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Conserved domains on  [gi|1622909230|ref|XP_028700442|]
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protein Aster-C isoform X3 [Macaca mulatta]

Protein Classification

GRAM and VASt domain-containing protein( domain architecture ID 10987411)

GRAM and VASt domain-containing protein, with similarity to Saccharomyces cerevisiae membrane-anchored lipid-binding protein YSP2

CATH:  2.30.29.30
Gene Ontology:  GO:0016020
PubMed:  11050430|18201690|24965341
SCOP:  4000903

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 ...
 198-345 4.58e-48

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: 163.54  E-value: 4.58e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909230 198 LFINRVFHISADRMFELLFT-SSRFMQKFASSRNIIDVVSTPWTAELGGDQLRTMTYTIVLNSPLTGKCTTATEKQTLYK 276
Cdd:pfam16016   1 VLLDEVFPISVGKLFELLFGdDSSFLQKFLEERGDTDISVGPWEPDEEGGLTREISYTKPLNGSIGPKQTKCTETQTILL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622909230 277 ESQEARFYlVDSEVLTHDVPYHDYFYTVNRYCIIRSSKQKCRLRVSTDVKYRKQPWglVKSLIEKNSWS 345
Cdd:pfam16016  81 EHDDLEVY-VVTTTKTPDVPYGDSFSVETRYCITWGSNNSTRLQVSTGVEWTKSSW--LKGKIEKGAID 146
PH-like super family cl17171
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
 1-42 1.91e-16

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: 74.46  E-value: 1.91e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1622909230   1 MTKEKTARLIPNAIQIVTESEKFFFTSFGARDRSYLSIFRLW 42
Cdd:cd13220    53 IEKKKTALIFPNAIEITTKGEKYFFTSFLSRDSAYKLLTRVW 94
 
Name Accession Description Interval E-value
VASt pfam16016
VAD1 Analog of StAR-related lipid transfer domain; The VASt (VAD1 Analog of StAR-related lipid ...
 198-345 4.58e-48

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: 163.54  E-value: 4.58e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909230 198 LFINRVFHISADRMFELLFT-SSRFMQKFASSRNIIDVVSTPWTAELGGDQLRTMTYTIVLNSPLTGKCTTATEKQTLYK 276
Cdd:pfam16016   1 VLLDEVFPISVGKLFELLFGdDSSFLQKFLEERGDTDISVGPWEPDEEGGLTREISYTKPLNGSIGPKQTKCTETQTILL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622909230 277 ESQEARFYlVDSEVLTHDVPYHDYFYTVNRYCIIRSSKQKCRLRVSTDVKYRKQPWglVKSLIEKNSWS 345
Cdd:pfam16016  81 EHDDLEVY-VVTTTKTPDVPYGDSFSVETRYCITWGSNNSTRLQVSTGVEWTKSSW--LKGKIEKGAID 146
PH-GRAM_GRAMDC cd13220
GRAM domain-containing protein (GRAMDC) Pleckstrin Homology-Glucosyltransferases, Rab-like ...
 1-42 1.91e-16

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: 74.46  E-value: 1.91e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1622909230   1 MTKEKTARLIPNAIQIVTESEKFFFTSFGARDRSYLSIFRLW 42
Cdd:cd13220    53 IEKKKTALIFPNAIEITTKGEKYFFTSFLSRDSAYKLLTRVW 94
 
Name Accession Description Interval E-value
VASt pfam16016
VAD1 Analog of StAR-related lipid transfer domain; The VASt (VAD1 Analog of StAR-related lipid ...
 198-345 4.58e-48

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: 163.54  E-value: 4.58e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622909230 198 LFINRVFHISADRMFELLFT-SSRFMQKFASSRNIIDVVSTPWTAELGGDQLRTMTYTIVLNSPLTGKCTTATEKQTLYK 276
Cdd:pfam16016   1 VLLDEVFPISVGKLFELLFGdDSSFLQKFLEERGDTDISVGPWEPDEEGGLTREISYTKPLNGSIGPKQTKCTETQTILL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622909230 277 ESQEARFYlVDSEVLTHDVPYHDYFYTVNRYCIIRSSKQKCRLRVSTDVKYRKQPWglVKSLIEKNSWS 345
Cdd:pfam16016  81 EHDDLEVY-VVTTTKTPDVPYGDSFSVETRYCITWGSNNSTRLQVSTGVEWTKSSW--LKGKIEKGAID 146
PH-GRAM_GRAMDC cd13220
GRAM domain-containing protein (GRAMDC) Pleckstrin Homology-Glucosyltransferases, Rab-like ...
 1-42 1.91e-16

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: 74.46  E-value: 1.91e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1622909230   1 MTKEKTARLIPNAIQIVTESEKFFFTSFGARDRSYLSIFRLW 42
Cdd:cd13220    53 IEKKKTALIFPNAIEITTKGEKYFFTSFLSRDSAYKLLTRVW 94
 
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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