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Conserved domains on  [gi|418713878|gb|AFX65772|]
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Hfr-2-like protein, partial [Senecio aethnensis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PFM_HFR-2-like cd20216
pore-forming module of wheat HFR-2 toxin, FEM32, and similar aerolysin-type beta-barrel ...
 219-345 4.95e-48

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: 158.91  E-value: 4.95e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 418713878 219 IYNERIIEVDHSYGDNNTSEANTMNLRFSQNNTKTRSWTNSISVKFGVTASLEVNlVPAIVSGAIELSAEYGSTHEWGEE 298
Cdd:cd20216    1 IYDEKVLTLATGEATNNTSEPQTVTLKLSYTDTKTSTWNSSVSLKLGVKTTISAG-VPFIVDGKIEISAEFSGSYEWGET 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 418713878 299 ESTETIREANYTITIPPFSKMKVSMMCKRGHCDVPFSYTQRDLQTSG 345
Cdd:cd20216   80 KTETTEVETTYTVTVPPMTKVTVTLIATRGSCDVPFSYTQRDTLTNG 126
Agglutinin super family cl06484
Agglutinin domain;
6-123 3.57e-11

Agglutinin domain;


The actual alignment was detected with superfamily member pfam07468:

Pssm-ID: 141938  Cd Length: 141  Bit Score: 60.41  E-value: 3.57e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 418713878    6 LPSFFVLQSG--GKYLSVtdnISSNlPSGFLKFGDEPIWSPRVKFAVEQTNtdeDRFVHIRSCYNNKYLVMNqidSNSWI 83
Cdd:pfam07468   3 FPKIYVTFKGnnGKYLGV---ITIN-QLPCLQFGYDNLNDPKVAHQMFVTS---NGTICIKSNYMNKFWRLS---TDNWI 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 418713878   84 VASAKklEEDDSKDSCTLFEPyslEDDETTNVRLRPVQLT 123
Cdd:pfam07468  73 LVDGN--DPRETNEAAALFRS---DVHDFNVISLLNMQKT 107
 
Name Accession Description Interval E-value
PFM_HFR-2-like cd20216
pore-forming module of wheat HFR-2 toxin, FEM32, and similar aerolysin-type beta-barrel ...
 219-345 4.95e-48

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: 158.91  E-value: 4.95e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 418713878 219 IYNERIIEVDHSYGDNNTSEANTMNLRFSQNNTKTRSWTNSISVKFGVTASLEVNlVPAIVSGAIELSAEYGSTHEWGEE 298
Cdd:cd20216    1 IYDEKVLTLATGEATNNTSEPQTVTLKLSYTDTKTSTWNSSVSLKLGVKTTISAG-VPFIVDGKIEISAEFSGSYEWGET 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 418713878 299 ESTETIREANYTITIPPFSKMKVSMMCKRGHCDVPFSYTQRDLQTSG 345
Cdd:cd20216   80 KTETTEVETTYTVTVPPMTKVTVTLIATRGSCDVPFSYTQRDTLTNG 126
Agglutinin pfam07468
Agglutinin domain;
6-123 3.57e-11

Agglutinin domain;


Pssm-ID: 116089  Cd Length: 141  Bit Score: 60.41  E-value: 3.57e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 418713878    6 LPSFFVLQSG--GKYLSVtdnISSNlPSGFLKFGDEPIWSPRVKFAVEQTNtdeDRFVHIRSCYNNKYLVMNqidSNSWI 83
Cdd:pfam07468   3 FPKIYVTFKGnnGKYLGV---ITIN-QLPCLQFGYDNLNDPKVAHQMFVTS---NGTICIKSNYMNKFWRLS---TDNWI 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 418713878   84 VASAKklEEDDSKDSCTLFEPyslEDDETTNVRLRPVQLT 123
Cdd:pfam07468  73 LVDGN--DPRETNEAAALFRS---DVHDFNVISLLNMQKT 107
Agglutinin smart00791
Amaranthus caudatus agglutinin or amaranthin is a lectin from the ancient South American crop, ...
 4-123 4.46e-08

Amaranthus caudatus agglutinin or amaranthin is a lectin from the ancient South American crop, amaranth grain; Although its biological function is unknown, it has a high binding specificity for the methyl-glycoside of the T-antigen, found linked to serine or threonine residues of cell surface glycoproteins. The protein is comprised of a homodimer, with each homodimer consisting of two beta-trefoil domains.


