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Conserved domains on  [gi|1169472|sp|P46058|]
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RecName: Full=Epidermal differentiation-specific protein

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PFM_EP37-like cd20230
pore-forming module of Cynops pyrrhogaster EP37, and similar aerolysin-type beta-barrel ...
 191-333 3.71e-61

pore-forming module of Cynops pyrrhogaster EP37, and similar aerolysin-type beta-barrel pore-forming proteins; Cynops pyrrhogaster (Japanese newt EP37) EP37 is an epidermis-specific protein which has a non-lens beta/gamma-crystallin domain in tandem and N-terminal to this pore-forming module. C. pyrrhogaster has several EP37-like proteins present in skin, gastric epithelium and fundic glands of an adult newt and in the swimming larva. This group also includes the alpha subunit of Bombina maxima betagamma-CAT (a non-lens betagamma-crystallin (alpha-subunit) and trefoil factor (beta subunit) complex) identified from skin secretions. Betagamma-CAT shows potent hemolytic activity on mammalian erythrocytes. Many proteins belonging to this group have N-terminal crystallin (beta/gamma crystallin) 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: 380800  Cd Length: 146  Bit Score: 192.12  E-value: 3.71e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169472  191 NVQIDQYFYTNNTSIEQQFTATSTKEFEKYVSHSFEFSNETSIKVGTSFTLKGVVD---INTEVSNTFTVKKGETESFTT 267
Cdd:cd20230   1 SVVIDEICGVNKTDIEQTFTTELSREYEVSVTQSFTFSNATQIKVGTSFTVDLGGDkfeLNLELSNTFTVEKGKSESRTT 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1169472  268 RKKAELSMPVKAPPRSKLTVNFMCKEITISVPVELKIVRGSKTDIETGTYRCESGTETYIDVQSLP 333
Cdd:cd20230  81 TKKREVELPAKVPPHTKLTVNVVRKEVTYSVPVELIITRGSKTKTEYGEYRCQSGTSITTEYTEEP 146
XTALbg smart00247
Beta/gamma crystallins; Beta/gamma crystallins
 4-80 8.75e-27

Beta/gamma crystallins; Beta/gamma crystallins


:

Pssm-ID: 214583  Cd Length: 82  Bit Score: 101.05  E-value: 8.75e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169472       4 ITVYEHSNFQGLHKTFTSDVPNLVNESFNDCISSVKIVGQPWILHQDINYSGQCLPLEEGEYSGIS----MNDGASSLRL 79
Cdd:smart00247   2 ITLYEDENFQGRSYELSDDCPSLQDYGSRDNVSSVRVESGCWVLYEQPNYRGRQYVLEPGEYPDYQewggFNDQISSIRR 81


                   .
gi 1169472      80 I 80
Cdd:smart00247  82 I 82
XTALbg smart00247
Beta/gamma crystallins; Beta/gamma crystallins
 88-168 1.09e-24

Beta/gamma crystallins; Beta/gamma crystallins


:

Pssm-ID: 214583  Cd Length: 82  Bit Score: 95.27  E-value: 1.09e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169472      88 QITVYEHVNGGGKALVLTEET-NLAFGNMHDNISSHRVQRGAWALYEHINRGGRCIVARAGEYLANYCTIGFNDQVSHVY 166
Cdd:smart00247   1 KITLYEDENFQGRSYELSDDCpSLQDYGSRDNVSSVRVESGCWVLYEQPNYRGRQYVLEPGEYPDYQEWGGFNDQISSIR 80


