uncharacterized protein Dmel_CG1416, isoform B [Drosophila melanogaster]
AHA1 family protein( domain architecture ID 10557909)
AHA1 family protein such as Saccharomyces cerevisiae Hsp90 co-chaperone AHA1 (Activator of Hsp90 ATPase protein 1) that binds to HSP82 and stimulates its ATPase activity
List of domain hits
Name | Accession | Description | Interval | E-value | |||
SRPBCC_Aha1 | cd08892 | Putative hydrophobic ligand-binding SRPBCC domain of the Hsp90 co-chaperone Aha1 and related ... |
221-346 | 1.46e-68 | |||
Putative hydrophobic ligand-binding SRPBCC domain of the Hsp90 co-chaperone Aha1 and related proteins; This subfamily includes the C-terminal SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain of Aha1, and related domains. Proteins in this group belong to the SRPBCC domain superfamily of proteins which bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. Aha1 is one of several co-chaperones, which regulate the dimeric chaperone Hsp90. Hsp90, Aha1, and other accessory proteins interact in a chaperone cycle driven by ATP binding and hydrolysis. Aha1 promotes dimerization of the N-terminal domains of Hsp90, and stimulates its low intrinsic ATPase activity. One Aha1 molecule binds per Hsp90 dimer. The N- and C- terminal domains of Aha1 cooperatively bind across the dimer interface of Hsp90. The C-terminal domain of Aha1 binds the N-terminal Hsp90 ATPase domain. Aha1 may regulate the dwell time of Hsp90 with client proteins. Aha1 may act as either a negative or positive regulator of chaperone-dependent activation, depending on the client protein; for example, it acts as a negative regulator in the case of Saccharomyces cerevisiae MAL63 MAL-activator, and acts as a positive regulator in the case of glucocorticoid receptor and v-Src kinase. The mechanisms by which these opposing functions are achieved are unclear. Aha1 is upregulated in a number of tumor lines co-incident with the activation of several signaling kinases. : Pssm-ID: 176901 [Multi-domain] Cd Length: 126 Bit Score: 210.88 E-value: 1.46e-68
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Aha1_N | pfam09229 | Activator of Hsp90 ATPase, N-terminal; Members of this family, which are predominantly found ... |
29-162 | 3.97e-47 | |||
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: 156.17 E-value: 3.97e-47
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Name | Accession | Description | Interval | E-value | |||
SRPBCC_Aha1 | cd08892 | Putative hydrophobic ligand-binding SRPBCC domain of the Hsp90 co-chaperone Aha1 and related ... |
221-346 | 1.46e-68 | |||
Putative hydrophobic ligand-binding SRPBCC domain of the Hsp90 co-chaperone Aha1 and related proteins; This subfamily includes the C-terminal SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain of Aha1, and related domains. Proteins in this group belong to the SRPBCC domain superfamily of proteins which bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. Aha1 is one of several co-chaperones, which regulate the dimeric chaperone Hsp90. Hsp90, Aha1, and other accessory proteins interact in a chaperone cycle driven by ATP binding and hydrolysis. Aha1 promotes dimerization of the N-terminal domains of Hsp90, and stimulates its low intrinsic ATPase activity. One Aha1 molecule binds per Hsp90 dimer. The N- and C- terminal domains of Aha1 cooperatively bind across the dimer interface of Hsp90. The C-terminal domain of Aha1 binds the N-terminal Hsp90 ATPase domain. Aha1 may regulate the dwell time of Hsp90 with client proteins. Aha1 may act as either a negative or positive regulator of chaperone-dependent activation, depending on the client protein; for example, it acts as a negative regulator in the case of Saccharomyces cerevisiae MAL63 MAL-activator, and acts as a positive regulator in the case of glucocorticoid receptor and v-Src kinase. The mechanisms by which these opposing functions are achieved are unclear. Aha1 is upregulated in a number of tumor lines co-incident with the activation of several signaling kinases. Pssm-ID: 176901 [Multi-domain] Cd Length: 126 Bit Score: 210.88 E-value: 1.46e-68
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Aha1_N | pfam09229 | Activator of Hsp90 ATPase, N-terminal; Members of this family, which are predominantly found ... |
