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Conserved domains on  [gi|15228924|ref|NP_191204|]
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alpha-soluble NSF attachment protein 1 [Arabidopsis thaliana]

Protein Classification

soluble NSF attachment family protein( domain architecture ID 708914)

soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein (SNAP) is involved in intracellular membrane trafficking; may contain TPR repeats

CATH:  1.25.40.10
Gene Ontology:  GO:0005483|GO:0000149
PubMed:  11536358|17634982
SCOP:  4001344

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SNAP super family cl25938
Soluble NSF attachment protein, SNAP; The soluble NSF attachment protein (SNAP) proteins are ...
 102-314 6.82e-79

Soluble NSF attachment protein, SNAP; The soluble NSF attachment protein (SNAP) proteins are involved in vesicular transport between the endoplasmic reticulum and Golgi apparatus. They act as adaptors between SNARE (integral membrane SNAP receptor) proteins and NSF (N-ethylmaleimide-sensitive factor). They are structurally similar to TPR repeats.


The actual alignment was detected with superfamily member pfam14938:

Pssm-ID: 405606 [Multi-domain]  Cd Length: 273  Bit Score: 243.63  E-value: 6.82e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228924   102 KAEKKLNRRRRF-------DTKYEDAADLLEKARDSYKLAKSWDQAGIAYLKLADCHLKANSL---ANTY-----MIM-- 164
Cdd:pfam14938   1 KAEKKLKSSSGFfsffgskSSKYEEAADLYIQAANAYKLAKNWEEAGEAFEKAAECQLKLGSKdeaANAYveaakCYKkv 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228924   165 --DECMDH----------------------EIAEYYESD-EMFEQAIAYYETAAEFFQIEEVTTSANQCNLKVAQYASQL 219
Cdd:pfam14938  81 dpEEAVRAlekaieiytemgrfrraakhkkEIAELYEQElGDLEKAIEAYEQAADWYEGEGASALANKCYLKVADLSAEL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228924   220 EQQSRFMK---TQARHSLNNKLLKYGVKGHLLTAGMCHLCKADVVSITNALEKYQDLDPTFSGTRECKFLADLASAIDEE 296
Cdd:pfam14938 161 EDYPKAIEiyeKVAKNSLENNLLKYSVKEYFLKAGLCHLAAGDLVAAQRALERYEELDPSFADTREYKLLNDLLEAVEEG 240

                         250
                  ....*....|....*...
gi 15228924   297 DIAKFTDVSKEIDSVSPL 314
Cdd:pfam14938 241 DVEAFTDAVFEFDQISKL 258
 
Name Accession Description Interval E-value
SNAP pfam14938
Soluble NSF attachment protein, SNAP; The soluble NSF attachment protein (SNAP) proteins are ...
 102-314 6.82e-79

Soluble NSF attachment protein, SNAP; The soluble NSF attachment protein (SNAP) proteins are involved in vesicular transport between the endoplasmic reticulum and Golgi apparatus. They act as adaptors between SNARE (integral membrane SNAP receptor) proteins and NSF (N-ethylmaleimide-sensitive factor). They are structurally similar to TPR repeats.


Pssm-ID: 405606 [Multi-domain]  Cd Length: 273  Bit Score: 243.63  E-value: 6.82e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228924   102 KAEKKLNRRRRF-------DTKYEDAADLLEKARDSYKLAKSWDQAGIAYLKLADCHLKANSL---ANTY-----MIM-- 164
Cdd:pfam14938   1 KAEKKLKSSSGFfsffgskSSKYEEAADLYIQAANAYKLAKNWEEAGEAFEKAAECQLKLGSKdeaANAYveaakCYKkv 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228924   165 --DECMDH----------------------EIAEYYESD-EMFEQAIAYYETAAEFFQIEEVTTSANQCNLKVAQYASQL 219
Cdd:pfam14938  81 dpEEAVRAlekaieiytemgrfrraakhkkEIAELYEQElGDLEKAIEAYEQAADWYEGEGASALANKCYLKVADLSAEL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228924   220 EQQSRFMK---TQARHSLNNKLLKYGVKGHLLTAGMCHLCKADVVSITNALEKYQDLDPTFSGTRECKFLADLASAIDEE 296
Cdd:pfam14938 161 EDYPKAIEiyeKVAKNSLENNLLKYSVKEYFLKAGLCHLAAGDLVAAQRALERYEELDPSFADTREYKLLNDLLEAVEEG 240

                         250
                  ....*....|....*...
gi 15228924   297 DIAKFTDVSKEIDSVSPL 314
Cdd:pfam14938 241 DVEAFTDAVFEFDQISKL 258
SNAP cd15832
Soluble N-ethylmaleimide-sensitive factor (NSF) Attachment Protein family; Members of the ...
 99-314 1.82e-72

