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Conserved domains on  [gi|323309761|gb|EGA62967|]
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Aha1p [Saccharomyces cerevisiae FostersO]

Protein Classification

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

CATH:  3.15.10.20|3.30.530.20
Gene Ontology:  GO:0001671|GO:0006457
PubMed:  15039704|12504007|12604615|18922149
SCOP:  4001260|4002780

Graphical summary

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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 ...
 215-346 6.65e-51

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: 165.43  E-value: 6.65e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323309761 215 SIYLEPTFNVPSSELYETFLDKQRILAWTRSAqffnsgPKLETKE--KFELFGGNVISELVSCEKDKKLVFHWKLKDWSA 292
Cdd:cd08892    1 TISLTETFQVPAEELYEALTDEERVQAFTRSP------AKVDAKVggKFSLFGGNITGEFVELVPGKKIVQKWRFKSWPE 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 323309761 293 AFNSTIEMTFHESQefHETKLQVKWTGIPVGEEDRVRANFEEYYVRSIKLTFGF 346
Cdd:cd08892   75 GHYSTVTLTFTEKD--DETELKLTQTGVPAGEEERTREGWERYYFESIKQTFGY 126
Aha1_N pfam09229
Activator of Hsp90 ATPase, N-terminal; Members of this family, which are predominantly found ...
 13-150 1.71e-48

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: 159.64  E-value: 1.71e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323309761   13 DKNCIGWAKEYFKQKLVGVEAGSVkDKKYAKIKSVSSIEGDCEVNQRKGKVISLFDLKITVLIEGHVDSKDGSalpFEGS 92
Cdd:pfam09229   1 EKNCTPWAKEYLKELLLGLEIEGD-EGKSVKITEVSSVEGDASVNQRKGKVITIYDLKLTLEWEGTTKEDGEE---VKGT 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 323309761   93 INVPEVAFDSEASSYQFDISIFKETSELSEAKPLIRSELLPKLRQIFQQFGKDLLATH 150
Cdd:pfam09229  77 ITIPELSHDNEDDEYEFEVSVYDESKEKDKLKDLVRKKLVPKLREKLAKFVKELIEEH 134
 
Name Accession Description Interval E-value
SRPBCC_Aha1 cd08892
Putative hydrophobic ligand-binding SRPBCC domain of the Hsp90 co-chaperone Aha1 and related ...
 215-346 6.65e-51

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: 165.43  E-value: 6.65e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323309761 215 SIYLEPTFNVPSSELYETFLDKQRILAWTRSAqffnsgPKLETKE--KFELFGGNVISELVSCEKDKKLVFHWKLKDWSA 292
Cdd:cd08892    1 TISLTETFQVPAEELYEALTDEERVQAFTRSP------AKVDAKVggKFSLFGGNITGEFVELVPGKKIVQKWRFKSWPE 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 323309761 293 AFNSTIEMTFHESQefHETKLQVKWTGIPVGEEDRVRANFEEYYVRSIKLTFGF 346
Cdd:cd08892   75 GHYSTVTLTFTEKD--DETELKLTQTGVPAGEEERTREGWERYYFESIKQTFGY 126
Aha1_N pfam09229
Activator of Hsp90 ATPase, N-terminal; Members of this family, which are predominantly found ...
 13-150 1.71e-48

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: 159.64  E-value: 1.71e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323309761   13 DKNCIGWAKEYFKQKLVGVEAGSVkDKKYAKIKSVSSIEGDCEVNQRKGKVISLFDLKITVLIEGHVDSKDGSalpFEGS 92
Cdd:pfam09229   1 EKNCTPWAKEYLKELLLGLEIEGD-EGKSVKITEVSSVEGDASVNQRKGKVITIYDLKLTLEWEGTTKEDGEE---VKGT 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 323309761   93 INVPEVAFDSEASSYQFDISIFKETSELSEAKPLIRSELLPKLRQIFQQFGKDLLATH 150
Cdd:pfam09229  77 ITIPELSHDNEDDEYEFEVSVYDESKEKDKLKDLVRKKLVPKLREKLAKFVKELIEEH 134
Aha1_N smart01000
Activator of Hsp90 ATPase, N-terminal; This domain is predominantly found in the protein ...
 13-149 1.28e-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: 157.43  E-value: 1.28e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323309761    13 DKNCIGWAKEYFKQKLVGVEAGSVKDKKYAKIKSVSSIEGDCEVNQRKGKVISLFDLKITVLIEGHVdSKDGSalPFEGS 92
Cdd:smart01000   1 EKDCTPWAKEYLKELLVGLKISSEDEEGKIEISSVSSVSGDASVSQRKGKLICLYDLKITLKWSGTV-AKDGK--KVKGS 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 323309761    93 INVPEVAFDSEASSYQFDISIFKETSELSEAKPLIRSELLPKLRQIFQQFGKDLLAT 149
Cdd:smart01000  78 IEIPELSHDNEEDDYQFEISITKDKEEKLELKDLVRKKGVPKLREALGKFQKELLTE 134
AHSA1 pfam08327
Activator of Hsp90 ATPase homolog 1-like protein; This family includes eukaryotic, prokaryotic ...
 223-345 2.98e-14

