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Conserved domains on  [gi|1251770405|ref|NP_001343383|]
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synaptosomal-associated protein 47 isoform 2 [Mus musculus]

Protein Classification

PH domain-containing protein; PH domain-containing RhoGEF family protein( domain architecture ID 10351656)

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 7.73e-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: 116.31  E-value: 7.73e-33
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1251770405 106 PGTAANIPSHVTRGQELIGLMANSQKRMEDTAKDLQQQSEQLDSVLKGLEKMESDLDVADRLLTE 170
Cdd:cd15888     1 PYGAHEASEPTTRGKELLGLAAGSQRRLEDTAKVLHHQGEQLDSVMKGLDKMESDLDVADRLLTE 65
PH-like super family cl17171
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
 2-98 7.19e-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: 46.73  E-value: 7.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770405   2 SSDMRVHSWSCSYYLDLEKQwvsGKLTLTPHSL----KFIVEKTEEVLvglPLSSIIEIRKESSLFIF-GAITVLEKGQt 76
Cdd:cd13220     1 EDERLIDDFSCALQRDILLQ---GRLYISENHLcfysNIFGWETKLVI---PFKDITSIEKKKTALIFpNAIEITTKGE- 73

                          90       100
                  ....*....|....*....|..
gi 1251770405  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 7.73e-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: 116.31  E-value: 7.73e-33
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1251770405 106 PGTAANIPSHVTRGQELIGLMANSQKRMEDTAKDLQQQSEQLDSVLKGLEKMESDLDVADRLLTE 170
Cdd:cd15888     1 PYGAHEASEPTTRGKELLGLAAGSQRRLEDTAKVLHHQGEQLDSVMKGLDKMESDLDVADRLLTE 65
PH-GRAM_GRAMDC cd13220
GRAM domain-containing protein (GRAMDC) Pleckstrin Homology-Glucosyltransferases, Rab-like ...
 2-98 7.19e-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: 46.73  E-value: 7.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770405   2 SSDMRVHSWSCSYYLDLEKQwvsGKLTLTPHSL----KFIVEKTEEVLvglPLSSIIEIRKESSLFIF-GAITVLEKGQt 76
Cdd:cd13220     1 EDERLIDDFSCALQRDILLQ---GRLYISENHLcfysNIFGWETKLVI---PFKDITSIEKKKTALIFpNAIEITTKGE- 73

                          90       100
                  ....*....|....*....|..
gi 1251770405  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 1.05e-03

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: 38.12  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770405  11 SCSYYLDLEKQWVSGKLTLTPH-----SLKFIVEKTeevlVGLPLSSIIEIRKESSL--FIFGAITVLEKGQTKHWFSSL 83
Cdd:pfam02893  18 SYSCYLNRDGGPVQGRLYLTNYrlcfrSLPKGWSTK----VVIPLVDIEEIEKLKGGanLFPNGIQVETGSNDKFSFAGF 93

                          90
                  ....*....|....*.
gi 1251770405  84 QpSRNVVFNVIEHFWR 99
Cdd:pfam02893  94 V-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 7.73e-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: 116.31  E-value: 7.73e-33
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1251770405 106 PGTAANIPSHVTRGQELIGLMANSQKRMEDTAKDLQQQSEQLDSVLKGLEKMESDLDVADRLLTE 170
Cdd:cd15888     1 PYGAHEASEPTTRGKELLGLAAGSQRRLEDTAKVLHHQGEQLDSVMKGLDKMESDLDVADRLLTE 65
SNARE_SNAP25N_23N_29N_SEC9N cd15861
N-terminal SNARE motif of SNAP25, SNAP23, SNAP29, and SEC9; N-terminal SNARE motif of members ...
 120-170 2.77e-08

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: 49.88  E-value: 2.77e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1251770405 120 QELIGLMANSQKRMEDTAKDLQQQSEQLDSVLKGLEKMESDLDVADRLLTE 170
Cdd:cd15861    15 RRALRLAEETKEIGADTLEELHRQGEQLERIHNDVDDIDSNLKRAEKLLKE 65
PH-GRAM_GRAMDC cd13220
GRAM domain-containing protein (GRAMDC) Pleckstrin Homology-Glucosyltransferases, Rab-like ...
 2-98 7.19e-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: 46.73  E-value: 7.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770405   2 SSDMRVHSWSCSYYLDLEKQwvsGKLTLTPHSL----KFIVEKTEEVLvglPLSSIIEIRKESSLFIF-GAITVLEKGQt 76
Cdd:cd13220     1 EDERLIDDFSCALQRDILLQ---GRLYISENHLcfysNIFGWETKLVI---PFKDITSIEKKKTALIFpNAIEITTKGE- 73

                          90       100
                  ....*....|....*....|..
gi 1251770405  77 KHWFSSLQpSRNVVFNVIEHFW 98
Cdd:cd13220    74 KYFFTSFL-SRDSAYKLLTRVW 94
SNARE_SNAP29N cd15887
N-terminal SNARE motif of SNAP29; N-terminal SNARE motif of SNAP29, a member of the Qb/Qc ...
 124-169 5.67e-06

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: 43.41  E-value: 5.67e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1251770405 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 1.05e-03

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: 38.12  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770405  11 SCSYYLDLEKQWVSGKLTLTPH-----SLKFIVEKTeevlVGLPLSSIIEIRKESSL--FIFGAITVLEKGQTKHWFSSL 83
Cdd:pfam02893  18 SYSCYLNRDGGPVQGRLYLTNYrlcfrSLPKGWSTK----VVIPLVDIEEIEKLKGGanLFPNGIQVETGSNDKFSFAGF 93

                          90
                  ....*....|....*.
gi 1251770405  84 QpSRNVVFNVIEHFWR 99
Cdd:pfam02893  94 V-TRDEAIEFILALLK 108
 
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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