Clostridium epsilon toxin ETX/Bacillus mosquitocidal toxin MTX2; This family appears to be distantly related to pfam01117.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153807051 229 PDFITTWFYSNNTSVQQSMTT-GFSKRASFSSNWSKTTGGSLSVNTTLKVGIPIIAEGKITTTVNTNYSSTYGKSETMED 307
Cdd:pfam03318  28 PLYTGSNTLTNNTDSTQTLQTqSFSKKVTTTTSTTTTHGFKIGAKASGKFGIPFVAEGGITLSVSGEYNFSSTTTNTTSV 107

                          90       100
                  ....*....|....*....|...
gi 1153807051 308 TQTYNFP---IVIAPRTSVTATA 327
Cdd:pfam03318 108 TTTYWVPsqkVTVPPHTTVRVTL 130

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).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153807051 208 DDFEIISLEYDnPDTGTIIK-QPDFITTWFYSNNTSVQQSMTTGFSKRASFSSNWSKTTGGSLSVNTTLKVGIPIIAEGK 286
Cdd:cd20215     1 EDMEIVSVEYD-LDKGKILSsTPLVLARQTLRNDTDVEQTMSFTLTETETHTSTFEYTAGFTITVGTSFKAGIPGVAEGK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153807051 287 ITTTVNTNYSSTYGKSETMEDTQTYNFPIVIAPRTSVTATATVGRYLINLNYTAKLRGKNTGKLITLKGTWNGVSCTDIK 366
Cdd:cd20215    80 IKVDTTVSNEWKWGESTTFTKTYTATFPVKAPPGSTVRAVATVTKSNLEVPFTMTLKSKSTGYEVETKGIYRGVSTWNLR 159

                  ....*
gi 1153807051 367 VTLEQ 371
Cdd:cd20215   160 TAIRE 164

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).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153807051 239 NNTSVQQSMTTGFSKRASFSSNWSKTTGGSLSVNTTLKVGIPIIAEGKITTTVNTNYSSTYGKSETMEDTQTYNFPIVIA 318
Cdd:cd20241    10 NNGNTPATLKANMSRSVSETGSFSFTHGFSIGVGTTIKAGIPFIVEGEIETELSTSHDFTWGKSTTVTTTVGSSVTVEVP 89

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1153807051 319 PRTSVTATATVGRYLINLNYTAKLRGKNTGKLITLKGTWNGVSCTDIKVT 368
Cdd:cd20241    90 PRSTQTVVGTFKRSKMTVPAKIYSKSKSTGVEVITEAVYRGTPVWDFEYT 139

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).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153807051 227 KQPDFITTWFYSNNTSVQQSMTTGFSKRASFSSNWSKTTGGSLSVNTTLKVGIPIIAEGKIttTVNTNYSSTY--GKSET 304
Cdd:cd20216     4 EKVLTLATGEATNNTSEPQTVTLKLSYTDTKTSTWNSSVSLKLGVKTTISAGVPFIVDGKI--EISAEFSGSYewGETKT 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1153807051 305 MEDTQTYNFPIVIAPRTSVTAT--ATVGRYLINLNYTAKLRGKNTGKLITLK--GTWNGVSCTDIKVTLEQ 371
Cdd:cd20216    82 ETTEVETTYTVTVPPMTKVTVTliATRGSCDVPFSYTQRDTLTNGTTVTYEKddGLYTGVNSYNFKYETKE 152

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).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153807051 242 SVQQSMTTGFSKRASFSSNWSKTTGGSLSVN--TTLKVGIPIIAEGKITTTVNTNYSSTYGKSETMEDTQTY--NFPIVI 317
Cdd:cd20229    15 TVPLNDTFTFSKTITEVSSFSHSHGFTVAEGaeTTFKAGIPVIGEEGIKVILDNSTTHQWNFTTTNEREVTFslTTNVVV 94

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1153807051 318 APRTSVTATATVGRYLINLNYTAKLRgKNTGKLITLKGTWNGVSCTDIKVTLE 370
Cdd:cd20229    95 PPGKAVRLEASVQKAKIDVPYRAEVI-TGFGYEVTITGTWTGVTVYDLRVKQE 146

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).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153807051 227 KQPDFITTWFYSNNTSVQQSMTT-GFSKRASFSSNWSKTTGGSLSVNTTLKVGIPIIAEGKITTTVNTNYSSTygKSETM 305
Cdd:cd20223    12 GEPLYVGSNTLTNDTDEEQTLKTpSFSKTVTDTVTTTTTNGFKLGVSTSAKFKIPFPGGGSTELSAEYNFSTT--NTNTT 89

                          90       100
                  ....*....|....*....|....*....
gi 1153807051 306 EDTQTYNFP---IVIAPRTSVTATATVGR 331
Cdd:cd20223    90 SETKTYTAPsqtIKVPPGKTYKVTVYLKK 118

