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Conserved domains on  [gi|2448922026|gb|KAJ5959911|]
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hypothetical protein N7479_007061 [Penicillium vulpinum]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PFM_aerolysin-like cd20241
pore-forming module of aerolysin-type beta-barrel pore-forming proteins; uncharacterized ...
 187-325 2.94e-77

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: 233.15  E-value: 2.94e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2448922026 187 PEIFRTTVRNNAQEKATLKCDFRREKSAKGSFTHSHGFSFGVKTEIKASIPFIVDGKIETELKTDHKFTWGQEESWSKTL 266
Cdd:cd20241     1 PHAFEVTVRNNGNTPATLKANMSRSVSETGSFSFTHGFSIGVGTTIKAGIPFIVEGEIETELSTSHDFTWGKSTTVTTTV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2448922026 267 GTELGVEVPGYSTRDVVGTFKDSDMTVPAKIYSQTKSTGVEIITEVEYRGTSVWDFEYT 325
Cdd:cd20241    81 GSSVTVEVPPRSTQTVVGTFKRSKMTVPAKIYSKSKSTGVEVITEAVYRGTPVWDFEYT 139
beta-trefoil_Ricin_BEL-like cd23424
ricin B-type lectin domain, beta-trefoil fold, found in Boletus edulis lectin (BEL), ...
 9-165 1.81e-36

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.


:

Pssm-ID: 467302  Cd Length: 144  Bit Score: 128.63  E-value: 1.81e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2448922026   9 IPTKGLRFRLLGYYSdNIPVPSGKQISCRSKDSVSSE---DGWFTLVPIDGGK--FYYIQSAlkhDDEAAISSRPGEmeg 83
Cdd:cd23424     1 IPPPGLRFRLLGYAS-QQVIFSRTSNSPRVGHSPSSEvydDQYFTLIPGTGPHagLYAIKSK---ATGKVIFSRRGA--- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2448922026  84 crfqPVDVRNIFDDS---FMRFTFQPAVVDrFAGHFRIVSAA-GRILASKRSYkdGTFWDNFPALFllsqdanhSDSPEQ 159
Cdd:cd23424    74 ----SPQVGSIDGDGsydDQWFKFEPGKGD-FKGYFRLVNPAtDTVLFSRTTL--EPQFGNIPADQ--------PVFDDQ 138


                  ....*.
gi 2448922026 160 YFSFVF 165
Cdd:cd23424   139 YFSFLF 144
 
Name Accession Description Interval E-value
PFM_aerolysin-like cd20241
pore-forming module of aerolysin-type beta-barrel pore-forming proteins; uncharacterized ...
 187-325 2.94e-77

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: 233.15  E-value: 2.94e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2448922026 187 PEIFRTTVRNNAQEKATLKCDFRREKSAKGSFTHSHGFSFGVKTEIKASIPFIVDGKIETELKTDHKFTWGQEESWSKTL 266
Cdd:cd20241     1 PHAFEVTVRNNGNTPATLKANMSRSVSETGSFSFTHGFSIGVGTTIKAGIPFIVEGEIETELSTSHDFTWGKSTTVTTTV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2448922026 267 GTELGVEVPGYSTRDVVGTFKDSDMTVPAKIYSQTKSTGVEIITEVEYRGTSVWDFEYT 325
Cdd:cd20241    81 GSSVTVEVPPRSTQTVVGTFKRSKMTVPAKIYSKSKSTGVEVITEAVYRGTPVWDFEYT 139
beta-trefoil_Ricin_BEL-like cd23424
ricin B-type lectin domain, beta-trefoil fold, found in Boletus edulis lectin (BEL), ...
 9-165 1.81e-36

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.