29-162 | 3.97e-47 | |||
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: 156.17 E-value: 3.97e-47
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Aha1_N | smart01000 | Activator of Hsp90 ATPase, N-terminal; This domain is predominantly found in the protein ... |
29-161 | 4.64e-47 | |||
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: 155.89 E-value: 4.64e-47
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AHSA1 | pfam08327 | Activator of Hsp90 ATPase homolog 1-like protein; This family includes eukaryotic, prokaryotic ... |
229-345 | 6.65e-25 | |||
Activator of Hsp90 ATPase homolog 1-like protein; This family includes eukaryotic, prokaryotic and archaeal proteins that bear similarity to a C-terminal region of human activator of 90 kDa heat shock protein ATPase homolog 1 (AHSA1/p38). This protein is known to interact with the middle domain of Hsp90, and stimulate its ATPase activity. It is probably a general upregulator of Hsp90 function, particularly contributing to its efficiency in conditions of increased stress. p38 is also known to interact with the cytoplasmic domain of the VSV G protein, and may thus be involved in protein transport. It has also been reported as being underexpressed in Down's syndrome. This region is found repeated in two members of this family (Swiss:Q8XY04 and Swiss:Q6MH87). The structure of YndB from Bacillus subtilis showed the helix-grip fold consisting of a beta-sheet with two small and one long alpha-helix which form a hydrophobic cavity that preferentially binds lipid-like molecules. This structure confirms its similarity with the eukaryote protein Aha1 and its classification as a member of the AHSA1 family). Pssm-ID: 429921 [Multi-domain] Cd Length: 125 Bit Score: 97.77 E-value: 6.65e-25
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PTZ00220 | PTZ00220 | Activator of HSP-90 ATPase; Provisional |
228-346 | 6.36e-24 | |||
Activator of HSP-90 ATPase; Provisional Pssm-ID: 173484 Cd Length: 132 Bit Score: 95.27 E-value: 6.36e-24
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YndB | COG3832 | Chalcone/flavanone-binding protein YndB, AHSA1/START/SRPBCC domain [Lipid transport and ... |
220-340 | 2.76e-10 | |||
Chalcone/flavanone-binding protein YndB, AHSA1/START/SRPBCC domain [Lipid transport and metabolism]; Pssm-ID: 443044 [Multi-domain] Cd Length: 142 Bit Score: 57.74 E-value: 2.76e-10
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Name | Accession | Description | Interval | E-value | |||
SRPBCC_Aha1 | cd08892 | Putative hydrophobic ligand-binding SRPBCC domain of the Hsp90 co-chaperone Aha1 and related ... |
221-346 | 1.46e-68 | |||
Putative hydrophobic ligand-binding SRPBCC domain of the Hsp90 co-chaperone Aha1 and related proteins; This subfamily includes the C-terminal SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain of Aha1, and related domains. Proteins in this group belong to the SRPBCC domain superfamily of proteins which bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. Aha1 is one of several co-chaperones, which regulate the dimeric chaperone Hsp90. Hsp90, Aha1, and other accessory proteins interact in a chaperone cycle driven by ATP binding and hydrolysis. Aha1 promotes dimerization of the N-terminal domains of Hsp90, and stimulates its low intrinsic ATPase activity. One Aha1 molecule binds per Hsp90 dimer. The N- and C- terminal domains of Aha1 cooperatively bind across the dimer interface of Hsp90. The C-terminal domain of Aha1 binds the N-terminal Hsp90 ATPase domain. Aha1 may regulate the dwell time of Hsp90 with client proteins. Aha1 may act as either a negative or positive regulator of chaperone-dependent activation, depending on the client protein; for example, it acts as a negative regulator in the case of Saccharomyces cerevisiae MAL63 MAL-activator, and acts as a positive regulator in the case of glucocorticoid receptor and v-Src kinase. The mechanisms by which these opposing functions are achieved are unclear. Aha1 is upregulated in a number of tumor lines co-incident with the activation of several signaling kinases. Pssm-ID: 176901 [Multi-domain] Cd Length: 126 Bit Score: 210.88 E-value: 1.46e-68
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Aha1_N | pfam09229 | Activator of Hsp90 ATPase, N-terminal; Members of this family, which are predominantly found ... |