                   ..
gi 1169472     167 PL 168
Cdd:smart00247  81 RI 82
 
Name Accession Description Interval E-value
PFM_EP37-like cd20230
pore-forming module of Cynops pyrrhogaster EP37, and similar aerolysin-type beta-barrel ...
 191-333 3.71e-61

pore-forming module of Cynops pyrrhogaster EP37, and similar aerolysin-type beta-barrel pore-forming proteins; Cynops pyrrhogaster (Japanese newt EP37) EP37 is an epidermis-specific protein which has a non-lens beta/gamma-crystallin domain in tandem and N-terminal to this pore-forming module. C. pyrrhogaster has several EP37-like proteins present in skin, gastric epithelium and fundic glands of an adult newt and in the swimming larva. This group also includes the alpha subunit of Bombina maxima betagamma-CAT (a non-lens betagamma-crystallin (alpha-subunit) and trefoil factor (beta subunit) complex) identified from skin secretions. Betagamma-CAT shows potent hemolytic activity on mammalian erythrocytes. Many proteins belonging to this group have N-terminal crystallin (beta/gamma crystallin) 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: 380800  Cd Length: 146  Bit Score: 192.12  E-value: 3.71e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169472  191 NVQIDQYFYTNNTSIEQQFTATSTKEFEKYVSHSFEFSNETSIKVGTSFTLKGVVD---INTEVSNTFTVKKGETESFTT 267
Cdd:cd20230   1 SVVIDEICGVNKTDIEQTFTTELSREYEVSVTQSFTFSNATQIKVGTSFTVDLGGDkfeLNLELSNTFTVEKGKSESRTT 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1169472  268 RKKAELSMPVKAPPRSKLTVNFMCKEITISVPVELKIVRGSKTDIETGTYRCESGTETYIDVQSLP 333
Cdd:cd20230  81 TKKREVELPAKVPPHTKLTVNVVRKEVTYSVPVELIITRGSKTKTEYGEYRCQSGTSITTEYTEEP 146
XTALbg smart00247
Beta/gamma crystallins; Beta/gamma crystallins
 4-80 8.75e-27

Beta/gamma crystallins; Beta/gamma crystallins


Pssm-ID: 214583  Cd Length: 82  Bit Score: 101.05  E-value: 8.75e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169472       4 ITVYEHSNFQGLHKTFTSDVPNLVNESFNDCISSVKIVGQPWILHQDINYSGQCLPLEEGEYSGIS----MNDGASSLRL 79
Cdd:smart00247   2 ITLYEDENFQGRSYELSDDCPSLQDYGSRDNVSSVRVESGCWVLYEQPNYRGRQYVLEPGEYPDYQewggFNDQISSIRR 81


                   .
gi 1169472      80 I 80
Cdd:smart00247  82 I 82
XTALbg smart00247
Beta/gamma crystallins; Beta/gamma crystallins
 88-168 1.09e-24

Beta/gamma crystallins; Beta/gamma crystallins


Pssm-ID: 214583  Cd Length: 82  Bit Score: 95.27  E-value: 1.09e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169472      88 QITVYEHVNGGGKALVLTEET-NLAFGNMHDNISSHRVQRGAWALYEHINRGGRCIVARAGEYLANYCTIGFNDQVSHVY 166
Cdd:smart00247   1 KITLYEDENFQGRSYELSDDCpSLQDYGSRDNVSSVRVESGCWVLYEQPNYRGRQYVLEPGEYPDYQEWGGFNDQISSIR 80


                   ..
gi 1169472     167 PL 168
Cdd:smart00247  81 RI 82
Crystall pfam00030
Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity ...
 4-80 1.40e-18

Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity between them is very low.


Pssm-ID: 459639  Cd Length: 82  Bit Score: 79.07  E-value: 1.40e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169472      4 ITVYEHSNFQGLHKTFTSDVPNLVNESFNDCISSVKIVGQPWILHQDINYSGQCLPLEEGEYS-----GiSMNDGASSLR 78
Cdd:pfam00030   2 IVLYEKENFQGRSIELTDDCPSLQERGFNSRVNSIRVLSGAWVLYEHPNFRGRQYVLEPGEYPdwsdwG-APNDRIGSLR 80


                  ..
gi 1169472     79 LI 80
Cdd:pfam00030  81 PI 82
Crystall pfam00030
Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity ...
 88-168 1.27e-11

Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity between them is very low.


