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Conserved domains on  [gi|1370940691|ref|WP_106593456|]
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ETX/MTX2 family pore-forming toxin [Dyadobacter jiangsuensis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PFM_aerolysin-like cd20242
pore-forming module of aerolysin-type beta-barrel pore-forming proteins; uncharacterized ...
 158-302 1.70e-65

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: 203.42  E-value: 1.70e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370940691 158 PAELYRQTVTNDSLQPQVSSITGSATVTETTGWSGSLSVKVGVSTSFKTGIPFVAEGKVKVSVEVTNTYTWNGSTSQSKT 237
Cdd:cd20242     1 PASLYSQTVTNDTGQPQTPSISGSETVTETSTWEDEVGLKLGVSTSFSAGVPVVAEGKVEVSAEVHNNYTWNGSNTRSKT 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370940691 238 WGFNTPVSVAPHTVIVALVTATISTIAVPYTMTGTVILKSGIRlPNRKIKGTYLGTNSHDLTVRF 302
Cdd:cd20242    81 WSFSTPVNVPAHSAVRATATVTESTISVPYTLTWKSIFESGAR-VTGTIEGMYKGSNSHDLTTNF 144
B_lectin super family cl24013
Bulb-type mannose-specific lectin. The domain contains a three-fold internal repeat ...
 8-128 5.37e-08

Bulb-type mannose-specific lectin. The domain contains a three-fold internal repeat (beta-prism architecture). The consensus sequence motif QXDXNXVXY is involved in alpha-D-mannose recognition. Lectins are carbohydrate-binding proteins which specifically recognize diverse carbohydrates and mediate a wide variety of biological processes, such as cell-cell and host-pathogen interactions, serum glycoprotein turnover, and innate immune responses.


The actual alignment was detected with superfamily member cd00028:

Pssm-ID: 474126  Cd Length: 116  Bit Score: 50.77  E-value: 5.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370940691   8 LKSGQYLgtqdilVSNNGLF------FAALQPDGNLCVYRGTGPGdnlgLLWSSRTSAGPIGQYFLAMQGDGNLCVYKGT 81
Cdd:cd00028     4 LSSGQTL------VSSGSLFelgffkLIMQSRDYNLILYKGSSRT----VVWVANRDNPSGSSCTLTLQSDGNLVIYDGS 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1370940691  82 GpqdnkGFFWGSQSSRQTGEYFVVLQDDGNFCIYkgtapENNQGFVW 128
Cdd:cd00028    74 G-----TVVWSSNTTRVNGNYVLVLLDDGNLVLY-----DSDGNFLW 110
 
Name Accession Description Interval E-value
PFM_aerolysin-like cd20242
pore-forming module of aerolysin-type beta-barrel pore-forming proteins; uncharacterized ...
 158-302 1.70e-65

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: 203.42  E-value: 1.70e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370940691 158 PAELYRQTVTNDSLQPQVSSITGSATVTETTGWSGSLSVKVGVSTSFKTGIPFVAEGKVKVSVEVTNTYTWNGSTSQSKT 237
Cdd:cd20242     1 PASLYSQTVTNDTGQPQTPSISGSETVTETSTWEDEVGLKLGVSTSFSAGVPVVAEGKVEVSAEVHNNYTWNGSNTRSKT 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370940691 238 WGFNTPVSVAPHTVIVALVTATISTIAVPYTMTGTVILKSGIRlPNRKIKGTYLGTNSHDLTVRF 302
Cdd:cd20242    81 WSFSTPVNVPAHSAVRATATVTESTISVPYTLTWKSIFESGAR-VTGTIEGMYKGSNSHDLTTNF 144
ETX_MTX2 pfam03318
Clostridium epsilon toxin ETX/Bacillus mosquitocidal toxin MTX2; This family appears to be ...
 164-282 4.33e-12

