NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1407815475|gb|RAL07684|]
View 

hypothetical protein BO97DRAFT_463410 [Aspergillus homomorphus CBS 101889]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PFM_jacalin-like cd20231
pore-forming module of uncharacterized proteins which have an N-terminal jacalin-like lectin ...
 164-307 9.84e-42

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: 141.72  E-value: 9.84e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407815475 164 THITLDTQDFDGNH-EYEWDFHGSKTKTTTSTWSQTLAS--SFDLQVKVKAGVPELAE-VESTIKWGLSASSTHSQAEQD 239
Cdd:cd20231     3 VPVTLDSFLPTNNStDYTWTFSGSRTKTTSRTWSQSSTSgfELSVSVSVSAGIPEIGEaVTTSAGWSLSATSSESETETT 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1407815475 240 SSEIGWDVHSTVSPGQTVHCEAYCFQGTSDVDYTSTVTVTFQSGETLQFKESGTFSGVTYSEAKTTVN 307
Cdd:cd20231    83 TDELGWSVSGTLPPGEGVKCRATAQEGKLDSDYTSTVTVTLQDGETFSFPEPGTFKGVGYSEVDVVCK 150
Jacalin_like super family cl03205
Jacalin-like lectin domain; Jacalin-like lectins are sugar-binding protein domains mostly ...
 25-137 1.34e-09

Jacalin-like lectin domain; Jacalin-like lectins are sugar-binding protein domains mostly found in plants. They adopt a beta-prism topology consistent with a circularly permuted three-fold repeat of a structural motif. Proteins containing this domain may bind mono- or oligosaccharides with high specificity. The domain can occur in tandem-repeat arrangements with up to six copies, and in architectures combined with a variety of other functional domains. Taxonomic distribution is not restricted to plants, the domain is also found in various mammalian proteins, for example.


The actual alignment was detected with superfamily member cd09302:

Pssm-ID: 446042  Cd Length: 128  Bit Score: 55.49  E-value: 1.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407815475  25 DKGAMVEEIIVWKeGNILRGLKLSWTDGSDStMIGKSSGSSQS-FTFKVKEKCTEMVLR--GNGIGTRCGHIEFKTDQGN 101
Cdd:cd09302     9 GDGARLTEIRVRS-GGAVDAIRVVLRDYTDG-RHGGNGGPNTSsVFLDPGEYITITSVSsgDNGGGTRIDAIQFTTNKGR 86

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1407815475 102 SFSWGDGGSDN---YYMDVGsGFLVGFQGRANLDIDSLG 137
Cdd:cd09302    87 SGTYGTTSGALgteFTVPVG-GEIVGIYGRAGDDVDAFG 124
 
Name Accession Description Interval E-value
PFM_jacalin-like cd20231
pore-forming module of uncharacterized proteins which have an N-terminal jacalin-like lectin ...
 164-307 9.84e-42

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: 141.72  E-value: 9.84e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407815475 164 THITLDTQDFDGNH-EYEWDFHGSKTKTTTSTWSQTLAS--SFDLQVKVKAGVPELAE-VESTIKWGLSASSTHSQAEQD 239
Cdd:cd20231     3 VPVTLDSFLPTNNStDYTWTFSGSRTKTTSRTWSQSSTSgfELSVSVSVSAGIPEIGEaVTTSAGWSLSATSSESETETT 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1407815475 240 SSEIGWDVHSTVSPGQTVHCEAYCFQGTSDVDYTSTVTVTFQSGETLQFKESGTFSGVTYSEAKTTVN 307
Cdd:cd20231    83 TDELGWSVSGTLPPGEGVKCRATAQEGKLDSDYTSTVTVTLQDGETFSFPEPGTFKGVGYSEVDVVCK 150
Jacalin_like cd09302
Jacalin-like lectin domain; Jacalin-like lectins are sugar-binding protein domains mostly ...
 25-137 1.34e-09

Jacalin-like lectin domain; Jacalin-like lectins are sugar-binding protein domains mostly found in plants. They adopt a beta-prism topology consistent with a circularly permuted three-fold repeat of a structural motif. Proteins containing this domain may bind mono- or oligosaccharides with high specificity. The domain can occur in tandem-repeat arrangements with up to six copies, and in architectures combined with a variety of other functional domains. Taxonomic distribution is not restricted to plants, the domain is also found in various mammalian proteins, for example.