Pssm-ID: 459639  Cd Length: 82  Bit Score: 59.81  E-value: 1.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169472     88 QITVYEHVNGGGKALVLTEET-NLAFGNMHDNISSHRVQRGAWALYEHINRGGRCIVARAGEYlANYCTIGF-NDQVSHV 165
Cdd:pfam00030   1 KIVLYEKENFQGRSIELTDDCpSLQERGFNSRVNSIRVLSGAWVLYEHPNFRGRQYVLEPGEY-PDWSDWGApNDRIGSL 79


                  ...
gi 1169472    166 YPL 168
Cdd:pfam00030  80 RPI 82
ETX_MTX2 pfam03318
Clostridium epsilon toxin ETX/Bacillus mosquitocidal toxin MTX2; This family appears to be ...
 178-303 5.36e-06

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: 46.63  E-value: 5.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169472    178 TILWDRKKVESERNVQIDQYFYTNNTSIEQQF-TATSTKEFEKYVSHSFEFSNETSIKVGTSFTLKGVVDINTEVSNTFT 256
Cdd:pfam03318  15 TVLIEETTVKTLTPLYTGSNTLTNNTDSTQTLqTQSFSKKVTTTTSTTTTHGFKIGAKASGKFGIPFVAEGGITLSVSGE 94

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1169472    257 VKKGETESFTTRKKAEL---SMPVKAPPRSKLTVNFMCKEITISVPVELK 303
Cdd:pfam03318  95 YNFSSTTTNTTSVTTTYwvpSQKVTVPPHTTVRVTLVLYKTTYSVPVDLY 144
 
Name Accession Description Interval E-value
PFM_EP37-like cd20230
pore-forming module of Cynops pyrrhogaster EP37, and similar aerolysin-type beta-barrel ...
 191-333 3.71e-61

pore-forming module of Cynops pyrrhogaster EP37, and similar aerolysin-type beta-barrel pore-forming proteins; Cynops pyrrhogaster (Japanese newt EP37) EP37 is an epidermis-specific protein which has a non-lens beta/gamma-crystallin domain in tandem and N-terminal to this pore-forming module. C. pyrrhogaster has several EP37-like proteins present in skin, gastric epithelium and fundic glands of an adult newt and in the swimming larva. This group also includes the alpha subunit of Bombina maxima betagamma-CAT (a non-lens betagamma-crystallin (alpha-subunit) and trefoil factor (beta subunit) complex) identified from skin secretions. Betagamma-CAT shows potent hemolytic activity on mammalian erythrocytes. Many proteins belonging to this group have N-terminal crystallin (beta/gamma crystallin) 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: 380800  Cd Length: 146  Bit Score: 192.12  E-value: 3.71e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169472  191 NVQIDQYFYTNNTSIEQQFTATSTKEFEKYVSHSFEFSNETSIKVGTSFTLKGVVD---INTEVSNTFTVKKGETESFTT 267
Cdd:cd20230   1 SVVIDEICGVNKTDIEQTFTTELSREYEVSVTQSFTFSNATQIKVGTSFTVDLGGDkfeLNLELSNTFTVEKGKSESRTT 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1169472  268 RKKAELSMPVKAPPRSKLTVNFMCKEITISVPVELKIVRGSKTDIETGTYRCESGTETYIDVQSLP 333
Cdd:cd20230  81 TKKREVELPAKVPPHTKLTVNVVRKEVTYSVPVELIITRGSKTKTEYGEYRCQSGTSITTEYTEEP 146
XTALbg smart00247
Beta/gamma crystallins; Beta/gamma crystallins
 4-80 8.75e-27