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: 64.73  E-value: 4.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370940691 164 QTVTND-SLQPQVSSITGSATVTETTGWSGSLSVKVGVSTSFKTGIPFVAEGKVKVSVEV----TNTYTWNGSTSQsKTW 238
Cdd:pfam03318  34 NTLTNNtDSTQTLQTQSFSKKVTTTTSTTTTHGFKIGAKASGKFGIPFVAEGGITLSVSGeynfSSTTTNTTSVTT-TYW 112

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1370940691 239 GFNTPVSVAPHTVIVALVTATISTIAVPYTMTGTVILKSGIRLP 282
Cdd:pfam03318 113 VPSQKVTVPPHTTVRVTLVLYKTTYSVPVDLYTTLSGTFSIEGT 156
B_lectin cd00028
Bulb-type mannose-specific lectin. The domain contains a three-fold internal repeat ...
 8-128 5.37e-08

Bulb-type mannose-specific lectin. The domain contains a three-fold internal repeat (beta-prism architecture). The consensus sequence motif QXDXNXVXY is involved in alpha-D-mannose recognition. Lectins are carbohydrate-binding proteins which specifically recognize diverse carbohydrates and mediate a wide variety of biological processes, such as cell-cell and host-pathogen interactions, serum glycoprotein turnover, and innate immune responses.


Pssm-ID: 237995  Cd Length: 116  Bit Score: 50.77  E-value: 5.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370940691   8 LKSGQYLgtqdilVSNNGLF------FAALQPDGNLCVYRGTGPGdnlgLLWSSRTSAGPIGQYFLAMQGDGNLCVYKGT 81
Cdd:cd00028     4 LSSGQTL------VSSGSLFelgffkLIMQSRDYNLILYKGSSRT----VVWVANRDNPSGSSCTLTLQSDGNLVIYDGS 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1370940691  82 GpqdnkGFFWGSQSSRQTGEYFVVLQDDGNFCIYkgtapENNQGFVW 128
Cdd:cd00028    74 G-----TVVWSSNTTRVNGNYVLVLLDDGNLVLY-----DSDGNFLW 110
B_lectin smart00108
Bulb-type mannose-specific lectin;
12-130 2.24e-07

Bulb-type mannose-specific lectin;


Pssm-ID: 214519 [Multi-domain]  Cd Length: 114  Bit Score: 48.85  E-value: 2.24e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370940691   12 QYLGTQDILVSNNGLFFA-----ALQPDGNLCVYRGTGPGdnlgLLWSS-RTSAGPiGQYFLAMQGDGNLCVYKGTGPqd 85
Cdd:smart00108   2 NTLSSGQTLVSGNSLFELgfftlIMQNDYNLILYKSSSRT----VVWVAnRDNPVS-DSCTLTLQSDGNLVLYDGDGR-- 74

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1370940691   86 nkgFFWGSQSSRQTGEYFVVLQDDGNFCIYkgtapENNQGFVWGT 130
Cdd:smart00108  75 ---VVWSSNTTGANGNYVLVLLDDGNLVIY-----DSDGNFLWQS 111
 
Name Accession Description Interval E-value
PFM_aerolysin-like cd20242
pore-forming module of aerolysin-type beta-barrel pore-forming proteins; uncharacterized ...
 158-302 1.70e-65

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: 203.42  E-value: 1.70e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370940691 158 PAELYRQTVTNDSLQPQVSSITGSATVTETTGWSGSLSVKVGVSTSFKTGIPFVAEGKVKVSVEVTNTYTWNGSTSQSKT 237
Cdd:cd20242     1 PASLYSQTVTNDTGQPQTPSISGSETVTETSTWEDEVGLKLGVSTSFSAGVPVVAEGKVEVSAEVHNNYTWNGSNTRSKT 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370940691 238 WGFNTPVSVAPHTVIVALVTATISTIAVPYTMTGTVILKSGIRlPNRKIKGTYLGTNSHDLTVRF 302
Cdd:cd20242    81 WSFSTPVNVPAHSAVRATATVTESTISVPYTLTWKSIFESGAR-VTGTIEGMYKGSNSHDLTTNF 144
PFM_LSL-like cd20215
pore-forming module of Laetiporus sulphureus LSL lectin and similar aerolysin-type beta-barrel ...
 138-304 9.81e-36

