NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|446750482|ref|WP_000827738|]
View 

cysteine protease staphopain A [Staphylococcus aureus]

Protein Classification

cysteine protease staphopain( domain architecture ID 10631631)

cysteine protease staphopain is a C47 family peptidase such as staphopain A that plays an important role in the inhibition of host innate immune response, cleaving host elastins found in connective tissues, pulmonary surfactant protein A in the lungs, and the chemokine receptor CXCR2 on leukocytes

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
Peptidase_C47 pfam05543
Staphopain peptidase C47; Staphopains are one of four major families of proteinases secreted ...
215-388 1.39e-118

Staphopain peptidase C47; Staphopains are one of four major families of proteinases secreted by the Gram-positive Staphylococcus aureus. These staphylococcal cysteine proteases are secreted as preproenzymes that are proteolytically cleaved to generate the mature enzyme.


:

Pssm-ID: 398922  Cd Length: 174  Bit Score: 341.55  E-value: 1.39e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446750482  215 YNEQYVNKLENFKIRETQGNNGWCAGYTMSALLNATYNTNKYHAEAVMRFLHPNLQGQQFQFTGLTPREMIYFGQTQGRS 294
Cdd:pfam05543   1 DQVQYENTLKNFKIRETQGDNSWCAGYTMSALLNATYNTNTYNAEDVMRTLHPNLSGQDFQFTGLTPNEMIEFGKSQGRD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446750482  295 PQLLNRMTTYNEVDNLTKNNKGIAILGSRVESRNGMHAGHAMAVVGNAKLDNGQEVIIIWNPWDNGFMTQDAKNNVIPVS 374
Cdd:pfam05543  81 IQYLNRMTSYNEVDQLTKNNVGIAILGQRVESPNGPHAGHAMAVVGNAKINNGQEVIIIWNPWDNGLMTQDADSNLIPVS 160
                         170
                  ....*....|....
gi 446750482  375 NGDHYQWYSSIYGY 388
Cdd:pfam05543 161 NGDHYNWYGSIYGY 174
Staphopain_pro pfam14731
Staphopain proregion; This domain is the proregion of the cysteine protease staphopain. Like ...
37-203 1.59e-85

Staphopain proregion; This domain is the proregion of the cysteine protease staphopain. Like many papain type peptidases, staphopain is synthesized as an inactive precursor and cleavage of the proregion is required for activation. This proregion has a half-barrel or barrel-sandwich hybrid fold. The proregion blocks the active site cleft of the mature enzyme on one side of the nucleophilic cysteine


:

Pssm-ID: 291401  Cd Length: 169  Bit Score: 257.21  E-value: 1.59e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446750482   37 RHVQVNVEDKSVPTDVRNLAQKDYLSYVTSLDKIYNKEKASYTLGEPFKIYKFNKKSDGNYYFPVLNTEGNIDYIVTISP 116
Cdd:pfam14731   1 KQLEVNVKSKKVPQKVRDLAQQQYLSYVKALDKQSNAKTGSYTLGEPFKIYKFNKESDGNYYYPVLNKDGKIVYTVTISP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446750482  117 KVTKD--SSSSSKYTINVSSFLSKALNQYKDQQITILTNSKGYYVVTQNHKAKLVLKTPRLEDKKVKKTESIPTGNNVTQ 194
Cdd:pfam14731  81 KNKDDkkSKEDMNYSINVSPFLSKDLNQYKDQNITILTNEKGYYVFTEDGKVRLVLKTPRLNNKKEKESAKTVSPKLKQE 160

                  ....*....
gi 446750482  195 LKQKASVTM 203
Cdd:pfam14731 161 LKQTASVTK 169
 
Name Accession Description Interval E-value
Peptidase_C47 pfam05543
Staphopain peptidase C47; Staphopains are one of four major families of proteinases secreted ...
215-388 1.39e-118

Staphopain peptidase C47; Staphopains are one of four major families of proteinases secreted by the Gram-positive Staphylococcus aureus. These staphylococcal cysteine proteases are secreted as preproenzymes that are proteolytically cleaved to generate the mature enzyme.


Pssm-ID: 398922  Cd Length: 174  Bit Score: 341.55  E-value: 1.39e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446750482  215 YNEQYVNKLENFKIRETQGNNGWCAGYTMSALLNATYNTNKYHAEAVMRFLHPNLQGQQFQFTGLTPREMIYFGQTQGRS 294
Cdd:pfam05543   1 DQVQYENTLKNFKIRETQGDNSWCAGYTMSALLNATYNTNTYNAEDVMRTLHPNLSGQDFQFTGLTPNEMIEFGKSQGRD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446750482  295 PQLLNRMTTYNEVDNLTKNNKGIAILGSRVESRNGMHAGHAMAVVGNAKLDNGQEVIIIWNPWDNGFMTQDAKNNVIPVS 374
Cdd:pfam05543  81 IQYLNRMTSYNEVDQLTKNNVGIAILGQRVESPNGPHAGHAMAVVGNAKINNGQEVIIIWNPWDNGLMTQDADSNLIPVS 160
                         170
                  ....*....|....
gi 446750482  375 NGDHYQWYSSIYGY 388
Cdd:pfam05543 161 NGDHYNWYGSIYGY 174
Staphopain_pro pfam14731
Staphopain proregion; This domain is the proregion of the cysteine protease staphopain. Like ...
37-203 1.59e-85

