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Conserved domains on  [gi|1279803595|ref|XP_022955116|]
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RPM1-interacting protein 4-like [Cucurbita moschata]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AvrRpt-cleavage super family cl05281
Cleavage site for pathogenic type III effector avirulence factor Avr; This domain is conserved ...
124-155 4.45e-10

Cleavage site for pathogenic type III effector avirulence factor Avr; This domain is conserved in small families of otherwise unrelated proteins in both mono-cots and di-cots, suggesting that it has a conserved, plant-specific function. It is found both in the plant RIN4 (resistance R membrane-bound host-target protein) where it appears to contribute to the binding of the protein to both RCS (AvrRpt2 auto-cleavage site) and AvrB, the virulence factor from the infecting bacterium. The cleavage site for the AvrRpt2 avirulence protein would appear to be the sequence motifs VPQFGDW and LPKFGEW, both of which are highly conserved within the domain.


The actual alignment was detected with superfamily member pfam05627:

Pssm-ID: 398967  Cd Length: 36  Bit Score: 52.78  E-value: 4.45e-10
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1279803595 124 ASVPKFGSWDARDPKSGDGYTAIFNKMKIEKQ 155
Cdd:pfam05627   4 RAVPKFGEWDESNPASADGFTVIFNKVREEKK 35
 
Name Accession Description Interval E-value
AvrRpt-cleavage pfam05627
Cleavage site for pathogenic type III effector avirulence factor Avr; This domain is conserved ...
124-155 4.45e-10

Cleavage site for pathogenic type III effector avirulence factor Avr; This domain is conserved in small families of otherwise unrelated proteins in both mono-cots and di-cots, suggesting that it has a conserved, plant-specific function. It is found both in the plant RIN4 (resistance R membrane-bound host-target protein) where it appears to contribute to the binding of the protein to both RCS (AvrRpt2 auto-cleavage site) and AvrB, the virulence factor from the infecting bacterium. The cleavage site for the AvrRpt2 avirulence protein would appear to be the sequence motifs VPQFGDW and LPKFGEW, both of which are highly conserved within the domain.


Pssm-ID: 398967  Cd Length: 36  Bit Score: 52.78  E-value: 4.45e-10
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1279803595 124 ASVPKFGSWDARDPKSGDGYTAIFNKMKIEKQ 155
Cdd:pfam05627   4 RAVPKFGEWDESNPASADGFTVIFNKVREEKK 35
 
Name Accession Description Interval E-value
AvrRpt-cleavage pfam05627
Cleavage site for pathogenic type III effector avirulence factor Avr; This domain is conserved ...
124-155 4.45e-10

Cleavage site for pathogenic type III effector avirulence factor Avr; This domain is conserved in small families of otherwise unrelated proteins in both mono-cots and di-cots, suggesting that it has a conserved, plant-specific function. It is found both in the plant RIN4 (resistance R membrane-bound host-target protein) where it appears to contribute to the binding of the protein to both RCS (AvrRpt2 auto-cleavage site) and AvrB, the virulence factor from the infecting bacterium. The cleavage site for the AvrRpt2 avirulence protein would appear to be the sequence motifs VPQFGDW and LPKFGEW, both of which are highly conserved within the domain.


Pssm-ID: 398967  Cd Length: 36  Bit Score: 52.78  E-value: 4.45e-10
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1279803595 124 ASVPKFGSWDARDPKSGDGYTAIFNKMKIEKQ 155
Cdd:pfam05627   4 RAVPKFGEWDESNPASADGFTVIFNKVREEKK 35
 
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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