Pssm-ID: 467302  Cd Length: 144  Bit Score: 128.63  E-value: 1.81e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2448922026   9 IPTKGLRFRLLGYYSdNIPVPSGKQISCRSKDSVSSE---DGWFTLVPIDGGK--FYYIQSAlkhDDEAAISSRPGEmeg 83
Cdd:cd23424     1 IPPPGLRFRLLGYAS-QQVIFSRTSNSPRVGHSPSSEvydDQYFTLIPGTGPHagLYAIKSK---ATGKVIFSRRGA--- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2448922026  84 crfqPVDVRNIFDDS---FMRFTFQPAVVDrFAGHFRIVSAA-GRILASKRSYkdGTFWDNFPALFllsqdanhSDSPEQ 159
Cdd:cd23424    74 ----SPQVGSIDGDGsydDQWFKFEPGKGD-FKGYFRLVNPAtDTVLFSRTTL--EPQFGNIPADQ--------PVFDDQ 138


                  ....*.
gi 2448922026 160 YFSFVF 165
Cdd:cd23424   139 YFSFLF 144
ETX_MTX2 pfam03318
Clostridium epsilon toxin ETX/Bacillus mosquitocidal toxin MTX2; This family appears to be ...
 184-300 6.52e-04

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: 40.47  E-value: 6.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2448922026 184 NTKPEIF--RTTVRNNAQEKATLKCD-FRREKSAKGSFTHSHGFSFGVKTEIKASIPFIVDGKIETELKTDHKFTWGQEE 260
Cdd:pfam03318  24 KTLTPLYtgSNTLTNNTDSTQTLQTQsFSKKVTTTTSTTTTHGFKIGAKASGKFGIPFVAEGGITLSVSGEYNFSSTTTN 103

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2448922026 261 SWSKT-LGTELG--VEVPGYSTRDVVGTFKDSDMTVPAKIYSQ 300
Cdd:pfam03318 104 TTSVTtTYWVPSqkVTVPPHTTVRVTLVLYKTTYSVPVDLYTT 146
 
Name Accession Description Interval E-value
PFM_aerolysin-like cd20241
pore-forming module of aerolysin-type beta-barrel pore-forming proteins; uncharacterized ...
 187-325 2.94e-77

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: 233.15  E-value: 2.94e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2448922026 187 PEIFRTTVRNNAQEKATLKCDFRREKSAKGSFTHSHGFSFGVKTEIKASIPFIVDGKIETELKTDHKFTWGQEESWSKTL 266
Cdd:cd20241     1 PHAFEVTVRNNGNTPATLKANMSRSVSETGSFSFTHGFSIGVGTTIKAGIPFIVEGEIETELSTSHDFTWGKSTTVTTTV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2448922026 267 GTELGVEVPGYSTRDVVGTFKDSDMTVPAKIYSQTKSTGVEIITEVEYRGTSVWDFEYT 325
Cdd:cd20241    81 GSSVTVEVPPRSTQTVVGTFKRSKMTVPAKIYSKSKSTGVEVITEAVYRGTPVWDFEYT 139
beta-trefoil_Ricin_BEL-like cd23424
ricin B-type lectin domain, beta-trefoil fold, found in Boletus edulis lectin (BEL), ...
 9-165 1.81e-36

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.


Pssm-ID: 467302  Cd Length: 144  Bit Score: 128.63  E-value: 1.81e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2448922026   9 IPTKGLRFRLLGYYSdNIPVPSGKQISCRSKDSVSSE---DGWFTLVPIDGGK--FYYIQSAlkhDDEAAISSRPGEmeg 83
Cdd:cd23424     1 IPPPGLRFRLLGYAS-QQVIFSRTSNSPRVGHSPSSEvydDQYFTLIPGTGPHagLYAIKSK---ATGKVIFSRRGA--- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2448922026  84 crfqPVDVRNIFDDS---FMRFTFQPAVVDrFAGHFRIVSAA-GRILASKRSYkdGTFWDNFPALFllsqdanhSDSPEQ 159
Cdd:cd23424    74 ----SPQVGSIDGDGsydDQWFKFEPGKGD-FKGYFRLVNPAtDTVLFSRTTL--EPQFGNIPADQ--------PVFDDQ 138


                  ....*.
gi 2448922026 160 YFSFVF 165
Cdd:cd23424   139 YFSFLF 144
PFM_LSL-like cd20215
pore-forming module of Laetiporus sulphureus LSL lectin and similar aerolysin-type beta-barrel ...
 166-328 4.47e-35

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: 125.52  E-value: 4.47e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2448922026 166 EDTEIVKVVYNLSAGRVFNTKPEIFRT-TVRNNAQEKATLKCDFRREKSAKGSFTHSHGFSFGVKTEIKASIPFIVDGKI 244
Cdd:cd20215     1 EDMEIVSVEYDLDKGKILSSTPLVLARqTLRNDTDVEQTMSFTLTETETHTSTFEYTAGFTITVGTSFKAGIPGVAEGKI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2448922026 245 ETELKTDHKFTWGQEESWSKTLGTELGVEVPGYSTRDVVGTFKDSDMTVPAKIYSQTKSTGVEIITEVEYRGTSVWDFEY 324
Cdd:cd20215    81 KVDTTVSNEWKWGESTTFTKTYTATFPVKAPPGSTVRAVATVTKSNLEVPFTMTLKSKSTGYEVETKGIYRGVSTWNLRT 160


                  ....
gi 2448922026 325 TIDD 328
Cdd:cd20215   161 AIRE 164
PFM_HFR-2-like cd20216
pore-forming module of wheat HFR-2 toxin, FEM32, and similar aerolysin-type beta-barrel ...
 182-328 1.75e-13

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: 67.23  E-value: 1.75e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2448922026 182 VFNTKP-EIFRTTVRNNAQEKATLKCDFRREKSAKGSFTHSHGFSFGVKTEIKASIPFIVDGKIETELKTDHKFTWGQEE 260
Cdd:cd20216     1 IYDEKVlTLATGEATNNTSEPQTVTLKLSYTDTKTSTWNSSVSLKLGVKTTISAGVPFIVDGKIEISAEFSGSYEWGETK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2448922026 261 SWSKTLGTELGVEVPGYS--TRDVVGTFKDSDmtVPAKiYSQ--TKSTGVEIITEVE---YRGTSVWDFEYTIDD 328
Cdd:cd20216    81 TETTEVETTYTVTVPPMTkvTVTLIATRGSCD--VPFS-YTQrdTLTNGTTVTYEKDdglYTGVNSYNFKYETKE 152
PFM_aerolysin-like cd20239
pore-forming module of aerolysin-type beta-barrel pore-forming proteins; uncharacterized ...
 187-327 8.84e-13

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: 64.79  E-value: 8.84e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2448922026 187 PEI-FRTTVRNNAQEKATLKCDFRREKSAKGSFTHSHGFSFGVKTEIKASIPFIVDGKIETELKTDHKFTWGQEESWSKT 265
Cdd:cd20239     1 PTVaLSTVVRNDSDSPASQTLTYSYSKSEEGTWNNTAGIELGVKVTFKAGVPFVASGELEVSVSASYSHTWGGSTTVTKT 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2448922026 266 LGTELGVEVPGYSTRDVVGTFKDSDMTVPAKIYSQTKSTGVEIITEVE---YRGTSVWDFEYTID 327
Cdd:cd20239    81 VSSSTTVVVPPRKKGVASVLIRKAEIDVPFTYTERITYTGGRMEEEVKtgiYHNVDSYHVDVQLS 145
PFM_aerolysin-like cd20242
pore-forming module of aerolysin-type beta-barrel pore-forming proteins; uncharacterized ...
 188-322 7.19e-12

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: 62.44  E-value: 7.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2448922026 188 EIFRTTVRNNAQEKATLKCDFRREKSAKGSFTHSHGFSFGVKTEIKASIPFIVDGKIETELKTDHKFTWGQEESWSKTLG 267
Cdd:cd20242     3 SLYSQTVTNDTGQPQTPSISGSETVTETSTWEDEVGLKLGVSTSFSAGVPVVAEGKVEVSAEVHNNYTWNGSNTRSKTWS 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2448922026 268 TELGVEVPGYSTRDVVGTFKDSDMTVPakiYSQT------KSTGVEIITEVEYRGTSVWDF 322
Cdd:cd20242    83 FSTPVNVPAHSAVRATATVTESTISVP---YTLTwksifeSGARVTGTIEGMYKGSNSHDL 140
PFM_tachylectin-like cd20229
pore-forming module (PFM) of uncharacterized proteins having tachylectin domain(s), and ...
 187-294 1.10e-10

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: 59.08  E-value: 1.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2448922026 187 PEIFRTTVRNNAQEKATLKCDFRREKS--AKGSFTHSHGFSFGVKTEI--KASIPFIVDGKIETEL--KTDHKFTWGQEE 260
Cdd:cd20229     1 PEVVKQETYDNRRGTVPLNDTFTFSKTitEVSSFSHSHGFTVAEGAETtfKAGIPVIGEEGIKVILdnSTTHQWNFTTTN 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2448922026 261 SWSKTLGTELGVEVPGYSTRDVVGTFKDSDMTVP 294
Cdd:cd20229    81 EREVTFSLTTNVVVPPGKAVRLEASVQKAKIDVP 114
PFM_aerolysin-like cd20240
pore-forming module of aerolysin-type beta-barrel pore-forming proteins; uncharacterized ...
 188-326 3.00e-09

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: 54.96  E-value: 3.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2448922026 188 EIFRTTVRNNAQEKATLKCDFRREKSAKGSFTHSHGFSFGVKTEIKASIPFIVDGKIETELKTDHKFTWGQEESWSKTLG 267
Cdd:cd20240     7 FIVTWTYTNNTSIEQTMTTNFSETATETSSFSETEGVSTTVSTSLKVGIPFIAGGEITTTTTTSQSWTYGKSETKTDTIS 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2448922026 268 TELGVEVPGYSTRDVVGTFKDSDMTVPAKIYSQTKSTGVEIITEVEYRGTSVWDFEYTI 326
Cdd:cd20240    87 YTFPIVVPPNTTVTATAVVTKYNMDVTYVATLRGINTGKRIKIKGKWSGVDCTDISYNL 145
PFM_natterin-3-like cd20220
pore-forming module of Thalassophryne nattereri fish venom natterins 1-4, and similar ...
 182-306 1.46e-06

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: 47.24  E-value: 1.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2448922026 182 VFNTKPEI-FRTTVRNN----AQEKATLKCDFRREKSAKGSFTHSHGfsfgVKTEIKASIPFIVDGKIETELKTDhkFTW 256
Cdd:cd20220     1 IESYPPETlKESTVTNNgckpVKKTVTLSKTTEVEHRWDTSFSITLG----VSTTITAGIPIIAGGGWEVSTETT--FTW 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2448922026 257 GQEESWSKTLGTELGVEV---PGYS-TRDVVGtfKDSDMTVP-----AKIYS--QTKSTGV 306
Cdd:cd20220    75 SGGTSVTESVTHSVSVEVtvpPNHScTVKMVG--YKYKADIPftarlTRTYRngETHTTTI 133
PFM_LIN24-like cd20237
pore-forming module of Caenorhabditis elegans LIN-24 and similar aerolysin-type beta-barrel ...
 189-313 4.34e-06

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: 45.26  E-value: 4.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2448922026 189 IFRTTVRNNAQEKATLKcdFRREKSAKGSFTHS--HGFSFGVKTEIKASIPFIVdGKIETELKTDHKFTWGQEESWSKTL 266
Cdd:cd20237     5 LFKTTFTNNTSTEQEYT--FKTERTTTSSCTWSvtEGFTIGGEVSLKLGPPPDI-AEANAGFSRELSLSKTQEETFEEEL 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2448922026 267 GTELgvevpgystrdvvgtfkDSDMTVPAKiySQTKSTGVeiITEVE 313
Cdd:cd20237    82 TWSV-----------------DSQVTVPPK--TKVTAELV--ITEDE 107
PFM_epsilon-toxin-like cd20223
pore-forming module of Clostridium perfringens epsilon-toxin and similar aerolysin-type ...
 189-314 4.73e-04

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: 39.91  E-value: 4.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2448922026 189 IFRTTVRNNAQEKATLKCD-FRREKSAKGSFTHSHGFSFGVKTEIKASIPFIVDGKIETELktdhKFTWGQEESWSKTLG 267
Cdd:cd20223    17 VGSNTLTNDTDEEQTLKTPsFSKTVTDTVTTTTTNGFKLGVSTSAKFKIPFPGGGSTELSA----EYNFSTTNTNTTSET 92

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2448922026 268 TEL-----GVEVPGYSTRDVVGTFKdsDMTVPAKIYSQTKSTGVEIITEVEY 314
Cdd:cd20223    93 KTYtapsqTIKVPPGKTYKVTVYLK--KVKFSGTVGTFTGVYGTDFTVKVKD 142
ETX_MTX2 pfam03318
Clostridium epsilon toxin ETX/Bacillus mosquitocidal toxin MTX2; This family appears to be ...
 184-300 6.52e-04

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: 40.47  E-value: 6.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2448922026 184 NTKPEIF--RTTVRNNAQEKATLKCD-FRREKSAKGSFTHSHGFSFGVKTEIKASIPFIVDGKIETELKTDHKFTWGQEE 260
Cdd:pfam03318  24 KTLTPLYtgSNTLTNNTDSTQTLQTQsFSKKVTTTTSTTTTHGFKIGAKASGKFGIPFVAEGGITLSVSGEYNFSSTTTN 103

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2448922026 261 SWSKT-LGTELG--VEVPGYSTRDVVGTFKDSDMTVPAKIYSQ 300
Cdd:pfam03318 104 TTSVTtTYWVPSqkVTVPPHTTVRVTLVLYKTTYSVPVDLYTT 146
PFM_jacalin-like cd20231
pore-forming module of uncharacterized proteins which have an N-terminal jacalin-like lectin ...
 196-276 1.36e-03

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: 38.49  E-value: 1.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2448922026 196 NNAQEKATLKCDFRREKSAKGSFTHSHGFSFGVKTEIKASIPFIVDGkieTELKTDHKFTWGQEESWSKTLGTELGVEVP 275
Cdd:cd20231    15 NSTDYTWTFSGSRTKTTSRTWSQSSTSGFELSVSVSVSAGIPEIGEA---VTTSAGWSLSATSSESETETTTDELGWSVS 91


                  .
gi 2448922026 276 G 276
Cdd:cd20231    92 G 92
PFM_ABFB-like cd20238
pore-forming module (PFM) of uncharacterized proteins which have an N-terminal ABFB ...
 217-279 1.56e-03

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).


Pssm-ID: 380808 [Multi-domain]  Cd Length: 146  Bit Score: 38.36  E-value: 1.56e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2448922026 217 SFTHSHGF--SFGVKTEIKASIPFI-VDGKIETELKTDHKFTWGQEESWSKTLGTELGVEVPGYST 279
Cdd:cd20238    33 SYERTDGFelTIGESYTVKASAIIVdEEGQIFFESKTIRNVTYGNQNTTTKTFAYETPLIVPGFST 98
PFM_aerolysin_family cd10140
pore-forming module of aerolysin-type beta-barrel pore-forming proteins; Pore-forming proteins ...
 263-325 2.21e-03

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: 36.76  E-value: 2.21e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2448922026 263 SKTLGTELGVEVPGYSTRDVVGTFKDSDMTVPA----KIYSQTKSTGVEIITEVEYRGTSVWDFEYT 325
Cdd:cd10140    26 TKTVSVTVTVTVPPGKTVKVTVTVTKAKIDVPYtatlKATYSTSGTGTTGTVSGVFTGVNYANVETT 92
PFM_parasporin-2-like cd20222
pore-forming module of parasporin-2, hydralysin and similar aerolysin-type beta-barrel ...
 183-292 8.64e-03

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: 36.15  E-value: 8.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2448922026 183 FNTKPEIFRTTVRNNAQEKATlkcDFRREKSAKGSFTHSHGFSFGVKT--EIKASIPFIVDGKIETELKTDHKFTWGQEE 260
Cdd:cd20222    11 PPTPDILGTTEAVNNGDEEEI---TVTYSYKVGGKWTWKTSWSSSSTTgaTFSSGIPLEGVFEVGTEFSVSGTTGESGST 87

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2448922026 261 SWSKTLGTELGVEVPGYSTR--DVVGTFKDSDMT 292
Cdd:cd20222    88 STEKTLTSSVTVKVPPNSKVkiTMVTKMKKSSVN 121
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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