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39  structures 163  species 0  interactions 260  sequences 8  architectures

Family: Aegerolysin (PF06355)

Summary: Aegerolysin

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Aegerolysin Provide feedback

This family consists of several bacterial and fungal Aegerolysin-like proteins. It has been found that aegerolysin and ostreolysin are expressed during formation of primordia and fruiting bodies. It has been suggested that these haemolysins play an important role in initial phase of fungal fruiting. The bacterial members of this family are expressed during sporulation [1]. Ostreolysin was found cytolytic to various erythrocytes and tumour cells [2]. It forms transmembrane pores 4 nm in diameter. The activity is inhibited by total membrane lipids, and modulated by lysophosphatides. The potential use of aegerolysins is reviewed [8] with special emphasis on their properties which would allow their use in therapeutics. Aegerolysin is part of the pleurotolysin pore-forming (Pleurotolysin) transporter superfamily. Member proteins assemble into a transmembrane pore complex [7].

Literature references

  1. Berne S, Krizaj I, Pohleven F, Turk T, Macek P, Sepcic K; , Biochim Biophys Acta 2002;1570:153-159.: Pleurotus and Agrocybe hemolysins, new proteins hypothetically involved in fungal fruiting. PUBMED:12020804 EPMC:12020804

  2. Sepcic K, Berne S, Potrich C, Turk T, Macek P, Menestrina G; , Eur J Biochem 2003;270:1199-1210.: Interaction of ostreolysin, a cytolytic protein from the edible mushroom Pleurotus ostreatus, with lipid membranes and modulation by lysophospholipids. PUBMED:12631278 EPMC:12631278

  3. Rebolj K, Ulrih NP, Macek P, Sepcic K; , Biochim Biophys Acta. 2006;1758:1662-1670.: Steroid structural requirements for interaction of ostreolysin, a lipid-raft binding cytolysin, with lipid monolayers and bilayers. PUBMED:16857161 EPMC:16857161

  4. Zuzek MC, Macek P, Sepcic K, Cestnik V, Frangez R; , Toxicon. 2006;48:264-271.: Toxic and lethal effects of ostreolysin, a cytolytic protein from edible oyster mushroom (Pleurotus ostreatus), in rodents. PUBMED:16860832 EPMC:16860832

  5. Berne S, Sepcic K, Anderluh G, Turk T, Macek P, Poklar Ulrih N; , Biochemistry. 2005;44:11137-11147.: Effect of pH on the pore forming activity and conformational stability of ostreolysin, a lipid raft-binding protein from the edible mushroom Pleurotus ostreatus. PUBMED:16101298 EPMC:16101298

  6. Vidic I, Berne S, Drobne D, Macek P, Frangez R, Turk T, Strus J, Sepcic K; , Mycol Res. 2005;109:377-382.: Temporal and spatial expression of ostreolysin during development of the oyster mushroom (Pleurotus ostreatus). PUBMED:15912956 EPMC:15912956

  7. Sepcic K, Berne S, Rebolj K, Batista U, Plemenitas A, Sentjurc M, Macek P; , FEBS Lett. 2004;575:81-85.: Ostreolysin, a pore-forming protein from the oyster mushroom, interacts specifically with membrane cholesterol-rich lipid domains. PUBMED:15388337 EPMC:15388337

  8. Berne S, Lah L, Sepcic K;, Protein Sci. 2009;18:694-706.: Aegerolysins: structure, function, and putative biological role. PUBMED:19309687 EPMC:19309687

  9. Bhat HB, Kishimoto T, Abe M, Makino A, Inaba T, Murate M, Dohmae N, Kurahashi A, Nishibori K, Fujimori F, Greimel P, Ishitsuka R, Kobayashi T;, J Lipid Res. 2013;54:2933-2943.: Binding of a pleurotolysin ortholog from Pleurotus eryngii to sphingomyelin and cholesterol-rich membrane domains. PUBMED:23918047 EPMC:23918047

  10. Sakurai N, Kaneko J, Kamio Y, Tomita T;, Biochim Biophys Acta. 2004;1679:65-73.: Cloning, expression, and pore-forming properties of mature and precursor forms of pleurotolysin, a sphingomyelin-specific two-component cytolysin from the edible mushroom Pleurotus ostreatus. PUBMED:15245918 EPMC:15245918


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR009413

This family consists of several bacterial and eukaryotic Aegerolysin-like proteins. Aegerolysin and ostreolysin are expressed during formation of primordia and fruiting bodies, and these haemolysins may play an important role in initial phase of fungal fruiting. The bacterial members of this family are expressed during sporulation [PUBMED:12020804]. Ostreolysin was found cytolytic to various erythrocytes and tumour cells [PUBMED:15912956]. It forms transmembrane pores 4 nm in diameter. Its activity is inhibited by total membrane lipids, and modulated by lysophosphatides.

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 CDC (CL0293), which has the following description:

This superfamily includes the MACPF domain as well as the Cholesterol-dependent cytolysins [1].

The clan contains the following 8 members:

Aegerolysin Anemone_cytotox FB_lectin Gasdermin MACPF TDH Thaumatin Thiol_cytolysin

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 (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the UniProtKB sequence database, the NCBI sequence database, and our metagenomics sequence database. More...

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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
(18)
Full
(260)
Representative proteomes UniProt
(421)
NCBI
(489)
Meta
(0)
RP15
(51)
RP35
(121)
RP55
(191)
RP75
(291)
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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
(18)
Full
(260)
Representative proteomes UniProt
(421)
NCBI
(489)
Meta
(0)
RP15
(51)
RP35
(121)
RP55
(191)
RP75
(291)
Alignment:
Format:
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Sequence:
Gaps:
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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
(18)
Full
(260)
Representative proteomes UniProt
(421)
NCBI
(489)
Meta
(0)
RP15
(51)
RP35
(121)
RP55
(191)
RP75
(291)
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.

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_13415 (release 9.0)
Previous IDs: none
Type: Family
Sequence Ontology: SO:0100021
Author: Moxon SJ , Bateman A , Macek P
Number in seed: 18
Number in full: 260
Average length of the domain: 124.20 aa
Average identity of full alignment: 25 %
Average coverage of the sequence by the domain: 81.68 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 45638612 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 20.6 20.6
Trusted cut-off 21.1 21.1
Noise cut-off 20.2 20.5
Model length: 131
Family (HMM) version: 13
Download: download the raw HMM for this family

Species distribution

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Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence

Selections

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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 Aegerolysin domain has been found. There are 39 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 sequence.

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