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Conserved domains on  [gi|1005574734|ref|WP_061667036|]
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MULTISPECIES: hypothetical protein [Bacillus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PFM_parasporin-2-like cd20222
pore-forming module of parasporin-2, hydralysin and similar aerolysin-type beta-barrel ...
 66-245 9.32e-35

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: 121.67  E-value: 9.32e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005574734  66 PFIFRDLEKPSIDEITLKEQFVCNPNN---EEKEIVVTIKEQWANIQSWTSKSITGLTLKSDLIIAGKFQSGNEFNISTF 142
Cdd:cd20222     1 PPQVVVREEGPPTPDILGTTEAVNNGDeeeITVTYSYKVGGKWTWKTSWSSSSTTGATFSSGIPLEGVFEVGTEFSVSGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005574734 143 VGESTSKSIHTSPSIEHSIKVPPNTKMKIAMIGTLITEVLHFQSiitvqgmfgacfprmvrghyvgfksaghilnktfgm 222
Cdd:cd20222    81 TGESGSTSTEKTLTSSVTVKVPPNSKVKITMVTKMKKSSVNYTV------------------------------------ 124

                         170       180
                  ....*....|....*....|...
gi 1005574734 223 IEGSINNTVLQDIEIHIKGIEPY 245
Cdd:cd20222   125 EKGTIKSVSNFDVKILISPAEPL 147
parasporin-2-like_N-term cd21130
N-terminal region of parasporin-2, hydralysin and similar aerolysin-type beta-barrel ...
 2-61 6.73e-30

N-terminal region of parasporin-2, hydralysin and similar aerolysin-type beta-barrel pore-forming proteins; Bacillus thuringiensis 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) 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. This model represents helix1 (H1), H2 and strand (S1) that forms part of a 4-stranded beta-sheet.


:

Pssm-ID: 467846  Cd Length: 60  Bit Score: 106.29  E-value: 6.73e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005574734   2 IIQEKLSFSDLESLDSTTDSIMDAFKDLYGILPDEIAVNNETFPIHNKPAITERYNHACY 61
Cdd:cd21130     1 MIQEYLSFSDLSALDSSPDAVRDAFKRQYGTTPDGIALNDETYYNAVNPAITEQYGHYCY 60
 
Name Accession Description Interval E-value
PFM_parasporin-2-like cd20222
pore-forming module of parasporin-2, hydralysin and similar aerolysin-type beta-barrel ...
 66-245 9.32e-35

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: 121.67  E-value: 9.32e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005574734  66 PFIFRDLEKPSIDEITLKEQFVCNPNN---EEKEIVVTIKEQWANIQSWTSKSITGLTLKSDLIIAGKFQSGNEFNISTF 142
Cdd:cd20222     1 PPQVVVREEGPPTPDILGTTEAVNNGDeeeITVTYSYKVGGKWTWKTSWSSSSTTGATFSSGIPLEGVFEVGTEFSVSGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005574734 143 VGESTSKSIHTSPSIEHSIKVPPNTKMKIAMIGTLITEVLHFQSiitvqgmfgacfprmvrghyvgfksaghilnktfgm 222
Cdd:cd20222    81 TGESGSTSTEKTLTSSVTVKVPPNSKVKITMVTKMKKSSVNYTV------------------------------------ 124

                         170       180
                  ....*....|....*....|...
gi 1005574734 223 IEGSINNTVLQDIEIHIKGIEPY 245
Cdd:cd20222   125 EKGTIKSVSNFDVKILISPAEPL 147
parasporin-2-like_N-term cd21130
N-terminal region of parasporin-2, hydralysin and similar aerolysin-type beta-barrel ...
 2-61 6.73e-30

N-terminal region of parasporin-2, hydralysin and similar aerolysin-type beta-barrel pore-forming proteins; Bacillus thuringiensis 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) 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. This model represents helix1 (H1), H2 and strand (S1) that forms part of a 4-stranded beta-sheet.


Pssm-ID: 467846  Cd Length: 60  Bit Score: 106.29  E-value: 6.73e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005574734   2 IIQEKLSFSDLESLDSTTDSIMDAFKDLYGILPDEIAVNNETFPIHNKPAITERYNHACY 61
Cdd:cd21130     1 MIQEYLSFSDLSALDSSPDAVRDAFKRQYGTTPDGIALNDETYYNAVNPAITEQYGHYCY 60
 
Name Accession Description Interval E-value
PFM_parasporin-2-like cd20222
pore-forming module of parasporin-2, hydralysin and similar aerolysin-type beta-barrel ...
 66-245 9.32e-35

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: 121.67  E-value: 9.32e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005574734  66 PFIFRDLEKPSIDEITLKEQFVCNPNN---EEKEIVVTIKEQWANIQSWTSKSITGLTLKSDLIIAGKFQSGNEFNISTF 142
Cdd:cd20222     1 PPQVVVREEGPPTPDILGTTEAVNNGDeeeITVTYSYKVGGKWTWKTSWSSSSTTGATFSSGIPLEGVFEVGTEFSVSGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005574734 143 VGESTSKSIHTSPSIEHSIKVPPNTKMKIAMIGTLITEVLHFQSiitvqgmfgacfprmvrghyvgfksaghilnktfgm 222
Cdd:cd20222    81 TGESGSTSTEKTLTSSVTVKVPPNSKVKITMVTKMKKSSVNYTV------------------------------------ 124

                         170       180
                  ....*....|....*....|...
gi 1005574734 223 IEGSINNTVLQDIEIHIKGIEPY 245
Cdd:cd20222   125 EKGTIKSVSNFDVKILISPAEPL 147
parasporin-2-like_N-term cd21130
N-terminal region of parasporin-2, hydralysin and similar aerolysin-type beta-barrel ...
 2-61 6.73e-30

N-terminal region of parasporin-2, hydralysin and similar aerolysin-type beta-barrel pore-forming proteins; Bacillus thuringiensis 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) 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. This model represents helix1 (H1), H2 and strand (S1) that forms part of a 4-stranded beta-sheet.


Pssm-ID: 467846  Cd Length: 60  Bit Score: 106.29  E-value: 6.73e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005574734   2 IIQEKLSFSDLESLDSTTDSIMDAFKDLYGILPDEIAVNNETFPIHNKPAITERYNHACY 61
Cdd:cd21130     1 MIQEYLSFSDLSALDSSPDAVRDAFKRQYGTTPDGIALNDETYYNAVNPAITEQYGHYCY 60
PFM_HFR-2-like cd20216
pore-forming module of wheat HFR-2 toxin, FEM32, and similar aerolysin-type beta-barrel ...
 80-176 2.86e-06

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: 46.04  E-value: 2.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005574734  80 ITLKEQFVCNPNNEEKEIVVTIK------EQWANIQSWTSKSITGLTLKSDLIIAGKFQSGNEFNISTFVGESTSKSIHT 153
Cdd:cd20216     7 LTLATGEATNNTSEPQTVTLKLSytdtktSTWNSSVSLKLGVKTTISAGVPFIVDGKIEISAEFSGSYEWGETKTETTEV 86

                          90       100
                  ....*....|....*....|...
gi 1005574734 154 SpsIEHSIKVPPNTKMKIAMIGT 176
Cdd:cd20216    87 E--TTYTVTVPPMTKVTVTLIAT 107
PFM_natterin-3-like cd20220
pore-forming module of Thalassophryne nattereri fish venom natterins 1-4, and similar ...
 91-179 2.68e-03

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: 37.22  E-value: 2.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005574734  91 NNEEKEIV--VTIKEQWANIQSW-TSKSITG-----LTLKSDLIIAGKFQSGNEFNISTFVGESTSKSIHTSPSIEhsIK 162
Cdd:cd20220    16 NNGCKPVKktVTLSKTTEVEHRWdTSFSITLgvsttITAGIPIIAGGGWEVSTETTFTWSGGTSVTESVTHSVSVE--VT 93

                          90
                  ....*....|....*..
gi 1005574734 163 VPPNTKMKIAMIGTLIT 179
Cdd:cd20220    94 VPPNHSCTVKMVGYKYK 110
 
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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