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Conserved domains on  [gi|518817539|ref|WP_019973493|]
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hypothetical protein [Mycobacterium sp. 141]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
EspB_PE pfam18625
ESX-1 secreted protein B PE domain; The ESX-1 secretion system is an important virulence ...
13-89 2.72e-11

ESX-1 secreted protein B PE domain; The ESX-1 secretion system is an important virulence determinant in Mycobacterium tuberculosis. ESX-1 secreted protein B (EspB) contains putative PE (Pro-Glu) and PPE (Pro-Pro-Glu) domains, and a C-terminal domain, which is processed by MycP1 protease during secretion. This domain represents the PE domain located at the N-terminal region of EspB which carries the conserved YxxxD/E secretion motif.


:

Pssm-ID: 465827  Cd Length: 78  Bit Score: 59.28  E-value: 2.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518817539   13 ETLDAKATALEA----DLPTVPEMPslgdtPCELQLARKALAIIAASLENLRTAVAAGNAEAKRLATCLHATADVYRIVD 88
Cdd:pfam18625   1 EELRARATEVEApiadWPPTDVPAA-----PDGLPSTKAAAENLNASADALRKYLAAGDQERQRLADTLRSAAKAYEEVD 75

                  .
gi 518817539   89 E 89
Cdd:pfam18625  76 E 76
 
Name Accession Description Interval E-value
EspB_PE pfam18625
ESX-1 secreted protein B PE domain; The ESX-1 secretion system is an important virulence ...
13-89 2.72e-11

ESX-1 secreted protein B PE domain; The ESX-1 secretion system is an important virulence determinant in Mycobacterium tuberculosis. ESX-1 secreted protein B (EspB) contains putative PE (Pro-Glu) and PPE (Pro-Pro-Glu) domains, and a C-terminal domain, which is processed by MycP1 protease during secretion. This domain represents the PE domain located at the N-terminal region of EspB which carries the conserved YxxxD/E secretion motif.


Pssm-ID: 465827  Cd Length: 78  Bit Score: 59.28  E-value: 2.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518817539   13 ETLDAKATALEA----DLPTVPEMPslgdtPCELQLARKALAIIAASLENLRTAVAAGNAEAKRLATCLHATADVYRIVD 88
Cdd:pfam18625   1 EELRARATEVEApiadWPPTDVPAA-----PDGLPSTKAAAENLNASADALRKYLAAGDQERQRLADTLRSAAKAYEEVD 75

                  .
gi 518817539   89 E 89
Cdd:pfam18625  76 E 76
 
Name Accession Description Interval E-value
EspB_PE pfam18625
ESX-1 secreted protein B PE domain; The ESX-1 secretion system is an important virulence ...
13-89 2.72e-11

ESX-1 secreted protein B PE domain; The ESX-1 secretion system is an important virulence determinant in Mycobacterium tuberculosis. ESX-1 secreted protein B (EspB) contains putative PE (Pro-Glu) and PPE (Pro-Pro-Glu) domains, and a C-terminal domain, which is processed by MycP1 protease during secretion. This domain represents the PE domain located at the N-terminal region of EspB which carries the conserved YxxxD/E secretion motif.


Pssm-ID: 465827  Cd Length: 78  Bit Score: 59.28  E-value: 2.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518817539   13 ETLDAKATALEA----DLPTVPEMPslgdtPCELQLARKALAIIAASLENLRTAVAAGNAEAKRLATCLHATADVYRIVD 88
Cdd:pfam18625   1 EELRARATEVEApiadWPPTDVPAA-----PDGLPSTKAAAENLNASADALRKYLAAGDQERQRLADTLRSAAKAYEEVD 75

                  .
gi 518817539   89 E 89
Cdd:pfam18625  76 E 76
 
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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