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Conserved domains on  [gi|581673214|gb|EVQ78626|]
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complement inhibitor SCIN [Staphylococcus aureus M1417]

Protein Classification

complement inhibitor SCIN( domain architecture ID 10568967)

complement inhibitor SCIN is involved in countering the first line of host defense mechanisms; it efficiently inhibits opsonization, phagocytosis and killing of S.aureus by human neutrophils

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CompInhib_SCIN pfam11546
Staphylococcal complement inhibitor SCIN; SCIN is released by Staphylococcus aureus to ...
 1-114 1.47e-48

Staphylococcal complement inhibitor SCIN; SCIN is released by Staphylococcus aureus to counteract the host immune defense. The protein binds to and inhibits C3 convertases on the bacterial surface, reducing phagocytosis and blocking downstream effector functions by C3b deposition on its surface. An 18 residue stretch 31-48 is crucial for SCIN activity.


:

Pssm-ID: 371594  Cd Length: 114  Bit Score: 150.89  E-value: 1.47e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581673214    1 MKIRKSILAGTLAIVLASPLVTNLDKNEAQASTSLPTSNEYQNEKLANELKSLLDELNVNELATGSLNTYYKRTIKISGL 80
Cdd:pfam11546   1 MKIKKYILAGTLAALLDSTGIKLASKNEADASSLDKTSHTYQHQALADELHELLANTNVNKLAYGSLNAYYKRTILAAHY 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 581673214   81 KAMYALKSKDFKKMSEAKYQLQKIYNEIDEALKS 114
Cdd:pfam11546  81 IAKSALKTKDFDQMTKAKQRLEKIYNEIDEPLHS 114
 
Name Accession Description Interval E-value
CompInhib_SCIN pfam11546
Staphylococcal complement inhibitor SCIN; SCIN is released by Staphylococcus aureus to ...
 1-114 1.47e-48

Staphylococcal complement inhibitor SCIN; SCIN is released by Staphylococcus aureus to counteract the host immune defense. The protein binds to and inhibits C3 convertases on the bacterial surface, reducing phagocytosis and blocking downstream effector functions by C3b deposition on its surface. An 18 residue stretch 31-48 is crucial for SCIN activity.


Pssm-ID: 371594  Cd Length: 114  Bit Score: 150.89  E-value: 1.47e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581673214    1 MKIRKSILAGTLAIVLASPLVTNLDKNEAQASTSLPTSNEYQNEKLANELKSLLDELNVNELATGSLNTYYKRTIKISGL 80
Cdd:pfam11546   1 MKIKKYILAGTLAALLDSTGIKLASKNEADASSLDKTSHTYQHQALADELHELLANTNVNKLAYGSLNAYYKRTILAAHY 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 581673214   81 KAMYALKSKDFKKMSEAKYQLQKIYNEIDEALKS 114
Cdd:pfam11546  81 IAKSALKTKDFDQMTKAKQRLEKIYNEIDEPLHS 114
 
Name Accession Description Interval E-value
CompInhib_SCIN pfam11546
Staphylococcal complement inhibitor SCIN; SCIN is released by Staphylococcus aureus to ...
 1-114 1.47e-48

Staphylococcal complement inhibitor SCIN; SCIN is released by Staphylococcus aureus to counteract the host immune defense. The protein binds to and inhibits C3 convertases on the bacterial surface, reducing phagocytosis and blocking downstream effector functions by C3b deposition on its surface. An 18 residue stretch 31-48 is crucial for SCIN activity.


Pssm-ID: 371594  Cd Length: 114  Bit Score: 150.89  E-value: 1.47e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581673214    1 MKIRKSILAGTLAIVLASPLVTNLDKNEAQASTSLPTSNEYQNEKLANELKSLLDELNVNELATGSLNTYYKRTIKISGL 80
Cdd:pfam11546   1 MKIKKYILAGTLAALLDSTGIKLASKNEADASSLDKTSHTYQHQALADELHELLANTNVNKLAYGSLNAYYKRTILAAHY 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 581673214   81 KAMYALKSKDFKKMSEAKYQLQKIYNEIDEALKS 114
Cdd:pfam11546  81 IAKSALKTKDFDQMTKAKQRLEKIYNEIDEPLHS 114
 
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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