Aerolisin/ETX pore-forming domain-containing protein [Armillaria solidipes]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | |||
| PFM_aerolysin-like | cd20239 | pore-forming module of aerolysin-type beta-barrel pore-forming proteins; uncharacterized ... |
185-329 | 1.04e-74 | |||
pore-forming module of aerolysin-type beta-barrel pore-forming proteins; uncharacterized subgroup; Generally, pore-forming proteins (PFPs) are secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores detrimental to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel. Many of this family are bacterial toxins. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin). : Pssm-ID: 380809 [Multi-domain] Cd Length: 145 Bit Score: 226.57 E-value: 1.04e-74
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| beta-trefoil_FSCN-like super family | cl49611 | fascin-like domain, beta-trefoil fold, found in the fascin-like family; The fascin-like family ... |
42-159 | 3.04e-03 | |||
fascin-like domain, beta-trefoil fold, found in the fascin-like family; The fascin-like family includes actin-bundling/crosslinking proteins facsin1-4, singed, hisactophilin, and FSHD region gene 1 protein (FRG1). Fascin, also called fascin-1, is an actin-binding protein that contains 2 major actin binding sites. It is involved in the organization of actin filament bundles and the formation of microspikes, membrane ruffles, and stress fibers. It plays an important role for the formation of a diverse set of cell protrusions, such as filopodia, and for cell motility and migration. It mediates reorganization of the actin cytoskeleton and axon growth cone collapse in response to nerve growth factor (NGF). Fascin-2, also called retinal fascin, is a photoreceptor-specific paralog of the actin-bundling protein fascin. It may play a pivotal role in photoreceptor cell-specific events, such as disk morphogenesis. Fascin-3, also called testis fascin, is a novel paralog of the actin-bundling protein fascin expressed specifically in the elongate spermatid head. Protein singed acts as an actin-bundling protein that may have a role in the asymmetric organization and/or movement of cytoplasmic components. It has a role in somatic cells during the formation of adult bristles and hairs, and in the female germline during oogenesis. Hisactophilin is a histidine-rich actin-binding protein from Dictyostelium discoideum. It exists in two isoforms, hisactophilin-1 (HatA, also called HS I) and hisactophilin-2 (HatB, also called HS II), which are both myristoylated and distributed between plasma membrane and cytoplasm. Hisactophilin may act as an intracellular pH sensor that links chemotactic signals to responses in the microfilament system of the cells by nucleating actin polymerization or stabilizing the filaments. Protein FRG1 binds to mRNA in a sequence-independent manner. It may play a role in regulation of pre-mRNA splicing or in the assembly of rRNA into ribosomal subunits. It may be involved in mRNA transport, as well as in epigenetic regulation of muscle differentiation through regulation of activity of the histone-lysine N-methyltransferase KMT5B. This family also contains many homologs from bacteria, such as Zobellia galactanivorans beta-porphyranase A (PorA). PorA (EC 3.2.1.178) cleaves the sulfated polysaccharide porphyran at the (1->4) linkages between beta-D-galactopyranose and alpha-L-galactopyranose-6-sulfate, forming mostly the disaccharide alpha-L-galactopyranose-6-sulfate-(1->3)-beta-D-galactose. It is inactive on the non-sulfated agarose portion of the porphyran backbone and displays a strict requirement for C6-sulfate in the -2 and +1-binding subsites. Members of this family contain a fascin-like domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The fascin subfamily contains four copies of the fascin-like domain. The actual alignment was detected with superfamily member cd00257: Pssm-ID: 483951 [Multi-domain] Cd Length: 124 Bit Score: 37.25 E-value: 3.04e-03
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| Name | Accession | Description | Interval | E-value | |||
| PFM_aerolysin-like | cd20239 | pore-forming module of aerolysin-type beta-barrel pore-forming proteins; uncharacterized ... |
185-329 | 1.04e-74 | |||
pore-forming module of aerolysin-type beta-barrel pore-forming proteins; uncharacterized subgroup; Generally, pore-forming proteins (PFPs) are secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores detrimental to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel. Many of this family are bacterial toxins. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin). Pssm-ID: 380809 [Multi-domain] Cd Length: 145 Bit Score: 226.57 E-value: 1.04e-74