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: 68.50  E-value: 2.98e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323309761  223 NVPSSELYETFLDKQRILAWtrsaqFFNSGPKLETKE--KFEL--------FGGNVisELVSCEKDKKLVFHWKLKDWSA 292
Cdd:pfam08327   1 DAPPERVFRALTDPELLARW-----FTRTVAEMDLRPggKFRFmrgpdgeeFGGNG--TYLELVPPKRIVYTWRLDDWPE 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 323309761  293 AFNSTIEMTFHESQEfhETKLQVKWTGIPVGEEDR--VRANFEEYYvRSIKLTFG 345
Cdd:pfam08327  74 GGYSTVTVELEEVGG--GTRLTLTHTGEPAGEKEEmgMEEGWEQSL-DQLKALLE 125
PTZ00220 PTZ00220
Activator of HSP-90 ATPase; Provisional
 222-346 6.82e-12

Activator of HSP-90 ATPase; Provisional


Pssm-ID: 173484  Cd Length: 132  Bit Score: 62.14  E-value: 6.82e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323309761 222 FNVPSSELYETFLDKQRIlawTRSAQffNSGPKLETKE--KFELFGGNVISELVSCEKDKKLVFHWKLKDWSAAFNSTIE 299
Cdd:PTZ00220   1 FYVPPEVLYNAFLDAYTL---TRLSL--GSPAEMDAKVggKFSLFNGSVEGEFTELEKPKKIVQKWRFRDWEEDVYSKVT 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 323309761 300 MTFHESQEFHeTKLQVKWTGIPV-------GEEDRVRANFEEYYVRSIKLTFGF 346
Cdd:PTZ00220  76 IEFRAVEEDH-TELKLTQTGIPSldkfgngGCLERCRNGWTQNFLDRFEKILGY 128
 
Name Accession Description Interval E-value
SRPBCC_Aha1 cd08892
Putative hydrophobic ligand-binding SRPBCC domain of the Hsp90 co-chaperone Aha1 and related ...
 215-346 6.65e-51

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: 165.43  E-value: 6.65e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323309761 215 SIYLEPTFNVPSSELYETFLDKQRILAWTRSAqffnsgPKLETKE--KFELFGGNVISELVSCEKDKKLVFHWKLKDWSA 292
Cdd:cd08892    1 TISLTETFQVPAEELYEALTDEERVQAFTRSP------AKVDAKVggKFSLFGGNITGEFVELVPGKKIVQKWRFKSWPE 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 323309761 293 AFNSTIEMTFHESQefHETKLQVKWTGIPVGEEDRVRANFEEYYVRSIKLTFGF 346
Cdd:cd08892   75 GHYSTVTLTFTEKD--DETELKLTQTGVPAGEEERTREGWERYYFESIKQTFGY 126
Aha1_N pfam09229
Activator of Hsp90 ATPase, N-terminal; Members of this family, which are predominantly found ...
 13-150 1.71e-48

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: 159.64  E-value: 1.71e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323309761   13 DKNCIGWAKEYFKQKLVGVEAGSVkDKKYAKIKSVSSIEGDCEVNQRKGKVISLFDLKITVLIEGHVDSKDGSalpFEGS 92
Cdd:pfam09229   1 EKNCTPWAKEYLKELLLGLEIEGD-EGKSVKITEVSSVEGDASVNQRKGKVITIYDLKLTLEWEGTTKEDGEE---VKGT 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 323309761   93 INVPEVAFDSEASSYQFDISIFKETSELSEAKPLIRSELLPKLRQIFQQFGKDLLATH 150
Cdd:pfam09229  77 ITIPELSHDNEDDEYEFEVSVYDESKEKDKLKDLVRKKLVPKLREKLAKFVKELIEEH 134
Aha1_N smart01000
Activator of Hsp90 ATPase, N-terminal; This domain is predominantly found in the protein ...
 13-149 1.28e-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: 157.43  E-value: 1.28e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323309761    13 DKNCIGWAKEYFKQKLVGVEAGSVKDKKYAKIKSVSSIEGDCEVNQRKGKVISLFDLKITVLIEGHVdSKDGSalPFEGS 92
Cdd:smart01000   1 EKDCTPWAKEYLKELLVGLKISSEDEEGKIEISSVSSVSGDASVSQRKGKLICLYDLKITLKWSGTV-AKDGK--KVKGS 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 323309761    93 INVPEVAFDSEASSYQFDISIFKETSELSEAKPLIRSELLPKLRQIFQQFGKDLLAT 149
Cdd:smart01000  78 IEIPELSHDNEEDDYQFEISITKDKEEKLELKDLVRKKGVPKLREALGKFQKELLTE 134
AHSA1 pfam08327
Activator of Hsp90 ATPase homolog 1-like protein; This family includes eukaryotic, prokaryotic ...
 223-345 2.98e-14