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: 127.44  E-value: 9.81e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370940691 138 NVETGNIEYDVAAAKILQSGPAELYRQTVTNDSLQPQVSSITGSATVTETTGWSGSLSVKVGVSTSFKTGIPFVAEGKVK 217
Cdd:cd20215     2 DMEIVSVEYDLDKGKILSSTPLVLARQTLRNDTDVEQTMSFTLTETETHTSTFEYTAGFTITVGTSFKAGIPGVAEGKIK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370940691 218 VSVEVTNTYTWNGSTSQSKTWGFNTPVSVAPHTVIVALVTATISTIAVPYTMTgtviLKS---GIRLpnrKIKGTYLGTN 294
Cdd:cd20215    82 VDTTVSNEWKWGESTTFTKTYTATFPVKAPPGSTVRAVATVTKSNLEVPFTMT----LKSkstGYEV---ETKGIYRGVS 154

                         170
                  ....*....|
gi 1370940691 295 SHDLTVRFVQ 304
Cdd:cd20215   155 TWNLRTAIRE 164
PFM_HFR-2-like cd20216
pore-forming module of wheat HFR-2 toxin, FEM32, and similar aerolysin-type beta-barrel ...
 160-304 4.64e-27

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: 104.21  E-value: 4.64e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370940691 160 ELYRQTVTNDSLQPQVSSITGSATVTETTGWSGSLSVKVGVSTSFKTGIPFVAEGKVKVSVEVTNTYTWNGSTSQSKTWG 239
Cdd:cd20216     8 TLATGEATNNTSEPQTVTLKLSYTDTKTSTWNSSVSLKLGVKTTISAGVPFIVDGKIEISAEFSGSYEWGETKTETTEVE 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370940691 240 FNTPVSVAPHTVIVALVTATISTIAVPYTMTGTVILKSGIRLPNRKIKGTYLGTNSHDLTVRFVQ 304
Cdd:cd20216    88 TTYTVTVPPMTKVTVTLIATRGSCDVPFSYTQRDTLTNGTTVTYEKDDGLYTGVNSYNFKYETKE 152
PFM_aerolysin-like cd20240
pore-forming module of aerolysin-type beta-barrel pore-forming proteins; uncharacterized ...
 158-293 4.63e-18

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: 79.61  E-value: 4.63e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370940691 158 PAELYRQTVTNDSLQPQVSSITGSATVTETTGWSGSLSVKVGVSTSFKTGIPFVAEGKVKVSVEVTNTYTWNGSTSQSKT 237
Cdd:cd20240     5 PDFIVTWTYTNNTSIEQTMTTNFSETATETSSFSETEGVSTTVSTSLKVGIPFIAGGEITTTTTTSQSWTYGKSETKTDT 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1370940691 238 WGFNTPVSVAPHTVIVALVTATISTIAVPYTMTgTVILKSGIRLpnrKIKGTYLGT 293
Cdd:cd20240    85 ISYTFPIVVPPNTTVTATAVVTKYNMDVTYVAT-LRGINTGKRI---KIKGKWSGV 136
PFM_aerolysin-like cd20239
pore-forming module of aerolysin-type beta-barrel pore-forming proteins; uncharacterized ...
 163-278 1.15e-17

pore-forming module of aerolysin-type beta-barrel pore-forming proteins; uncharacterized subgroup; Generally, pore-forming proteins (PFPs) are secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores detrimental to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel. Many of this family are bacterial toxins. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin).