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| ETX_MTX2 | pfam03318 | Clostridium epsilon toxin ETX/Bacillus mosquitocidal toxin MTX2; This family appears to be ... |
164-292 | 6.53e-09 | |||
Clostridium epsilon toxin ETX/Bacillus mosquitocidal toxin MTX2; This family appears to be distantly related to pfam01117. Pssm-ID: 427241 [Multi-domain] Cd Length: 222 Bit Score: 55.49 E-value: 6.53e-09
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| beta-trefoil_FSCN-like | cd00257 | fascin-like domain, beta-trefoil fold, found in the fascin-like family; The fascin-like family ... |
42-159 | 3.04e-03 | |||
fascin-like domain, beta-trefoil fold, found in the fascin-like family; The fascin-like family includes actin-bundling/crosslinking proteins facsin1-4, singed, hisactophilin, and FSHD region gene 1 protein (FRG1). Fascin, also called fascin-1, is an actin-binding protein that contains 2 major actin binding sites. It is involved in the organization of actin filament bundles and the formation of microspikes, membrane ruffles, and stress fibers. It plays an important role for the formation of a diverse set of cell protrusions, such as filopodia, and for cell motility and migration. It mediates reorganization of the actin cytoskeleton and axon growth cone collapse in response to nerve growth factor (NGF). Fascin-2, also called retinal fascin, is a photoreceptor-specific paralog of the actin-bundling protein fascin. It may play a pivotal role in photoreceptor cell-specific events, such as disk morphogenesis. Fascin-3, also called testis fascin, is a novel paralog of the actin-bundling protein fascin expressed specifically in the elongate spermatid head. Protein singed acts as an actin-bundling protein that may have a role in the asymmetric organization and/or movement of cytoplasmic components. It has a role in somatic cells during the formation of adult bristles and hairs, and in the female germline during oogenesis. Hisactophilin is a histidine-rich actin-binding protein from Dictyostelium discoideum. It exists in two isoforms, hisactophilin-1 (HatA, also called HS I) and hisactophilin-2 (HatB, also called HS II), which are both myristoylated and distributed between plasma membrane and cytoplasm. Hisactophilin may act as an intracellular pH sensor that links chemotactic signals to responses in the microfilament system of the cells by nucleating actin polymerization or stabilizing the filaments. Protein FRG1 binds to mRNA in a sequence-independent manner. It may play a role in regulation of pre-mRNA splicing or in the assembly of rRNA into ribosomal subunits. It may be involved in mRNA transport, as well as in epigenetic regulation of muscle differentiation through regulation of activity of the histone-lysine N-methyltransferase KMT5B. This family also contains many homologs from bacteria, such as Zobellia galactanivorans beta-porphyranase A (PorA). PorA (EC 3.2.1.178) cleaves the sulfated polysaccharide porphyran at the (1->4) linkages between beta-D-galactopyranose and alpha-L-galactopyranose-6-sulfate, forming mostly the disaccharide alpha-L-galactopyranose-6-sulfate-(1->3)-beta-D-galactose. It is inactive on the non-sulfated agarose portion of the porphyran backbone and displays a strict requirement for C6-sulfate in the -2 and +1-binding subsites. Members of this family contain a fascin-like domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The fascin subfamily contains four copies of the fascin-like domain. Pssm-ID: 467441 [Multi-domain] Cd Length: 124 Bit Score: 37.25 E-value: 3.04e-03
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| Name | Accession | Description | Interval | E-value | ||||
| PFM_aerolysin-like | cd20239 | pore-forming module of aerolysin-type beta-barrel pore-forming proteins; uncharacterized ... |
185-329 | 1.04e-74 | ||||
pore-forming module of aerolysin-type beta-barrel pore-forming proteins; uncharacterized subgroup; Generally, pore-forming proteins (PFPs) are secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores detrimental to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel. Many of this family are bacterial toxins. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin). Pssm-ID: 380809 [Multi-domain] Cd Length: 145 Bit Score: 226.57 E-value: 1.04e-74