Beta/gamma crystallins; Beta/gamma crystallins


Pssm-ID: 214583  Cd Length: 82  Bit Score: 101.05  E-value: 8.75e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169472       4 ITVYEHSNFQGLHKTFTSDVPNLVNESFNDCISSVKIVGQPWILHQDINYSGQCLPLEEGEYSGIS----MNDGASSLRL 79
Cdd:smart00247   2 ITLYEDENFQGRSYELSDDCPSLQDYGSRDNVSSVRVESGCWVLYEQPNYRGRQYVLEPGEYPDYQewggFNDQISSIRR 81


                   .
gi 1169472      80 I 80
Cdd:smart00247  82 I 82
XTALbg smart00247
Beta/gamma crystallins; Beta/gamma crystallins
 88-168 1.09e-24

Beta/gamma crystallins; Beta/gamma crystallins


Pssm-ID: 214583  Cd Length: 82  Bit Score: 95.27  E-value: 1.09e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169472      88 QITVYEHVNGGGKALVLTEET-NLAFGNMHDNISSHRVQRGAWALYEHINRGGRCIVARAGEYLANYCTIGFNDQVSHVY 166
Cdd:smart00247   1 KITLYEDENFQGRSYELSDDCpSLQDYGSRDNVSSVRVESGCWVLYEQPNYRGRQYVLEPGEYPDYQEWGGFNDQISSIR 80


                   ..
gi 1169472     167 PL 168
Cdd:smart00247  81 RI 82
Crystall pfam00030
Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity ...
 4-80 1.40e-18

Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity between them is very low.


Pssm-ID: 459639  Cd Length: 82  Bit Score: 79.07  E-value: 1.40e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169472      4 ITVYEHSNFQGLHKTFTSDVPNLVNESFNDCISSVKIVGQPWILHQDINYSGQCLPLEEGEYS-----GiSMNDGASSLR 78
Cdd:pfam00030   2 IVLYEKENFQGRSIELTDDCPSLQERGFNSRVNSIRVLSGAWVLYEHPNFRGRQYVLEPGEYPdwsdwG-APNDRIGSLR 80


                  ..
gi 1169472     79 LI 80
Cdd:pfam00030  81 PI 82
Crystall pfam00030
Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity ...
 88-168 1.27e-11

Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity between them is very low.


Pssm-ID: 459639  Cd Length: 82  Bit Score: 59.81  E-value: 1.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169472     88 QITVYEHVNGGGKALVLTEET-NLAFGNMHDNISSHRVQRGAWALYEHINRGGRCIVARAGEYlANYCTIGF-NDQVSHV 165
Cdd:pfam00030   1 KIVLYEKENFQGRSIELTDDCpSLQERGFNSRVNSIRVLSGAWVLYEHPNFRGRQYVLEPGEY-PDWSDWGApNDRIGSL 79


                  ...
gi 1169472    166 YPL 168
Cdd:pfam00030  80 RPI 82
PFM_epsilon-toxin-like cd20223
pore-forming module of Clostridium perfringens epsilon-toxin and similar aerolysin-type ...
 178-333 2.02e-08

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: 52.62  E-value: 2.02e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169472  178 TILWDRKKVESERNVQIDQYFYTNNTSIEQQFTatsTKEFEKYVSHSFEFSNETSIKVGTSFTLKGVVDINTEVSNTFTV 257
Cdd:cd20223   1 VILIGDPKITNGEPLYVGSNTLTNDTDEEQTLK---TPSFSKTVTDTVTTTTTNGFKLGVSTSAKFKIPFPGGGSTELSA 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169472  258 --KKGETESFTTRKKAELSMP---VKAPPRSKLTVNfmckeitisvpVELKIVRGSKTdieTGTYRCESGTETYIDVQSL 332
Cdd:cd20223  78 eyNFSTTNTNTTSETKTYTAPsqtIKVPPGKTYKVT-----------VYLKKVKFSGT---VGTFTGVYGTDFTVKVKDI 143


                .
gi 1169472  333 P 333
Cdd:cd20223 144 T 144
PFM_LIN24-like cd20237
pore-forming module of Caenorhabditis elegans LIN-24 and similar aerolysin-type beta-barrel ...
 194-293 4.61e-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: 50.65  E-value: 4.61e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169472  194 IDQYFYTNNTSIEQQFTATstkeFEKYVSHSFEFSNETSIKVGTSFTLK-----GVVDINTEVSNTFTVKKGETESFTTR 268
Cdd:cd20237   5 LFKTTFTNNTSTEQEYTFK----TERTTTSSCTWSVTEGFTIGGEVSLKlgpppDIAEANAGFSRELSLSKTQEETFEEE 80

                        90       100
                ....*....|....*....|....*
gi 1169472  269 KKAELSMPVKAPPRSKLTVNFMCKE 293
Cdd:cd20237  81 LTWSVDSQVTVPPKTKVTAELVITE 105
PFM_LSL-like cd20215
pore-forming module of Laetiporus sulphureus LSL lectin and similar aerolysin-type beta-barrel ...
 182-299 5.16e-08

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: 51.94  E-value: 5.16e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169472  182 DRKKVESERNVQIDQYFYTNNTSIEQQFTATSTkEFEKYVShSFEFSNETSIKVGTSFT--LKGVVD--INTEVSNTFTV 257
Cdd:cd20215  13 DKGKILSSTPLVLARQTLRNDTDVEQTMSFTLT-ETETHTS-TFEYTAGFTITVGTSFKagIPGVAEgkIKVDTTVSNEW 90

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 1169472  258 KKGETESFTtrKKAELSMPVKAPPRSKLTVNFMCKEITISVP 299
Cdd:cd20215  91 KWGESTTFT--KTYTATFPVKAPPGSTVRAVATVTKSNLEVP 130
PFM_Dln1-like cd20221
pore-forming module of Danio rerio Dln1, and similar aerolysin-type beta-barrel pore-forming ...
 194-331 9.50e-08

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: 51.21  E-value: 9.50e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169472  194 IDQYFYTNNTSIEQQFTATSTKEFEKYVSHSFEFSNETSIKVGTSFTLKGVVDINTEVSNTFTVKKGETESFTTRKKAEL 273
Cdd:cd20221  25 IKSMSYENDTSVPQEYTIETSKKITKTSSWSVTNKLESTFSVEVSAGIPEVVEVSTGFSLTVGVESTHSLENTEEKTETL 104

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1169472  274 SMPVKAPPRSKLTVNFMCKEITISVP----VELKIVRGSKTDIET-GTYRCESGTETYIDVQS 331
Cdd:cd20221 105 SFPVKVPPGKTVDVEITIGRATVDLPytgtVKITCYNGSVLKFPTsGIYKGVTYTDAKVVVKE 167
PFM_Cry51Aa-like cd20226
pore-forming module of Bacillus thuringiensis insecticidal Cry51A toxin, Bacillus ...
 200-335 1.08e-07

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: 51.12  E-value: 1.08e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169472  200 TNNTSIEQQ----FTATSTKEFEKYVSHSFEFSneTSIKVGTSFTLKGVVDINTEVSNTFTVKKG------ETESFTTRK 269
Cdd:cd20226  30 TNNTSVPQSqtvsFSEKTTETTSTTTTEGYKIG--TSIKSTTKFKVKFGFVVGGEQSIEVSVSFEynysttTTYTTTTEK 107

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1169472  270 KAELSMPVKAPPRSKLTVNFMCKEITISVPVELKI-----VRGSktdietGTYRCESGTETYIDVQSLPIS 335
Cdd:cd20226 108 LWEDTQPVTVPPRTKVTATLIIYGGPFNVPVTLNCtislnFKGS------GTLTGSLGLYSTVRFTEEPLP 172
PFM_HFR-2-like cd20216
pore-forming module of wheat HFR-2 toxin, FEM32, and similar aerolysin-type beta-barrel ...
 189-299 2.32e-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: 46.81  E-value: 2.32e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169472  189 ERNVQIDQYFYTNNTSIEQQFTATSTKEFEKY----VSHSFEFSNETSIKVGTSFTLKGVVDINTEVSNTFTVkkGETES 264
Cdd:cd20216   4 EKVLTLATGEATNNTSEPQTVTLKLSYTDTKTstwnSSVSLKLGVKTTISAGVPFIVDGKIEISAEFSGSYEW--GETKT 81

                        90       100       110
                ....*....|....*....|....*....|....*
gi 1169472  265 FTTrkKAELSMPVKAPPRSKLTVNFMCKEITISVP 299
Cdd:cd20216  82 ETT--EVETTYTVTVPPMTKVTVTLIATRGSCDVP 114
ETX_MTX2 pfam03318
Clostridium epsilon toxin ETX/Bacillus mosquitocidal toxin MTX2; This family appears to be ...
 178-303 5.36e-06

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: 46.63  E-value: 5.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169472    178 TILWDRKKVESERNVQIDQYFYTNNTSIEQQF-TATSTKEFEKYVSHSFEFSNETSIKVGTSFTLKGVVDINTEVSNTFT 256
Cdd:pfam03318  15 TVLIEETTVKTLTPLYTGSNTLTNNTDSTQTLqTQSFSKKVTTTTSTTTTHGFKIGAKASGKFGIPFVAEGGITLSVSGE 94

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1169472    257 VKKGETESFTTRKKAEL---SMPVKAPPRSKLTVNFMCKEITISVPVELK 303
Cdd:pfam03318  95 YNFSSTTTNTTSVTTTYwvpSQKVTVPPHTTVRVTLVLYKTTYSVPVDLY 144
PFM_aerolysin-like cd20240
pore-forming module of aerolysin-type beta-barrel pore-forming proteins; uncharacterized ...
 188-298 7.52e-06

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: 44.95  E-value: 7.52e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169472  188 SERNVQIDQYFYTNNTSIEQQFT------ATSTKEFEKyvSHSFEFSNETSIKVGTSFTLKGVVDINTEVSNTFTVKKGE 261
Cdd:cd20240   2 SEIPDFIVTWTYTNNTSIEQTMTtnfsetATETSSFSE--TEGVSTTVSTSLKVGIPFIAGGEITTTTTTSQSWTYGKSE 79

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 1169472  262 TESFTTrkkaELSMPVKAPPRSKLTVNFMCKEITISV 298
Cdd:cd20240  80 TKTDTI----SYTFPIVVPPNTTVTATAVVTKYNMDV 112
PFM_aerolysin-like cd20241
pore-forming module of aerolysin-type beta-barrel pore-forming proteins; uncharacterized ...
 200-316 1.50e-05

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: 44.02  E-value: 1.50e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169472  200 TNNTSIEQQFTATSTKEFekyvSHSFEFSNETSIKVGTSFTLKGVVDINTEVSNTFTVkkGETESFTTRKKAELSmpVKA 279
Cdd:cd20241  17 TLKANMSRSVSETGSFSF----THGFSIGVGTTIKAGIPFIVEGEIETELSTSHDFTW--GKSTTVTTTVGSSVT--VEV 88

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 1169472  280 PPRSKLTVNFMCKEITISVPVelKIVRGSK-TDIETGT 316
Cdd:cd20241  89 PPRSTQTVVGTFKRSKMTVPA--KIYSKSKsTGVEVIT 124
PFM_aerolysin-like cd20242
pore-forming module of aerolysin-type beta-barrel pore-forming proteins; uncharacterized ...
 200-325 6.23e-05

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: 42.41  E-value: 6.23e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169472  200 TNNTSIEQqftaTSTKEFEKYVSHSFEFSNETSIKVGTSFTLK--------GVVDINTEVSNTFTVKKgeteSFTTRKKA 271
Cdd:cd20242  10 TNDTGQPQ----TPSISGSETVTETSTWEDEVGLKLGVSTSFSagvpvvaeGKVEVSAEVHNNYTWNG----SNTRSKTW 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 1169472  272 ELSMPVKAPPRSKLTVNFMCKEITISVPVELkivrgsktdieTGTYRCESGTET 325
Cdd:cd20242  82 SFSTPVNVPAHSAVRATATVTESTISVPYTL-----------TWKSIFESGARV 124
PFM_crystallin-like cd20232
pore-forming module (PFM) of uncharacterized proteins which have N-terminal crystallin domain ...
 201-309 7.79e-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: 7.79e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169472  201 NNTSIEQQFTATSTKEFEKYVSHSFEFSNETSIKVGTSFTL---KGVV--DINTEVS----NTFTVKKGETESFTTRKKA 271
Cdd:cd20232  11 NGSDIEQVATLTLERELSKSTTRSFSESTLIGIEVSTTASVgvsAGPVsaEVEQTVTstleNTFTIGKEETKSETITFSK 90

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 1169472  272 ELSMPVKAPPRSKLTVNFMCKEITISVPVELKiVRGSK 309
Cdd:cd20232  91 SVNVTIPPGNIGEAVMTLTPKKYKVEAIYTFR-LKGTE 127
Aerolysin pfam01117
Aerolysin toxin; This family represents the pore forming lobe of aerolysin.
 180-307 3.25e-04

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


Pssm-ID: 366474  Cd Length: 359  Bit Score: 42.24  E-value: 3.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169472    180 LWDRKKVESERNVQ--IDQYFYtNNTSIEQQFTATSTKEFEKYVS--HSFEFSNETSIKVGTSFTLKGVVDI--NTEVSN 253
Cdd:pfam01117  89 LKYGDPVISDREPYkyIVGYAR-NDSDTPQQRVLTLSYDEVTNWSktDTYKYSEKVTIKNKYKFPLIGETELslELGANQ 167

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1169472    254 TFTVKKGETESFTTRKKAELSMPvkapPRSKLTVNFMCKEITISVPVELKIVRG 307
Cdd:pfam01117 168 SWATTNGNSSTKTISDVARVLVP----ANTKIPVRLKLEKARVDYPYEFNAQVS 217
PFM_parasporin-2-like cd20222
pore-forming module of parasporin-2, hydralysin and similar aerolysin-type beta-barrel ...
 199-298 4.27e-04

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: 40.00  E-value: 4.27e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169472  199 YTNNTSIEQQFTATSTKEFEKYVSHSFEFSNETSIKVGtsFTLKGVVDINTEVSNTFTVKKGETESFTtrKKAELSMPVK 278
Cdd:cd20222  25 NGDEEEITVTYSYKVGGKWTWKTSWSSSSTTGATFSSG--IPLEGVFEVGTEFSVSGTTGESGSTSTE--KTLTSSVTVK 100

                        90       100
                ....*....|....*....|
gi 1169472  279 APPRSKLTVNFMCKEITISV 298
Cdd:cd20222 101 VPPNSKVKITMVTKMKKSSV 120
PFM_natterin-3-like cd20220
pore-forming module of Thalassophryne nattereri fish venom natterins 1-4, and similar ...
 210-299 6.48e-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: 36.84  E-value: 6.48e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1169472  210 TATSTKEFEkyVSHSFEFSNETSIKVGTSFT------LKGVVDINTEVsnTFTVKKG--ETESFTTRkkaeLSMPVKAPP 281
Cdd:cd20220  25 TVTLSKTTE--VEHRWDTSFSITLGVSTTITagipiiAGGGWEVSTET--TFTWSGGtsVTESVTHS----VSVEVTVPP 96

                        90
                ....*....|....*...
gi 1169472  282 RSKLTVNFMCKEITISVP 299
Cdd:cd20220  97 NHSCTVKMVGYKYKADIP 114
 
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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