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Conserved domains on  [gi|1811667868|gb|KAF2731385|]
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hypothetical protein EJ04DRAFT_579188 [Polyplosphaeria fusca]

Protein Classification

Graphical summary

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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 ...
 200-351 4.59e-39

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: 136.33  E-value: 4.59e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811667868 200 GLDTVILDYADHTNDHPEanETFTFGKSETRTATKKYSTTATHTFGWSNAIELSGKILDLGASSTTTLSYGYSNAQTEES 279
Cdd:cd20231     1 GIVPVTLDSFLPTNNSTD--YTWTFSGSRTKTTSRTWSQSSTSGFELSVSVSVSAGIPEIGEAVTTSAGWSLSATSSESE 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1811667868 280 STENSVTLTYTVATMLKPGQRVFCRATAMGGKYKGDYSSNINIWLEDGDTFTFTERGTMEQVNWSKASSVCQ 351
Cdd:cd20231    79 TETTTDELGWSVSGTLPPGEGVKCRATAQEGKLDSDYTSTVTVTLQDGETFSFPEPGTFKGVGYSEVDVVCK 150
Jacalin_like super family cl03205
Jacalin-like lectin domain; Jacalin-like lectins are sugar-binding protein domains mostly ...
 55-171 1.64e-05

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: 43.93  E-value: 1.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811667868  55 GTVITGVEVWAnDKTVRAIQFYFSDGTNSQQWGkpDGNKHArmdwdSAVDQIGQ-------IKTWGNGKGQSLGRVYIRT 127
Cdd:cd09302    11 GARLTEIRVRS-GGAVDAIRVVLRDYTDGRHGG--NGGPNT-----SSVFLDPGeyititsVSSGDNGGGTRIDAIQFTT 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1811667868 128 KSGKELDVGKDTSGQDTFETNVASGVMLGAFGTAGDVIDSLGFI 171
Cdd:cd09302    83 NKGRSGTYGTTSGALGTEFTVPVGGEIVGIYGRAGDDVDAFGFI 126
 
Name Accession Description Interval E-value
PFM_jacalin-like cd20231
pore-forming module of uncharacterized proteins which have an N-terminal jacalin-like lectin ...
 200-351 4.59e-39

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: 136.33  E-value: 4.59e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811667868 200 GLDTVILDYADHTNDHPEanETFTFGKSETRTATKKYSTTATHTFGWSNAIELSGKILDLGASSTTTLSYGYSNAQTEES 279
Cdd:cd20231     1 GIVPVTLDSFLPTNNSTD--YTWTFSGSRTKTTSRTWSQSSTSGFELSVSVSVSAGIPEIGEAVTTSAGWSLSATSSESE 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1811667868 280 STENSVTLTYTVATMLKPGQRVFCRATAMGGKYKGDYSSNINIWLEDGDTFTFTERGTMEQVNWSKASSVCQ 351
Cdd:cd20231    79 TETTTDELGWSVSGTLPPGEGVKCRATAQEGKLDSDYTSTVTVTLQDGETFSFPEPGTFKGVGYSEVDVVCK 150
Jacalin_like cd09302
Jacalin-like lectin domain; Jacalin-like lectins are sugar-binding protein domains mostly ...
 55-171 1.64e-05

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: 43.93  E-value: 1.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811667868  55 GTVITGVEVWAnDKTVRAIQFYFSDGTNSQQWGkpDGNKHArmdwdSAVDQIGQ-------IKTWGNGKGQSLGRVYIRT 127
Cdd:cd09302    11 GARLTEIRVRS-GGAVDAIRVVLRDYTDGRHGG--NGGPNT-----SSVFLDPGeyititsVSSGDNGGGTRIDAIQFTT 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1811667868 128 KSGKELDVGKDTSGQDTFETNVASGVMLGAFGTAGDVIDSLGFI 171
Cdd:cd09302    83 NKGRSGTYGTTSGALGTEFTVPVGGEIVGIYGRAGDDVDAFGFI 126
ETX_MTX2 pfam03318
Clostridium epsilon toxin ETX/Bacillus mosquitocidal toxin MTX2; This family appears to be ...
 177-316 6.82e-04

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: 40.47  E-value: 6.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811667868 177 IEKITVSDIVFDETPEalNAQQEGLDTVILDYADHTNDHPEANeTFTFGKSETRTAtkkySTTATHTFGWSNAIELSGKI 256
Cdd:pfam03318   7 PSYINFNTTVLIEETT--VKTLTPLYTGSNTLTNNTDSTQTLQ-TQSFSKKVTTTT----STTTTHGFKIGAKASGKFGI 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1811667868 257 ---LDLGASSTTTLSYGYSNAQTeessTENSVTLTYTVAT---MLKPGQRVFCRATAMGGKYKGDY 316
Cdd:pfam03318  80 pfvAEGGITLSVSGEYNFSSTTT----NTTSVTTTYWVPSqkvTVPPHTTVRVTLVLYKTTYSVPV 141
 