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| PFM_HFR-2-like | cd20216 | pore-forming module of wheat HFR-2 toxin, FEM32, and similar aerolysin-type beta-barrel ... |
182-319 | 1.09e-21 | ||||
pore-forming module of wheat HFR-2 toxin, FEM32, and similar aerolysin-type beta-barrel pore-forming proteins; HFR-2 is a wheat cytolytic toxin which may normally function in defense against certain insects or pathogens. The Hfr-2 gene is upregulated in virulent Hessian fly larval feedingdouble dagger. The HFR-2 protein may insert in plant cell membranes at the feeding sites and by forming pores provide water, ions and other small nutritive molecules to the developing larvae. This group also contains FEM32, a flower-specific lectin-like protein from the dioecious plant Rumex acetosa, which alters flower development and induces male sterility in transgenic tobacco. It has been suggested that the FEM32 gene activates some form of programmed cell death (PCD), a process that could be mediated by the action of its lectin domains for binding to specific glycoproteins on the cell membrane and facilitated by the formation of pore structures in the membranes and the subsequent leakage of the cytosolic content through its pore-forming aerolysin domain. Most proteins belonging to this group have N-terminal agglutatin (also known as amaranthin) lectin domains; most have two agglutatin domains, in combination with one aerolysin domain. Members of this group belong to the aerolysin family of beta-pore-forming proteins (beta-PFPs). PFPs are generally secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores harmful to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel, are found in all kingdoms of life and many are bacterial toxins. In addition to having a role in microbial infection, they have potential as biotechnological sensors and delivery systems. They share a similar monomeric architecture, with a variable membrane-binding domain and a structurally conserved pore-forming region. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin). Pssm-ID: 380786 [Multi-domain] Cd Length: 152 Bit Score: 89.57 E-value: 1.09e-21
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| PFM_LSL-like | cd20215 | pore-forming module of Laetiporus sulphureus LSL lectin and similar aerolysin-type beta-barrel ... |
167-322 | 2.55e-18 | ||||
pore-forming module of Laetiporus sulphureus LSL lectin and similar aerolysin-type beta-barrel pore-forming proteins; LSL is a lectin, produced by the parasitic mushroom Laetiporus sulphureus, which exhibits hemolytic and hemagglutinating activities. Members of this family belong to the aerolysin family of beta-pore-forming proteins (beta-PFPs). PFPs are generally secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores harmful to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel, are found in all kingdoms of life and many are bacterial toxins. In addition to having a role in microbial infection, they have potential as biotechnological sensors and delivery systems. They share a similar monomeric architecture, with a variable membrane-binding domain and a structurally conserved pore-forming region. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin). Pssm-ID: 380785 [Multi-domain] Cd Length: 164 Bit Score: 80.83 E-value: 2.55e-18
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| PFM_aerolysin-like | cd20242 | pore-forming module of aerolysin-type beta-barrel pore-forming proteins; uncharacterized ... |
190-321 | 1.79e-16 | ||||
pore-forming module of aerolysin-type beta-barrel pore-forming proteins; uncharacterized subgroup; Members of this group belong to the aerolysin family of beta-pore-forming proteins (beta-PFPs). PFPs are generally secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores harmful to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel, are found in all kingdoms of life and many are bacterial toxins. In addition to having a role in microbial infection, they have potential as biotechnological sensors and delivery systems. They share a similar monomeric architecture, with a variable membrane-binding domain and a structurally conserved pore-forming region. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin). Pssm-ID: 380812 [Multi-domain] Cd Length: 144 Bit Score: 75.15 E-value: 1.79e-16
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| PFM_natterin-3-like | cd20220 | pore-forming module of Thalassophryne nattereri fish venom natterins 1-4, and similar ... |
185-319 | 3.51e-14 | ||||