Soluble N-ethylmaleimide-sensitive factor (NSF) Attachment Protein family; Members of the soluble NSF attachment protein (SNAP) family are involved in intracellular membrane trafficking, including vesicular transport between the endoplasmic reticulum and Golgi apparatus. Higher eukaryotes contain three isoforms of SNAPs: alpha, beta, and gamma. Alpha-SNAP is universally present in eukaryotes and acts as an adaptor protein between SNARE (integral membrane SNAP receptor) and NSF for recruitment to the 20S complex. Beta-SNAP is brain-specific and shares high sequence identity (about 85%) with alpha-SNAP. Gamma-SNAP is weakly related (about 20-25% identity) to the two other isoforms, and is ubiquitous. It may help regulate the activity of the 20S complex. The X-ray structures of vertebrate gamma-SNAP and yeast Sec17, a SNAP family member, show similar all-helical structures consisting of an N-terminal extended twisted sheet of four Tetratricopeptide repeat (TPR)-like helical hairpins and a C-terminal helical bundle.


Pssm-ID: 276937 [Multi-domain]  Cd Length: 278  Bit Score: 227.46  E-value: 1.82e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228924  99 FQKKAEKKLN-----RRRRFDTKYEDAADLLEKARDSYKLAKSWDQAGIAYLKLADCHLKANSL---ANTY-----MIM- 164
Cdd:cd15832   5 LMAKAEKKLKgsggfFFGSGGSKYEEAAELYEKAANAFKLAKNWEEAGDAFLKAAECQLKLDSKhdaANAYveaakCYKk 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228924 165 ---DECMDH----------------------EIAEYYESDEM-FEQAIAYYETAAEFFQIEEVTTSANQCNLKVAQYASQ 218
Cdd:cd15832  85 vdpQEAVNClekaieiytemgrfrqaakhlkEIAELYENELGdLDKAIEAYEQAADYYEGEGANSLANKCYLKVADLAAQ 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228924 219 LEQQSR---FMKTQARHSLNNKLLKYGVKGHLLTAGMCHLCKADVVSITNALEKYQDLDPTFSGTRECKFLADLASAIDE 295
Cdd:cd15832 165 LEDYDKaieIYEQVARSSLENNLLKYSAKDYFLKAGLCHLAAGDVVAAQRALEKYAELDPSFAGSRECKLLEDLLEAVEE 244

                       250
                ....*....|....*....
gi 15228924 296 EDIAKFTDVSKEIDSVSPL 314
Cdd:cd15832 245 GDVEAFTDAVKEYDSISKL 263
 
Name Accession Description Interval E-value
SNAP pfam14938
Soluble NSF attachment protein, SNAP; The soluble NSF attachment protein (SNAP) proteins are ...
 102-314 6.82e-79

Soluble NSF attachment protein, SNAP; The soluble NSF attachment protein (SNAP) proteins are involved in vesicular transport between the endoplasmic reticulum and Golgi apparatus. They act as adaptors between SNARE (integral membrane SNAP receptor) proteins and NSF (N-ethylmaleimide-sensitive factor). They are structurally similar to TPR repeats.


Pssm-ID: 405606 [Multi-domain]  Cd Length: 273  Bit Score: 243.63  E-value: 6.82e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228924   102 KAEKKLNRRRRF-------DTKYEDAADLLEKARDSYKLAKSWDQAGIAYLKLADCHLKANSL---ANTY-----MIM-- 164
Cdd:pfam14938   1 KAEKKLKSSSGFfsffgskSSKYEEAADLYIQAANAYKLAKNWEEAGEAFEKAAECQLKLGSKdeaANAYveaakCYKkv 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228924   165 --DECMDH----------------------EIAEYYESD-EMFEQAIAYYETAAEFFQIEEVTTSANQCNLKVAQYASQL 219
Cdd:pfam14938  81 dpEEAVRAlekaieiytemgrfrraakhkkEIAELYEQElGDLEKAIEAYEQAADWYEGEGASALANKCYLKVADLSAEL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228924   220 EQQSRFMK---TQARHSLNNKLLKYGVKGHLLTAGMCHLCKADVVSITNALEKYQDLDPTFSGTRECKFLADLASAIDEE 296
Cdd:pfam14938 161 EDYPKAIEiyeKVAKNSLENNLLKYSVKEYFLKAGLCHLAAGDLVAAQRALERYEELDPSFADTREYKLLNDLLEAVEEG 240

                         250
                  ....*....|....*...
gi 15228924   297 DIAKFTDVSKEIDSVSPL 314
Cdd:pfam14938 241 DVEAFTDAVFEFDQISKL 258
SNAP cd15832
Soluble N-ethylmaleimide-sensitive factor (NSF) Attachment Protein family; Members of the ...
 99-314 1.82e-72

