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Conserved domains on  [gi|2086767960|ref|XP_043186787|]
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uncharacterized protein RhiXN_12211 [Rhizoctonia solani]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PFM_aerolysin_family super family cl40431
pore-forming module of aerolysin-type beta-barrel pore-forming proteins; Pore-forming proteins ...
 97-213 6.71e-03

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.


The actual alignment was detected with superfamily member cd20231:

Pssm-ID: 394801 [Multi-domain]  Cd Length: 150  Bit Score: 36.56  E-value: 6.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2086767960  97 PTTVDLIDKSNNAPG-TVTINVQSGTKTSTTLTETDSLATAAGVSMTMSGSIPLVG-KVSTTVSFTETYTKTYGKSQTFE 174
Cdd:cd20231     4 PVTLDSFLPTNNSTDyTWTFSGSRTKTTSRTWSQSSTSGFELSVSVSVSAGIPEIGeAVTTSAGWSLSATSSESETETTT 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2086767960 175 TNTLTSISraINIGSGNS-NCTAkltttTCQheaRGKYPI 213
Cdd:cd20231    84 DELGWSVS--GTLPPGEGvKCRA-----TAQ---EGKLDS 113
 
Name Accession Description Interval E-value
PFM_jacalin-like cd20231
pore-forming module of uncharacterized proteins which have an N-terminal jacalin-like lectin ...
 97-213 6.71e-03

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: 36.56  E-value: 6.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2086767960  97 PTTVDLIDKSNNAPG-TVTINVQSGTKTSTTLTETDSLATAAGVSMTMSGSIPLVG-KVSTTVSFTETYTKTYGKSQTFE 174
Cdd:cd20231     4 PVTLDSFLPTNNSTDyTWTFSGSRTKTTSRTWSQSSTSGFELSVSVSVSAGIPEIGeAVTTSAGWSLSATSSESETETTT 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2086767960 175 TNTLTSISraINIGSGNS-NCTAkltttTCQheaRGKYPI 213
Cdd:cd20231    84 DELGWSVS--GTLPPGEGvKCRA-----TAQ---EGKLDS 113
 
Name Accession Description Interval E-value
PFM_jacalin-like cd20231
pore-forming module of uncharacterized proteins which have an N-terminal jacalin-like lectin ...
 97-213 6.71e-03

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: 36.56  E-value: 6.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2086767960  97 PTTVDLIDKSNNAPG-TVTINVQSGTKTSTTLTETDSLATAAGVSMTMSGSIPLVG-KVSTTVSFTETYTKTYGKSQTFE 174
Cdd:cd20231     4 PVTLDSFLPTNNSTDyTWTFSGSRTKTTSRTWSQSSTSGFELSVSVSVSAGIPEIGeAVTTSAGWSLSATSSESETETTT 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2086767960 175 TNTLTSISraINIGSGNS-NCTAkltttTCQheaRGKYPI 213
Cdd:cd20231    84 DELGWSVS--GTLPPGEGvKCRA-----TAQ---EGKLDS 113
 
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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