Pssm-ID: 380809 [Multi-domain]  Cd Length: 145  Bit Score: 78.65  E-value: 1.15e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370940691 163 RQTVTNDSLQPQVSSITGSATVTETTGWSGSLSVKVGVSTSFKTGIPFVAEGKVKVSVEVTNTYTWNGSTSQSKTWGFNT 242
Cdd:cd20239     6 STVVRNDSDSPASQTLTYSYSKSEEGTWNNTAGIELGVKVTFKAGVPFVASGELEVSVSASYSHTWGGSTTVTKTVSSST 85

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1370940691 243 PVSVAPHTVIVALVTATISTIAVPYTMTGTVILKSG 278
Cdd:cd20239    86 TVVVPPRKKGVASVLIRKAEIDVPFTYTERITYTGG 121
PFM_aerolysin-like cd20241
pore-forming module of aerolysin-type beta-barrel pore-forming proteins; uncharacterized ...
 160-269 4.95e-16

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: 73.68  E-value: 4.95e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370940691 160 ELYRQTVTNDSLQPQVSSITGSATVTETTGWSGSLSVKVGVSTSFKTGIPFVAEGKVKVSVEVTNTYTWNGSTSQSKTWG 239
Cdd:cd20241     2 HAFEVTVRNNGNTPATLKANMSRSVSETGSFSFTHGFSIGVGTTIKAGIPFIVEGEIETELSTSHDFTWGKSTTVTTTVG 81

                          90       100       110
                  ....*....|....*....|....*....|
gi 1370940691 240 FNTPVSVAPHTVIVALVTATISTIAVPYTM 269
Cdd:cd20241    82 SSVTVEVPPRSTQTVVGTFKRSKMTVPAKI 111
PFM_natterin-3-like cd20220
pore-forming module of Thalassophryne nattereri fish venom natterins 1-4, and similar ...
 153-294 1.47e-14

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: 69.96  E-value: 1.47e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370940691 153 ILQSGPAELYRQTVTNDSLQPQVSSITGSATVTETTGWSGSLSVKVGVSTSFKTGIPFVAEGKVKVSVEVTNTYTWNGST 232
Cdd:cd20220     1 IESYPPETLKESTVTNNGCKPVKKTVTLSKTTEVEHRWDTSFSITLGVSTTITAGIPIIAGGGWEVSTETTFTWSGGTSV 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370940691 233 SQSKTWGFNTPVSVAP-HTVIVALVtATISTIAVPYTMTGTVILKSGiRLPNRKIKGTYLGTN 294
Cdd:cd20220    81 TESVTHSVSVEVTVPPnHSCTVKMV-GYKYKADIPFTARLTRTYRNG-ETHTTTITGTYKGVQ 141
PFM_tachylectin-like cd20229
pore-forming module (PFM) of uncharacterized proteins having tachylectin domain(s), and ...
 176-300 4.32e-13

pore-forming module (PFM) of uncharacterized proteins having tachylectin domain(s), and similar aerolysin-type beta-barrel pore-forming proteins; Many proteins belonging to this group have tachylectin domain(s), N-terminal to this PFM; some also have an immunoglobulin (Ig) domain. Tachylectins are lectins which bind N-acetylglucosamine and N-acetylgalactosamine. 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: 380799 [Multi-domain]  Cd Length: 148  Bit Score: 66.01  E-value: 4.32e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370940691 176 SSITGSATVTETTGWSGS--LSVKVGVSTSFKTGIPFVAEGKVKVSVEVTNTYTWNGSTSQSKTWGF--NTPVSVAPHTV 251
Cdd:cd20229    20 DTFTFSKTITEVSSFSHShgFTVAEGAETTFKAGIPVIGEEGIKVILDNSTTHQWNFTTTNEREVTFslTTNVVVPPGKA 99

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1370940691 252 IVALVTATISTIAVPYtmTGTVILKSGIRLPnrkIKGTYLGTNSHDLTV 300
Cdd:cd20229   100 VRLEASVQKAKIDVPY--RAEVITGFGYEVT---ITGTWTGVTVYDLRV 143
ETX_MTX2 pfam03318
Clostridium epsilon toxin ETX/Bacillus mosquitocidal toxin MTX2; This family appears to be ...
 164-282 4.33e-12