Soluble N-ethylmaleimide-sensitive factor (NSF) Attachment Protein family; Members of the soluble NSF attachment protein (SNAP) family are involved in intracellular membrane trafficking, including vesicular transport between the endoplasmic reticulum and Golgi apparatus. Higher eukaryotes contain three isoforms of SNAPs: alpha, beta, and gamma. Alpha-SNAP is universally present in eukaryotes and acts as an adaptor protein between SNARE (integral membrane SNAP receptor) and NSF for recruitment to the 20S complex. Beta-SNAP is brain-specific and shares high sequence identity (about 85%) with alpha-SNAP. Gamma-SNAP is weakly related (about 20-25% identity) to the two other isoforms, and is ubiquitous. It may help regulate the activity of the 20S complex. The X-ray structures of vertebrate gamma-SNAP and yeast Sec17, a SNAP family member, show similar all-helical structures consisting of an N-terminal extended twisted sheet of four Tetratricopeptide repeat (TPR)-like helical hairpins and a C-terminal helical bundle.


Pssm-ID: 276937 [Multi-domain]  Cd Length: 278  Bit Score: 227.46  E-value: 1.82e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228924  99 FQKKAEKKLN-----RRRRFDTKYEDAADLLEKARDSYKLAKSWDQAGIAYLKLADCHLKANSL---ANTY-----MIM- 164
Cdd:cd15832   5 LMAKAEKKLKgsggfFFGSGGSKYEEAAELYEKAANAFKLAKNWEEAGDAFLKAAECQLKLDSKhdaANAYveaakCYKk 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228924 165 ---DECMDH----------------------EIAEYYESDEM-FEQAIAYYETAAEFFQIEEVTTSANQCNLKVAQYASQ 218
Cdd:cd15832  85 vdpQEAVNClekaieiytemgrfrqaakhlkEIAELYENELGdLDKAIEAYEQAADYYEGEGANSLANKCYLKVADLAAQ 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228924 219 LEQQSR---FMKTQARHSLNNKLLKYGVKGHLLTAGMCHLCKADVVSITNALEKYQDLDPTFSGTRECKFLADLASAIDE 295
Cdd:cd15832 165 LEDYDKaieIYEQVARSSLENNLLKYSAKDYFLKAGLCHLAAGDVVAAQRALEKYAELDPSFAGSRECKLLEDLLEAVEE 244

                       250
                ....*....|....*....
gi 15228924 296 EDIAKFTDVSKEIDSVSPL 314
Cdd:cd15832 245 GDVEAFTDAVKEYDSISKL 263
DHR2_DOCK cd11684
Dock Homology Region 2, a GEF domain, of Dedicator of Cytokinesis proteins; DOCK proteins ...
 122-198 6.69e-03

Dock Homology Region 2, a GEF domain, of Dedicator of Cytokinesis proteins; DOCK proteins comprise a family of atypical guanine nucleotide exchange factors (GEFs) that lack the conventional Dbl homology (DH) domain. As GEFs, they activate the small GTPases Rac and Cdc42 by exchanging bound GDP for free GTP. They are also called the CZH (CED-5, Dock180, and MBC-zizimin homology) family, after the first family members identified. Dock180 was first isolated as a binding partner for the adaptor protein Crk. The Caenorhabditis elegans protein, Ced-5, is essential for cell migration and phagocytosis, while the Drosophila ortholog, Myoblast city (MBC), is necessary for myoblast fusion and dorsal closure. DOCKs are divided into four classes (A-D) based on sequence similarity and domain architecture: class A includes Dock1 (or Dock180), 2 and 5; class B includes Dock3 and 4; class C includes Dock6, 7, and 8; and class D includes Dock9, 10 and 11. All DOCKs contain two homology domains: the DHR-1 (Dock homology region-1), also called CZH1, and DHR-2 (also called CZH2 or Docker). This alignment model represents the DHR-2 domain of DOCK proteins, which contains the catalytic GEF activity for Rac and/or Cdc42.


Pssm-ID: 212566 [Multi-domain]  Cd Length: 392  Bit Score: 38.43  E-value: 6.69e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228924 122 DLLEKARDSYKLAKSWDQAGIAYLKLADCHLKANSLANTYMIMDECMD------------HEIAEYYESDEMFEQAIAYY 189
Cdd:cd11684   5 RYLHKLADLHEERGNYVEAALCLLLHADLYAWDLKALVPALAESLSFPeqtsferkealyKKAIDLFDKGKAWEFAIALY 84


                ....*....
gi 15228924 190 ETAAEFFQI 198
Cdd:cd11684  85 KELIPQYEN 93
 
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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