Pssm-ID: 129027  Cd Length: 139  Bit Score: 51.45  E-value: 4.46e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 418713878     4 ALLPSFFVLQSG--GKYLSVtdnISSNlPSGFLKFGDEPIWSPRVKFAVEQTNtdeDRFVHIRSCYNNKYLVMNqidsNS 81
Cdd:smart00791   1 AGLPKIYVLFKGnnQKYLRY---QSIQ-QYGLLQFSADKILDPLVQFEVFPTY---NGLVHIKSNYTNKFWRLS----HY 69

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 418713878    82 WIVASAKklEEDDSKDSCTLFEPYSLEDDEttnVRLRPVQLT 123
Cdd:smart00791  70 WITADAN--DPDENKSACTLFRPLYVEMKK---IRLLNVQLG 106
Aerolysin pfam01117
Aerolysin toxin; This family represents the pore forming lobe of aerolysin.
 231-337 5.39e-05

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


Pssm-ID: 366474  Cd Length: 359  Bit Score: 44.55  E-value: 5.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 418713878  231 YGDNNTSEANTMNLRFSQnntkTRSWTNSISVKFGVTASLEVNLVPAIVsGAIELSAEYGSTHEWGEEE--STETIREAN 308
Cdd:pfam01117 110 RNDSDTPQQRVLTLSYDE----VTNWSKTDTYKYSEKVTIKNKYKFPLI-GETELSLELGANQSWATTNgnSSTKTISDV 184

                          90       100
                  ....*....|....*....|....*....
gi 418713878  309 YTITIPPFSKMKVSMMCKRGHCDVPFSYT 337
Cdd:pfam01117 185 ARVLVPANTKIPVRLKLEKARVDYPYEFN 213
Aerolysin smart00999
Aerolysin toxin; This family represents the pore forming lobe of aerolysin.
 204-334 1.25e-04

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


Pssm-ID: 198067  Cd Length: 368  Bit Score: 43.34  E-value: 1.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 418713878   204 KRKLLDLDYRLNDSRIYNERIIEVD-----------HSYGDNNTSEANTMNLRFSQNNTKTRSWtnSISVKFGVTASLEV 272
Cdd:smart00999  74 KITLSNFAYNLNPKSFKLGDVTVSDrelvktvtavaYNDGDTPDTIVVTLRYDETTSWSKTDTY--SFSEKVTTKNKFEW 151

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 418713878   273 NLVpaivsGAIELSAEYGSTHEWGEEE--STETIREANYTITIPPFSKMKVSMMCKRGHCDVPF 334
Cdd:smart00999 152 PLI-----GSTEISAEFDANQGWSESNggSTTTSLSAQYRATMPARSKRPIKIELYKQKIDYPY 210
 
Name Accession Description Interval E-value
PFM_HFR-2-like cd20216
pore-forming module of wheat HFR-2 toxin, FEM32, and similar aerolysin-type beta-barrel ...
 219-345 4.95e-48

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: 158.91  E-value: 4.95e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 418713878 219 IYNERIIEVDHSYGDNNTSEANTMNLRFSQNNTKTRSWTNSISVKFGVTASLEVNlVPAIVSGAIELSAEYGSTHEWGEE 298
Cdd:cd20216    1 IYDEKVLTLATGEATNNTSEPQTVTLKLSYTDTKTSTWNSSVSLKLGVKTTISAG-VPFIVDGKIEISAEFSGSYEWGET 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 418713878 299 ESTETIREANYTITIPPFSKMKVSMMCKRGHCDVPFSYTQRDLQTSG 345
Cdd:cd20216   80 KTETTEVETTYTVTVPPMTKVTVTLIATRGSCDVPFSYTQRDTLTNG 126
PFM_aerolysin-like cd20239
pore-forming module of aerolysin-type beta-barrel pore-forming proteins; uncharacterized ...
 234-345 1.23e-16

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: 75.96  E-value: 1.23e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 418713878 234 NNTSEANTMNLRFSQNNTKTRSWTNSISVKFGVTASLEVNlVPAIVSGAIELSAEYGSTHEWGEEESTETIREANYTITI 313
Cdd:cd20239   11 NDSDSPASQTLTYSYSKSEEGTWNNTAGIELGVKVTFKAG-VPFVASGELEVSVSASYSHTWGGSTTVTKTVSSSTTVVV 89

                         90       100       110
                 ....*....|....*....|....*....|..
gi 418713878 314 PPFSKMKVSMMCKRGHCDVPFSYTQRDLQTSG 345
Cdd:cd20239   90 PPRKKGVASVLIRKAEIDVPFTYTERITYTGG 121
PFM_agglutinin-like cd20217
pore-forming module (PFM) of uncharacterized proteins which have agglutatin domain(s), and ...
 225-345 1.37e-16

pore-forming module (PFM) of uncharacterized proteins which have agglutatin domain(s), and similar aerolysin-type beta-barrel pore-forming proteins; Most proteins belonging to this group have an N-terminal agglutatin (also known as amaranthin) lectin domain; some have fascin-like domains which adopt a beta-trefoil topology. Members of this group belong to the aerolysin family of beta-pore-forming proteins (beta-PFPs). PFPs are generally secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores harmful to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel, are found in all kingdoms of life and many are bacterial toxins. In addition to having a role in microbial infection, they have potential as biotechnological sensors and delivery systems. They share a similar monomeric architecture, with a variable membrane-binding domain and a structurally conserved pore-forming region. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin).


Pssm-ID: 380787 [Multi-domain]  Cd Length: 150  Bit Score: 75.62  E-value: 1.37e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 418713878 225 IEVDHSYGDNNTSEANTMNLR--FSQNNTKTRSWTNSISVKFGVTASLEVNlVPAI--VSGAIELSAEYGSTHEWGEEES 300
Cdd:cd20217    2 LVVGQGSATNNGSEPADMQVQvtLTETVSTSRTWSNSFTFSQSISTTFTAG-VPEIasAETTITIGAEQTFGTEWGETTE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 418713878 301 TETIREANYTIT-IPPFSKMKVSMMCKRGHCDVPFSYTQRDLQTSG 345
Cdd:cd20217   81 EAVQFQSTYLVKdVPPGEEATVTVECSTGKCRVPFTYKTRDTRLDG 126
PFM_aerolysin-like cd20240
pore-forming module of aerolysin-type beta-barrel pore-forming proteins; uncharacterized ...
 233-347 7.20e-14

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: 68.06  E-value: 7.20e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 418713878 233 DNNTSEANTMNLRFSQNNTKTRSWTNSISVKFGVTASLEVNlVPAIVSGAIELSAEYGSTHEWGEEESTETIREANYTIT 312
Cdd:cd20240   14 TNNTSIEQTMTTNFSETATETSSFSETEGVSTTVSTSLKVG-IPFIAGGEITTTTTTSQSWTYGKSETKTDTISYTFPIV 92

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 418713878 313 IPPFSKMKVSMMCKRGHCDVPFSYTQRDLQT------SGSW 347
Cdd:cd20240   93 VPPNTTVTATAVVTKYNMDVTYVATLRGINTgkrikiKGKW 133
Agglutinin pfam07468
Agglutinin domain;
6-123 3.57e-11

Agglutinin domain;


Pssm-ID: 116089  Cd Length: 141  Bit Score: 60.41  E-value: 3.57e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 418713878    6 LPSFFVLQSG--GKYLSVtdnISSNlPSGFLKFGDEPIWSPRVKFAVEQTNtdeDRFVHIRSCYNNKYLVMNqidSNSWI 83
Cdd:pfam07468   3 FPKIYVTFKGnnGKYLGV---ITIN-QLPCLQFGYDNLNDPKVAHQMFVTS---NGTICIKSNYMNKFWRLS---TDNWI 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 418713878   84 VASAKklEEDDSKDSCTLFEPyslEDDETTNVRLRPVQLT 123
Cdd:pfam07468  73 LVDGN--DPRETNEAAALFRS---DVHDFNVISLLNMQKT 107
PFM_natterin-3-like cd20220
pore-forming module of Thalassophryne nattereri fish venom natterins 1-4, and similar ...
 234-335 7.73e-11

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: 59.56  E-value: 7.73e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 418713878 234 NNTSEANTMNLRFSQNNTKTRSWTNSISVKFGVTASLEVNlVPAIVSGAIELSAEYgsTHEWGEEES-TETI-REANYTI 311
Cdd:cd20220   16 NNGCKPVKKTVTLSKTTEVEHRWDTSFSITLGVSTTITAG-IPIIAGGGWEVSTET--TFTWSGGTSvTESVtHSVSVEV 92

                         90       100
                 ....*....|....*....|....
gi 418713878 312 TIPPFSKMKVSMMCKRGHCDVPFS 335
Cdd:cd20220   93 TVPPNHSCTVKMVGYKYKADIPFT 116
PFM_alpha-toxin-like cd20224
pore-forming module of Clostridium septicum alpha-toxin and similar aerolysin-type beta-barrel ...
 231-324 5.42e-09

pore-forming module of Clostridium septicum alpha-toxin and similar aerolysin-type beta-barrel pore-forming proteins; Clostridium septicum alpha-toxin is the main virulence factor of this bacterium, known for causing non-traumatic gas gangrene. Members of this family belong to the aerolysin family of beta-pore-forming proteins (beta-PFPs). PFPs are generally secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores harmful to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel, are found in all kingdoms of life and many are bacterial toxins. In addition to having a role in microbial infection, they have potential as biotechnological sensors and delivery systems. They share a similar monomeric architecture, with a variable membrane-binding domain and a structurally conserved pore-forming region. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin).


Pssm-ID: 380794  Cd Length: 121  Bit Score: 53.53  E-value: 5.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 418713878 231 YGDNNTSEANTMNLRFSQNNTKTRSWTNSISVKFGVTASLEVNLvPAIVSGAIELSAEYGSTHEWGEEES-TETI-REAN 308
Cdd:cd20224   10 ENHGNTEDTGTATFNYTESTSWSKTDNFKFSEGIKVTVKFTVGI-PLIGGAESETEFSFNAEQGWSDSTGnTETIqQSAQ 88

                         90
                 ....*....|....*.
gi 418713878 309 YTITIPPFSKMKVSMM 324
Cdd:cd20224   89 YTATVPPRSKRTITLT 104
PFM_aerolysin-like cd20242
pore-forming module of aerolysin-type beta-barrel pore-forming proteins; uncharacterized ...
 234-346 9.06e-09

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: 53.58  E-value: 9.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 418713878 234 NNTSEANTMNLRFSQNNTKTRSWTNSISVKFGVTASLEVNlVPAIVSGAIELSAEYGSTHEWGEEESTETIREANYTITI 313
Cdd:cd20242   11 NDTGQPQTPSISGSETVTETSTWEDEVGLKLGVSTSFSAG-VPVVAEGKVEVSAEVHNNYTWNGSNTRSKTWSFSTPVNV 89

                         90       100       110
                 ....*....|....*....|....*....|...
gi 418713878 314 PPFSKMKVSMMCKRGHCDVPFSYTQRDLQTSGS 346
Cdd:cd20242   90 PAHSAVRATATVTESTISVPYTLTWKSIFESGA 122
PFM_LIN24-like cd20237
pore-forming module of Caenorhabditis elegans LIN-24 and similar aerolysin-type beta-barrel ...
 233-324 2.47e-08

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: 51.81  E-value: 2.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 418713878 233 DNNTSEANTMNLRFSQNNTKTRSWTNSISVKFGVTASLEVNLVPAIVSGAIELSAEYG--STHEWGEEESTETirEANYT 310
Cdd:cd20237   11 TNNTSTEQEYTFKTERTTTSSCTWSVTEGFTIGGEVSLKLGPPPDIAEANAGFSRELSlsKTQEETFEEELTW--SVDSQ 88

                         90
                 ....*....|....
gi 418713878 311 ITIPPFSKMKVSMM 324
Cdd:cd20237   89 VTVPPKTKVTAELV 102
PFM_aerolysin-like cd20241
pore-forming module of aerolysin-type beta-barrel pore-forming proteins; uncharacterized ...
 234-333 2.87e-08

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: 52.10  E-value: 2.87e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 418713878 234 NNTSEANTMNLRFSQNNTKTRSWTNSISVKFGVTASLEVNlVPAIVSGAIELSAEYGSTHEWGEEESTETIREANYTITI 313
Cdd:cd20241   10 NNGNTPATLKANMSRSVSETGSFSFTHGFSIGVGTTIKAG-IPFIVEGEIETELSTSHDFTWGKSTTVTTTVGSSVTVEV 88

                         90       100
                 ....*....|....*....|
gi 418713878 314 PPFSKMKVSMMCKRGHCDVP 333
Cdd:cd20241   89 PPRSTQTVVGTFKRSKMTVP 108
Agglutinin smart00791
Amaranthus caudatus agglutinin or amaranthin is a lectin from the ancient South American crop, ...
 4-123 4.46e-08

Amaranthus caudatus agglutinin or amaranthin is a lectin from the ancient South American crop, amaranth grain; Although its biological function is unknown, it has a high binding specificity for the methyl-glycoside of the T-antigen, found linked to serine or threonine residues of cell surface glycoproteins. The protein is comprised of a homodimer, with each homodimer consisting of two beta-trefoil domains.


Pssm-ID: 129027  Cd Length: 139  Bit Score: 51.45  E-value: 4.46e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 418713878     4 ALLPSFFVLQSG--GKYLSVtdnISSNlPSGFLKFGDEPIWSPRVKFAVEQTNtdeDRFVHIRSCYNNKYLVMNqidsNS 81
Cdd:smart00791   1 AGLPKIYVLFKGnnQKYLRY---QSIQ-QYGLLQFSADKILDPLVQFEVFPTY---NGLVHIKSNYTNKFWRLS----HY 69

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 418713878    82 WIVASAKklEEDDSKDSCTLFEPYSLEDDEttnVRLRPVQLT 123
Cdd:smart00791  70 WITADAN--DPDENKSACTLFRPLYVEMKK---IRLLNVQLG 106
PFM_epsilon-toxin-like cd20223
pore-forming module of Clostridium perfringens epsilon-toxin and similar aerolysin-type ...
 221-317 1.14e-07

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: 50.31  E-value: 1.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 418713878 221 NERIIEVDHSYGDNNTSEANTMNLR-FSQNNTKTRSWTNSISVKFGVTASLEVNlVPAIVSGAIELSAEYGSTHEWGEEE 299
Cdd:cd20223   11 NGEPLYVGSNTLTNDTDEEQTLKTPsFSKTVTDTVTTTTTNGFKLGVSTSAKFK-IPFPGGGSTELSAEYNFSTTNTNTT 89

                         90
                 ....*....|....*...
gi 418713878 300 STETireanyTITIPPFS 317
Cdd:cd20223   90 SETK------TYTAPSQT 101
PFM_jacalin-like cd20231
pore-forming module of uncharacterized proteins which have an N-terminal jacalin-like lectin ...
 230-339 1.24e-07

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: 50.43  E-value: 1.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 418713878 230 SYGDNNTSEANTMNLRFSQNNTKTRSWTNSISVKFGVTASLEVNL-VPAIVSgAIELSAEYGSTHEWGEEESTETIREAN 308
Cdd:cd20231    9 SFLPTNNSTDYTWTFSGSRTKTTSRTWSQSSTSGFELSVSVSVSAgIPEIGE-AVTTSAGWSLSATSSESETETTTDELG 87

                         90       100       110
                 ....*....|....*....|....*....|...
gi 418713878 309 YTI--TIPPFSKMKVSMMCKRGHCDVPFSYTQR 339
Cdd:cd20231   88 WSVsgTLPPGEGVKCRATAQEGKLDSDYTSTVT 120
PFM_LSL-like cd20215
pore-forming module of Laetiporus sulphureus LSL lectin and similar aerolysin-type beta-barrel ...
 209-347 1.66e-06

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: 47.32  E-value: 1.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 418713878 209 DLDYRLNDSRIYNERIIEVDHSYGDNNTSEANTMNLRFSQNNTKTRS--WTNSISVKFGVTASLEVnlvPAIVSGAIELS 286
Cdd:cd20215    7 SVEYDLDKGKILSSTPLVLARQTLRNDTDVEQTMSFTLTETETHTSTfeYTAGFTITVGTSFKAGI---PGVAEGKIKVD 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 418713878 287 AEYGSTHEWGEEESTETIREANYTITIPPFSKMKVSMMCKRGHCDVPFSYTQR------DLQTSGSW 347
Cdd:cd20215   84 TTVSNEWKWGESTTFTKTYTATFPVKAPPGSTVRAVATVTKSNLEVPFTMTLKskstgyEVETKGIY 150
PFM_Dln1-like cd20221
pore-forming module of Danio rerio Dln1, and similar aerolysin-type beta-barrel pore-forming ...
 234-337 4.18e-06

pore-forming module of Danio rerio Dln1, and similar aerolysin-type beta-barrel pore-forming proteins; Since Danio rerio Dln1 has a specific affinity towards high-mannose glycans, which are common on the surface of virus and fungi, it has been suggested that it may play a defense role. Members of this group also include lamprey immune protein (LIP), a defense molecule derived from lamprey supraneural body tissue which has efficient cytocidal actions against tumor cells. Many proteins belonging to this group have a N-terminal Jacalin-like lectin domain. They belong to the aerolysin family of beta-pore-forming proteins (beta-PFPs). PFPs are generally secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores harmful to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel, are found in all kingdoms of life and many are bacterial toxins. In addition to having a role in microbial infection, they have potential as biotechnological sensors and delivery systems. They share a similar monomeric architecture, with a variable membrane-binding domain and a structurally conserved pore-forming region. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin).


Pssm-ID: 380791 [Multi-domain]  Cd Length: 168  Bit Score: 46.21  E-value: 4.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 418713878 234 NNTSEANTMNLRFSQNNTKTRSWtnSISVKFGVTASLEVNL-VPAIVSGAIELSAEYGSTHEWGEEESTETIREANYTIT 312
Cdd:cd20221   32 NDTSVPQEYTIETSKKITKTSSW--SVTNKLESTFSVEVSAgIPEVVEVSTGFSLTVGVESTHSLENTEEKTETLSFPVK 109

                         90       100
                 ....*....|....*....|....*
gi 418713878 313 IPPFSKMKVSMMCKRGHCDVPFSYT 337
Cdd:cd20221  110 VPPGKTVDVEITIGRATVDLPYTGT 134
PFM_parasporin-2-like cd20222
pore-forming module of parasporin-2, hydralysin and similar aerolysin-type beta-barrel ...
 212-326 8.16e-06

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: 45.01  E-value: 8.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 418713878 212 YRLNDSRIYNERIIEVDHSYGDNNTSEAN-TMNLRFSQNNTKTRSWTNSisVKFGVTASLEVNLVpaivsGAIELSAEY- 289
Cdd:cd20222    4 VVVREEGPPTPDILGTTEAVNNGDEEEITvTYSYKVGGKWTWKTSWSSS--STTGATFSSGIPLE-----GVFEVGTEFs 76

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 418713878 290 -GSTHEWGEEESTETIREANYTITIPPFSKMKVSMMCK 326
Cdd:cd20222   77 vSGTTGESGSTSTEKTLTSSVTVKVPPNSKVKITMVTK 114
Aerolysin pfam01117
Aerolysin toxin; This family represents the pore forming lobe of aerolysin.
 231-337 5.39e-05

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


Pssm-ID: 366474  Cd Length: 359  Bit Score: 44.55  E-value: 5.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 418713878  231 YGDNNTSEANTMNLRFSQnntkTRSWTNSISVKFGVTASLEVNLVPAIVsGAIELSAEYGSTHEWGEEE--STETIREAN 308
Cdd:pfam01117 110 RNDSDTPQQRVLTLSYDE----VTNWSKTDTYKYSEKVTIKNKYKFPLI-GETELSLELGANQSWATTNgnSSTKTISDV 184

                          90       100
                  ....*....|....*....|....*....
gi 418713878  309 YTITIPPFSKMKVSMMCKRGHCDVPFSYT 337
Cdd:pfam01117 185 ARVLVPANTKIPVRLKLEKARVDYPYEFN 213
PFM_spherulin-2a-like cd20235
pore-forming module of Physarum polycephalum spherulin-2a, Plodia interpunctella follicular ...
 233-337 5.89e-05

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).


Pssm-ID: 380805  Cd Length: 150  Bit Score: 42.59  E-value: 5.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 418713878 233 DNNTSEANTMNLRFSQN--NTKTRSWTNSISVKFGVTASLEVNLVPAIVSGaielSAEYGSTHEWGEE-ESTETIR---E 306
Cdd:cd20235   10 VNNSSKPATFNAGISQSveNTVSSTWSKSGEVSVGQSINYGVNFLGSGGGG----ETSFSYTSSWGEStTKSETVTvgsT 85

                         90       100       110
                 ....*....|....*....|....*....|.
gi 418713878 307 ANYTITIPPFSKMKVSMMCKRGHCDVPFSYT 337
Cdd:cd20235   86 SGVEVTLEPGQAVTAELTATKGTMKVEVTYE 116
PFM_crystallin-like cd20232
pore-forming module (PFM) of uncharacterized proteins which have N-terminal crystallin domain ...
 233-323 9.51e-05

pore-forming module (PFM) of uncharacterized proteins which have N-terminal crystallin domain(s), and similar aerolysin-type beta-barrel pore-forming proteins; Many proteins belonging to this group have N-terminal crystallin (beta/gamma crystallins) domain(s). Members of this group belong to the aerolysin family of beta-pore-forming proteins (beta-PFPs). PFPs are generally secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores harmful to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel, are found in all kingdoms of life and many are bacterial toxins. In addition to having a role in microbial infection, they have potential as biotechnological sensors and delivery systems. They share a similar monomeric architecture, with a variable membrane-binding domain and a structurally conserved pore-forming region. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin).


Pssm-ID: 380802 [Multi-domain]  Cd Length: 151  Bit Score: 42.17  E-value: 9.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 418713878 233 DNNTSEANTMNLRFSQNNTKTRSWTNS--ISVKFGVTASLEVNLVPaiVSGAIE--LSAEYGSTHEWGEEES-TETIR-E 306
Cdd:cd20232   12 GSDIEQVATLTLERELSKSTTRSFSEStlIGIEVSTTASVGVSAGP--VSAEVEqtVTSTLENTFTIGKEETkSETITfS 89

                         90
                 ....*....|....*..
gi 418713878 307 ANYTITIPPFSKMKVSM 323
Cdd:cd20232   90 KSVNVTIPPGNIGEAVM 106
Aerolysin smart00999
Aerolysin toxin; This family represents the pore forming lobe of aerolysin.
 204-334 1.25e-04

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


Pssm-ID: 198067  Cd Length: 368  Bit Score: 43.34  E-value: 1.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 418713878   204 KRKLLDLDYRLNDSRIYNERIIEVD-----------HSYGDNNTSEANTMNLRFSQNNTKTRSWtnSISVKFGVTASLEV 272
Cdd:smart00999  74 KITLSNFAYNLNPKSFKLGDVTVSDrelvktvtavaYNDGDTPDTIVVTLRYDETTSWSKTDTY--SFSEKVTTKNKFEW 151

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 418713878   273 NLVpaivsGAIELSAEYGSTHEWGEEE--STETIREANYTITIPPFSKMKVSMMCKRGHCDVPF 334
Cdd:smart00999 152 PLI-----GSTEISAEFDANQGWSESNggSTTTSLSAQYRATMPARSKRPIKIELYKQKIDYPY 210
PFM_Cry51Aa-like cd20226
pore-forming module of Bacillus thuringiensis insecticidal Cry51A toxin, Bacillus ...
 233-337 2.01e-04

pore-forming module of Bacillus thuringiensis insecticidal Cry51A toxin, Bacillus thuringiensis cytotoxic parasporin-5 and similar aerolysin-type beta-barrel pore-forming proteins; Bacillus thuringiensis parasporin-5 has strong cytocidal activity against several types of cancer cells and may or may not have insecticidal activity. Cry51A toxin is toxic to coleopteran (beetle) larvae. Other members of this family include Bacillus thuringiensis Cry15Aa which is toxic to lepidopteran (butterflies and moth) larvae. They belong to the aerolysin family of beta-pore-forming proteins (beta-PFPs). PFPs are generally secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores harmful to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel, are found in all kingdoms of life and many are bacterial toxins. In addition to having a role in microbial infection, they have potential as biotechnological sensors and delivery systems. They share a similar monomeric architecture, with a variable membrane-binding domain and a structurally conserved pore-forming region. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin).


Pssm-ID: 380796 [Multi-domain]  Cd Length: 172  Bit Score: 41.49  E-value: 2.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 418713878 233 DNNTSEANTMNLRFSQNNTKTRS------WTNSISVKFGVTASLEVNLVPAIVSG-AIELSAEYGSTHEWGEEESTETIR 305
Cdd:cd20226   30 TNNTSVPQSQTVSFSEKTTETTSttttegYKIGTSIKSTTKFKVKFGFVVGGEQSiEVSVSFEYNYSTTTTYTTTTEKLW 109

                         90       100       110
                 ....*....|....*....|....*....|..
gi 418713878 306 EANYTITIPPFSKMKVSMMCKRGHCDVPFSYT 337
Cdd:cd20226  110 EDTQPVTVPPRTKVTATLIIYGGPFNVPVTLN 141
ETX_MTX2 pfam03318
Clostridium epsilon toxin ETX/Bacillus mosquitocidal toxin MTX2; This family appears to be ...
 215-328 1.97e-03

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: 38.92  E-value: 1.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 418713878  215 NDSRIYNERIIeVDHSYGDNNTSEANTMN-LRFSQNNTKTRSWTNSISVKFGVTASLEVNLvPAIVSGAIELS--AEYGS 291
Cdd:pfam03318  20 ETTVKTLTPLY-TGSNTLTNNTDSTQTLQtQSFSKKVTTTTSTTTTHGFKIGAKASGKFGI-PFVAEGGITLSvsGEYNF 97

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 418713878  292 THEWGEEESTETireaNYT-----ITIPPFSKMKVSMMCKRG 328
Cdd:pfam03318  98 SSTTTNTTSVTT----TYWvpsqkVTVPPHTTVRVTLVLYKT 135
PFM_aerolysin_family cd10140
pore-forming module of aerolysin-type beta-barrel pore-forming proteins; Pore-forming proteins ...
 300-347 2.28e-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: 2.28e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 418713878 300 STETIREANYTITIPPFSKMKVSMMCKRGHCDVPFSYTQRDLQTSGSW 347
Cdd:cd10140   24 SETKTVSVTVTVTVPPGKTVKVTVTVTKAKIDVPYTATLKATYSTSGT 71
 
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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