29-162 | 3.97e-47 | |||
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: 156.17 E-value: 3.97e-47
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Aha1_N | smart01000 | Activator of Hsp90 ATPase, N-terminal; This domain is predominantly found in the protein ... |
29-161 | 4.64e-47 | |||
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: 155.89 E-value: 4.64e-47
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AHSA1 | pfam08327 | Activator of Hsp90 ATPase homolog 1-like protein; This family includes eukaryotic, prokaryotic ... |
229-345 | 6.65e-25 | |||
Activator of Hsp90 ATPase homolog 1-like protein; This family includes eukaryotic, prokaryotic and archaeal proteins that bear similarity to a C-terminal region of human activator of 90 kDa heat shock protein ATPase homolog 1 (AHSA1/p38). This protein is known to interact with the middle domain of Hsp90, and stimulate its ATPase activity. It is probably a general upregulator of Hsp90 function, particularly contributing to its efficiency in conditions of increased stress. p38 is also known to interact with the cytoplasmic domain of the VSV G protein, and may thus be involved in protein transport. It has also been reported as being underexpressed in Down's syndrome. This region is found repeated in two members of this family (Swiss:Q8XY04 and Swiss:Q6MH87). The structure of YndB from Bacillus subtilis showed the helix-grip fold consisting of a beta-sheet with two small and one long alpha-helix which form a hydrophobic cavity that preferentially binds lipid-like molecules. This structure confirms its similarity with the eukaryote protein Aha1 and its classification as a member of the AHSA1 family). Pssm-ID: 429921 [Multi-domain] Cd Length: 125 Bit Score: 97.77 E-value: 6.65e-25
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PTZ00220 | PTZ00220 | Activator of HSP-90 ATPase; Provisional |
228-346 | 6.36e-24 | |||
Activator of HSP-90 ATPase; Provisional Pssm-ID: 173484 Cd Length: 132 Bit Score: 95.27 E-value: 6.36e-24
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SRPBCC_CalC_Aha1-like | cd07814 | Putative hydrophobic ligand-binding SRPBCC domain of Micromonospora echinospora CalC, human ... |
221-332 | 7.72e-12 | |||
Putative hydrophobic ligand-binding SRPBCC domain of Micromonospora echinospora CalC, human Aha1, and related proteins; This family includes the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain of Micromonospora echinospora CalC, human Aha1, and related proteins. Proteins in this group belong to the SRPBCC domain superfamily of proteins, which bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. MeCalC confers resistance to the enediyne, calicheamicin gamma 1 (CLM), by a self sacrificing mechanism which results in inactivation of both CalC and the highly reactive diradical enediyne species. MeCalC can also inactivate two other enediynes, shishijimicin and namenamicin. A crucial Gly of the MeCalC CLM resistance mechanism is not conserved in this subgroup. This family also includes the C-terminal, Bet v1-like domain of Aha1, one of several co-chaperones, which regulate the dimeric chaperone Hsp90. Aha1 promotes dimerization of the N-terminal domains of Hsp90, and stimulates its low intrinsic ATPase activity, and may regulate the dwell time of Hsp90 with client proteins. Aha1 can act as either a positive or negative regulator of chaperone-dependent activation, depending on the client protein, but the mechanisms by which these opposing functions are achieved are unclear. Aha1 is upregulated in a number of tumor lines co-incident with the activation of several signaling kinases. Pssm-ID: 176856 [Multi-domain] Cd Length: 139 Bit Score: 62.38 E-value: 7.72e-12
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YndB | COG3832 | Chalcone/flavanone-binding protein YndB, AHSA1/START/SRPBCC domain [Lipid transport and ... |
220-340 | 2.76e-10 | |||
Chalcone/flavanone-binding protein YndB, AHSA1/START/SRPBCC domain [Lipid transport and metabolism]; Pssm-ID: 443044 [Multi-domain] Cd Length: 142 Bit Score: 57.74 E-value: 2.76e-10
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Blast search parameters | ||||
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