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63  structures 1661  species 1  interaction 4271  sequences 39  architectures

Family: AHSA1 (PF08327)

Summary: Activator of Hsp90 ATPase homolog 1-like protein

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This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

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 [1]. It is probably a general upregulator of Hsp90 function, particularly contributing to its efficiency in conditions of increased stress [2]. p38 is also known to interact with the cytoplasmic domain of the VSV G protein, and may thus be involved in protein transport [3]. 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).

Literature references

  1. 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

  2. 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

  3. Sevier CS, Machamer CE; , Biochem Biophys Res Commun 2001;287:574-582.: p38: A novel protein that associates with the vesicular stomatitis virus glycoprotein. PUBMED:11554768 EPMC:11554768


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).

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Pfam Clan

This family is a member of clan Bet_V_1_like (CL0209), which has the following description:

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 [1][2][3] 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

Alignments

We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the NCBI sequence database, and our metagenomics sequence database. More...

View options

We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

  Seed
(114)
Full
(4271)
Representative proteomes NCBI
(4537)
Meta
(461)
RP15
(625)
RP35
(1111)
RP55
(1404)
RP75
(1665)
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: ✓ available, x not generated, not available.

Format an alignment

  Seed
(114)
Full
(4271)
Representative proteomes NCBI
(4537)
Meta
(461)
RP15
(625)
RP35
(1111)
RP55
(1404)
RP75
(1665)
Alignment:
Format:
Order:
Sequence:
Gaps:
Download/view:

Download options

We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

  Seed
(114)
Full
(4271)
Representative proteomes NCBI
(4537)
Meta
(461)
RP15
(625)
RP35
(1111)
RP55
(1404)
RP75
(1665)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   Download   Download   Download   Download   Download   Download  

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

External links

MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.

Pfam alignments:

HMM logo

HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...

Trees

This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

Note: You can also download the data file for the tree.

Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Pfam-B_4145 (release 18.0)
Previous IDs: none
Type: Family
Author: Fenech M
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 information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 22.0 22.0
Trusted cut-off 22.0 22.0
Noise cut-off 21.9 21.9
Model length: 124
Family (HMM) version: 6
Download: download the raw HMM for this family

Species distribution

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This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...

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Interactions

There is 1 interaction for this family. More...

AHSA1

Structures

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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