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Conserved domains on  [gi|241933111|gb|EES06256|]
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hypothetical protein SORBI_3004G036600 [Sorghum bicolor]

Protein Classification

activator of Hsp90 ATPase N-terminal domain-containing protein( domain architecture ID 10557908)

activator of Hsp90 ATPase (Aha1) N-terminal domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Aha1_N pfam09229
Activator of Hsp90 ATPase, N-terminal; Members of this family, which are predominantly found ...
 68-202 3.44e-32

Activator of Hsp90 ATPase, N-terminal; Members of this family, which are predominantly found in the protein 'Activator of Hsp90 ATPase' adopt a secondary structure consisting of an N-terminal alpha-helix leading into a four-stranded meandering antiparallel beta-sheet, followed by a C-terminal alpha-helix. The two helices are packed together, with the beta-sheet curving around them. They bind to the molecular chaperone HSP82 and stimulate its ATPase activity.


:

Pssm-ID: 462716  Cd Length: 134  Bit Score: 113.03  E-value: 3.44e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241933111   68 EKNLNSWANGRIKDLLGSLGSLDFPTGKASIDEVSKCSGDAFQVTVRNKKRVGYNYELSLRFKGEWliKEENKKIKGHLD 147
Cdd:pfam09229   1 EKNCTPWAKEYLKELLLGLEIEGDEGKSVKITEVSSVEGDASVNQRKGKVITIYDLKLTLEWEGTT--KEDGEEVKGTIT 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 241933111  148 IPEFSFG-EIDDLEVQVRFSDDkglaSEDKTRICKDLKT-FLASIQEKMRVFEEELK 202
Cdd:pfam09229  79 IPELSHDnEDDEYEFEVSVYDE----SKEKDKLKDLVRKkLVPKLREKLAKFVKELI 131
 
Name Accession Description Interval E-value
Aha1_N pfam09229
Activator of Hsp90 ATPase, N-terminal; Members of this family, which are predominantly found ...
 68-202 3.44e-32

Activator of Hsp90 ATPase, N-terminal; Members of this family, which are predominantly found in the protein 'Activator of Hsp90 ATPase' adopt a secondary structure consisting of an N-terminal alpha-helix leading into a four-stranded meandering antiparallel beta-sheet, followed by a C-terminal alpha-helix. The two helices are packed together, with the beta-sheet curving around them. They bind to the molecular chaperone HSP82 and stimulate its ATPase activity.


Pssm-ID: 462716  Cd Length: 134  Bit Score: 113.03  E-value: 3.44e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241933111   68 EKNLNSWANGRIKDLLGSLGSLDFPTGKASIDEVSKCSGDAFQVTVRNKKRVGYNYELSLRFKGEWliKEENKKIKGHLD 147
Cdd:pfam09229   1 EKNCTPWAKEYLKELLLGLEIEGDEGKSVKITEVSSVEGDASVNQRKGKVITIYDLKLTLEWEGTT--KEDGEEVKGTIT 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 241933111  148 IPEFSFG-EIDDLEVQVRFSDDkglaSEDKTRICKDLKT-FLASIQEKMRVFEEELK 202
Cdd:pfam09229  79 IPELSHDnEDDEYEFEVSVYDE----SKEKDKLKDLVRKkLVPKLREKLAKFVKELI 131
Aha1_N smart01000
Activator of Hsp90 ATPase, N-terminal; This domain is predominantly found in the protein ...
 68-202 2.14e-23

Activator of Hsp90 ATPase, N-terminal; This domain is predominantly found in the protein 'Activator of Hsp90 ATPase', it adopts a secondary structure consisting of an N-terminal alpha-helix leading into a four-stranded meandering antiparallel beta-sheet, followed by a C-terminal alpha-helix. The two helices are packed together, with the beta-sheet curving around them. They bind to the molecular chaperone HSP82 and stimulate its ATPase activity.


Pssm-ID: 214964  Cd Length: 134  Bit Score: 90.40  E-value: 2.14e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241933111    68 EKNLNSWANGRIKDLLGSLG-SLDFPTGKASIDEVSKCSGDAFQVTVRNKKRVGYNYELSLRFKGEWliKEENKKIKGHL 146
Cdd:smart01000   1 EKDCTPWAKEYLKELLVGLKiSSEDEEGKIEISSVSSVSGDASVSQRKGKLICLYDLKITLKWSGTV--AKDGKKVKGSI 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 241933111   147 DIPEFSFGEIDDlEVQVRFSDDKglaSEDKTRICKDL--KTFLASIQEKMRVFEEELK 202
Cdd:smart01000  79 EIPELSHDNEED-DYQFEISITK---DKEEKLELKDLvrKKGVPKLREALGKFQKELL 132
 
Name Accession Description Interval E-value
Aha1_N pfam09229
Activator of Hsp90 ATPase, N-terminal; Members of this family, which are predominantly found ...
 68-202 3.44e-32

Activator of Hsp90 ATPase, N-terminal; Members of this family, which are predominantly found in the protein 'Activator of Hsp90 ATPase' adopt a secondary structure consisting of an N-terminal alpha-helix leading into a four-stranded meandering antiparallel beta-sheet, followed by a C-terminal alpha-helix. The two helices are packed together, with the beta-sheet curving around them. They bind to the molecular chaperone HSP82 and stimulate its ATPase activity.


Pssm-ID: 462716  Cd Length: 134  Bit Score: 113.03  E-value: 3.44e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241933111   68 EKNLNSWANGRIKDLLGSLGSLDFPTGKASIDEVSKCSGDAFQVTVRNKKRVGYNYELSLRFKGEWliKEENKKIKGHLD 147
Cdd:pfam09229   1 EKNCTPWAKEYLKELLLGLEIEGDEGKSVKITEVSSVEGDASVNQRKGKVITIYDLKLTLEWEGTT--KEDGEEVKGTIT 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 241933111  148 IPEFSFG-EIDDLEVQVRFSDDkglaSEDKTRICKDLKT-FLASIQEKMRVFEEELK 202
Cdd:pfam09229  79 IPELSHDnEDDEYEFEVSVYDE----SKEKDKLKDLVRKkLVPKLREKLAKFVKELI 131
Aha1_N smart01000
Activator of Hsp90 ATPase, N-terminal; This domain is predominantly found in the protein ...
 68-202 2.14e-23

Activator of Hsp90 ATPase, N-terminal; This domain is predominantly found in the protein 'Activator of Hsp90 ATPase', it adopts a secondary structure consisting of an N-terminal alpha-helix leading into a four-stranded meandering antiparallel beta-sheet, followed by a C-terminal alpha-helix. The two helices are packed together, with the beta-sheet curving around them. They bind to the molecular chaperone HSP82 and stimulate its ATPase activity.


Pssm-ID: 214964  Cd Length: 134  Bit Score: 90.40  E-value: 2.14e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241933111    68 EKNLNSWANGRIKDLLGSLG-SLDFPTGKASIDEVSKCSGDAFQVTVRNKKRVGYNYELSLRFKGEWliKEENKKIKGHL 146
Cdd:smart01000   1 EKDCTPWAKEYLKELLVGLKiSSEDEEGKIEISSVSSVSGDASVSQRKGKLICLYDLKITLKWSGTV--AKDGKKVKGSI 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 241933111   147 DIPEFSFGEIDDlEVQVRFSDDKglaSEDKTRICKDL--KTFLASIQEKMRVFEEELK 202
Cdd:smart01000  79 EIPELSHDNEED-DYQFEISITK---DKEEKLELKDLvrKKGVPKLREALGKFQKELL 132
 
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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