pore-forming module of Thalassophryne nattereri fish venom natterins 1-4, and similar aerolysin-type beta-barrel pore-forming proteins; This group includes 4 of the 5 Thalassophryne nattereri fish venom natterins: natterin-1, -2, -3, and 4. Natterins have kininogenase activity, kallikrein activity, and are allodynic and edema inducing. They also cleave type I and type IV collagen, resulting in necrosis of the affected cells. Contradictory to their edematic activity, Natterins also have anti-inflammatory effects through inhibition of interactions between leukocytes and the endothelium, and reduction in neutrophil accumulation. Many proteins belonging to this group have an N-terminal DUF3421 domain. They belong to the aerolysin family of beta-pore-forming proteins (beta-PFPs). PFPs are generally secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores harmful to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel, are found in all kingdoms of life and many are bacterial toxins. In addition to having a role in microbial infection, they have potential as biotechnological sensors and delivery systems. They share a similar monomeric architecture, with a variable membrane-binding domain and a structurally conserved pore-forming region. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin). Pssm-ID: 380790 [Multi-domain] Cd Length: 152 Bit Score: 68.81 E-value: 3.51e-14
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| PFM_aerolysin-like | cd20241 | pore-forming module of aerolysin-type beta-barrel pore-forming proteins; uncharacterized ... |
188-292 | 9.98e-14 | ||||
pore-forming module of aerolysin-type beta-barrel pore-forming proteins; uncharacterized subgroup; Members of this group belong to the aerolysin family of beta-pore-forming proteins (beta-PFPs). PFPs are generally secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores harmful to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel, are found in all kingdoms of life and many are bacterial toxins. In addition to having a role in microbial infection, they have potential as biotechnological sensors and delivery systems. They share a similar monomeric architecture, with a variable membrane-binding domain and a structurally conserved pore-forming region. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin). Pssm-ID: 380811 [Multi-domain] Cd Length: 139 Bit Score: 67.51 E-value: 9.98e-14
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| PFM_agglutinin-like | cd20217 | pore-forming module (PFM) of uncharacterized proteins which have agglutatin domain(s), and ... |
185-325 | 1.19e-13 | ||||
pore-forming module (PFM) of uncharacterized proteins which have agglutatin domain(s), and similar aerolysin-type beta-barrel pore-forming proteins; Most proteins belonging to this group have an N-terminal agglutatin (also known as amaranthin) lectin domain; some have fascin-like domains which adopt a beta-trefoil topology. Members of this group belong to the aerolysin family of beta-pore-forming proteins (beta-PFPs). PFPs are generally secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores harmful to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel, are found in all kingdoms of life and many are bacterial toxins. In addition to having a role in microbial infection, they have potential as biotechnological sensors and delivery systems. They share a similar monomeric architecture, with a variable membrane-binding domain and a structurally conserved pore-forming region. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin). Pssm-ID: 380787 [Multi-domain] Cd Length: 150 Bit Score: 67.53 E-value: 1.19e-13
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| PFM_aerolysin-like | cd20240 | pore-forming module of aerolysin-type beta-barrel pore-forming proteins; uncharacterized ... |
185-295 | 5.25e-12 | ||||
pore-forming module of aerolysin-type beta-barrel pore-forming proteins; uncharacterized subgroup; Generally, pore-forming proteins (PFPs) are secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores detrimental to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel. Many of this family are bacterial toxins. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin). Pssm-ID: 380810 [Multi-domain] Cd Length: 145 Bit Score: 62.67 E-value: 5.25e-12
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| PFM_LIN24-like | cd20237 | pore-forming module of Caenorhabditis elegans LIN-24 and similar aerolysin-type beta-barrel ... |
185-285 | 1.21e-10 | ||||
pore-forming module of Caenorhabditis elegans LIN-24 and similar aerolysin-type beta-barrel pore-forming proteins; The process of cytotoxic cell death occurs in Caenorhabditis elegans containing mutations in either of lin-24 and lin-33. The cytotoxicity caused by mutation of either gene requires the function of the other. Genes required for the engulfment of apoptotic corpses function in the cytotoxic cell deaths induced by mutations in lin-24 and lin-33. It has been proposed that Caenorhabditis elegans LIN-24 may function to interact with bacterial toxins having similarity with it, and inactivate these, thereby allowing C. elegans to consume or survive exposure to bacteria that produce such toxins. Members of this group belong to the aerolysin family of beta-pore-forming proteins (beta-PFPs). PFPs are generally secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores harmful to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel, are found in all kingdoms of life and many are bacterial toxins. In addition to having a role in microbial infection, they have potential as biotechnological sensors and delivery systems. They share a similar monomeric architecture, with a variable membrane-binding domain and a structurally conserved pore-forming region. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin). Pssm-ID: 380807 Cd Length: 120 Bit Score: 57.97 E-value: 1.21e-10
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| PFM_epsilon-toxin-like | cd20223 | pore-forming module of Clostridium perfringens epsilon-toxin and similar aerolysin-type ... |
172-290 | 1.19e-09 | ||||
pore-forming module of Clostridium perfringens epsilon-toxin and similar aerolysin-type beta-barrel pore-forming proteins; Clostridium perfringens epsilon-toxin is responsible for fatal enterotoxemia in ungulates. It forms a heptamer in the lipid rafts of Madin-Darby Canine Kidney (MDCK) cells, leading to cell death; its oligomer formation is induced by activation of neutral sphingomyelinase. This group also includes an insecticidal crystal protein Cry14-4 (encoded on plasmid pBMBt1 of Bacillus thuringiensis serovar darmstadiensis). Also included is pXO2-60 (a protein from the pathogenic pXO2 plasmid of Bacillus anthracis) which harbors a unique ubiquitin-like fold domain at the C-terminus of the aerolysin-like domain, and is involved in virulence. They belong to the aerolysin family of beta-pore-forming proteins (beta-PFPs). PFPs are generally secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores harmful to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel, are found in all kingdoms of life and many are bacterial toxins. In addition to having a role in microbial infection, they have potential as biotechnological sensors and delivery systems. They share a similar monomeric architecture, with a variable membrane-binding domain and a structurally conserved pore-forming region. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin). Pssm-ID: 380793 [Multi-domain] Cd Length: 144 Bit Score: 56.09 E-value: 1.19e-09
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| ETX_MTX2 | pfam03318 | Clostridium epsilon toxin ETX/Bacillus mosquitocidal toxin MTX2; This family appears to be ... |
164-292 | 6.53e-09 | ||||
Clostridium epsilon toxin ETX/Bacillus mosquitocidal toxin MTX2; This family appears to be distantly related to pfam01117. Pssm-ID: 427241 [Multi-domain] Cd Length: 222 Bit Score: 55.49 E-value: 6.53e-09
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| PFM_Dln1-like | cd20221 | pore-forming module of Danio rerio Dln1, and similar aerolysin-type beta-barrel pore-forming ... |
190-319 | 1.25e-08 | ||||
pore-forming module of Danio rerio Dln1, and similar aerolysin-type beta-barrel pore-forming proteins; Since Danio rerio Dln1 has a specific affinity towards high-mannose glycans, which are common on the surface of virus and fungi, it has been suggested that it may play a defense role. Members of this group also include lamprey immune protein (LIP), a defense molecule derived from lamprey supraneural body tissue which has efficient cytocidal actions against tumor cells. Many proteins belonging to this group have a N-terminal Jacalin-like lectin domain. They belong to the aerolysin family of beta-pore-forming proteins (beta-PFPs). PFPs are generally secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores harmful to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel, are found in all kingdoms of life and many are bacterial toxins. In addition to having a role in microbial infection, they have potential as biotechnological sensors and delivery systems. They share a similar monomeric architecture, with a variable membrane-binding domain and a structurally conserved pore-forming region. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin). Pssm-ID: 380791 [Multi-domain] Cd Length: 168 Bit Score: 53.53 E-value: 1.25e-08
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| PFM_parasporin-2-like | cd20222 | pore-forming module of parasporin-2, hydralysin and similar aerolysin-type beta-barrel ... |
184-295 | 2.31e-08 | ||||
pore-forming module of parasporin-2, hydralysin and similar aerolysin-type beta-barrel pore-forming proteins; Bacillus thuringiensis strain A1547 parasporin-2 (PS2, also named Cry46Aa1) is an anti-cancer protein which causes specific cell damage via PS2 oligomerization in the cell membrane. Glycosylphosphatidylinositol (GPI)-anchored proteins may be involved in the cytocidal action of PS2 as co-receptors for PS2's cytocidal action. This family also includes hydralysin (Hln-1) and Hln-2 produced by the green hydra Chlorohydra viridissima. Hydralysin is a paralysis-inducing protein not found in the stinging cells (nematocytes), with a cell type-selective cytolytic activity; it binds erythrocyte membranes and forms discrete pores. They belong to the aerolysin family of beta-pore-forming proteins (beta-PFPs). PFPs are generally secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores harmful to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel, are found in all kingdoms of life and many are bacterial toxins. In addition to having a role in microbial infection, they have potential as biotechnological sensors and delivery systems. They share a similar monomeric architecture, with a variable membrane-binding domain and a structurally conserved pore-forming region. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin). Pssm-ID: 380792 Cd Length: 147 Bit Score: 52.33 E-value: 2.31e-08
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| PFM_jacalin-like | cd20231 | pore-forming module of uncharacterized proteins which have an N-terminal jacalin-like lectin ... |
204-327 | 2.77e-08 | ||||
pore-forming module of uncharacterized proteins which have an N-terminal jacalin-like lectin domain, and similar aerolysin-type beta-barrel pore-forming proteins; Jacalin-like lectins are sugar-binding protein domains. Proteins having these lectin domains may bind mono- or oligosaccharides with high specificity. Generally, pore-forming proteins (PFPs) are secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores detrimental to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel. Many of this family are bacterial toxins. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin). Pssm-ID: 380801 [Multi-domain] Cd Length: 150 Bit Score: 52.36 E-value: 2.77e-08
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| PFM_tachylectin-like | cd20229 | pore-forming module (PFM) of uncharacterized proteins having tachylectin domain(s), and ... |
223-326 | 4.52e-08 | ||||
pore-forming module (PFM) of uncharacterized proteins having tachylectin domain(s), and similar aerolysin-type beta-barrel pore-forming proteins; Many proteins belonging to this group have tachylectin domain(s), N-terminal to this PFM; some also have an immunoglobulin (Ig) domain. Tachylectins are lectins which bind N-acetylglucosamine and N-acetylgalactosamine. Members of this group belong to the aerolysin family of beta-pore-forming proteins (beta-PFPs). PFPs are generally secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores harmful to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel, are found in all kingdoms of life and many are bacterial toxins. In addition to having a role in microbial infection, they have potential as biotechnological sensors and delivery systems. They share a similar monomeric architecture, with a variable membrane-binding domain and a structurally conserved pore-forming region. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin). Pssm-ID: 380799 [Multi-domain] Cd Length: 148 Bit Score: 51.76 E-value: 4.52e-08
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| PFM_fascin-like | cd20234 | pore-forming module (PFM) of uncharacterized proteins which have N-terminal fascin-like domain, ... |
185-325 | 6.91e-08 | ||||
