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Conserved domains on  [gi|485748052|ref|WP_001374302|]
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T3SS effector caspase inhibitor NleF [Escherichia coli]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
NleF_casp_inhib super family cl25126
NleF caspase inhibitor; Binds to and inhibits caspase-9, caspase-8 and caspase-4. therefore ...
36-157 3.35e-03

NleF caspase inhibitor; Binds to and inhibits caspase-9, caspase-8 and caspase-4. therefore preventing caspase-induced apoptosis in the host cell.


The actual alignment was detected with superfamily member pfam16809:

Pssm-ID: 293414  Cd Length: 145  Bit Score: 36.36  E-value: 3.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485748052   36 HFLSpELQDKLDVMVSIYSCARNNNE-LEDIYQELSAFVSGVMDKRNSVFEV----RNENTDEVVgaLRAGMTIEDRDSY 110
Cdd:pfam16809  11 KTLK-DIKSKLDDIYHNGISSTTGRKkIKELRDKLTQMINSVLSYRDDLYEViedyRTGGGQKII--LKEGCTATDRDNY 87
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 485748052  111 IRDLFFLHSLKVKIEESrqgKEGSKCKVYDLLC-----PHHSSELYGDLRAM 157
Cdd:pfam16809  88 LKGLIALYQIQDAVKNE---IDNAPIKTIKDSLskvfdVMHNGAVYGDLKAL 136
 
Name Accession Description Interval E-value
NleF_casp_inhib pfam16809
NleF caspase inhibitor; Binds to and inhibits caspase-9, caspase-8 and caspase-4. therefore ...
36-157 3.35e-03

NleF caspase inhibitor; Binds to and inhibits caspase-9, caspase-8 and caspase-4. therefore preventing caspase-induced apoptosis in the host cell.


Pssm-ID: 293414  Cd Length: 145  Bit Score: 36.36  E-value: 3.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485748052   36 HFLSpELQDKLDVMVSIYSCARNNNE-LEDIYQELSAFVSGVMDKRNSVFEV----RNENTDEVVgaLRAGMTIEDRDSY 110
Cdd:pfam16809  11 KTLK-DIKSKLDDIYHNGISSTTGRKkIKELRDKLTQMINSVLSYRDDLYEViedyRTGGGQKII--LKEGCTATDRDNY 87
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 485748052  111 IRDLFFLHSLKVKIEESrqgKEGSKCKVYDLLC-----PHHSSELYGDLRAM 157
Cdd:pfam16809  88 LKGLIALYQIQDAVKNE---IDNAPIKTIKDSLskvfdVMHNGAVYGDLKAL 136
 
Name Accession Description Interval E-value
NleF_casp_inhib pfam16809
NleF caspase inhibitor; Binds to and inhibits caspase-9, caspase-8 and caspase-4. therefore ...
36-157 3.35e-03

NleF caspase inhibitor; Binds to and inhibits caspase-9, caspase-8 and caspase-4. therefore preventing caspase-induced apoptosis in the host cell.


Pssm-ID: 293414  Cd Length: 145  Bit Score: 36.36  E-value: 3.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485748052   36 HFLSpELQDKLDVMVSIYSCARNNNE-LEDIYQELSAFVSGVMDKRNSVFEV----RNENTDEVVgaLRAGMTIEDRDSY 110
Cdd:pfam16809  11 KTLK-DIKSKLDDIYHNGISSTTGRKkIKELRDKLTQMINSVLSYRDDLYEViedyRTGGGQKII--LKEGCTATDRDNY 87
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 485748052  111 IRDLFFLHSLKVKIEESrqgKEGSKCKVYDLLC-----PHHSSELYGDLRAM 157
Cdd:pfam16809  88 LKGLIALYQIQDAVKNE---IDNAPIKTIKDSLskvfdVMHNGAVYGDLKAL 136
 
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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