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Conserved domains on  [gi|1015813314|pdb|5GAQ|B]
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Chain B, Lysenin

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PFM_lysenin-like cd20225
pore-forming module of lysenin and similar aerolysin-type beta-barrel pore-forming proteins; ...
 8-157 1.52e-109

pore-forming module of lysenin and similar aerolysin-type beta-barrel pore-forming proteins; Lysenin (also known as Efl1) is a sphingomyelin-binding defense protein found in the coelomic fluid of the annelid earthworm Eisenia fetida. This group also contains lysenin-related proteins LRP-1 , LRP-2 , and LRP-3 from Eisenia sp.. 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: 380795  Cd Length: 150  Bit Score: 314.30  E-value: 1.52e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5GAQ_B        8 GYEQIEVDVVAVWKEGYVYENRGSTSVDQKITITKGMKNVNSETRTVTATHSIGSTISTGDAFEIGSVEVSYSHSHEESQ 87
Cdd:cd20225   1 GYEQIEVDVVAVWKEGYVYENRGSTSVDQKITITKGMKNLNSETKTLTATHSIGSTISTGDAFEIGSVEVSYSHSHEESQ 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5GAQ_B       88 VSMTETEVYESKVIEHTITIPPTSKFTRWQLNADVGGADIEYMYLIDEVTPIGGTQSIPQVITSRAKIIV 157
Cdd:cd20225  81 VSMTETEVYESKVIEHTITIPPTSKFTRWQLNADVGGADIEYMYLIDEVTPIGGTQSIPQVITSRAKILV 150
 
Name Accession Description Interval E-value
PFM_lysenin-like cd20225
pore-forming module of lysenin and similar aerolysin-type beta-barrel pore-forming proteins; ...
 8-157 1.52e-109

pore-forming module of lysenin and similar aerolysin-type beta-barrel pore-forming proteins; Lysenin (also known as Efl1) is a sphingomyelin-binding defense protein found in the coelomic fluid of the annelid earthworm Eisenia fetida. This group also contains lysenin-related proteins LRP-1 , LRP-2 , and LRP-3 from Eisenia sp.. 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: 380795  Cd Length: 150  Bit Score: 314.30  E-value: 1.52e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5GAQ_B        8 GYEQIEVDVVAVWKEGYVYENRGSTSVDQKITITKGMKNVNSETRTVTATHSIGSTISTGDAFEIGSVEVSYSHSHEESQ 87
Cdd:cd20225   1 GYEQIEVDVVAVWKEGYVYENRGSTSVDQKITITKGMKNLNSETKTLTATHSIGSTISTGDAFEIGSVEVSYSHSHEESQ 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5GAQ_B       88 VSMTETEVYESKVIEHTITIPPTSKFTRWQLNADVGGADIEYMYLIDEVTPIGGTQSIPQVITSRAKIIV 157
Cdd:cd20225  81 VSMTETEVYESKVIEHTITIPPTSKFTRWQLNADVGGADIEYMYLIDEVTPIGGTQSIPQVITSRAKILV 150
 
Name Accession Description Interval E-value
PFM_lysenin-like cd20225
pore-forming module of lysenin and similar aerolysin-type beta-barrel pore-forming proteins; ...
 8-157 1.52e-109

pore-forming module of lysenin and similar aerolysin-type beta-barrel pore-forming proteins; Lysenin (also known as Efl1) is a sphingomyelin-binding defense protein found in the coelomic fluid of the annelid earthworm Eisenia fetida. This group also contains lysenin-related proteins LRP-1 , LRP-2 , and LRP-3 from Eisenia sp.. 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: 380795  Cd Length: 150  Bit Score: 314.30  E-value: 1.52e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5GAQ_B        8 GYEQIEVDVVAVWKEGYVYENRGSTSVDQKITITKGMKNVNSETRTVTATHSIGSTISTGDAFEIGSVEVSYSHSHEESQ 87
Cdd:cd20225   1 GYEQIEVDVVAVWKEGYVYENRGSTSVDQKITITKGMKNLNSETKTLTATHSIGSTISTGDAFEIGSVEVSYSHSHEESQ 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5GAQ_B       88 VSMTETEVYESKVIEHTITIPPTSKFTRWQLNADVGGADIEYMYLIDEVTPIGGTQSIPQVITSRAKIIV 157
Cdd:cd20225  81 VSMTETEVYESKVIEHTITIPPTSKFTRWQLNADVGGADIEYMYLIDEVTPIGGTQSIPQVITSRAKILV 150
PFM_Cry51Aa-like cd20226
pore-forming module of Bacillus thuringiensis insecticidal Cry51A toxin, Bacillus ...
 25-114 3.92e-03

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: 37.64  E-value: 3.92e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5GAQ_B       25 VYENRgsTSVDQKITITKGMKNVNSETRTVTATHSIGSTISTGDAFEIG---------SVEVS----YSHSHEESQVSmT 91
Cdd:cd20226  28 VITNN--TSVPQSQTVSFSEKTTETTSTTTTEGYKIGTSIKSTTKFKVKfgfvvggeqSIEVSvsfeYNYSTTTTYTT-T 104

                        90       100
                ....*....|....*....|...
5GAQ_B       92 ETEVYEskvIEHTITIPPTSKFT 114
Cdd:cd20226 105 TEKLWE---DTQPVTVPPRTKVT 124
 
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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