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Conserved domains on  [gi|1821229960|gb|QIL81673|]
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general secretion pathway protein C [Diaphorobacter sp. HDW4A]

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 ...
 17-123 3.05e-07

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: 47.76  E-value: 3.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821229960  17 VLWFLAIACV---VFWGL-KLSASQLGQGAPALPVAPTV----VDVSSLVR--LLGGTEVVAKVASVAPT---------R 77
Cdd:pfam11356   1 LLLLALLAWLaarLTWRLlAPAPPATAAAASWAPSPASSsadrLDVAGIASlnLFGKAAPQALAPKTAPVvvdapatrlN 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1821229960  78 YTLVGVLAGTRSGHGAALIEVDGKPAKPFRVGSTVAEGLVLQSVNK 123
Cdd:pfam11356  81 LTLLGVVASSDPERGLAIIAERGKQEQTYRIGDEIPGGATLVAVYA 126
 
Name Accession Description Interval E-value
T2SSC pfam11356
Type II secretion system protein C; This is the greater N-terminal region of GspC-type ...
 17-123 3.05e-07

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: 47.76  E-value: 3.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821229960  17 VLWFLAIACV---VFWGL-KLSASQLGQGAPALPVAPTV----VDVSSLVR--LLGGTEVVAKVASVAPT---------R 77
Cdd:pfam11356   1 LLLLALLAWLaarLTWRLlAPAPPATAAAASWAPSPASSsadrLDVAGIASlnLFGKAAPQALAPKTAPVvvdapatrlN 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1821229960  78 YTLVGVLAGTRSGHGAALIEVDGKPAKPFRVGSTVAEGLVLQSVNK 123
Cdd:pfam11356  81 LTLLGVVASSDPERGLAIIAERGKQEQTYRIGDEIPGGATLVAVYA 126
PulC COG3031
Type II secretory pathway, component PulC [Intracellular trafficking, secretion, and vesicular ...
 67-159 1.52e-06

Type II secretory pathway, component PulC [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 442267 [Multi-domain]  Cd Length: 220  Bit Score: 46.90  E-value: 1.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821229960  67 VAKVASVAPTRYTLVGVLAGTRSGHGAALIEVDGKPAKPFRVGSTVAEGLVLQSV---------NKREALLGFDLKGPTS 137
Cdd:COG3031    15 VLTDAPETRLNLTLLGVVASSDPERSFAIIAEGGGKQKSYRVGDEIPGGATLVAVyrdrvilsnNGRLETLMLDGEDYAA 94

                          90       100
                  ....*....|....*....|..
gi 1821229960 138 mtlqiPLKVASNTSALPVSPPA 159
Cdd:COG3031    95 -----PAAAAAAPASSPAASSA 111
 
Name Accession Description Interval E-value
T2SSC pfam11356
Type II secretion system protein C; This is the greater N-terminal region of GspC-type ...
 17-123 3.05e-07

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: 47.76  E-value: 3.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821229960  17 VLWFLAIACV---VFWGL-KLSASQLGQGAPALPVAPTV----VDVSSLVR--LLGGTEVVAKVASVAPT---------R 77
Cdd:pfam11356   1 LLLLALLAWLaarLTWRLlAPAPPATAAAASWAPSPASSsadrLDVAGIASlnLFGKAAPQALAPKTAPVvvdapatrlN 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1821229960  78 YTLVGVLAGTRSGHGAALIEVDGKPAKPFRVGSTVAEGLVLQSVNK 123
Cdd:pfam11356  81 LTLLGVVASSDPERGLAIIAERGKQEQTYRIGDEIPGGATLVAVYA 126
PulC COG3031
Type II secretory pathway, component PulC [Intracellular trafficking, secretion, and vesicular ...
 67-159 1.52e-06

Type II secretory pathway, component PulC [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 442267 [Multi-domain]  Cd Length: 220  Bit Score: 46.90  E-value: 1.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821229960  67 VAKVASVAPTRYTLVGVLAGTRSGHGAALIEVDGKPAKPFRVGSTVAEGLVLQSV---------NKREALLGFDLKGPTS 137
Cdd:COG3031    15 VLTDAPETRLNLTLLGVVASSDPERSFAIIAEGGGKQKSYRVGDEIPGGATLVAVyrdrvilsnNGRLETLMLDGEDYAA 94

                          90       100
                  ....*....|....*....|..
gi 1821229960 138 mtlqiPLKVASNTSALPVSPPA 159
Cdd:COG3031    95 -----PAAAAAAPASSPAASSA 111
 
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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