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Conserved domains on  [gi|262100043|gb|EEY58095|]
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secreted RxLR effector peptide protein, putative, partial [Phytophthora infestans T30-4]

Protein Classification

RxLR effector protein( domain architecture ID 11245607)

RxLR (Arg-Xaa-Leu-Arg) effector protein belongs to a class of secreted proteins that are transferred into host cells to manipulate host immunity

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RXLR pfam16810
RXLR phytopathogen effector protein, Avirulence activity; RXLR is a family of phytopathogen ...
 1-123 7.24e-35

RXLR phytopathogen effector protein, Avirulence activity; RXLR is a family of phytopathogen avirulence or effector proteins. RXLR proteins are defined by a secretion signal peptide - not in this family - followed by a conserved N-terminal domain with the sequence motif RXLR (Arg-Xaa-Leu-Arg) consensus sequence. The RXLR part is required for translocation inside plant cells, although it appears to be dispensable for the biochemical activity of the effectors when expressed directly inside host cells. The effector activity resides in the C-terminal part of the family, which activate effector-triggered immunity in plants that carry a corresponding resistance (R) protein. The C-terminal region exhibits a fold appears to be able to evolve to outwit the host as the latter tries to acquire new immunity.


:

Pssm-ID: 465277  Cd Length: 138  Bit Score: 117.57  E-value: 7.24e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262100043    1 MRVSYVLLVAVATLLITCDVVSAQ--------PSTLSLPASDGAMIEDTNNQPLRLLEI-TTADDGEERMAEARLMDSEI 71
Cdd:pfam16810   1 MRLSSVLLVAAATLLLASGTASSAstsadqttVTMSSPSSILLAVGDAADKRFLRSHKTeNDDDTSEERGAGANLLDEKK 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 262100043   72 LEKIVNDHAYAKQVFRSWLQNGQTKEDIENRLKTLGLLT---KYGNVVKQYAQYL 123
Cdd:pfam16810  81 LKKMLANSKYAKKLFRRWYKNGYTLKDIANRLKQSGNRKlgqKYQTLANQYAAYL 135
 
Name Accession Description Interval E-value
RXLR pfam16810
RXLR phytopathogen effector protein, Avirulence activity; RXLR is a family of phytopathogen ...
 1-123 7.24e-35

RXLR phytopathogen effector protein, Avirulence activity; RXLR is a family of phytopathogen avirulence or effector proteins. RXLR proteins are defined by a secretion signal peptide - not in this family - followed by a conserved N-terminal domain with the sequence motif RXLR (Arg-Xaa-Leu-Arg) consensus sequence. The RXLR part is required for translocation inside plant cells, although it appears to be dispensable for the biochemical activity of the effectors when expressed directly inside host cells. The effector activity resides in the C-terminal part of the family, which activate effector-triggered immunity in plants that carry a corresponding resistance (R) protein. The C-terminal region exhibits a fold appears to be able to evolve to outwit the host as the latter tries to acquire new immunity.


Pssm-ID: 465277  Cd Length: 138  Bit Score: 117.57  E-value: 7.24e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262100043    1 MRVSYVLLVAVATLLITCDVVSAQ--------PSTLSLPASDGAMIEDTNNQPLRLLEI-TTADDGEERMAEARLMDSEI 71
Cdd:pfam16810   1 MRLSSVLLVAAATLLLASGTASSAstsadqttVTMSSPSSILLAVGDAADKRFLRSHKTeNDDDTSEERGAGANLLDEKK 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 262100043   72 LEKIVNDHAYAKQVFRSWLQNGQTKEDIENRLKTLGLLT---KYGNVVKQYAQYL 123
Cdd:pfam16810  81 LKKMLANSKYAKKLFRRWYKNGYTLKDIANRLKQSGNRKlgqKYQTLANQYAAYL 135
 
Name Accession Description Interval E-value
RXLR pfam16810
RXLR phytopathogen effector protein, Avirulence activity; RXLR is a family of phytopathogen ...
 1-123 7.24e-35

RXLR phytopathogen effector protein, Avirulence activity; RXLR is a family of phytopathogen avirulence or effector proteins. RXLR proteins are defined by a secretion signal peptide - not in this family - followed by a conserved N-terminal domain with the sequence motif RXLR (Arg-Xaa-Leu-Arg) consensus sequence. The RXLR part is required for translocation inside plant cells, although it appears to be dispensable for the biochemical activity of the effectors when expressed directly inside host cells. The effector activity resides in the C-terminal part of the family, which activate effector-triggered immunity in plants that carry a corresponding resistance (R) protein. The C-terminal region exhibits a fold appears to be able to evolve to outwit the host as the latter tries to acquire new immunity.


Pssm-ID: 465277  Cd Length: 138  Bit Score: 117.57  E-value: 7.24e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262100043    1 MRVSYVLLVAVATLLITCDVVSAQ--------PSTLSLPASDGAMIEDTNNQPLRLLEI-TTADDGEERMAEARLMDSEI 71
Cdd:pfam16810   1 MRLSSVLLVAAATLLLASGTASSAstsadqttVTMSSPSSILLAVGDAADKRFLRSHKTeNDDDTSEERGAGANLLDEKK 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 262100043   72 LEKIVNDHAYAKQVFRSWLQNGQTKEDIENRLKTLGLLT---KYGNVVKQYAQYL 123
Cdd:pfam16810  81 LKKMLANSKYAKKLFRRWYKNGYTLKDIANRLKQSGNRKlgqKYQTLANQYAAYL 135
 
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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