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Conserved domains on  [gi|665403662|ref|NP_001286875|]
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unzipped, isoform B [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PFM_unzipped-like cd20233
pore-forming module (PFM) of proteins having a DUF3421 domain including Drosophila unzipped, ...
 233-367 2.09e-73

pore-forming module (PFM) of proteins having a DUF3421 domain including Drosophila unzipped, honey bee anarchy 1, and similar aerolysin-type beta-barrel pore-forming proteins; Many proteins belonging to this group have N-terminal DUF3421. Drosophila melanogaster unzipped protein is required for normal axon patterning during neurogenesis, and honey bee anarchy 1 may play a role in worker sterility in a social insect. 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: 380803  Cd Length: 134  Bit Score: 227.80  E-value: 2.09e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665403662 233 MTELVTRKLENLEDKYSTVETILSYTFNYNQYWGSHEGVARGLPTKIFEKDEAVPAEINWALKHTEKRSENKAVHTKLWP 312
Cdd:cd20233    1 PTELGNATIVNNGDEAATMATAFTYTYNYSIYWGQGHAILKGLNTSIYLTNGTALSNIMWGTKETTNRTDTYTVETMLEP 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 665403662 313 GTAINVTLRGNYVTLEAPYSGKLFAfYYGSDESVSRKISAEVRKSYLKEVKLEFS 367
Cdd:cd20233   81 GTGINVTLRGNYTDMEVPYSGKLIS-HYEDGETVSRKISGIRVEETMFDVKPEFG 134
 
Name Accession Description Interval E-value
PFM_unzipped-like cd20233
pore-forming module (PFM) of proteins having a DUF3421 domain including Drosophila unzipped, ...
 233-367 2.09e-73

pore-forming module (PFM) of proteins having a DUF3421 domain including Drosophila unzipped, honey bee anarchy 1, and similar aerolysin-type beta-barrel pore-forming proteins; Many proteins belonging to this group have N-terminal DUF3421. Drosophila melanogaster unzipped protein is required for normal axon patterning during neurogenesis, and honey bee anarchy 1 may play a role in worker sterility in a social insect. 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: 380803  Cd Length: 134  Bit Score: 227.80  E-value: 2.09e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665403662 233 MTELVTRKLENLEDKYSTVETILSYTFNYNQYWGSHEGVARGLPTKIFEKDEAVPAEINWALKHTEKRSENKAVHTKLWP 312
Cdd:cd20233    1 PTELGNATIVNNGDEAATMATAFTYTYNYSIYWGQGHAILKGLNTSIYLTNGTALSNIMWGTKETTNRTDTYTVETMLEP 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 665403662 313 GTAINVTLRGNYVTLEAPYSGKLFAfYYGSDESVSRKISAEVRKSYLKEVKLEFS 367
Cdd:cd20233   81 GTGINVTLRGNYTDMEVPYSGKLIS-HYEDGETVSRKISGIRVEETMFDVKPEFG 134
 
Name Accession Description Interval E-value
PFM_unzipped-like cd20233
pore-forming module (PFM) of proteins having a DUF3421 domain including Drosophila unzipped, ...
 233-367 2.09e-73

pore-forming module (PFM) of proteins having a DUF3421 domain including Drosophila unzipped, honey bee anarchy 1, and similar aerolysin-type beta-barrel pore-forming proteins; Many proteins belonging to this group have N-terminal DUF3421. Drosophila melanogaster unzipped protein is required for normal axon patterning during neurogenesis, and honey bee anarchy 1 may play a role in worker sterility in a social insect. 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: 380803  Cd Length: 134  Bit Score: 227.80  E-value: 2.09e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665403662 233 MTELVTRKLENLEDKYSTVETILSYTFNYNQYWGSHEGVARGLPTKIFEKDEAVPAEINWALKHTEKRSENKAVHTKLWP 312
Cdd:cd20233    1 PTELGNATIVNNGDEAATMATAFTYTYNYSIYWGQGHAILKGLNTSIYLTNGTALSNIMWGTKETTNRTDTYTVETMLEP 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 665403662 313 GTAINVTLRGNYVTLEAPYSGKLFAfYYGSDESVSRKISAEVRKSYLKEVKLEFS 367
Cdd:cd20233   81 GTGINVTLRGNYTDMEVPYSGKLIS-HYEDGETVSRKISGIRVEETMFDVKPEFG 134
 
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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