ricin B-type lectin domain, beta-trefoil fold, found in Boletus edulis lectin (BEL), Laetiporus sulphureus lectin (LSL) and similar proteins; BEL has potent anti-proliferative effects on human cancer cells. It functions as a homodimer and each protomer folds as a beta-trefoil. The BEL beta-trefoil binds galactose and other galactose-containing carbohydrates. LSL is a lectin that exhibits hemolytic and hemagglutinating activities. It functions as a hexamer. Its monomeric protein consists of two distinct modules: an N-terminal beta-trefoil lectin module (LSL150) and a C-terminal membrane pore-forming module (PFM). All members of this subfamily contain a ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (called alpha, beta, and gamma, respectively) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may contain a potential sugar-binding site. Due to the lack of an aromatic residue, the sugar binding within alpha-site of LSL150 might be absent.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399692001   7 IPPGGVRFRLQGKRSGCVLVGNTNDT--LTDYDGSEVYDDQWFTLaeVPGSSD---TYYIRSTYNrnnNKVIFCREEAY- 80
Cdd:cd23424     1 IPPPGLRFRLLGYASQQVIFSRTSNSprVGHSPSSEVYDDQYFTL--IPGTGPhagLYAIKSKAT---GKVIFSRRGASp 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1399692001  81 DVGLYRTD--YADQHFRLDPGEGEFRGLFRLLAPATNRVITSN-GRSNGVGNYPADEDKYDDQYFAFLF 146
Cdd:cd23424    76 QVGSIDGDgsYDDQWFKFEPGKGDFKGYFRLVNPATDTVLFSRtTLEPQFGNIPADQPVFDDQYFSFLF 144

ricin B-type lectin domain, beta-trefoil fold, found in Boletus edulis lectin (BEL), Laetiporus sulphureus lectin (LSL) and similar proteins; BEL has potent anti-proliferative effects on human cancer cells. It functions as a homodimer and each protomer folds as a beta-trefoil. The BEL beta-trefoil binds galactose and other galactose-containing carbohydrates. LSL is a lectin that exhibits hemolytic and hemagglutinating activities. It functions as a hexamer. Its monomeric protein consists of two distinct modules: an N-terminal beta-trefoil lectin module (LSL150) and a C-terminal membrane pore-forming module (PFM). All members of this subfamily contain a ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (called alpha, beta, and gamma, respectively) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may contain a potential sugar-binding site. Due to the lack of an aromatic residue, the sugar binding within alpha-site of LSL150 might be absent.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399692001   7 IPPGGVRFRLQGKRSGCVLVGNTNDT--LTDYDGSEVYDDQWFTLaeVPGSSD---TYYIRSTYNrnnNKVIFCREEAY- 80
Cdd:cd23424     1 IPPPGLRFRLLGYASQQVIFSRTSNSprVGHSPSSEVYDDQYFTL--IPGTGPhagLYAIKSKAT---GKVIFSRRGASp 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1399692001  81 DVGLYRTD--YADQHFRLDPGEGEFRGLFRLLAPATNRVITSN-GRSNGVGNYPADEDKYDDQYFAFLF 146
Cdd:cd23424    76 QVGSIDGDgsYDDQWFKFEPGKGDFKGYFRLVNPATDTVLFSRtTLEPQFGNIPADQPVFDDQYFSFLF 144

Pili PilJ C-terminal domain; This is the C-terminal domain of PilJ, a Type IV pilin found in gram-positive Clostridium difficile. Incorporation of PilJ into pili exposes the C-terminal domain of PilJ to create a novel interaction surface. This C-terminal domain is not observed in other Type IV pilin proteins.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1399692001  28 NTNDTLTDYDGSEVYDDQWFT-----LAEVPGSSDTYYIRSTYNRNNN 70
Cdd:pfam18223   6 KNNDDFREYLLKNKYNGGWPTvdeefLAKYNYEGDTLYIQPYYYGPTK 53

ricin B-type lectin domain, beta-trefoil fold, found in Boletus edulis lectin (BEL), Laetiporus sulphureus lectin (LSL) and similar proteins; BEL has potent anti-proliferative effects on human cancer cells. It functions as a homodimer and each protomer folds as a beta-trefoil. The BEL beta-trefoil binds galactose and other galactose-containing carbohydrates. LSL is a lectin that exhibits hemolytic and hemagglutinating activities. It functions as a hexamer. Its monomeric protein consists of two distinct modules: an N-terminal beta-trefoil lectin module (LSL150) and a C-terminal membrane pore-forming module (PFM). All members of this subfamily contain a ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (called alpha, beta, and gamma, respectively) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may contain a potential sugar-binding site. Due to the lack of an aromatic residue, the sugar binding within alpha-site of LSL150 might be absent.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399692001   7 IPPGGVRFRLQGKRSGCVLVGNTNDT--LTDYDGSEVYDDQWFTLaeVPGSSD---TYYIRSTYNrnnNKVIFCREEAY- 80
Cdd:cd23424     1 IPPPGLRFRLLGYASQQVIFSRTSNSprVGHSPSSEVYDDQYFTL--IPGTGPhagLYAIKSKAT---GKVIFSRRGASp 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1399692001  81 DVGLYRTD--YADQHFRLDPGEGEFRGLFRLLAPATNRVITSN-GRSNGVGNYPADEDKYDDQYFAFLF 146
Cdd:cd23424    76 QVGSIDGDgsYDDQWFKFEPGKGDFKGYFRLVNPATDTVLFSRtTLEPQFGNIPADQPVFDDQYFSFLF 144

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 1399692001 169 PHSWMGQTINETNDPNDSMEINMEETLSETVSFEHTSGITLteGMTASF--GIPGVMEGEITLEMSIVDSFTFGKSKTVQ 246
Cdd:cd20242     1 PASLYSQTVTNDTGQPQTPSISGSETVTETSTWEDEVGLKL--GVSTSFsaGVPVVAEGKVEVSAEVHNNYTWNGSNTRS 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1399692001 247 HTVGSSVTVAAPARTITTVEATVTQSKITIP----AKIYSKSKAlGITVITEAMYEG 299
Cdd:cd20242    79 KTWSFSTPVNVPAHSAVRATATVTESTISVPytltWKSIFESGA-RVTGTIEGMYKG 134

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 1399692001 173 MGQTINETNDPNdSMEINMEETLSETVSFEHTSGITLTEGMTASFGIPGVMEGEITLEMSIVDSFTFGKSKTVQHTVGSS 252
Cdd:cd20216    11 TGEATNNTSEPQ-TVTLKLSYTDTKTSTWNSSVSLKLGVKTTISAGVPFIVDGKIEISAEFSGSYEWGETKTETTEVETT 89

                          90       100
                  ....*....|....*....|....*
gi 1399692001 253 VTVAAPARTITTVEATVTQSKITIP 277
Cdd:cd20216    90 YTVTVPPMTKVTVTLIATRGSCDVP 114

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 1399692001 180 TNDPNDSMEInmEETLSETVSFEHTSGITLTEGMTASF--GIPGVMEGEIT--LEMSIVDSFTFGKS--KTVQHTVGSSV 253
Cdd:cd20229    15 TVPLNDTFTF--SKTITEVSSFSHSHGFTVAEGAETTFkaGIPVIGEEGIKviLDNSTTHQWNFTTTneREVTFSLTTNV 92

                          90       100
                  ....*....|....*....|....
gi 1399692001 254 TVaaPARTITTVEATVTQSKITIP 277
Cdd:cd20229    93 VV--PPGKAVRLEASVQKAKIDVP 114

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 1399692001 180 TNDPNDSMEIN---MEETLSETVSFEHTSGITLTEGMTASFGIP--GVMEGEITLEMSIVDSFTFGKSKTVQHTVGsSVT 254
Cdd:cd20223    23 TNDTDEEQTLKtpsFSKTVTDTVTTTTTNGFKLGVSTSAKFKIPfpGGGSTELSAEYNFSTTNTNTTSETKTYTAP-SQT 101

                          90       100
                  ....*....|....*....|.
gi 1399692001 255 VAAPARTITTVEATVTQSKIT 275
Cdd:cd20223   102 IKVPPGKTYKVTVYLKKVKFS 122

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).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399692001 176 TINETNDPND-----SMEINMEETLSETVSFEHTSGITLTE----------GMTASFGIPGVMEGEITLEMSIVDSFTFG 240
Cdd:cd20222     5 VVREEGPPTPdilgtTEAVNNGDEEEITVTYSYKVGGKWTWktswssssttGATFSSGIPLEGVFEVGTEFSVSGTTGES 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1399692001 241 KSKTVQHTVGSSVTVAAPARtittveatvTQSKITIPAKIySKSKA 286
Cdd:cd20222    85 GSTSTEKTLTSSVTVKVPPN---------SKVKITMVTKM-KKSSV 120

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).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399692001 169 PHSWMGQTINETN-DPNDSMEINMEETLSETVSFEHTSGITLTEGMTASFGIPGV-MEGEI--TLEMSIVDSFTFGK--S 242
Cdd:cd20232     2 PIGISSSTQNGSDiEQVATLTLERELSKSTTRSFSESTLIGIEVSTTASVGVSAGpVSAEVeqTVTSTLENTFTIGKeeT 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1399692001 243 KTVQHTVGSSVTVAAPARTITTVEATVTQSKITIPAkIYS 282
Cdd:cd20232    82 KSETITFSKSVNVTIPPGNIGEAVMTLTPKKYKVEA-IYT 120

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        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1399692001 181 NDPNDSMEINMEETLSETVSfeHTSGITLTEGMT----ASFGIPGVMEGEITLEMSIVD----SFTFGKSKTVQHTVGSS 252
Cdd:cd20224    13 GNTEDTGTATFNYTESTSWS--KTDNFKFSEGIKvtvkFTVGIPLIGGAESETEFSFNAeqgwSDSTGNTETIQQSAQYT 90

                          90       100
                  ....*....|....*....|...
gi 1399692001 253 VTVaaPARTITTVEATVTQSKIT 275
Cdd:cd20224    91 ATV--PPRSKRTITLTAFKTKGT 111

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1399692001 232 SIVDSFTFGKSKTVqhTVGSSVTVAAPARTITTVEATVTQSKITIPAKIYSKSKALGITVITEAMYEG 299
Cdd:cd10140    14 STTQTQTVTLSETK--TVSVTVTVTVPPGKTVKVTVTVTKAKIDVPYTATLKATYSTSGTGTTGTVSG 79