Name Accession Description Interval E-value
PFM_jacalin-like cd20231
pore-forming module of uncharacterized proteins which have an N-terminal jacalin-like lectin ...
 200-351 4.59e-39

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: 136.33  E-value: 4.59e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811667868 200 GLDTVILDYADHTNDHPEanETFTFGKSETRTATKKYSTTATHTFGWSNAIELSGKILDLGASSTTTLSYGYSNAQTEES 279
Cdd:cd20231     1 GIVPVTLDSFLPTNNSTD--YTWTFSGSRTKTTSRTWSQSSTSGFELSVSVSVSAGIPEIGEAVTTSAGWSLSATSSESE 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1811667868 280 STENSVTLTYTVATMLKPGQRVFCRATAMGGKYKGDYSSNINIWLEDGDTFTFTERGTMEQVNWSKASSVCQ 351
Cdd:cd20231    79 TETTTDELGWSVSGTLPPGEGVKCRATAQEGKLDSDYTSTVTVTLQDGETFSFPEPGTFKGVGYSEVDVVCK 150
PFM_epsilon-toxin-like cd20223
pore-forming module of Clostridium perfringens epsilon-toxin and similar aerolysin-type ...
 195-326 7.05e-07

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: 48.38  E-value: 7.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811667868 195 NAQQEGLDTVILDYADHTNDHPEANETFTFGKSETRTATKKYSTTATHTFGWSNAIELSGKILdLGASSTTTLSYGYSNA 274
Cdd:cd20223     6 DPKITNGEPLYVGSNTLTNDTDEEQTLKTPSFSKTVTDTVTTTTTNGFKLGVSTSAKFKIPFP-GGGSTELSAEYNFSTT 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1811667868 275 QTEESSTENSVTL-----------TYTVATMLKPGQrvfcrATAMGGKYKGDYSSNINIWLED 326
Cdd:cd20223    85 NTNTTSETKTYTApsqtikvppgkTYKVTVYLKKVK-----FSGTVGTFTGVYGTDFTVKVKD 142
Jacalin_like cd09302
Jacalin-like lectin domain; Jacalin-like lectins are sugar-binding protein domains mostly ...
 55-171 1.64e-05

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: 43.93  E-value: 1.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811667868  55 GTVITGVEVWAnDKTVRAIQFYFSDGTNSQQWGkpDGNKHArmdwdSAVDQIGQ-------IKTWGNGKGQSLGRVYIRT 127
Cdd:cd09302    11 GARLTEIRVRS-GGAVDAIRVVLRDYTDGRHGG--NGGPNT-----SSVFLDPGeyititsVSSGDNGGGTRIDAIQFTT 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1811667868 128 KSGKELDVGKDTSGQDTFETNVASGVMLGAFGTAGDVIDSLGFI 171
Cdd:cd09302    83 NKGRSGTYGTTSGALGTEFTVPVGGEIVGIYGRAGDDVDAFGFI 126
PFM_physalysin-1-like cd20219
pore-forming module of Physella acuta physalysin1 and similar aerolysin-type beta-barrel ...
 212-297 4.20e-04

pore-forming module of Physella acuta physalysin1 and similar aerolysin-type beta-barrel pore-forming proteins; From a comparative immunological study of the snail Physella acuta, physalysin1 was identified as one of three physalysins in the snail. 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: 380789  Cd Length: 125  Bit Score: 40.00  E-value: 4.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811667868 212 TNDHP-EANETFTFGKSETRTATkkYSTTAThtfgWSNAIELSGKI-------LDLGASSTTTLSYGYSNAQTEESSTEN 283
Cdd:cd20219    10 YNEDStPVTHTIERSKTVTRTVT--HSTTSS----WKNSHELGISLsysppglTGFSGSASYKFNYEYSSSTTDENSNTQ 83

                          90
                  ....*....|....
gi 1811667868 284 SVTLTYTVATMLKP 297
Cdd:cd20219    84 SQTFKVTSSKTIPP 97
ETX_MTX2 pfam03318
Clostridium epsilon toxin ETX/Bacillus mosquitocidal toxin MTX2; This family appears to be ...
 177-316 6.82e-04

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: 40.47  E-value: 6.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811667868 177 IEKITVSDIVFDETPEalNAQQEGLDTVILDYADHTNDHPEANeTFTFGKSETRTAtkkySTTATHTFGWSNAIELSGKI 256
Cdd:pfam03318   7 PSYINFNTTVLIEETT--VKTLTPLYTGSNTLTNNTDSTQTLQ-TQSFSKKVTTTT----STTTTHGFKIGAKASGKFGI 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1811667868 257 ---LDLGASSTTTLSYGYSNAQTeessTENSVTLTYTVAT---MLKPGQRVFCRATAMGGKYKGDY 316
Cdd:pfam03318  80 pfvAEGGITLSVSGEYNFSSTTT----NTTSVTTTYWVPSqkvTVPPHTTVRVTLVLYKTTYSVPV 141
 
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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