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Conserved domains on  [gi|446206599|ref|WP_000284454|]
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staphostatin B [Staphylococcus aureus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Staphostatin_B super family cl07583
Staphostatin B; Staphostatin B inhibits the cysteine protease Staphopain B, produced by ...
 3-107 1.77e-39

Staphostatin B; Staphostatin B inhibits the cysteine protease Staphopain B, produced by Staphylococcus aureus, by blocking the active site of the enzyme. The domain adopts an eight-stranded mixed beta-barrel structure, with a deviation from the up-down topology of canonical beta-barrels in the amino-terminal part of the molecule.


The actual alignment was detected with superfamily member pfam09023:

Pssm-ID: 462656  Cd Length: 105  Bit Score: 127.13  E-value: 1.77e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206599    3 QLQFINLVYDTSKLTHLEQTNINLFIGNWSNHQLQKSICIRHGDDTSHNQYHILFIDTAHQRIKFSSIDNEEITYILDYD 82
Cdd:pfam09023   1 MLQFIFINLDTDKLKHLELENINIFIFIGNNHNHQKQICICHGDDDDHNHNHIHFIDIAHAHIKFKFFDFDEEEIILDLD 80

                          90       100
                  ....*....|....*....|....*
gi 446206599   83 DTQHILMQTSSKQGIGTSRPIVYER 107
Cdd:pfam09023  81 DDDHIHILMQSKQGIGIGRPIPIER 105
 
Name Accession Description Interval E-value
Staphostatin_B pfam09023
Staphostatin B; Staphostatin B inhibits the cysteine protease Staphopain B, produced by ...
 3-107 1.77e-39

Staphostatin B; Staphostatin B inhibits the cysteine protease Staphopain B, produced by Staphylococcus aureus, by blocking the active site of the enzyme. The domain adopts an eight-stranded mixed beta-barrel structure, with a deviation from the up-down topology of canonical beta-barrels in the amino-terminal part of the molecule.


Pssm-ID: 462656  Cd Length: 105  Bit Score: 127.13  E-value: 1.77e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206599    3 QLQFINLVYDTSKLTHLEQTNINLFIGNWSNHQLQKSICIRHGDDTSHNQYHILFIDTAHQRIKFSSIDNEEITYILDYD 82
Cdd:pfam09023   1 MLQFIFINLDTDKLKHLELENINIFIFIGNNHNHQKQICICHGDDDDHNHNHIHFIDIAHAHIKFKFFDFDEEEIILDLD 80

                          90       100
                  ....*....|....*....|....*
gi 446206599   83 DTQHILMQTSSKQGIGTSRPIVYER 107
Cdd:pfam09023  81 DDDHIHILMQSKQGIGIGRPIPIER 105
 
Name Accession Description Interval E-value
Staphostatin_B pfam09023
Staphostatin B; Staphostatin B inhibits the cysteine protease Staphopain B, produced by ...
 3-107 1.77e-39

Staphostatin B; Staphostatin B inhibits the cysteine protease Staphopain B, produced by Staphylococcus aureus, by blocking the active site of the enzyme. The domain adopts an eight-stranded mixed beta-barrel structure, with a deviation from the up-down topology of canonical beta-barrels in the amino-terminal part of the molecule.


Pssm-ID: 462656  Cd Length: 105  Bit Score: 127.13  E-value: 1.77e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206599    3 QLQFINLVYDTSKLTHLEQTNINLFIGNWSNHQLQKSICIRHGDDTSHNQYHILFIDTAHQRIKFSSIDNEEITYILDYD 82
Cdd:pfam09023   1 MLQFIFINLDTDKLKHLELENINIFIFIGNNHNHQKQICICHGDDDDHNHNHIHFIDIAHAHIKFKFFDFDEEEIILDLD 80

                          90       100
                  ....*....|....*....|....*
gi 446206599   83 DTQHILMQTSSKQGIGTSRPIVYER 107
Cdd:pfam09023  81 DDDHIHILMQSKQGIGIGRPIPIER 105
Staphostatin_B pfam09023
Staphostatin B; Staphostatin B inhibits the cysteine protease Staphopain B, produced by ...
 1-105 1.91e-39

Staphostatin B; Staphostatin B inhibits the cysteine protease Staphopain B, produced by Staphylococcus aureus, by blocking the active site of the enzyme. The domain adopts an eight-stranded mixed beta-barrel structure, with a deviation from the up-down topology of canonical beta-barrels in the amino-terminal part of the molecule.


Pssm-ID: 462656  Cd Length: 105  Bit Score: 127.13  E-value: 1.91e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446206599    1 MYQLQFINLVYDTSKLTHLEQTNINLFIGNWSNHQLQKSICIRHGDDTSHNQYHILFIDTAHQRIKFSSIDNEEITYILD 80
Cdd:pfam09023   1 MLQFIFINLDTDKLKHLELENINIFIFIGNNHNHQKQICICHGDDDDHNHNHIHFIDIAHAHIKFKFFDFDEEEIILDLD 80

                          90       100
                  ....*....|....*....|....*
gi 446206599   81 YDDTQHILMQTSSKQGIGTSRPIVY 105
Cdd:pfam09023  81 DDDHIHILMQSKQGIGIGRPIPIER 105
 
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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