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Conserved domains on  [gi|1406027052|gb|PZY58531|]
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EspF protein [Escherichia coli]

Protein Classification

EspF domain-containing protein( domain architecture ID 10267734)

EspF domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
EspF pfam04806
EspF protein repeat; The enteropathogenic Escherichia coli EspF secreted protein induces host ...
103-149 3.76e-25

EspF protein repeat; The enteropathogenic Escherichia coli EspF secreted protein induces host cell apoptosis. Its proline-rich structure suggests that it may act by binding to SH3 domains or EVH1 domains of host cell signalling proteins.


:

Pssm-ID: 398464 [Multi-domain]  Cd Length: 47  Bit Score: 90.97  E-value: 3.76e-25
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1406027052 103 IQPARNMAEHIPPAPNWPAPTPPVQNEQSRPLPDVAQRLMQHLAEHG 149
Cdd:pfam04806   1 IQPARSMAEHIPPAPNWPAPTPPVQNEQSRPLPDVAQRLVQHLAEHG 47
EspF super family cl04765
EspF protein repeat; The enteropathogenic Escherichia coli EspF secreted protein induces host ...
80-102 9.67e-04

EspF protein repeat; The enteropathogenic Escherichia coli EspF secreted protein induces host cell apoptosis. Its proline-rich structure suggests that it may act by binding to SH3 domains or EVH1 domains of host cell signalling proteins.


The actual alignment was detected with superfamily member pfam04806:

Pssm-ID: 398464 [Multi-domain]  Cd Length: 47  Bit Score: 35.50  E-value: 9.67e-04
                          10        20
                  ....*....|....*....|...
gi 1406027052  80 KNALHRPLPDVAKRLVQHLAEHG 102
Cdd:pfam04806  25 QNEQSRPLPDVAQRLVQHLAEHG 47
 
Name Accession Description Interval E-value
EspF pfam04806
EspF protein repeat; The enteropathogenic Escherichia coli EspF secreted protein induces host ...
103-149 3.76e-25

EspF protein repeat; The enteropathogenic Escherichia coli EspF secreted protein induces host cell apoptosis. Its proline-rich structure suggests that it may act by binding to SH3 domains or EVH1 domains of host cell signalling proteins.


Pssm-ID: 398464 [Multi-domain]  Cd Length: 47  Bit Score: 90.97  E-value: 3.76e-25
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1406027052 103 IQPARNMAEHIPPAPNWPAPTPPVQNEQSRPLPDVAQRLMQHLAEHG 149
Cdd:pfam04806   1 IQPARSMAEHIPPAPNWPAPTPPVQNEQSRPLPDVAQRLVQHLAEHG 47
EspF pfam04806
EspF protein repeat; The enteropathogenic Escherichia coli EspF secreted protein induces host ...
80-102 9.67e-04

EspF protein repeat; The enteropathogenic Escherichia coli EspF secreted protein induces host cell apoptosis. Its proline-rich structure suggests that it may act by binding to SH3 domains or EVH1 domains of host cell signalling proteins.


Pssm-ID: 398464 [Multi-domain]  Cd Length: 47  Bit Score: 35.50  E-value: 9.67e-04
                          10        20
                  ....*....|....*....|...
gi 1406027052  80 KNALHRPLPDVAKRLVQHLAEHG 102
Cdd:pfam04806  25 QNEQSRPLPDVAQRLVQHLAEHG 47
 
Name Accession Description Interval E-value
EspF pfam04806
EspF protein repeat; The enteropathogenic Escherichia coli EspF secreted protein induces host ...
103-149 3.76e-25

EspF protein repeat; The enteropathogenic Escherichia coli EspF secreted protein induces host cell apoptosis. Its proline-rich structure suggests that it may act by binding to SH3 domains or EVH1 domains of host cell signalling proteins.


Pssm-ID: 398464 [Multi-domain]  Cd Length: 47  Bit Score: 90.97  E-value: 3.76e-25
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1406027052 103 IQPARNMAEHIPPAPNWPAPTPPVQNEQSRPLPDVAQRLMQHLAEHG 149
Cdd:pfam04806   1 IQPARSMAEHIPPAPNWPAPTPPVQNEQSRPLPDVAQRLVQHLAEHG 47
EspF pfam04806
EspF protein repeat; The enteropathogenic Escherichia coli EspF secreted protein induces host ...
80-102 9.67e-04

EspF protein repeat; The enteropathogenic Escherichia coli EspF secreted protein induces host cell apoptosis. Its proline-rich structure suggests that it may act by binding to SH3 domains or EVH1 domains of host cell signalling proteins.


Pssm-ID: 398464 [Multi-domain]  Cd Length: 47  Bit Score: 35.50  E-value: 9.67e-04
                          10        20
                  ....*....|....*....|...
gi 1406027052  80 KNALHRPLPDVAKRLVQHLAEHG 102
Cdd:pfam04806  25 QNEQSRPLPDVAQRLVQHLAEHG 47
 
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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