRATLNVDKQNRRMRK 411
Cdd:cd15884     6 ENLTQvgsILGNLKSMALDMGNELDKQNKQIGRINEKADMNSDRIDEANVRAKK 59
t_SNARE smart00397
Helical region found in SNAREs; All alpha-helical motifs that form twisted and parallel ...
 356-412 3.31e-03

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


Pssm-ID: 197699 [Multi-domain]  Cd Length: 66  Bit Score: 36.02  E-value: 3.31e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720367240  356 SEGEAQELTQILSKMKGLALDTEAELERQDAALDGITVAVDRATLNVDKQNRRMRKL 412
Cdd:smart00397  10 RDEELEQLEKSIQELKQIFLDMGTELEEQGEQLDRIEDNVDDADVNLKKANKRLKKA 66
SNARE_SEC9C cd15857
C-terminal SNARE motif of SEC9; C-terminal SNARE motif of fungal SEC9, a member of the Qb/Qc ...
 362-411 4.10e-03

C-terminal SNARE motif of SEC9; C-terminal SNARE motif of fungal SEC9, a member of the Qb/Qc subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins. SEC9 interacts with Sso1(Qa) and the lysosomal R-SNARE Snc1. The complex plays a role in post-Golgi transport. 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 SNAP29.


Pssm-ID: 277210  Cd Length: 59  Bit Score: 35.24  E-value: 4.10e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720367240 362 ELTQILSKMKGLALDTEAELERQDAALDGITVAVDRATLNVDKQNRRMRK 411
Cdd:cd15857    10 EIGGVVGRLKALAMAMGEEVDSQNKRLDRIEEKTDRLDDKVHMNTERLKR 59
SNARE_VAM7 cd15858
SNARE motif of VAM7; Fungal VAM7 (vacuolar morphogenesis protein 7) is a member of the Qc ...
 359-411 5.04e-03

SNARE motif of VAM7; Fungal VAM7 (vacuolar morphogenesis protein 7) is a member of the Qc subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) protein family involved in vacuolar protein transport and membrane fusion. 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). Qc-, as well as Qa- and Qb-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: 277211 [Multi-domain]  Cd Length: 59  Bit Score: 35.17  E-value: 5.04e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720367240 359 EAQELTQILSKMKGLALDTEAELERQDAALDGITVAVDRATLNVDKQNRRMRK 411
Cdd:cd15858     7 QLEQLRKIVQRQKELGLAINQELEEQNELLDELDEDVDRTGGKLRVANKRAKR 59
 
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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