NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|109659018|gb|AAI17279|]
View 

AHA1, activator of heat shock 90kDa protein ATPase homolog 2 (yeast) [Homo sapiens]

Protein Classification

SRPBCC family protein( domain architecture ID 51693)

SRPBCC (START/RHOalphaC/PITP/Bet v1/CoxG/CalC) family protein may have a deep hydrophobic ligand-binding pocket

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
SRPBCC super family cl14643
START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC ...
 43-127 3.01e-20

START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC (SRPBCC) ligand-binding domain superfamily; SRPBCC domains have a deep hydrophobic ligand-binding pocket; they bind diverse ligands. Included in this superfamily are the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD1-STARD15, and the C-terminal catalytic domains of the alpha oxygenase subunit of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs_alpha_C), as well as the SRPBCC domains of phosphatidylinositol transfer proteins (PITPs), Bet v 1 (the major pollen allergen of white birch, Betula verrucosa), CoxG, CalC, and related proteins. Other members of this superfamily include PYR/PYL/RCAR plant proteins, the aromatase/cyclase (ARO/CYC) domains of proteins such as Streptomyces glaucescens tetracenomycin, and the SRPBCC domains of Streptococcus mutans Smu.440 and related proteins.


The actual alignment was detected with superfamily member cd08892:

Pssm-ID: 472699 [Multi-domain]  Cd Length: 126  Bit Score: 79.91  E-value: 3.01e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109659018  43 LHMMELFDTTVEQLYSIFTVKELT----------------------------------NKKIIMKWRCGNWPEEHYAMVA 88
Cdd:cd08892    2 ISLTETFQVPAEELYEALTDEERVqaftrspakvdakvggkfslfggnitgefvelvpGKKIVQKWRFKSWPEGHYSTVT 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 109659018  89 LNFVPTLGQTELQLKefLS---ICKEENMKFCWQKQHFEEIK 127
Cdd:cd08892   82 LTFTEKDDETELKLT--QTgvpAGEEERTREGWERYYFESIK 121
 
Name Accession Description Interval E-value
SRPBCC_Aha1 cd08892
Putative hydrophobic ligand-binding SRPBCC domain of the Hsp90 co-chaperone Aha1 and related ...
 43-127 3.01e-20

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: 79.91  E-value: 3.01e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109659018  43 LHMMELFDTTVEQLYSIFTVKELT----------------------------------NKKIIMKWRCGNWPEEHYAMVA 88
Cdd:cd08892    2 ISLTETFQVPAEELYEALTDEERVqaftrspakvdakvggkfslfggnitgefvelvpGKKIVQKWRFKSWPEGHYSTVT 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 109659018  89 LNFVPTLGQTELQLKefLS---ICKEENMKFCWQKQHFEEIK 127
Cdd:cd08892   82 LTFTEKDDETELKLT--QTgvpAGEEERTREGWERYYFESIK 121
AHSA1 pfam08327
Activator of Hsp90 ATPase homolog 1-like protein; This family includes eukaryotic, prokaryotic ...
 61-131 7.89e-06

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: 42.30  E-value: 7.89e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 109659018   61 TVKELT-NKKIIMKWRCGNWPEEHYAMVALNFVPTLGQTELQL---KEFLSICKEENMKFCWQkQHFEEIKGSLQ 131
Cdd:pfam08327  52 TYLELVpPKRIVYTWRLDDWPEGGYSTVTVELEEVGGGTRLTLthtGEPAGEKEEMGMEEGWE-QSLDQLKALLE 125
PTZ00220 PTZ00220
Activator of HSP-90 ATPase; Provisional
 48-104 1.54e-03

Activator of HSP-90 ATPase; Provisional


Pssm-ID: 173484  Cd Length: 132  Bit Score: 36.33  E-value: 1.54e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 109659018  48 LFDTTVEQlysifTVKELT-NKKIIMKWRCGNWPEEHYAMVALNFVPT-LGQTELQLKE 104
Cdd:PTZ00220  39 LFNGSVEG-----EFTELEkPKKIVQKWRFRDWEEDVYSKVTIEFRAVeEDHTELKLTQ 92
 
Name Accession Description Interval E-value
SRPBCC_Aha1 cd08892
Putative hydrophobic ligand-binding SRPBCC domain of the Hsp90 co-chaperone Aha1 and related ...
 43-127 3.01e-20

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: 79.91  E-value: 3.01e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109659018  43 LHMMELFDTTVEQLYSIFTVKELT----------------------------------NKKIIMKWRCGNWPEEHYAMVA 88
Cdd:cd08892    2 ISLTETFQVPAEELYEALTDEERVqaftrspakvdakvggkfslfggnitgefvelvpGKKIVQKWRFKSWPEGHYSTVT 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 109659018  89 LNFVPTLGQTELQLKefLS---ICKEENMKFCWQKQHFEEIK 127
Cdd:cd08892   82 LTFTEKDDETELKLT--QTgvpAGEEERTREGWERYYFESIK 121
AHSA1 pfam08327
Activator of Hsp90 ATPase homolog 1-like protein; This family includes eukaryotic, prokaryotic ...
 61-131 7.89e-06

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: 42.30  E-value: 7.89e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 109659018   61 TVKELT-NKKIIMKWRCGNWPEEHYAMVALNFVPTLGQTELQL---KEFLSICKEENMKFCWQkQHFEEIKGSLQ 131
Cdd:pfam08327  52 TYLELVpPKRIVYTWRLDDWPEGGYSTVTVELEEVGGGTRLTLthtGEPAGEKEEMGMEEGWE-QSLDQLKALLE 125
PTZ00220 PTZ00220
Activator of HSP-90 ATPase; Provisional
 48-104 1.54e-03

Activator of HSP-90 ATPase; Provisional


Pssm-ID: 173484  Cd Length: 132  Bit Score: 36.33  E-value: 1.54e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 109659018  48 LFDTTVEQlysifTVKELT-NKKIIMKWRCGNWPEEHYAMVALNFVPT-LGQTELQLKE 104
Cdd:PTZ00220  39 LFNGSVEG-----EFTELEkPKKIVQKWRFRDWEEDVYSKVTIEFRAVeEDHTELKLTQ 92
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH