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Conserved domains on  [gi|285403140|ref|NP_001165578|]
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protein Aster-C isoform 1 [Mus musculus]

Protein Classification

VASt domain-containing protein( domain architecture ID 11240314)

VASt (VAD1 Analog of StAR-related lipid transfer) domain-containing protein adopts a two-layer sandwich alpha beta fold, also called 'helix grip fold', and may bind large hydrophobic ligands

Gene Ontology:  GO:0008289
PubMed:  24965341|26001273

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
VASt pfam16016
VAD1 Analog of StAR-related lipid transfer domain; The VASt (VAD1 Analog of StAR-related lipid ...
 124-271 2.21e-47

VAD1 Analog of StAR-related lipid transfer domain; The VASt (VAD1 Analog of StAR-related lipid transfer) domain is conserved across eukaryotes and is structurally related to Bet v1-like domains, including START lipid-binding domains. The 190-amino acid VASt domain is predominantly associated with lipid binding domains such as GRAM pfam02893, C2 and PH domains. The VASt domain is likely to have a function in binding large hydrophobic ligands and may be specific for sterol. The predicted structure of the VASt domain is a two-layer sandwich alpha beta fold, also called 'helix grip fold', containing three alpha helices (alpha1 to 3), six beta-sheets (beta1 to 6) and two loops (omega1 and 2) numbered from N to C terminus. Some proteins known to contain a VASt domain are : Plant vascular associated death1 (VAD1), a regulator of programmed cell death (PCD) harboring a GRAM putative lipid-binding domain. Yeast SNF1 Interacting Protein 3 (SIP3), may be involved in sterol transfer between intracellular membranes. Yeast Suicide Protein 1 (YSP1), a mitochondrial protein specifically required for the mitochondrial thread-grain transition, de-energization, and the cell death. May be involved in sterol transfer between intracellular membranes. Yeast Suicide Protein 2 (YSP2), a mitochondrial membrane protein involved in mitochondrial fragmentation and may be involved in sterol transfer between intracellular membranes.It is also found in human GramD1a-c.


:

Pssm-ID: 464975  Cd Length: 147  Bit Score: 160.08  E-value: 2.21e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285403140  124 LYINRVFHISAERMFELLFT-SSHFMQRFANSRNIIDVVSTPWTVESGGNQLRTMTYTIVLSNPLTGKYTAATEKQTLYK 202
Cdd:pfam16016   1 VLLDEVFPISVGKLFELLFGdDSSFLQKFLEERGDTDISVGPWEPDEEGGLTREISYTKPLNGSIGPKQTKCTETQTILL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 285403140  203 ESREAQFYlVDSEVLTHDVPYHDYFYTLNRYCIVRSAKQRCRLRVSTDLKYRKQPWglIKSLIEKNSWS 271
Cdd:pfam16016  81 EHDDLEVY-VVTTTKTPDVPYGDSFSVETRYCITWGSNNSTRLQVSTGVEWTKSSW--LKGKIEKGAID 146
 
Name Accession Description Interval E-value
VASt pfam16016
VAD1 Analog of StAR-related lipid transfer domain; The VASt (VAD1 Analog of StAR-related lipid ...
 124-271 2.21e-47

VAD1 Analog of StAR-related lipid transfer domain; The VASt (VAD1 Analog of StAR-related lipid transfer) domain is conserved across eukaryotes and is structurally related to Bet v1-like domains, including START lipid-binding domains. The 190-amino acid VASt domain is predominantly associated with lipid binding domains such as GRAM pfam02893, C2 and PH domains. The VASt domain is likely to have a function in binding large hydrophobic ligands and may be specific for sterol. The predicted structure of the VASt domain is a two-layer sandwich alpha beta fold, also called 'helix grip fold', containing three alpha helices (alpha1 to 3), six beta-sheets (beta1 to 6) and two loops (omega1 and 2) numbered from N to C terminus. Some proteins known to contain a VASt domain are : Plant vascular associated death1 (VAD1), a regulator of programmed cell death (PCD) harboring a GRAM putative lipid-binding domain. Yeast SNF1 Interacting Protein 3 (SIP3), may be involved in sterol transfer between intracellular membranes. Yeast Suicide Protein 1 (YSP1), a mitochondrial protein specifically required for the mitochondrial thread-grain transition, de-energization, and the cell death. May be involved in sterol transfer between intracellular membranes. Yeast Suicide Protein 2 (YSP2), a mitochondrial membrane protein involved in mitochondrial fragmentation and may be involved in sterol transfer between intracellular membranes.It is also found in human GramD1a-c.


Pssm-ID: 464975  Cd Length: 147  Bit Score: 160.08  E-value: 2.21e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285403140  124 LYINRVFHISAERMFELLFT-SSHFMQRFANSRNIIDVVSTPWTVESGGNQLRTMTYTIVLSNPLTGKYTAATEKQTLYK 202
Cdd:pfam16016   1 VLLDEVFPISVGKLFELLFGdDSSFLQKFLEERGDTDISVGPWEPDEEGGLTREISYTKPLNGSIGPKQTKCTETQTILL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 285403140  203 ESREAQFYlVDSEVLTHDVPYHDYFYTLNRYCIVRSAKQRCRLRVSTDLKYRKQPWglIKSLIEKNSWS 271
Cdd:pfam16016  81 EHDDLEVY-VVTTTKTPDVPYGDSFSVETRYCITWGSNNSTRLQVSTGVEWTKSSW--LKGKIEKGAID 146
 
Name Accession Description Interval E-value
VASt pfam16016
VAD1 Analog of StAR-related lipid transfer domain; The VASt (VAD1 Analog of StAR-related lipid ...
 124-271 2.21e-47

VAD1 Analog of StAR-related lipid transfer domain; The VASt (VAD1 Analog of StAR-related lipid transfer) domain is conserved across eukaryotes and is structurally related to Bet v1-like domains, including START lipid-binding domains. The 190-amino acid VASt domain is predominantly associated with lipid binding domains such as GRAM pfam02893, C2 and PH domains. The VASt domain is likely to have a function in binding large hydrophobic ligands and may be specific for sterol. The predicted structure of the VASt domain is a two-layer sandwich alpha beta fold, also called 'helix grip fold', containing three alpha helices (alpha1 to 3), six beta-sheets (beta1 to 6) and two loops (omega1 and 2) numbered from N to C terminus. Some proteins known to contain a VASt domain are : Plant vascular associated death1 (VAD1), a regulator of programmed cell death (PCD) harboring a GRAM putative lipid-binding domain. Yeast SNF1 Interacting Protein 3 (SIP3), may be involved in sterol transfer between intracellular membranes. Yeast Suicide Protein 1 (YSP1), a mitochondrial protein specifically required for the mitochondrial thread-grain transition, de-energization, and the cell death. May be involved in sterol transfer between intracellular membranes. Yeast Suicide Protein 2 (YSP2), a mitochondrial membrane protein involved in mitochondrial fragmentation and may be involved in sterol transfer between intracellular membranes.It is also found in human GramD1a-c.


Pssm-ID: 464975  Cd Length: 147  Bit Score: 160.08  E-value: 2.21e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285403140  124 LYINRVFHISAERMFELLFT-SSHFMQRFANSRNIIDVVSTPWTVESGGNQLRTMTYTIVLSNPLTGKYTAATEKQTLYK 202
Cdd:pfam16016   1 VLLDEVFPISVGKLFELLFGdDSSFLQKFLEERGDTDISVGPWEPDEEGGLTREISYTKPLNGSIGPKQTKCTETQTILL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 285403140  203 ESREAQFYlVDSEVLTHDVPYHDYFYTLNRYCIVRSAKQRCRLRVSTDLKYRKQPWglIKSLIEKNSWS 271
Cdd:pfam16016  81 EHDDLEVY-VVTTTKTPDVPYGDSFSVETRYCITWGSNNSTRLQVSTGVEWTKSSW--LKGKIEKGAID 146
 
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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