pore-forming module of Cynops pyrrhogaster EP37, and similar aerolysin-type beta-barrel pore-forming proteins; Cynops pyrrhogaster (Japanese newt EP37) EP37 is an epidermis-specific protein which has a non-lens beta/gamma-crystallin domain in tandem and N-terminal to this pore-forming module. C. pyrrhogaster has several EP37-like proteins present in skin, gastric epithelium and fundic glands of an adult newt and in the swimming larva. This group also includes the alpha subunit of Bombina maxima betagamma-CAT (a non-lens betagamma-crystallin (alpha-subunit) and trefoil factor (beta subunit) complex) identified from skin secretions. Betagamma-CAT shows potent hemolytic activity on mammalian erythrocytes. Many proteins belonging to this group have N-terminal crystallin (beta/gamma crystallin) 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 1624349576 193 SVVIDSICGVNRGKHEQTFSSELSREYEGSVTESFNFSNATQISVGMSFGFDIGIVKSEVNVSVSNTFTVEKGSSNTKTE 272
Cdd:cd20230     1 SVVIDEICGVNKTDIEQTFTTELSREYEVSVTQSFTFSNATQIKVGTSFTVDLGGDKFELNLELSNTFTVEKGKSESRTT 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1624349576 273 KKGVKISIPATIHPHTKLTVNVVRKEVDVKVPVKITIQSGYSSSTEYGEYRCQAGNSILAEYQEED 338
Cdd:cd20230    81 TKKREVELPAKVPPHTKLTVNVVRKEVTYSVPVELIITRGSKTKTEYGEYRCQSGTSITTEYTEEP 146

Beta/gamma crystallins; Beta/gamma crystallins

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624349576   93 QITLYENQNYGGRSITLNCET-NLCFGSFNDMISSCRVDRGAWVLYEHPNRGGRSILVRAG--RKFPSIGWIDNQVSWVR 169
Cdd:smart00247   1 KITLYEDENFQGRSYELSDDCpSLQDYGSRDNVSSVRVESGCWVLYEQPNYRGRQYVLEPGeyPDYQEWGGFNDQISSIR 80

                   ..
gi 1624349576  170 PL 171
Cdd:smart00247  81 RI 82

pore-forming module of Cynops pyrrhogaster EP37, and similar aerolysin-type beta-barrel pore-forming proteins; Cynops pyrrhogaster (Japanese newt EP37) EP37 is an epidermis-specific protein which has a non-lens beta/gamma-crystallin domain in tandem and N-terminal to this pore-forming module. C. pyrrhogaster has several EP37-like proteins present in skin, gastric epithelium and fundic glands of an adult newt and in the swimming larva. This group also includes the alpha subunit of Bombina maxima betagamma-CAT (a non-lens betagamma-crystallin (alpha-subunit) and trefoil factor (beta subunit) complex) identified from skin secretions. Betagamma-CAT shows potent hemolytic activity on mammalian erythrocytes. Many proteins belonging to this group have N-terminal crystallin (beta/gamma crystallin) 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 1624349576 193 SVVIDSICGVNRGKHEQTFSSELSREYEGSVTESFNFSNATQISVGMSFGFDIGIVKSEVNVSVSNTFTVEKGSSNTKTE 272
Cdd:cd20230     1 SVVIDEICGVNKTDIEQTFTTELSREYEVSVTQSFTFSNATQIKVGTSFTVDLGGDKFELNLELSNTFTVEKGKSESRTT 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1624349576 273 KKGVKISIPATIHPHTKLTVNVVRKEVDVKVPVKITIQSGYSSSTEYGEYRCQAGNSILAEYQEED 338
Cdd:cd20230    81 TKKREVELPAKVPPHTKLTVNVVRKEVTYSVPVELIITRGSKTKTEYGEYRCQSGTSITTEYTEEP 146

Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity between them is very low.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624349576   8 KIFVYEHPDFQGVSREFTEYCPDLRDVSFNDCISSVKVIGQPWVLYEHPHCQGAQFYFEEGECRSV-VW---HDAISSLE 83
Cdd:pfam00030   1 KIVLYEKENFQGRSIELTDDCPSLQERGFNSRVNSIRVLSGAWVLYEHPNFRGRQYVLEPGEYPDWsDWgapNDRIGSLR 80

                  ..
gi 1624349576  84 QV 85
Cdd:pfam00030  81 PI 82

Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity between them is very low.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624349576  93 QITLYENQNYGGRSITLNCETNLCFGS-FNDMISSCRVDRGAWVLYEHPNRGGRSILVRAG--RKFPSIGWIDNQVSWVR 169
Cdd:pfam00030   1 KIVLYEKENFQGRSIELTDDCPSLQERgFNSRVNSIRVLSGAWVLYEHPNFRGRQYVLEPGeyPDWSDWGAPNDRIGSLR 80

                  ..
gi 1624349576 170 PL 171
Cdd:pfam00030  81 PI 82

pore-forming module of Cynops pyrrhogaster EP37, and similar aerolysin-type beta-barrel pore-forming proteins; Cynops pyrrhogaster (Japanese newt EP37) EP37 is an epidermis-specific protein which has a non-lens beta/gamma-crystallin domain in tandem and N-terminal to this pore-forming module. C. pyrrhogaster has several EP37-like proteins present in skin, gastric epithelium and fundic glands of an adult newt and in the swimming larva. This group also includes the alpha subunit of Bombina maxima betagamma-CAT (a non-lens betagamma-crystallin (alpha-subunit) and trefoil factor (beta subunit) complex) identified from skin secretions. Betagamma-CAT shows potent hemolytic activity on mammalian erythrocytes. Many proteins belonging to this group have N-terminal crystallin (beta/gamma crystallin) 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 1624349576 193 SVVIDSICGVNRGKHEQTFSSELSREYEGSVTESFNFSNATQISVGMSFGFDIGIVKSEVNVSVSNTFTVEKGSSNTKTE 272
Cdd:cd20230     1 SVVIDEICGVNKTDIEQTFTTELSREYEVSVTQSFTFSNATQIKVGTSFTVDLGGDKFELNLELSNTFTVEKGKSESRTT 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1624349576 273 KKGVKISIPATIHPHTKLTVNVVRKEVDVKVPVKITIQSGYSSSTEYGEYRCQAGNSILAEYQEED 338
Cdd:cd20230    81 TKKREVELPAKVPPHTKLTVNVVRKEVTYSVPVELIITRGSKTKTEYGEYRCQSGTSITTEYTEEP 146

Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity between them is very low.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624349576   8 KIFVYEHPDFQGVSREFTEYCPDLRDVSFNDCISSVKVIGQPWVLYEHPHCQGAQFYFEEGECRSV-VW---HDAISSLE 83
Cdd:pfam00030   1 KIVLYEKENFQGRSIELTDDCPSLQERGFNSRVNSIRVLSGAWVLYEHPNFRGRQYVLEPGEYPDWsDWgapNDRIGSLR 80

                  ..
gi 1624349576  84 QV 85
Cdd:pfam00030  81 PI 82

Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity between them is very low.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624349576  93 QITLYENQNYGGRSITLNCETNLCFGS-FNDMISSCRVDRGAWVLYEHPNRGGRSILVRAG--RKFPSIGWIDNQVSWVR 169
Cdd:pfam00030   1 KIVLYEKENFQGRSIELTDDCPSLQERgFNSRVNSIRVLSGAWVLYEHPNFRGRQYVLEPGeyPDWSDWGAPNDRIGSLR 80

                  ..
gi 1624349576 170 PL 171
Cdd:pfam00030  81 PI 82

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 1624349576 190 NTKSVVIDSICGVNRGKHEQTFSSELSReyegSVTE--SFNFSNATQISVGMSFGFDIGIV---KSEVNVSVSNTFTVek 264
Cdd:cd20215    19 SSTPLVLARQTLRNDTDVEQTMSFTLTE----TETHtsTFEYTAGFTITVGTSFKAGIPGVaegKIKVDTTVSNEWKW-- 92

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1624349576 265 GSSNTKTEKkgVKISIPATIHPHTKLTVNVVRKEVDVKVPVKITIQS---GYSSSTEyGEYR 323
Cdd:cd20215    93 GESTTFTKT--YTATFPVKAPPGSTVRAVATVTKSNLEVPFTMTLKSkstGYEVETK-GIYR 151

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).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624349576 192 KSVVIDSICGVNRGKHEQTFSSELSRE----YEGSVTESFnfsnatqiSVGMSFGFDIGIVKS--EVNVSVSNTFTVEKG 265
Cdd:cd20237     1 KSVVLFKTTFTNNTSTEQEYTFKTERTttssCTWSVTEGF--------TIGGEVSLKLGPPPDiaEANAGFSRELSLSKT 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1624349576 266 SSNTKTEKKGVKISIPATIHPHTKLTVNVVRKEVD-VKVPVKIT 308
Cdd:cd20237    73 QEETFEEELTWSVDSQVTVPPKTKVTAELVITEDEgIEQRVRVT 116

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 1624349576 202 VNRGKHEQTFSSELSREYEGSVTESFNFS--NATQISVGMSFGFDIGIVKSEVNVSVS----NTFTV--EKGSSNTKTEK 273
Cdd:cd20232    10 QNGSDIEQVATLTLERELSKSTTRSFSEStlIGIEVSTTASVGVSAGPVSAEVEQTVTstleNTFTIgkEETKSETITFS 89

                  ....*...
gi 1624349576 274 KGVKISIP 281
Cdd:cd20232    90 KSVNVTIP 97

Aerolysin toxin; This family represents the pore forming lobe of aerolysin.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624349576 142 RGGRSILVRAGRKFPSIG-WIDNQVS-----WVRPLKPGRPKITAELIWDKKEENTKSVVIdsicgVNRGKHEQTFSSEL 215
Cdd:pfam01117  49 RNGDSWLVEANNNGPCNGyRCDHRLKmhfsdFKFGVKPSSLKYGDPVISDREPYKYIVGYA-----RNDSDTPQQRVLTL 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624349576 216 SREYEGSVTESFNFSNATQISVGMSFGFD-IGIVKSEVNVSVSNTFTvekgSSNTKTEKKGVKISIPATIHPHTKLTVNV 294
Cdd:pfam01117 124 SYDEVTNWSKTDTYKYSEKVTIKNKYKFPlIGETELSLELGANQSWA----TTNGNSSTKTISDVARVLVPANTKIPVRL 199

                         170       180
                  ....*....|....*....|
gi 1624349576 295 VRKEVDVKVPVKITIQSGYS 314
Cdd:pfam01117 200 KLEKARVDYPYEFNAQVSYD 219

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).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624349576 196 IDSICGVNRGKHEQTFSSELSreyeGSVTESFNFSNATQISVGMSFGFDIGIVKseVNVSVSNTfTVEKGSSNT--KTEK 273
Cdd:cd20240     8 IVTWTYTNNTSIEQTMTTNFS----ETATETSSFSETEGVSTTVSTSLKVGIPF--IAGGEITT-TTTTSQSWTygKSET 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1624349576 274 KGVKIS--IPATIHPHTKLTVNVV--RKEVDVK 302
Cdd:cd20240    81 KTDTISytFPIVVPPNTTVTATAVvtKYNMDVT 113

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 1624349576 222 SVTESFNFSNATQIS----VGMSFGFDIGIVKS-EVNVSVSNTFTVEKG--SSNTKTEKKGVKISIPatihPHTKLTVNV 294
Cdd:cd20222    36 SYKVGGKWTWKTSWSssstTGATFSSGIPLEGVfEVGTEFSVSGTTGESgsTSTEKTLTSSVTVKVP----PNSKVKITM 111

                  ...
gi 1624349576 295 VRK 297
Cdd:cd20222   112 VTK 114

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).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624349576 202 VNRGKHEQTFSSELSREYEgsVTESFNFSNATQISVGMSF--GFDIgIVKSEVNVSVSNTFTVEKGSSNTKTEKKGVKIS 279
Cdd:cd20220    15 TNNGCKPVKKTVTLSKTTE--VEHRWDTSFSITLGVSTTItaGIPI-IAGGGWEVSTETTFTWSGGTSVTESVTHSVSVE 91

                          90       100
                  ....*....|....*....|....*
gi 1624349576 280 IpaTIHPHTKLTVNVVRKEVDVKVP 304
Cdd:cd20220    92 V--TVPPNHSCTVKMVGYKYKADIP 114

Peptidase inhibitor family I36; This domain is currently only found in a small set of S. coelicolor secreted proteins. There are four conserved cysteines that probably form two disulphide bonds. Proteins 2SCK31.15C and SCO3675 also have probable beta-propellers at their C-termini. This family includes Swiss:P01077 a known peptidase inhibitor of known structure. This protein has a crystallin like fold pfam00030 and is distantly related by sequence. It is not known whether other members of this family are peptidase inhibitors.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1624349576  96 LYENQNYGGRSITLNCETNLCFGSFNDMISSCRVDRGAWV-LYEHPNRGGRSILV 149
Cdd:pfam03995  15 LWSGANGTGRMAELSGSDALVGAGMNDKARSVWNRTGSWVtVYTDANYGGRLAVL 69

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 1624349576 202 VNRGKHEQTFSSELSREYEGSVTESFnfSNATQISVGMSFGFDIGIVKSEVNVSVSNTFTVEKGSSNTKTEKKGVKISIP 281
Cdd:cd20235    10 VNNSSKPATFNAGISQSVENTVSSTW--SKSGEVSVGQSINYGVNFLGSGGGGETSFSYTSSWGESTTKSETVTVGSTSG 87

                          90       100
                  ....*....|....*....|....*.
gi 1624349576 282 ATIH--PHTKLTVNVVRKEVDVKVPV 305
Cdd:cd20235    88 VEVTlePGQAVTAELTATKGTMKVEV 113