pore-forming module (PFM) of uncharacterized proteins which have N-terminal fascin-like domain, and similar aerolysin-type beta-barrel pore-forming proteins; Most proteins belonging to this group have an N-terminal Fascin-like domains which adopt a beta-trefoil topology. Members of this group belong to the aerolysin family of beta-pore-forming proteins (beta-PFPs). PFPs are generally secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores harmful to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel, are found in all kingdoms of life and many are bacterial toxins. In addition to having a role in microbial infection, they have potential as biotechnological sensors and delivery systems. They share a similar monomeric architecture, with a variable membrane-binding domain and a structurally conserved pore-forming region. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin). Pssm-ID: 380804 Cd Length: 139 Bit Score: 50.98 E-value: 6.91e-08
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| PFM_alpha-toxin-like | cd20224 | pore-forming module of Clostridium septicum alpha-toxin and similar aerolysin-type beta-barrel ... |
194-284 | 1.35e-07 | ||||
pore-forming module of Clostridium septicum alpha-toxin and similar aerolysin-type beta-barrel pore-forming proteins; Clostridium septicum alpha-toxin is the main virulence factor of this bacterium, known for causing non-traumatic gas gangrene. Members of this family belong to the aerolysin family of beta-pore-forming proteins (beta-PFPs). PFPs are generally secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores harmful to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel, are found in all kingdoms of life and many are bacterial toxins. In addition to having a role in microbial infection, they have potential as biotechnological sensors and delivery systems. They share a similar monomeric architecture, with a variable membrane-binding domain and a structurally conserved pore-forming region. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin). Pssm-ID: 380794 Cd Length: 121 Bit Score: 49.68 E-value: 1.35e-07
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| PFM_Cry51Aa-like | cd20226 | pore-forming module of Bacillus thuringiensis insecticidal Cry51A toxin, Bacillus ... |
168-320 | 2.15e-06 | ||||
pore-forming module of Bacillus thuringiensis insecticidal Cry51A toxin, Bacillus thuringiensis cytotoxic parasporin-5 and similar aerolysin-type beta-barrel pore-forming proteins; Bacillus thuringiensis parasporin-5 has strong cytocidal activity against several types of cancer cells and may or may not have insecticidal activity. Cry51A toxin is toxic to coleopteran (beetle) larvae. Other members of this family include Bacillus thuringiensis Cry15Aa which is toxic to lepidopteran (butterflies and moth) larvae. They belong to the aerolysin family of beta-pore-forming proteins (beta-PFPs). PFPs are generally secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores harmful to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel, are found in all kingdoms of life and many are bacterial toxins. In addition to having a role in microbial infection, they have potential as biotechnological sensors and delivery systems. They share a similar monomeric architecture, with a variable membrane-binding domain and a structurally conserved pore-forming region. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin). Pssm-ID: 380796 [Multi-domain] Cd Length: 172 Bit Score: 47.27 E-value: 2.15e-06
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| Aerolysin | pfam01117 | Aerolysin toxin; This family represents the pore forming lobe of aerolysin. |
179-297 | 3.09e-06 | ||||
Aerolysin toxin; This family represents the pore forming lobe of aerolysin. Pssm-ID: 366474 Cd Length: 359 Bit Score: 48.41 E-value: 3.09e-06
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| PFM_crystallin-like | cd20232 | pore-forming module (PFM) of uncharacterized proteins which have N-terminal crystallin domain ... |
187-299 | 3.48e-06 | ||||
pore-forming module (PFM) of uncharacterized proteins which have N-terminal crystallin domain(s), and similar aerolysin-type beta-barrel pore-forming proteins; Many proteins belonging to this group have N-terminal crystallin (beta/gamma crystallins) domain(s). Members of this group belong to the aerolysin family of beta-pore-forming proteins (beta-PFPs). PFPs are generally secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores harmful to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel, are found in all kingdoms of life and many are bacterial toxins. In addition to having a role in microbial infection, they have potential as biotechnological sensors and delivery systems. They share a similar monomeric architecture, with a variable membrane-binding domain and a structurally conserved pore-forming region. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin). Pssm-ID: 380802 [Multi-domain] Cd Length: 151 Bit Score: 46.41 E-value: 3.48e-06
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| PFM_aerolysin_family | cd10140 | pore-forming module of aerolysin-type beta-barrel pore-forming proteins; Pore-forming proteins ... |
265-327 | 7.14e-05 | ||||
pore-forming module of aerolysin-type beta-barrel pore-forming proteins; Pore-forming proteins (PFPs) are generally secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores harmful to cells. Beta pore-forming proteins (beta-PFPs) form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel, are found in all kingdoms of life and many are bacterial toxins. In addition to having a role in microbial infection, they have potential as biotechnological sensors and delivery systems. They share a similar monomeric architecture, with a variable membrane-binding domain and a structurally conserved pore-forming region. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin). Members of this family includes enterolobin, a cytolytic, inflammatory and insecticidal protein from the Brazilian tree Enterolobium contortisiliquum. Pssm-ID: 380782 Cd Length: 92 Bit Score: 40.99 E-value: 7.14e-05
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| beta-trefoil_FSCN-like | cd00257 | fascin-like domain, beta-trefoil fold, found in the fascin-like family; The fascin-like family ... |
42-159 | 3.04e-03 | ||||
fascin-like domain, beta-trefoil fold, found in the fascin-like family; The fascin-like family includes actin-bundling/crosslinking proteins facsin1-4, singed, hisactophilin, and FSHD region gene 1 protein (FRG1). Fascin, also called fascin-1, is an actin-binding protein that contains 2 major actin binding sites. It is involved in the organization of actin filament bundles and the formation of microspikes, membrane ruffles, and stress fibers. It plays an important role for the formation of a diverse set of cell protrusions, such as filopodia, and for cell motility and migration. It mediates reorganization of the actin cytoskeleton and axon growth cone collapse in response to nerve growth factor (NGF). Fascin-2, also called retinal fascin, is a photoreceptor-specific paralog of the actin-bundling protein fascin. It may play a pivotal role in photoreceptor cell-specific events, such as disk morphogenesis. Fascin-3, also called testis fascin, is a novel paralog of the actin-bundling protein fascin expressed specifically in the elongate spermatid head. Protein singed acts as an actin-bundling protein that may have a role in the asymmetric organization and/or movement of cytoplasmic components. It has a role in somatic cells during the formation of adult bristles and hairs, and in the female germline during oogenesis. Hisactophilin is a histidine-rich actin-binding protein from Dictyostelium discoideum. It exists in two isoforms, hisactophilin-1 (HatA, also called HS I) and hisactophilin-2 (HatB, also called HS II), which are both myristoylated and distributed between plasma membrane and cytoplasm. Hisactophilin may act as an intracellular pH sensor that links chemotactic signals to responses in the microfilament system of the cells by nucleating actin polymerization or stabilizing the filaments. Protein FRG1 binds to mRNA in a sequence-independent manner. It may play a role in regulation of pre-mRNA splicing or in the assembly of rRNA into ribosomal subunits. It may be involved in mRNA transport, as well as in epigenetic regulation of muscle differentiation through regulation of activity of the histone-lysine N-methyltransferase KMT5B. This family also contains many homologs from bacteria, such as Zobellia galactanivorans beta-porphyranase A (PorA). PorA (EC 3.2.1.178) cleaves the sulfated polysaccharide porphyran at the (1->4) linkages between beta-D-galactopyranose and alpha-L-galactopyranose-6-sulfate, forming mostly the disaccharide alpha-L-galactopyranose-6-sulfate-(1->3)-beta-D-galactose. It is inactive on the non-sulfated agarose portion of the porphyran backbone and displays a strict requirement for C6-sulfate in the -2 and +1-binding subsites. Members of this family contain a fascin-like domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The fascin subfamily contains four copies of the fascin-like domain. Pssm-ID: 467441 [Multi-domain] Cd Length: 124 Bit Score: 37.25 E-value: 3.04e-03
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