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Conserved domains on  [gi|2524490330|ref|WP_286617365|]
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Rap1a/Tai family immunity protein [Citrobacter sp. Cpo065]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Rap1a pfam18602
Rap1a immunity proteins; The structures of the immunity proteins, Rap1a, responsible for the ...
 34-116 1.93e-19

Rap1a immunity proteins; The structures of the immunity proteins, Rap1a, responsible for the inhibition and neutralization of Ssp1 endopeptidase, revealed two distinct folds. The structure of the Ssp1-Rap1a complex revealed a tightly bound heteromeric assembly with two effector molecules flanking a Rap1a dimer. The Rap1a subunit displays a compact globular structure constructed from five alpha-helices that assemble to form the highly stable symmetric dimer.


:

Pssm-ID: 465818  Cd Length: 91  Bit Score: 76.05  E-value: 1.93e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524490330  34 GESLMRVRENRTMGSDISDANMYYGYVSGVYD-------LGSGVIFCASNQLNLNQISDVVYQYLKQYPKRRAENASDLA 106
Cdd:pfam18602   2 GNDLLELCKAPGASDDPLDAGFCLGYIAGVVDalaqdrgATEGTLFCLPPGVTPGQLVDAVVAYLKAHPERLHEPAASLV 81

                          90
                  ....*....|
gi 2524490330 107 VDALSEAFPC 116
Cdd:pfam18602  82 LEALAAAFPC 91
 
Name Accession Description Interval E-value
Rap1a pfam18602
Rap1a immunity proteins; The structures of the immunity proteins, Rap1a, responsible for the ...
 34-116 1.93e-19

Rap1a immunity proteins; The structures of the immunity proteins, Rap1a, responsible for the inhibition and neutralization of Ssp1 endopeptidase, revealed two distinct folds. The structure of the Ssp1-Rap1a complex revealed a tightly bound heteromeric assembly with two effector molecules flanking a Rap1a dimer. The Rap1a subunit displays a compact globular structure constructed from five alpha-helices that assemble to form the highly stable symmetric dimer.


Pssm-ID: 465818  Cd Length: 91  Bit Score: 76.05  E-value: 1.93e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524490330  34 GESLMRVRENRTMGSDISDANMYYGYVSGVYD-------LGSGVIFCASNQLNLNQISDVVYQYLKQYPKRRAENASDLA 106
Cdd:pfam18602   2 GNDLLELCKAPGASDDPLDAGFCLGYIAGVVDalaqdrgATEGTLFCLPPGVTPGQLVDAVVAYLKAHPERLHEPAASLV 81

                          90
                  ....*....|
gi 2524490330 107 VDALSEAFPC 116
Cdd:pfam18602  82 LEALAAAFPC 91
 
Name Accession Description Interval E-value
Rap1a pfam18602
Rap1a immunity proteins; The structures of the immunity proteins, Rap1a, responsible for the ...
 34-116 1.93e-19

Rap1a immunity proteins; The structures of the immunity proteins, Rap1a, responsible for the inhibition and neutralization of Ssp1 endopeptidase, revealed two distinct folds. The structure of the Ssp1-Rap1a complex revealed a tightly bound heteromeric assembly with two effector molecules flanking a Rap1a dimer. The Rap1a subunit displays a compact globular structure constructed from five alpha-helices that assemble to form the highly stable symmetric dimer.


Pssm-ID: 465818  Cd Length: 91  Bit Score: 76.05  E-value: 1.93e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2524490330  34 GESLMRVRENRTMGSDISDANMYYGYVSGVYD-------LGSGVIFCASNQLNLNQISDVVYQYLKQYPKRRAENASDLA 106
Cdd:pfam18602   2 GNDLLELCKAPGASDDPLDAGFCLGYIAGVVDalaqdrgATEGTLFCLPPGVTPGQLVDAVVAYLKAHPERLHEPAASLV 81

                          90
                  ....*....|
gi 2524490330 107 VDALSEAFPC 116
Cdd:pfam18602  82 LEALAAAFPC 91
 
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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