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Conserved domains on  [gi|122011122|sp|Q3LX99|]
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RecName: Full=Lysenin-related protein 3; Short=LRP-3; AltName: Full=eflr3; Short=efL3

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; ...
 10-159 2.16e-110

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: 316.23  E-value: 2.16e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122011122  10 GLEEIEVDVVAVWKEGYVYENRGDTSVEQKITMTKGMKNLNSETKTLTATHTVGRTLKVGDPFEIGSVEVSYSFSHQESQ 89
Cdd:cd20225    1 GYEQIEVDVVAVWKEGYVYENRGSTSVDQKITITKGMKNLNSETKTLTATHSIGSTISTGDAFEIGSVEVSYSHSHEESQ 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122011122  90 VSMTQTEVYSSQVIEHTVTIPPTSKFTRWKLNADVGGTDIEYMYLIDEVTPISVTQTIPQVIRSRAKILV 159
Cdd:cd20225   81 VSMTETEVYESKVIEHTITIPPTSKFTRWQLNADVGGADIEYMYLIDEVTPIGGTQSIPQVITSRAKILV 150
beta-trefoil_Ricin-like super family cl49609
ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a ...
 227-293 3.71e-03

ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a carbohydrate-binding domain formed from presumed gene triplication. It shows a beta-trefoil fold characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain was originally found in Ricin, which is a legume lectin from the seeds of the castor bean plant, Ricinus communis. It is also found in many carbohydrate-recognition proteins like plant and bacterial AB-toxins, glycosidases, or proteases, which serve diverse functions such as inhibitory toxicity, enzymatic activity, and signal transduction. The ricin B-type lectin domain can be present in one or more copies and has been shown in some instances to bind simple sugars, such as galactose or lactose. The most characteristic, though not completely conserved, sequence feature is the presence of a Q-W pattern. Consequently, the ricin B-type lectin domain has also been referred as the (QxW)3 domain and the three homologous regions as the QxW repeats. A disulfide bond is also conserved in some QxW repeats.


The actual alignment was detected with superfamily member cd23415:

Pssm-ID: 483949 [Multi-domain]  Cd Length: 120  Bit Score: 36.64  E-value: 3.71e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122011122 227 YSSDQGGVYFDESSDNPKQRWALSKalplRHGDVVTFMNKYftnSGLCYDDGPATNVY---CLDKREDKW 293
Cdd:cd23415   15 DSNAGGNVYTGPCNGGPYQRWTWSG----VGDGTVTLRNAA---TGRCLDSNGNGGVYtlpCNGGSYQRW 77
 
Name Accession Description Interval E-value
PFM_lysenin-like cd20225
pore-forming module of lysenin and similar aerolysin-type beta-barrel pore-forming proteins; ...
 10-159 2.16e-110

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: 316.23  E-value: 2.16e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122011122  10 GLEEIEVDVVAVWKEGYVYENRGDTSVEQKITMTKGMKNLNSETKTLTATHTVGRTLKVGDPFEIGSVEVSYSFSHQESQ 89
Cdd:cd20225    1 GYEQIEVDVVAVWKEGYVYENRGSTSVDQKITITKGMKNLNSETKTLTATHSIGSTISTGDAFEIGSVEVSYSHSHEESQ 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122011122  90 VSMTQTEVYSSQVIEHTVTIPPTSKFTRWKLNADVGGTDIEYMYLIDEVTPISVTQTIPQVIRSRAKILV 159
Cdd:cd20225   81 VSMTETEVYESKVIEHTITIPPTSKFTRWQLNADVGGADIEYMYLIDEVTPIGGTQSIPQVITSRAKILV 150
beta-trefoil_Ricin_AH cd23415
ricin B-type lectin domain, beta-trefoil fold, found in Actinomycete actinohivin and similar ...
 227-293 3.71e-03

ricin B-type lectin domain, beta-trefoil fold, found in Actinomycete actinohivin and similar proteins; Actinohivin is an actinomycete lectin with a potent specific anti-human immunodeficiency virus (anti-HIV) activity. It inhibits viral entry to cells by binding the high-mannose type sugar chains of gp120. Actinohivin contains a ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain contains a sugar-binding pocket.


Pssm-ID: 467294 [Multi-domain]  Cd Length: 120  Bit Score: 36.64  E-value: 3.71e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122011122 227 YSSDQGGVYFDESSDNPKQRWALSKalplRHGDVVTFMNKYftnSGLCYDDGPATNVY---CLDKREDKW 293
Cdd:cd23415   15 DSNAGGNVYTGPCNGGPYQRWTWSG----VGDGTVTLRNAA---TGRCLDSNGNGGVYtlpCNGGSYQRW 77
 
Name Accession Description Interval E-value
PFM_lysenin-like cd20225
pore-forming module of lysenin and similar aerolysin-type beta-barrel pore-forming proteins; ...
 10-159 2.16e-110

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: 316.23  E-value: 2.16e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122011122  10 GLEEIEVDVVAVWKEGYVYENRGDTSVEQKITMTKGMKNLNSETKTLTATHTVGRTLKVGDPFEIGSVEVSYSFSHQESQ 89
Cdd:cd20225    1 GYEQIEVDVVAVWKEGYVYENRGSTSVDQKITITKGMKNLNSETKTLTATHSIGSTISTGDAFEIGSVEVSYSHSHEESQ 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122011122  90 VSMTQTEVYSSQVIEHTVTIPPTSKFTRWKLNADVGGTDIEYMYLIDEVTPISVTQTIPQVIRSRAKILV 159
Cdd:cd20225   81 VSMTETEVYESKVIEHTITIPPTSKFTRWQLNADVGGADIEYMYLIDEVTPIGGTQSIPQVITSRAKILV 150
PFM_alpha-toxin-like cd20224
pore-forming module of Clostridium septicum alpha-toxin and similar aerolysin-type beta-barrel ...
 26-114 2.66e-06

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: 45.83  E-value: 2.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122011122  26 YVYENRGDTSVeqkiTMTKGMKNLNSETKTLTATHTVGRTLKVGDPFEIG-------SVEVSYSFSHQESQVSMTQTEVY 98
Cdd:cd20224    7 YVAENHGNTED----TGTATFNYTESTSWSKTDNFKFSEGIKVTVKFTVGipliggaESETEFSFNAEQGWSDSTGNTET 82

                         90
                 ....*....|....*.
gi 122011122  99 SSQVIEHTVTIPPTSK 114
Cdd:cd20224   83 IQQSAQYTATVPPRSK 98
PFM_natterin-3-like cd20220
pore-forming module of Thalassophryne nattereri fish venom natterins 1-4, and similar ...
 30-124 4.96e-05

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: 42.61  E-value: 4.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122011122  30 NRGDTSVEQKITMTKGMKNLNSETKTLTATHTVGRTLKVGDPFEIG-SVEVSYSFSHQESQ-VSMTQTEVYSSQViehTV 107
Cdd:cd20220   16 NNGCKPVKKTVTLSKTTEVEHRWDTSFSITLGVSTTITAGIPIIAGgGWEVSTETTFTWSGgTSVTESVTHSVSV---EV 92

                         90       100
                 ....*....|....*....|.
gi 122011122 108 TIPP----TSKFTRWKLNADV 124
Cdd:cd20220   93 TVPPnhscTVKMVGYKYKADI 113
beta-trefoil_Ricin_AH cd23415
ricin B-type lectin domain, beta-trefoil fold, found in Actinomycete actinohivin and similar ...
 227-293 3.71e-03

ricin B-type lectin domain, beta-trefoil fold, found in Actinomycete actinohivin and similar proteins; Actinohivin is an actinomycete lectin with a potent specific anti-human immunodeficiency virus (anti-HIV) activity. It inhibits viral entry to cells by binding the high-mannose type sugar chains of gp120. Actinohivin contains a ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain contains a sugar-binding pocket.


Pssm-ID: 467294 [Multi-domain]  Cd Length: 120  Bit Score: 36.64  E-value: 3.71e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122011122 227 YSSDQGGVYFDESSDNPKQRWALSKalplRHGDVVTFMNKYftnSGLCYDDGPATNVY---CLDKREDKW 293
Cdd:cd23415   15 DSNAGGNVYTGPCNGGPYQRWTWSG----VGDGTVTLRNAA---TGRCLDSNGNGGVYtlpCNGGSYQRW 77
PFM_LIN24-like cd20237
pore-forming module of Caenorhabditis elegans LIN-24 and similar aerolysin-type beta-barrel ...
 27-116 6.21e-03

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: 36.02  E-value: 6.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122011122  27 VYENrgDTSVEQKITMTKgmknlnseTKTLTATHTVGRT----------LKVGDPFEIGSVEVSYS--FSHQESQ-VSMT 93
Cdd:cd20237    9 TFTN--NTSTEQEYTFKT--------ERTTTSSCTWSVTegftiggevsLKLGPPPDIAEANAGFSreLSLSKTQeETFE 78

                         90       100
                 ....*....|....*....|...
gi 122011122  94 QTEVYSsqvIEHTVTIPPTSKFT 116
Cdd:cd20237   79 EELTWS---VDSQVTVPPKTKVT 98
PFM_fascin-like cd20234
pore-forming module (PFM) of uncharacterized proteins which have N-terminal fascin-like domain, ...
 28-116 7.47e-03

pore-forming module (PFM) of uncharacterized proteins which have N-terminal fascin-like domain, and similar aerolysin-type beta-barrel pore-forming proteins; Most proteins belonging to this group have an N-terminal 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: 380804  Cd Length: 139  Bit Score: 35.96  E-value: 7.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122011122  28 YENRGDTSVEQKITMTKGMknlnSETKTLTATHTVGRTLKVGDPF--EIGSVEVSYSFSHQesqvSMTQTEVYSSQVIEH 105
Cdd:cd20234    9 YTNRSSVPQKHTFNMSWTK----QCTETTFWNHTWGLNLTSSCEFsvENATLTVTYLGDNQ----RISSTTRSITEKEST 80

                         90
                 ....*....|.
gi 122011122 106 TVTIPPTSKFT 116
Cdd:cd20234   81 EVTVPPHTKVT 91
 
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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