Summary: Activator of Hsp90 ATPase homolog 1-like protein
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Activator of Hsp90 ATPase homolog 1-like protein Provide feedback
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, O95433). 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 (Q8XY04 and Q6MH87).
Lotz GP, Lin H, Harst A, Obermann WM; , J Biol Chem 2003;0:0-0.: Aha1 binds to the middle domain of Hsp90, contributes to client protein activation and stimulates the ATPase activity of the molecular chaperone. PUBMED:12604615 EPMC:12604615
Panaretou B, Siligardi G, Meyer P, Maloney A, Sullivan JK, Singh S, Millson SH, Clarke PA, Naaby-Hansen S, Stein R, Cramer R, Mollapour M, Workman P, Piper PW, Pearl LH, Prodromou C; , Mol Cell 2002;10:1307-1318.: Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1. PUBMED:12504007 EPMC:12504007
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR013538
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 homologue 1 (AHSA1/p38, SWISSPROT). This protein is known to interact with the middle domain of Hsp90, and stimulate its ATPase activity [PUBMED:12604615]. It is probably a general up regulator of Hsp90 function, particularly contributing to its efficiency in conditions of increased stress [PUBMED:12504007]. p38 is also known to interact with the cytoplasmic domain of the VSV G protein, and may thus be involved in protein transport [PUBMED:11554768]. It has also been reported as being under expressed in Down's syndrome. This region is found repeated in two members of this family (SWISSPROT and SWISSPROT).
|Biological process||response to stress (GO:0006950)|
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The Bet_V_I family is composed of sequences related to the major Birch (Betula verrucose) pollen antigen Betv1. This allergen is known to cause hayfever, dermatitis, asthma and occasionally anaphylactic shock. The other families in this clan share the same structure as Betv1 which is composed of antiparallel beta sheets and alpha helices. There is a cavity between the beta sheet and a long C terminal helix. The cavity appears to play roles in the binding of lipid molecules  which seems a common feature of the families in this clan.
The clan contains the following 14 members:AHSA1 Aromatic_hydrox Bet_v_1 COXG DUF1857 DUF2505 DUF3074 DUF3211 DUF3284 IP_trans Polyketide_cyc Polyketide_cyc2 Ring_hydroxyl_A START
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Curation and family details
|Seed source:||Pfam-B_4145 (release 18.0)|
|Number in seed:||114|
|Number in full:||4271|
|Average length of the domain:||127.90 aa|
|Average identity of full alignment:||18 %|
|Average coverage of the sequence by the domain:||71.07 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||6|
|Download:||download the raw HMM for this family|
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There is 1 interaction for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the AHSA1 domain has been found. There are 63 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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