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).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153807051 240 NTSVQQSMTTGFSKRASFSSNWSKTT--GGSLSVNTTLKVGIPIIAEGkITTTVNTNYSSTYGKS--ETMEDTQTYNFPI 315
Cdd:cd20231    14 NNSTDYTWTFSGSRTKTTSRTWSQSStsGFELSVSVSVSAGIPEIGEA-VTTSAGWSLSATSSESetETTTDELGWSVSG 92

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1153807051 316 VIAPRTSVTATATVGRYLINLNYTAKLR-GKNTGKLITLK--GTWNGVSCTDIKVT 368
Cdd:cd20231    93 TLPPGEGVKCRATAQEGKLDSDYTSTVTvTLQDGETFSFPepGTFKGVGYSEVDVV 148

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).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153807051 238 SNNTSVQQSMTtgFSKRASFSSNWSKTTGGSLSVNTTLKVGIPIIAEGKITTTVNTNYSSTYGKSETMEDTQTYNFPIVI 317
Cdd:cd20217    14 SEPADMQVQVT--LTETVSTSRTWSNSFTFSQSISTTFTAGVPEIASAETTITIGAEQTFGTEWGETTEEAVQFQSTYLV 91

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1153807051 318 ---APRT--SVTATATVGRYLINLNYTAK---LRGKNTGKLITLKGTWNGVSCTDIK 366
Cdd:cd20217    92 kdvPPGEeaTVTVECSTGKCRVPFTYKTRdtrLDGVDRPTVDEIDGVFEGVSAYNTR 148

pore-forming module (PFM) of uncharacterized proteins which have an N-terminal ABFB (alpha-L-arabinofuranosidase B) domain, and similar aerolysin-type beta-barrel pore-forming proteins; Most proteins belonging to this group have a PFM C-terminal to an ABFB domain. Alpha-L-arabinofuranosidase (Araf-ase, EC 3.2.1.55) belongs to the glycosyl hydrolase family GH54, and in Aspergillus niger exhibits both Araf-ase, (EC 3.2.1.55) and alpha-D-galactofuranose (Galf-ase) activities, with Galf-ase being less than Araf-ase. Some members have a Ricin-type carbohydrate-binding domain which adopts a beta-trefoil fold. 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).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153807051 229 PDFITTWFYSNNTSVQQSMTtGFSKRASFSSN--WSKTTGGSLSVNT--TLKVGIPIIA-EGKITTTVNTNYSSTYGKSE 303
Cdd:cd20238     1 PDLIVQDTLIDNSQGSQQMI-QFNGEISNTNTesYERTDGFELTIGEsyTVKASAIIVDeEGQIFFESKTIRNVTYGNQN 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1153807051 304 TMEDTQTYNFPIVIAPRTSVTATATVGRYLINLNYTAKLRGKNTGKLITLKGTWNGVSCTDIKVTL 369
Cdd:cd20238    80 TTTKTFAYETPLIVPGFSTYNATVIVKSMLLRIPFVATVHFEGLTWVTFFRGVYKGVQSYDYDVNI 145

pore-forming module of Physarum polycephalum spherulin-2a, Plodia interpunctella follicular epithelium yolk protein subunit YP4, and similar aerolysin-type beta-barrel pore-forming proteins; Spherulin 2a is a coat glycoprotein produced during encystment from the slime mold, Physarum polycephalum. YP4, is one of two subunits of the follicular epithelium yolk protein from Plodia interpunctella and other pyralid moths; it is produced in the follicle cells during vitellogenesis, and after secretion it is taken up into the oocyte and stored in the yolk spheres for utilization during embryogenesis. 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).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153807051 232 ITTWFYSNNTSVQQSMTTGFSK--RASFSSNWSKTtgGSLSVNTTLKVGIPIIAEGKITTTvNTNYSSTYG----KSETM 305
Cdd:cd20235     4 VKTQEFVNNSSKPATFNAGISQsvENTVSSTWSKS--GEVSVGQSINYGVNFLGSGGGGET-SFSYTSSWGesttKSETV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1153807051 306 EDTQTYNFPIVIAPRTSVTA--TATVGRYLINLNYTAKLRG 344
Cdd:cd20235    81 TVGSTSGVEVTLEPGQAVTAelTATKGTMKVEVTYEATLSG 121

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).

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1153807051 246 SMTTGFSKraSFSSNWSKTT----GGSLSVNTTLKVGIPIIAEGKITTTVNTN----YSSTYGKSETMEDTQTYNFPI 315
Cdd:cd20224    18 TGTATFNY--TESTSWSKTDnfkfSEGIKVTVKFTVGIPLIGGAESETEFSFNaeqgWSDSTGNTETIQQSAQYTATV 93

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153807051 289 TTVNTNYSSTYGKsetmedTQTYNFPIVIAPRTSVTATATVGRYLINLNYTAKLRGK----NTGKLITLKGTWNGVSCTD 364
Cdd:cd10140    15 TTQTQTVTLSETK------TVSVTVTVTVPPGKTVKVTVTVTKAKIDVPYTATLKATystsGTGTTGTVSGVFTGVNYAN 88

                  ....
gi 1153807051 365 IKVT 368
Cdd:cd10140    89 VETT 92