Pssm-ID: 187706  Cd Length: 128  Bit Score: 55.49  E-value: 1.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407815475  25 DKGAMVEEIIVWKeGNILRGLKLSWTDGSDStMIGKSSGSSQS-FTFKVKEKCTEMVLR--GNGIGTRCGHIEFKTDQGN 101
Cdd:cd09302     9 GDGARLTEIRVRS-GGAVDAIRVVLRDYTDG-RHGGNGGPNTSsVFLDPGEYITITSVSsgDNGGGTRIDAIQFTTNKGR 86

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1407815475 102 SFSWGDGGSDN---YYMDVGsGFLVGFQGRANLDIDSLG 137
Cdd:cd09302    87 SGTYGTTSGALgteFTVPVG-GEIVGIYGRAGDDVDAFG 124
 
Name Accession Description Interval E-value
PFM_jacalin-like cd20231
pore-forming module of uncharacterized proteins which have an N-terminal jacalin-like lectin ...
 164-307 9.84e-42

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: 141.72  E-value: 9.84e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407815475 164 THITLDTQDFDGNH-EYEWDFHGSKTKTTTSTWSQTLAS--SFDLQVKVKAGVPELAE-VESTIKWGLSASSTHSQAEQD 239
Cdd:cd20231     3 VPVTLDSFLPTNNStDYTWTFSGSRTKTTSRTWSQSSTSgfELSVSVSVSAGIPEIGEaVTTSAGWSLSATSSESETETT 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1407815475 240 SSEIGWDVHSTVSPGQTVHCEAYCFQGTSDVDYTSTVTVTFQSGETLQFKESGTFSGVTYSEAKTTVN 307
Cdd:cd20231    83 TDELGWSVSGTLPPGEGVKCRATAQEGKLDSDYTSTVTVTLQDGETFSFPEPGTFKGVGYSEVDVVCK 150
PFM_Dln1-like cd20221
pore-forming module of Danio rerio Dln1, and similar aerolysin-type beta-barrel pore-forming ...
 195-306 9.25e-18

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: 78.95  E-value: 9.25e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407815475 195 WSQTLASSFDLQVKVKAGVPELAEVESTIKWGLSASSTHS--QAEQDSSEIGWDVhsTVSPGQTVHCEAYCFQGTSDVDY 272
Cdd:cd20221    54 WSVTNKLESTFSVEVSAGIPEVVEVSTGFSLTVGVESTHSleNTEEKTETLSFPV--KVPPGKTVDVEITIGRATVDLPY 131

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1407815475 273 TSTVTVTFQSGETLQFKESGTFSGVTYSEAKTTV 306
Cdd:cd20221   132 TGTVKITCYNGSVLKFPTSGIYKGVTYTDAKVVV 165
Jacalin_like cd09302
Jacalin-like lectin domain; Jacalin-like lectins are sugar-binding protein domains mostly ...
 25-137 1.34e-09

Jacalin-like lectin domain; Jacalin-like lectins are sugar-binding protein domains mostly found in plants. They adopt a beta-prism topology consistent with a circularly permuted three-fold repeat of a structural motif. Proteins containing this domain may bind mono- or oligosaccharides with high specificity. The domain can occur in tandem-repeat arrangements with up to six copies, and in architectures combined with a variety of other functional domains. Taxonomic distribution is not restricted to plants, the domain is also found in various mammalian proteins, for example.