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: 64.73  E-value: 4.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370940691 164 QTVTND-SLQPQVSSITGSATVTETTGWSGSLSVKVGVSTSFKTGIPFVAEGKVKVSVEV----TNTYTWNGSTSQsKTW 238
Cdd:pfam03318  34 NTLTNNtDSTQTLQTQSFSKKVTTTTSTTTTHGFKIGAKASGKFGIPFVAEGGITLSVSGeynfSSTTTNTTSVTT-TYW 112

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1370940691 239 GFNTPVSVAPHTVIVALVTATISTIAVPYTMTGTVILKSGIRLP 282
Cdd:pfam03318 113 VPSQKVTVPPHTTVRVTLVLYKTTYSVPVDLYTTLSGTFSIEGT 156
PFM_Dln1-like cd20221
pore-forming module of Danio rerio Dln1, and similar aerolysin-type beta-barrel pore-forming ...
 143-305 6.94e-12

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: 63.16  E-value: 6.94e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370940691 143 NIEYDVAAAKILQSGPAELYRQTVTNDSLQPQVSSITGSATVTETTGWSGSLSVKVGVSTSFKTGIPFVAEGKVKVSVEV 222
Cdd:cd20221     7 NVNYPTLHQVIPQVAVEEIKSMSYENDTSVPQEYTIETSKKITKTSSWSVTNKLESTFSVEVSAGIPEVVEVSTGFSLTV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370940691 223 TNTYTWNGSTSQSKTWGFNTPVSVAPHTVIVALVTATISTIAVPYTMTGTVILKSGIRLpNRKIKGTYLGTNSHDLTVRF 302
Cdd:cd20221    87 GVESTHSLENTEEKTETLSFPVKVPPGKTVDVEITIGRATVDLPYTGTVKITCYNGSVL-KFPTSGIYKGVTYTDAKVVV 165


                  ...
gi 1370940691 303 VQQ 305
Cdd:cd20221   166 KEK 168
PFM_Cry51Aa-like cd20226
pore-forming module of Bacillus thuringiensis insecticidal Cry51A toxin, Bacillus ...
 163-276 8.23e-12

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: 62.68  E-value: 8.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370940691 163 RQTVTNDSLQPQVSSITGSATVTETT------GWSGSLSVKVgvSTSFKTGIPFVAEGKVKVSVEVTNTYtwNGSTSQ-- 234
Cdd:cd20226    26 RQVITNNTSVPQSQTVSFSEKTTETTstttteGYKIGTSIKS--TTKFKVKFGFVVGGEQSIEVSVSFEY--NYSTTTty 101

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1370940691 235 ----SKTWGFNTPVSVAPHTVIVALVTATISTIAVPYTMTGTVILK 276
Cdd:cd20226   102 ttttEKLWEDTQPVTVPPRTKVTATLIIYGGPFNVPVTLNCTISLN 147
PFM_LIN24-like cd20237
pore-forming module of Caenorhabditis elegans LIN-24 and similar aerolysin-type beta-barrel ...
 157-254 1.77e-11

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: 60.67  E-value: 1.77e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370940691 157 GPAELYRQTVTNDSLQPQVSSITGSATVTETTGWSGSLSVKVGVSTSFKTGIPF-VAEGKVKVSVEVTNTYTWNGSTSQS 235
Cdd:cd20237     1 KSVVLFKTTFTNNTSTEQEYTFKTERTTTSSCTWSVTEGFTIGGEVSLKLGPPPdIAEANAGFSRELSLSKTQEETFEEE 80

                          90
                  ....*....|....*....
gi 1370940691 236 KTWGFNTPVSVAPHTVIVA 254
Cdd:cd20237    81 LTWSVDSQVTVPPKTKVTA 99
PFM_parasporin-2-like cd20222
pore-forming module of parasporin-2, hydralysin and similar aerolysin-type beta-barrel ...
 158-273 2.18e-09

