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Conserved domains on  [gi|1883684762|ref|NP_444280|]
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synaptosomal-associated protein 47 isoform b [Homo sapiens]

Protein Classification

PH domain-containing protein; PH domain-containing RhoGEF family protein( domain architecture ID 10351657)

Pleckstrin homology (PH) domain-containing protein may be involved in targeting a protein to the appropriate cellular location or interacting with a binding partner; similar to the PH region of pleckstrin homology domain-containing family A member 2 (PLEKHA2/TAAP2) that binds specifically to phosphatidylinositol 3,4-diphosphate (PtdIns3,4P2)| PH domain-containing RhoGEF family protein may function as a guanine nucleotide exchange factor; similar to Homo sapiens pleckstrin homology domain-containing family G member 4B and Danio rerio quattro

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 4.42e-33

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: 118.63  E-value: 4.42e-33
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1883684762 106 PGAVADASVPRTRGEELTGLMAGSQKRLEDTARVLHHQGQQLDSVMRGLDKMESDLEVADRLLTE 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 ...
 359-417 2.03e-27

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: 103.40  E-value: 2.03e-27
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1883684762 359 PALSEADTQELTQILRRMKGLALEAESELERQDEALDGVAAAVDRATLTIDKHNRRMKR 417
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 ...
 6-99 1.36e-05

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 pfam02893:

Pssm-ID: 473070  Cd Length: 112  Bit Score: 43.89  E-value: 1.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883684762   6 CIHTWpCTYYLEPKRRWVTGQLSLTSLSLRFMTDSTG-EILVSFPLSSIVEIKKEAS-HFIFSSITILEKGHA-KHWFSS 82
Cdd:pfam02893  14 RLIAS-YSCYLNRDGGPVQGRLYLTNYRLCFRSLPKGwSTKVVIPLVDIEEIEKLKGgANLFPNGIQVETGSNdKFSFAG 92

                          90
                  ....*....|....*..
gi 1883684762  83 LRpSRNVVFSIIEHFWR 99
Cdd:pfam02893  93 FV-TRDEAIEFILALLK 108
 
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 4.42e-33

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: 118.63  E-value: 4.42e-33
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1883684762 106 PGAVADASVPRTRGEELTGLMAGSQKRLEDTARVLHHQGQQLDSVMRGLDKMESDLEVADRLLTE 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 ...
 359-417 2.03e-27

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: 103.40  E-value: 2.03e-27
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1883684762 359 PALSEADTQELTQILRRMKGLALEAESELERQDEALDGVAAAVDRATLTIDKHNRRMKR 417
Cdd:cd15854     1 PIVSEAETQELKQILRKLKSLALEAETELERQDEALDVLSDSVDRATLNIDKHNRRMKK 59
GRAM pfam02893
GRAM domain; The GRAM domain is found in in glucosyltransferases, myotubularins and other ...
 6-99 1.36e-05

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: 43.89  E-value: 1.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883684762   6 CIHTWpCTYYLEPKRRWVTGQLSLTSLSLRFMTDSTG-EILVSFPLSSIVEIKKEAS-HFIFSSITILEKGHA-KHWFSS 82
Cdd:pfam02893  14 RLIAS-YSCYLNRDGGPVQGRLYLTNYRLCFRSLPKGwSTKVVIPLVDIEEIEKLKGgANLFPNGIQVETGSNdKFSFAG 92

                          90
                  ....*....|....*..
gi 1883684762  83 LRpSRNVVFSIIEHFWR 99
Cdd:pfam02893  93 FV-TRDEAIEFILALLK 108
PH-GRAM_GRAMDC cd13220
GRAM domain-containing protein (GRAMDC) Pleckstrin Homology-Glucosyltransferases, Rab-like ...
 42-98 7.21e-05

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: 41.34  E-value: 7.21e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1883684762  42 GEILVSFPLSSIVEIKKEASHFIF-SSITIlEKGHAKHWFSSLRpSRNVVFSIIEHFW 98
Cdd:cd13220    39 WETKLVIPFKDITSIEKKKTALIFpNAIEI-TTKGEKYFFTSFL-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 4.42e-33

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: 118.63  E-value: 4.42e-33
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1883684762 106 PGAVADASVPRTRGEELTGLMAGSQKRLEDTARVLHHQGQQLDSVMRGLDKMESDLEVADRLLTE 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 ...
 359-417 2.03e-27

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: 103.40  E-value: 2.03e-27
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1883684762 359 PALSEADTQELTQILRRMKGLALEAESELERQDEALDGVAAAVDRATLTIDKHNRRMKR 417
Cdd:cd15854     1 PIVSEAETQELKQILRKLKSLALEAETELERQDEALDVLSDSVDRATLNIDKHNRRMKK 59
SNARE_SNAP25N_23N_29N_SEC9N cd15861
N-terminal SNARE motif of SNAP25, SNAP23, SNAP29, and SEC9; N-terminal SNARE motif of members ...
 106-170 2.00e-10

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: 56.43  E-value: 2.00e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1883684762 106 PGAVADASVPRTRGEELTGLMAGSQKRLEDTARVLHHQGQQLDSVMRGLDKMESDLEVADRLLTE 170
Cdd:cd15861     1 QEADKTQDETTESIRRALRLAEETKEIGADTLEELHRQGEQLERIHNDVDDIDSNLKRAEKLLKE 65
SNARE_SNAP29C cd15856
C-terminal SNARE motif of SNAP29; C-terminal SNARE motif of SNAP29, a member of the Qb/Qc ...
 363-417 9.80e-10

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: 54.10  E-value: 9.80e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1883684762 363 EADTQELTQILRRMKGLALEAESELERQDEALDGVAAAVDRATLTIDKHNRRMKR 417
Cdd:cd15856     5 DENLDEMSSGLSRLKGLALGLGTEIDSQNDLLDRITDKADKADIKIKKQNKQMNK 59
SNARE_Qc cd15841
SNARE motif, subgroup Qc; SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein ...
 368-417 2.68e-07

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: 47.17  E-value: 2.68e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1883684762 368 ELTQILRRMKGLALEAESELERQDEALDGVAAAVDRATLTIDKHNRRMKR 417
Cdd:cd15841    10 ELSGSVGRLKNIALAINEELDLQNRLLDDLDEDVDKTQSRLKKVNKKLKK 59
SNARE_VAM7 cd15858
SNARE motif of VAM7; Fungal VAM7 (vacuolar morphogenesis protein 7) is a member of the Qc ...
 361-417 5.33e-07

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: 46.34  E-value: 5.33e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1883684762 361 LSEADTQ--ELTQILRRMKGLALEAESELERQDEALDGVAAAVDRATLTIDKHNRRMKR 417
Cdd:cd15858     1 MQEQDQQleQLRKIVQRQKELGLAINQELEEQNELLDELDEDVDRTGGKLRVANKRAKR 59
GRAM pfam02893
GRAM domain; The GRAM domain is found in in glucosyltransferases, myotubularins and other ...
 6-99 1.36e-05

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: 43.89  E-value: 1.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1883684762   6 CIHTWpCTYYLEPKRRWVTGQLSLTSLSLRFMTDSTG-EILVSFPLSSIVEIKKEAS-HFIFSSITILEKGHA-KHWFSS 82
Cdd:pfam02893  14 RLIAS-YSCYLNRDGGPVQGRLYLTNYRLCFRSLPKGwSTKVVIPLVDIEEIEKLKGgANLFPNGIQVETGSNdKFSFAG 92

                          90
                  ....*....|....*..
gi 1883684762  83 LRpSRNVVFSIIEHFWR 99
Cdd:pfam02893  93 FV-TRDEAIEFILALLK 108
SNARE_SNAP25N_23N cd15889
N-terminal SNARE motif of SNAP25 and SNAP23; N-terminal SNARE motifs of SNAP25 and SNAP23, ...
 107-170 4.80e-05

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: 41.08  E-value: 4.80e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1883684762 107 GAVADASVPRTRgeELTGLMAGSQKRLEDTARVLHHQGQQLDSVMRGLDKMESDLEVADRLLTE 170
Cdd:cd15889     4 NQVTDESLESTR--RMLQLCEESQDAGIKTLVMLDEQGEQLDRIEEGMDQINADMKEAEKNLTG 65
SNARE_SNAP29N cd15887
N-terminal SNARE motif of SNAP29; N-terminal SNARE motif of SNAP29, a member of the Qb/Qc ...
 124-169 5.54e-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: 40.72  E-value: 5.54e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1883684762 124 GLMAGSQKRLEDTARVLHHQGQQLDSVMRGLDKMESDLEVADRLLT 169
Cdd:cd15887    19 GLLYESEQIGVATAEELVRQGEQLERTEKNLDKINQDLKTSQRHIN 64
PH-GRAM_GRAMDC cd13220
GRAM domain-containing protein (GRAMDC) Pleckstrin Homology-Glucosyltransferases, Rab-like ...
 42-98 7.21e-05

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: 41.34  E-value: 7.21e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1883684762  42 GEILVSFPLSSIVEIKKEASHFIF-SSITIlEKGHAKHWFSSLRpSRNVVFSIIEHFW 98
Cdd:cd13220    39 WETKLVIPFKDITSIEKKKTALIFpNAIEI-TTKGEKYFFTSFL-SRDSAYKLLTRVW 94
SNARE_SNAP23N cd15895
N-terminal SNARE motif of SNAP23; N-terminal SNARE motifs of SNAP23, a member of the Qb/Qc ...
 109-170 5.51e-04

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: 38.11  E-value: 5.51e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1883684762 109 VADASVPRTRgeELTGLMAGSQKRLEDTARVLHHQGQQLDSVMRGLDKMESDLEVADRLLTE 170
Cdd:cd15895     8 VTDESLESTR--RILGLAIESQDAGIKTITMLDEQGEQLNRIEEGMDQINKDMREAEKTLTE 67
 
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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