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: 68.50  E-value: 2.98e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323309761  223 NVPSSELYETFLDKQRILAWtrsaqFFNSGPKLETKE--KFEL--------FGGNVisELVSCEKDKKLVFHWKLKDWSA 292
Cdd:pfam08327   1 DAPPERVFRALTDPELLARW-----FTRTVAEMDLRPggKFRFmrgpdgeeFGGNG--TYLELVPPKRIVYTWRLDDWPE 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 323309761  293 AFNSTIEMTFHESQEfhETKLQVKWTGIPVGEEDR--VRANFEEYYvRSIKLTFG 345
Cdd:pfam08327  74 GGYSTVTVELEEVGG--GTRLTLTHTGEPAGEKEEmgMEEGWEQSL-DQLKALLE 125
PTZ00220 PTZ00220
Activator of HSP-90 ATPase; Provisional
 222-346 6.82e-12

Activator of HSP-90 ATPase; Provisional


Pssm-ID: 173484  Cd Length: 132  Bit Score: 62.14  E-value: 6.82e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323309761 222 FNVPSSELYETFLDKQRIlawTRSAQffNSGPKLETKE--KFELFGGNVISELVSCEKDKKLVFHWKLKDWSAAFNSTIE 299
Cdd:PTZ00220   1 FYVPPEVLYNAFLDAYTL---TRLSL--GSPAEMDAKVggKFSLFNGSVEGEFTELEKPKKIVQKWRFRDWEEDVYSKVT 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 323309761 300 MTFHESQEFHeTKLQVKWTGIPV-------GEEDRVRANFEEYYVRSIKLTFGF 346
Cdd:PTZ00220  76 IEFRAVEEDH-TELKLTQTGIPSldkfgngGCLERCRNGWTQNFLDRFEKILGY 128
SRPBCC_CalC_Aha1-like_8 cd08901
Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and ...
 225-330 3.50e-04

Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and Aha1-like proteins; SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain of a functionally uncharacterized subgroup of CalC- and Aha1-like proteins. This group shows similarity to the SRPBCC domains of Micromonospora echinospora CalC (a protein which confers resistance to enediynes) and human Aha1 (one of several co-chaperones which regulate the dimeric chaperone Hsp90), and belongs to the SRPBCC domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket and they bind diverse ligands.


Pssm-ID: 176910 [Multi-domain]  Cd Length: 136  Bit Score: 40.34  E-value: 3.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323309761 225 PSSELYETFLDKQRIlawtrSAQFFNSGP-KLETKE----KFELFGGNVISELVSCEKDKKLVFhwklkDWSAAFNST-I 298
Cdd:cd08901   11 PVAEVFEAFVDPEIT-----TKFWFTGSSgRLEEGKtvtwDWEMYGASVPVNVLEIEPNKRIVI-----EWGDPGEPTtV 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 323309761 299 EMTFhESQEFHETKLQVKWTGIPVGEEDRVRA 330
Cdd:cd08901   81 EWTF-EELDDGRTFVTITESGFPGTDDEGLKQ 111
SRPBCC_CalC_Aha1-like cd07814
Putative hydrophobic ligand-binding SRPBCC domain of Micromonospora echinospora CalC, human ...
 215-334 7.64e-04

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: 39.27  E-value: 7.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323309761 215 SIYLEPTFNVPSSELYETFLDKQRILAWTRSAQFFNSGPKLETKEKFELFGGN-----VISELVSCEKDKKLVFHWKLKD 289
Cdd:cd07814    1 TITIEREFDAPPELVWRALTDPELLAQWFGPTTTAEMDLRVGGRWFFFMTGPDgeegwVSGEVLEVEPPRRLVFTWAFSD 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 323309761 290 WSAAFNSTIEMTFHESQEfhETKLQVKWTGIPVGEEDR-VRANFEE 334
Cdd:cd07814   81 ETPGPETTVTVTLEETGG--GTRLTLTHSGFPEEDAEQeAREGMEE 124
 
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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