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: 55.41  E-value: 2.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370940691 158 PAELYRQTVTNDS---LQPQVSSITGSATVTETTGWSGSlsVKVGVStsFKTGIPFVAEGKVKVSVEVTNTYTWNGSTSQ 234
Cdd:cd20222    14 PDILGTTEAVNNGdeeEITVTYSYKVGGKWTWKTSWSSS--STTGAT--FSSGIPLEGVFEVGTEFSVSGTTGESGSTST 89

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1370940691 235 SKTWGFNTPVSVAPHT-VIVALVTaTISTIAVPYT-MTGTV 273
Cdd:cd20222    90 EKTLTSSVTVKVPPNSkVKITMVT-KMKKSSVNYTvEKGTI 129
PFM_agglutinin-like cd20217
pore-forming module (PFM) of uncharacterized proteins which have agglutatin domain(s), and ...
 158-297 5.86e-09

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


Pssm-ID: 380787 [Multi-domain]  Cd Length: 150  Bit Score: 54.05  E-value: 5.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370940691 158 PAELYRQTVTNDSLQPQ--VSSITGSATVTETTGWSGSLSVKVGVSTSFKTGIPFVA--EGKVKVSVEVTNTYTWNGSTS 233
Cdd:cd20217     1 PLVVGQGSATNNGSEPAdmQVQVTLTETVSTSRTWSNSFTFSQSISTTFTAGVPEIAsaETTITIGAEQTFGTEWGETTE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370940691 234 QSKTWGFNTPV-SVAPHTVIVALVTATISTIAVPYTMTGTVILKSGIRLPN-RKIKGTYLGTNSHD 297
Cdd:cd20217    81 EAVQFQSTYLVkDVPPGEEATVTVECSTGKCRVPFTYKTRDTRLDGVDRPTvDEIDGVFEGVSAYN 146
PFM_jacalin-like cd20231
pore-forming module of uncharacterized proteins which have an N-terminal jacalin-like lectin ...
 158-278 1.53e-08

pore-forming module of uncharacterized proteins which have an N-terminal jacalin-like lectin domain, and similar aerolysin-type beta-barrel pore-forming proteins; Jacalin-like lectins are sugar-binding protein domains. Proteins having these lectin domains may bind mono- or oligosaccharides with high specificity. Generally, pore-forming proteins (PFPs) are secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores detrimental to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel. Many of this family are bacterial toxins. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin).


Pssm-ID: 380801 [Multi-domain]  Cd Length: 150  Bit Score: 53.13  E-value: 1.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370940691 158 PAELYRQTVTNDSLQPQVS-SITGSATVTETTGWSGSLSVKVGVSTSFKTGIPFVAEG-KVKVSVEVTNTYTWNGSTSQS 235
Cdd:cd20231     4 PVTLDSFLPTNNSTDYTWTfSGSRTKTTSRTWSQSSTSGFELSVSVSVSAGIPEIGEAvTTSAGWSLSATSSESETETTT 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1370940691 236 KTWGFNTPVSVAPHTVIVALVTATISTIAVPYTMTGTVILKSG 278
Cdd:cd20231    84 DELGWSVSGTLPPGEGVKCRATAQEGKLDSDYTSTVTVTLQDG 126
PFM_epsilon-toxin-like cd20223
pore-forming module of Clostridium perfringens epsilon-toxin and similar aerolysin-type ...
 165-268 1.99e-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: 1.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370940691 165 TVTNDSLQPQV-SSITGSATVTETTGWSGSLSVKVGVSTSFKTGIPFVAEGKVKVSVEVTNTYTWNGSTSQSKTWGFNT- 242
Cdd:cd20223    21 TLTNDTDEEQTlKTPSFSKTVTDTVTTTTTNGFKLGVSTSAKFKIPFPGGGSTELSAEYNFSTTNTNTTSETKTYTAPSq 100

                          90       100
                  ....*....|....*....|....*....
gi 1370940691 243 PVSVAPHT---VIVALVTATISTIAVPYT 268
Cdd:cd20223   101 TIKVPPGKtykVTVYLKKVKFSGTVGTFT 129
B_lectin cd00028
Bulb-type mannose-specific lectin. The domain contains a three-fold internal repeat ...
 8-128 5.37e-08

Bulb-type mannose-specific lectin. The domain contains a three-fold internal repeat (beta-prism architecture). The consensus sequence motif QXDXNXVXY is involved in alpha-D-mannose recognition. Lectins are carbohydrate-binding proteins which specifically recognize diverse carbohydrates and mediate a wide variety of biological processes, such as cell-cell and host-pathogen interactions, serum glycoprotein turnover, and innate immune responses.


Pssm-ID: 237995  Cd Length: 116  Bit Score: 50.77  E-value: 5.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370940691   8 LKSGQYLgtqdilVSNNGLF------FAALQPDGNLCVYRGTGPGdnlgLLWSSRTSAGPIGQYFLAMQGDGNLCVYKGT 81
Cdd:cd00028     4 LSSGQTL------VSSGSLFelgffkLIMQSRDYNLILYKGSSRT----VVWVANRDNPSGSSCTLTLQSDGNLVIYDGS 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1370940691  82 GpqdnkGFFWGSQSSRQTGEYFVVLQDDGNFCIYkgtapENNQGFVW 128
Cdd:cd00028    74 G-----TVVWSSNTTRVNGNYVLVLLDDGNLVLY-----DSDGNFLW 110
B_lectin smart00108
Bulb-type mannose-specific lectin;
12-130 2.24e-07

Bulb-type mannose-specific lectin;


Pssm-ID: 214519 [Multi-domain]  Cd Length: 114  Bit Score: 48.85  E-value: 2.24e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370940691   12 QYLGTQDILVSNNGLFFA-----ALQPDGNLCVYRGTGPGdnlgLLWSS-RTSAGPiGQYFLAMQGDGNLCVYKGTGPqd 85
Cdd:smart00108   2 NTLSSGQTLVSGNSLFELgfftlIMQNDYNLILYKSSSRT----VVWVAnRDNPVS-DSCTLTLQSDGNLVLYDGDGR-- 74

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1370940691   86 nkgFFWGSQSSRQTGEYFVVLQDDGNFCIYkgtapENNQGFVWGT 130
Cdd:smart00108  75 ---VVWSSNTTGANGNYVLVLLDDGNLVIY-----DSDGNFLWQS 111
PFM_spherulin-2a-like cd20235
pore-forming module of Physarum polycephalum spherulin-2a, Plodia interpunctella follicular ...
 158-274 2.74e-06

pore-forming module of Physarum polycephalum spherulin-2a, Plodia interpunctella follicular epithelium yolk protein subunit YP4, and similar aerolysin-type beta-barrel pore-forming proteins; Spherulin 2a is a coat glycoprotein produced during encystment from the slime mold, Physarum polycephalum. YP4, is one of two subunits of the follicular epithelium yolk protein from Plodia interpunctella and other pyralid moths; it is produced in the follicle cells during vitellogenesis, and after secretion it is taken up into the oocyte and stored in the yolk spheres for utilization during embryogenesis. Members of this group belong to the aerolysin family of beta-pore-forming proteins (beta-PFPs). PFPs are generally secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores harmful to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel, are found in all kingdoms of life and many are bacterial toxins. In addition to having a role in microbial infection, they have potential as biotechnological sensors and delivery systems. They share a similar monomeric architecture, with a variable membrane-binding domain and a structurally conserved pore-forming region. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin).


Pssm-ID: 380805  Cd Length: 150  Bit Score: 46.44  E-value: 2.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370940691 158 PAELYRQTVTNDSLQPQVSSITGSATVTET--TGWSGSlsVKVGVSTSFKTGIPF-VAEGKVKVSVEVTNTYTWNGSTSQ 234
Cdd:cd20235     1 PVIVKTQEFVNNSSKPATFNAGISQSVENTvsSTWSKS--GEVSVGQSINYGVNFlGSGGGGETSFSYTSSWGESTTKSE 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1370940691 235 SKTWGFNTPVSV--APHTVIVALVTATIST--IAVPY--TMTGTVI 274
Cdd:cd20235    79 TVTVGSTSGVEVtlEPGQAVTAELTATKGTmkVEVTYeaTLSGSVA 124
Aerolysin pfam01117
Aerolysin toxin; This family represents the pore forming lobe of aerolysin.
 88-273 5.78e-06

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


Pssm-ID: 366474  Cd Length: 359  Bit Score: 47.64  E-value: 5.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370940691  88 GFFW-GSQSSRQTGEYFVVLQDDGNFCIykgTApeNNQGFVWGTQVVDPVAnVETGNIEYDVAAAKILQSGPAELYRQ-- 164
Cdd:pfam01117  29 GYGWcGGTRSQYVGEDFVVTRNGDSWLV---EA--NNNGPCNGYRCDHRLK-MHFSDFKFGVKPSSLKYGDPVISDREpy 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370940691 165 -----TVTNDSLQPQVSSITGSATvtETTGWSGSLSVKVGVSTSFKTGIPFVAEGKVKVSVEVTNTYTWNGST--SQSKT 237
Cdd:pfam01117 103 kyivgYARNDSDTPQQRVLTLSYD--EVTNWSKTDTYKYSEKVTIKNKYKFPLIGETELSLELGANQSWATTNgnSSTKT 180

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1370940691 238 WGFNTPVSVAPHTVIVALVTATISTIAVPYTMTGTV 273
Cdd:pfam01117 181 ISDVARVLVPANTKIPVRLKLEKARVDYPYEFNAQV 216
PFM_aerolysin_family cd10140
pore-forming module of aerolysin-type beta-barrel pore-forming proteins; Pore-forming proteins ...
 219-294 1.04e-04

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


Pssm-ID: 380782  Cd Length: 92  Bit Score: 40.61  E-value: 1.04e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370940691 219 SVEVTNTYTwngsTSQSKTWGFNTPVSVAPHTVIVALVTATISTIAVPYTMTGTVILKSGIRLPNRKIKGTYLGTN 294
Cdd:cd10140    14 STTQTQTVT----LSETKTVSVTVTVTVPPGKTVKVTVTVTKAKIDVPYTATLKATYSTSGTGTTGTVSGVFTGVN 85
PFM_alpha-toxin-like cd20224
pore-forming module of Clostridium septicum alpha-toxin and similar aerolysin-type beta-barrel ...
 176-237 1.16e-04

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: 41.21  E-value: 1.16e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370940691 176 SSITGSATVTETTGWSG----SLSVKVGVSTSFKTGIPFVAEGKVKVSVEVTNTYTWNGSTSQSKT 237
Cdd:cd20224    17 DTGTATFNYTESTSWSKtdnfKFSEGIKVTVKFTVGIPLIGGAESETEFSFNAEQGWSDSTGNTET 82
PFM_fascin-like cd20234
pore-forming module (PFM) of uncharacterized proteins which have N-terminal fascin-like domain, ...
 158-270 1.87e-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: 38.27  E-value: 1.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370940691 158 PAELYRQTVTNDSLQPQVSSITGS--ATVTETTGWSGSLSVkvGVSTSFktgiPFVAEGKvKVSVEVTNTYTWNGSTSQS 235
Cdd:cd20234     1 PTVVKKESYTNRSSVPQKHTFNMSwtKQCTETTFWNHTWGL--NLTSSC----EFSVENA-TLTVTYLGDNQRISSTTRS 73

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1370940691 236 KTWGFNTPVSVAPHTVIVA-LVTATISTIAVPYTMT 270
Cdd:cd20234    74 ITEKESTEVTVPPHTKVTAnLYVSKQENASIPFTAV 109
 
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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