Pssm-ID: 187706  Cd Length: 128  Bit Score: 55.49  E-value: 1.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407815475  25 DKGAMVEEIIVWKeGNILRGLKLSWTDGSDStMIGKSSGSSQS-FTFKVKEKCTEMVLR--GNGIGTRCGHIEFKTDQGN 101
Cdd:cd09302     9 GDGARLTEIRVRS-GGAVDAIRVVLRDYTDG-RHGGNGGPNTSsVFLDPGEYITITSVSsgDNGGGTRIDAIQFTTNKGR 86

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1407815475 102 SFSWGDGGSDN---YYMDVGsGFLVGFQGRANLDIDSLG 137
Cdd:cd09302    87 SGTYGTTSGALgteFTVPVG-GEIVGIYGRAGDDVDAFG 124
PFM_aerolysin_family cd10140
pore-forming module of aerolysin-type beta-barrel pore-forming proteins; Pore-forming proteins ...
 240-305 6.82e-08

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: 49.47  E-value: 6.82e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1407815475 240 SSEIGWDVHSTVSPGQTVHCEAYCFQGTSDVDYTSTVTVTF-QSGETLQFKESGTFSGVTYSEAKTT 305
Cdd:cd10140    26 TKTVSVTVTVTVPPGKTVKVTVTVTKAKIDVPYTATLKATYsTSGTGTTGTVSGVFTGVNYANVETT 92
PFM_tachylectin-like cd20229
pore-forming module (PFM) of uncharacterized proteins having tachylectin domain(s), and ...
 209-300 1.44e-05

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: 44.44  E-value: 1.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407815475 209 VKAGVPELAEVESTIKWGLSASSTHSQAEQDSSEIGWDVHST--VSPGQTVHCEAYCFQGTSDVDYTSTVTVTFQSGETL 286
Cdd:cd20229    50 FKAGIPVIGEEGIKVILDNSTTHQWNFTTTNEREVTFSLTTNvvVPPGKAVRLEASVQKAKIDVPYRAEVITGFGYEVTI 129

                          90
                  ....*....|....
gi 1407815475 287 qfkeSGTFSGVTYS 300
Cdd:cd20229   130 ----TGTWTGVTVY 139
Jacalin_EEP cd09615
Jacalin-like lectin domains of putative endonucleases/exonucleases/phosphatases and related ...
 39-140 1.52e-05

Jacalin-like lectin domains of putative endonucleases/exonucleases/phosphatases and related proteins; Members of this taxonomically diverse family co-occur with metal-dependent endonucleases/exonucleases/phosphatases. They have not been functionally characterized.


Pssm-ID: 187711  Cd Length: 134  Bit Score: 43.93  E-value: 1.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407815475  39 GNILRGLKLSWTDGSDSTMiGKSSGSSQSFTFKVKEKCTEMVL---RGNGiGTRCGHIEFKTDQGNSFSWGDGGSDNYYM 115
Cdd:cd09615    28 GSRVDGVSLTLTAGTTLAH-GGTGGTASSLTLGSGEYLTSATLcqgQKNG-HTRIFYASFTTSTGRTLAGGTTTSDCVTY 105

                          90       100
                  ....*....|....*....|....*.
gi 1407815475 116 DVGSGF-LVGFQGRANLDIDSLGPLF 140
Cdd:cd09615   106 TAPEGWqIVGFHGRAGDEVDKLGVIY 131
PFM_natterin-3-like cd20220
pore-forming module of Thalassophryne nattereri fish venom natterins 1-4, and similar ...
 195-307 9.51e-05

pore-forming module of Thalassophryne nattereri fish venom natterins 1-4, and similar aerolysin-type beta-barrel pore-forming proteins; This group includes 4 of the 5 Thalassophryne nattereri fish venom natterins: natterin-1, -2, -3, and 4. Natterins have kininogenase activity, kallikrein activity, and are allodynic and edema inducing. They also cleave type I and type IV collagen, resulting in necrosis of the affected cells. Contradictory to their edematic activity, Natterins also have anti-inflammatory effects through inhibition of interactions between leukocytes and the endothelium, and reduction in neutrophil accumulation. Many proteins belonging to this group have an N-terminal DUF3421 domain. They belong to the aerolysin family of beta-pore-forming proteins (beta-PFPs). PFPs are generally secreted as water-soluble monomers, which upon binding to target lipid membranes, oligomerize and form transmembrane pores harmful to cells. Beta-PFPs form pores by transmembrane beta-barrels. Aerolysin-type beta-PFPs are believed to use an amphipathic beta-hairpin to form the beta-barrel, are found in all kingdoms of life and many are bacterial toxins. In addition to having a role in microbial infection, they have potential as biotechnological sensors and delivery systems. They share a similar monomeric architecture, with a variable membrane-binding domain and a structurally conserved pore-forming region. A significant portion of the monomeric subunit structure is re-organized to form the pore. Oligomers formed by members of the aerolysin family include: hepta- (aerolysin), octa- (Dln1), and nonameric oligomers (lysenin and monalysin).


Pssm-ID: 380790 [Multi-domain]  Cd Length: 152  Bit Score: 41.84  E-value: 9.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407815475 195 WSQTLASSFDLQVKVKAGVPELAEvestIKWGLSASSTHSQAEQDS-SEIGWDVHS---TVSPGQ--TVHCEAYcfQGTS 268
Cdd:cd20220    38 WDTSFSITLGVSTTITAGIPIIAG----GGWEVSTETTFTWSGGTSvTESVTHSVSvevTVPPNHscTVKMVGY--KYKA 111

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1407815475 269 DVDYTSTVTVTFQSGETLQFKESGTFSGVTYSEAKTTVN 307
Cdd:cd20220   112 DIPFTARLTRTYRNGETHTTTITGTYKGVQVGEVRAVVE 150
PFM_aerolysin-like cd20242
pore-forming module of aerolysin-type beta-barrel pore-forming proteins; uncharacterized ...
 185-308 2.05e-04

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: 40.87  E-value: 2.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407815475 185 GSKTKTTTSTWSQTLASSFDLQVKVKAGVPELAE--------VESTIKWGlsASSTHSQAeqdsseIGWDVHSTVSPGQT 256
Cdd:cd20242    23 GSETVTETSTWEDEVGLKLGVSTSFSAGVPVVAEgkvevsaeVHNNYTWN--GSNTRSKT------WSFSTPVNVPAHSA 94

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1407815475 257 VHCEAYCFQGTSDVDYTSTVTVTFQSGETLQFKESGTFSGVTYSEakTTVNY 308
Cdd:cd20242    95 VRATATVTESTISVPYTLTWKSIFESGARVTGTIEGMYKGSNSHD--LTTNF 144
griffithsin_like cd09614
Jacalin-like lectin domain of griffithsin and related proteins; Griffithsin is a lectin ...
 59-142 2.12e-04

Jacalin-like lectin domain of griffithsin and related proteins; Griffithsin is a lectin isolated from a red alga, which has shown potential as an inhibitor of viral entry, exhibiting antiviral activity against HIV and SARS. The biological functions of griffithsin and griffithsin-like proteins with respect to their source organisms are not known.


Pssm-ID: 187710  Cd Length: 128  Bit Score: 40.46  E-value: 2.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407815475  59 GKSSGS-SQSFTFKVKEKCTEMVLRGngiGTRCGHIEFKTDQGNSF--SWGDGGSDNYYMDVGSGFLVGFQGRANLDIDS 135
Cdd:cd09614    45 GGGGGNlSPTLNFSSGEYITEVTGRS---GDRVDQVQFTTNYGGRTlpGGGGGGSAFTWTVPDNQKVIGFAGRSGSYLDQ 121


                  ....*..
gi 1407815475 136 LGPLFLK 142
Cdd:cd09614   122 LQVYYLS 128
PFM_aerolysin-like cd20240
pore-forming module of aerolysin-type beta-barrel pore-forming proteins; uncharacterized ...
 192-306 6.92e-03

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: 36.47  E-value: 6.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407815475 192 TSTWSQTLASSFDLQVKVKAGVPELAEVESTIKWGLSASSTHSQAEQDSSEIGWDVHSTVSPGQTVHCEAYCFQGTSDVD 271
Cdd:cd20240    34 TSSFSETEGVSTTVSTSLKVGIPFIAGGEITTTTTTSQSWTYGKSETKTDTISYTFPIVVPPNTTVTATAVVTKYNMDVT 113

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1407815475 272 YTSTVtVTFQSGETlqFKESGTFSGVTYSEAKTTV 306
Cdd:cd20240   114 YVATL-RGINTGKR--IKIKGKWSGVDCTDISYNL 145
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH