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Conserved domains on  [gi|15595876|ref|NP_249370|]
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hypothetical protein PA0679 [Pseudomonas aeruginosa PAO1]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
T2SSC super family cl44344
Type II secretion system protein C; This is the greater N-terminal region of GspC-type ...
15-121 3.96e-03

Type II secretion system protein C; This is the greater N-terminal region of GspC-type proteins. GspC proteins form part of the sophisticated transport mechanism of Gram-negative pathogens for injecting divers proteins into their hosts, a type-II secretion system - T2SS. The region is made up of a short N-terminal cytoplasmic domain that is followed by the single transmembrane helix, a Pro-rich linker, and the so-called homology region domain in the periplasm. This inner membrane GspC interacts with the outer membrane secretin GspD via periplasmic domains, an interaction which is critical for the effectiveness of type II secretion.


The actual alignment was detected with superfamily member pfam11356:

Pssm-ID: 457689  Cd Length: 142  Bit Score: 35.44  E-value: 3.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595876    15 FAAVLAILAGLLFWGYLLL-----------APIPGVVQADVADV-------------PPPSGEDAAQRWFAAPSGEVEVQ 70
Cdd:pfam11356   3 LLALLAWLAARLTWRLLAPappataaaaswAPSPASSSADRLDVagiaslnlfgkaaPQALAPKTAPVVVDAPATRLNLT 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 15595876    71 LAGLISGGPA--AIAILSVNGAPAQAYREGEVLARAAKVRRIEADAVLIEQNG 121
Cdd:pfam11356  83 LLGVVASSDPerGLAIIAERGKQEQTYRIGDEIPGGATLVAVYADRVIIRRNG 135
 
Name Accession Description Interval E-value
T2SSC pfam11356
Type II secretion system protein C; This is the greater N-terminal region of GspC-type ...
15-121 3.96e-03

Type II secretion system protein C; This is the greater N-terminal region of GspC-type proteins. GspC proteins form part of the sophisticated transport mechanism of Gram-negative pathogens for injecting divers proteins into their hosts, a type-II secretion system - T2SS. The region is made up of a short N-terminal cytoplasmic domain that is followed by the single transmembrane helix, a Pro-rich linker, and the so-called homology region domain in the periplasm. This inner membrane GspC interacts with the outer membrane secretin GspD via periplasmic domains, an interaction which is critical for the effectiveness of type II secretion.


Pssm-ID: 431837  Cd Length: 142  Bit Score: 35.44  E-value: 3.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595876    15 FAAVLAILAGLLFWGYLLL-----------APIPGVVQADVADV-------------PPPSGEDAAQRWFAAPSGEVEVQ 70
Cdd:pfam11356   3 LLALLAWLAARLTWRLLAPappataaaaswAPSPASSSADRLDVagiaslnlfgkaaPQALAPKTAPVVVDAPATRLNLT 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 15595876    71 LAGLISGGPA--AIAILSVNGAPAQAYREGEVLARAAKVRRIEADAVLIEQNG 121
Cdd:pfam11356  83 LLGVVASSDPerGLAIIAERGKQEQTYRIGDEIPGGATLVAVYADRVIIRRNG 135
 
Name Accession Description Interval E-value
T2SSC pfam11356
Type II secretion system protein C; This is the greater N-terminal region of GspC-type ...
15-121 3.96e-03

Type II secretion system protein C; This is the greater N-terminal region of GspC-type proteins. GspC proteins form part of the sophisticated transport mechanism of Gram-negative pathogens for injecting divers proteins into their hosts, a type-II secretion system - T2SS. The region is made up of a short N-terminal cytoplasmic domain that is followed by the single transmembrane helix, a Pro-rich linker, and the so-called homology region domain in the periplasm. This inner membrane GspC interacts with the outer membrane secretin GspD via periplasmic domains, an interaction which is critical for the effectiveness of type II secretion.


Pssm-ID: 431837  Cd Length: 142  Bit Score: 35.44  E-value: 3.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595876    15 FAAVLAILAGLLFWGYLLL-----------APIPGVVQADVADV-------------PPPSGEDAAQRWFAAPSGEVEVQ 70
Cdd:pfam11356   3 LLALLAWLAARLTWRLLAPappataaaaswAPSPASSSADRLDVagiaslnlfgkaaPQALAPKTAPVVVDAPATRLNLT 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 15595876    71 LAGLISGGPA--AIAILSVNGAPAQAYREGEVLARAAKVRRIEADAVLIEQNG 121
Cdd:pfam11356  83 LLGVVASSDPerGLAIIAERGKQEQTYRIGDEIPGGATLVAVYADRVIIRRNG 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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