Staphopain proregion; This domain is the proregion of the cysteine protease staphopain. Like many papain type peptidases, staphopain is synthesized as an inactive precursor and cleavage of the proregion is required for activation. This proregion has a half-barrel or barrel-sandwich hybrid fold. The proregion blocks the active site cleft of the mature enzyme on one side of the nucleophilic cysteine


Pssm-ID: 291401  Cd Length: 169  Bit Score: 257.21  E-value: 1.59e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446750482   37 RHVQVNVEDKSVPTDVRNLAQKDYLSYVTSLDKIYNKEKASYTLGEPFKIYKFNKKSDGNYYFPVLNTEGNIDYIVTISP 116
Cdd:pfam14731   1 KQLEVNVKSKKVPQKVRDLAQQQYLSYVKALDKQSNAKTGSYTLGEPFKIYKFNKESDGNYYYPVLNKDGKIVYTVTISP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446750482  117 KVTKD--SSSSSKYTINVSSFLSKALNQYKDQQITILTNSKGYYVVTQNHKAKLVLKTPRLEDKKVKKTESIPTGNNVTQ 194
Cdd:pfam14731  81 KNKDDkkSKEDMNYSINVSPFLSKDLNQYKDQNITILTNEKGYYVFTEDGKVRLVLKTPRLNNKKEKESAKTVSPKLKQE 160

                  ....*....
gi 446750482  195 LKQKASVTM 203
Cdd:pfam14731 161 LKQTASVTK 169
 
Name Accession Description Interval E-value
Peptidase_C47 pfam05543
Staphopain peptidase C47; Staphopains are one of four major families of proteinases secreted ...
215-388 1.39e-118

Staphopain peptidase C47; Staphopains are one of four major families of proteinases secreted by the Gram-positive Staphylococcus aureus. These staphylococcal cysteine proteases are secreted as preproenzymes that are proteolytically cleaved to generate the mature enzyme.


Pssm-ID: 398922  Cd Length: 174  Bit Score: 341.55  E-value: 1.39e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446750482  215 YNEQYVNKLENFKIRETQGNNGWCAGYTMSALLNATYNTNKYHAEAVMRFLHPNLQGQQFQFTGLTPREMIYFGQTQGRS 294
Cdd:pfam05543   1 DQVQYENTLKNFKIRETQGDNSWCAGYTMSALLNATYNTNTYNAEDVMRTLHPNLSGQDFQFTGLTPNEMIEFGKSQGRD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446750482  295 PQLLNRMTTYNEVDNLTKNNKGIAILGSRVESRNGMHAGHAMAVVGNAKLDNGQEVIIIWNPWDNGFMTQDAKNNVIPVS 374
Cdd:pfam05543  81 IQYLNRMTSYNEVDQLTKNNVGIAILGQRVESPNGPHAGHAMAVVGNAKINNGQEVIIIWNPWDNGLMTQDADSNLIPVS 160
                         170
                  ....*....|....
gi 446750482  375 NGDHYQWYSSIYGY 388
Cdd:pfam05543 161 NGDHYNWYGSIYGY 174
Staphopain_pro pfam14731
Staphopain proregion; This domain is the proregion of the cysteine protease staphopain. Like ...
37-203 1.59e-85

Staphopain proregion; This domain is the proregion of the cysteine protease staphopain. Like many papain type peptidases, staphopain is synthesized as an inactive precursor and cleavage of the proregion is required for activation. This proregion has a half-barrel or barrel-sandwich hybrid fold. The proregion blocks the active site cleft of the mature enzyme on one side of the nucleophilic cysteine


Pssm-ID: 291401  Cd Length: 169  Bit Score: 257.21  E-value: 1.59e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446750482   37 RHVQVNVEDKSVPTDVRNLAQKDYLSYVTSLDKIYNKEKASYTLGEPFKIYKFNKKSDGNYYFPVLNTEGNIDYIVTISP 116
Cdd:pfam14731   1 KQLEVNVKSKKVPQKVRDLAQQQYLSYVKALDKQSNAKTGSYTLGEPFKIYKFNKESDGNYYYPVLNKDGKIVYTVTISP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446750482  117 KVTKD--SSSSSKYTINVSSFLSKALNQYKDQQITILTNSKGYYVVTQNHKAKLVLKTPRLEDKKVKKTESIPTGNNVTQ 194
Cdd:pfam14731  81 KNKDDkkSKEDMNYSINVSPFLSKDLNQYKDQNITILTNEKGYYVFTEDGKVRLVLKTPRLNNKKEKESAKTVSPKLKQE 160

                  ....*....
gi 446750482  195 LKQKASVTM 203
Cdd:pfam14731 161 LKQTASVTK 169
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH