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Conserved domains on  [gi|15236547|ref|NP_193483|]
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carboxyl-terminal proteinase-like protein (DUF239) [Arabidopsis thaliana]

Protein Classification

neprosin family prolyl endopeptidase( domain architecture ID 10344120)

neprosin family prolyl endopeptidase which preferentially cleaves C-terminal to proline and may effectively degrade proteins of any size; contains a presumed activation peptide in addition to the peptidase domain

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Neprosin pfam03080
Neprosin; Pitcher plants are insectivorous and secrete a digestive fluid into the pitcher. ...
 120-317 1.04e-70

Neprosin; Pitcher plants are insectivorous and secrete a digestive fluid into the pitcher. This fluid contains a mixture of enzymes including peptidases. One of these is neprosin, characterized from the pitcher plant Nepenthes ventrata. This peptidase is of unknown catalytic type and is unaffected by standard peptidase inhibitors. Unusually, activity is directed towards prolyl bonds, but unlike most peptidase that cleave after proline, there is no restriction on sequence length or position of the proline residue. The peptidase is secreted and is presumed to possess an N-terminal activation peptide. The neprosin domain corresponds to the mature peptidase. It is not known if other proteins with this domain are peptidases.


:

Pssm-ID: 460797  Cd Length: 211  Bit Score: 218.27  E-value: 1.04e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236547   120 SNIWIEKGaPQGLNCIIFGWAIEPKFYGDNKTHFTTYWSNDGFYKTGCYNTVCKGFIQHFSDLYPGKPFDQVSTYGGRQV 199
Cdd:pfam03080   7 AQIWISSG-PGGLNSIEAGWQVNPSLYGDSRTRLFTYWTADGYQKTGCYNLLCPGFVQVSSDIPLGGAISPVSVYGGKQY 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236547   200 AANLSIIRDGPTGNWMLM-NSGALVGYWPKELFSHLGLG-ADTIRYGGLTVG------GAPMGNGKFPDKGNdlSKSSYF 271
Cdd:pfam03080  86 EITLSIFKDPKTGNWWLYyGGDEVIGYWPASLFTHLLAGsANLVEWGGEVYSptgshtSPPMGSGHFPSEGF--GKAAYF 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 15236547   272 KDMKYVDANFKNNPISELEMIVDTPKpyCFRLNYLKDQQT----ITYGGP 317
Cdd:pfam03080 164 RNIKIVDDSNGLPPPQDLETLADSPK--CYNVIIFGYSGDwgsyFYYGGP 211
Neprosin_AP super family cl16830
Neprosin activation peptide; Pitcher plants are insectivorous and secrete a digestive fluid ...
 29-82 1.28e-06

Neprosin activation peptide; Pitcher plants are insectivorous and secrete a digestive fluid into the pitcher. This fluid contains a mixture of enzymes including peptidases. One of these is neprosin, characterized from the pitcher plant Nepenthes ventrata. This peptidase is of unknown catalytic type and is unaffected by standard peptidase inhibitors. Unusually, activity is directed towards prolyl bonds, but unlike most peptidase that cleave after proline, there is no restriction on sequence length or position of the proline residue. The peptidase is secreted and is presumed to possess an N-terminal activation peptide. This domain corresponds to the presumed activation peptide.


The actual alignment was detected with superfamily member pfam14365:

Pssm-ID: 464153  Cd Length: 119  Bit Score: 46.54  E-value: 1.28e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 15236547    29 FECVDFYKQPSLQHPLLKHHKLQimsspRRSTICPRGMVPIQKFRNNANNLNAQ 82
Cdd:pfam14365  10 IDCVDIHKQPAFDHPLLKNHTIQ-----MKPPERPEGTLLESKNDGSSKEKTAW 58
 
Name Accession Description Interval E-value
Neprosin pfam03080
Neprosin; Pitcher plants are insectivorous and secrete a digestive fluid into the pitcher. ...
 120-317 1.04e-70

Neprosin; Pitcher plants are insectivorous and secrete a digestive fluid into the pitcher. This fluid contains a mixture of enzymes including peptidases. One of these is neprosin, characterized from the pitcher plant Nepenthes ventrata. This peptidase is of unknown catalytic type and is unaffected by standard peptidase inhibitors. Unusually, activity is directed towards prolyl bonds, but unlike most peptidase that cleave after proline, there is no restriction on sequence length or position of the proline residue. The peptidase is secreted and is presumed to possess an N-terminal activation peptide. The neprosin domain corresponds to the mature peptidase. It is not known if other proteins with this domain are peptidases.


Pssm-ID: 460797  Cd Length: 211  Bit Score: 218.27  E-value: 1.04e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236547   120 SNIWIEKGaPQGLNCIIFGWAIEPKFYGDNKTHFTTYWSNDGFYKTGCYNTVCKGFIQHFSDLYPGKPFDQVSTYGGRQV 199
Cdd:pfam03080   7 AQIWISSG-PGGLNSIEAGWQVNPSLYGDSRTRLFTYWTADGYQKTGCYNLLCPGFVQVSSDIPLGGAISPVSVYGGKQY 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236547   200 AANLSIIRDGPTGNWMLM-NSGALVGYWPKELFSHLGLG-ADTIRYGGLTVG------GAPMGNGKFPDKGNdlSKSSYF 271
Cdd:pfam03080  86 EITLSIFKDPKTGNWWLYyGGDEVIGYWPASLFTHLLAGsANLVEWGGEVYSptgshtSPPMGSGHFPSEGF--GKAAYF 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 15236547   272 KDMKYVDANFKNNPISELEMIVDTPKpyCFRLNYLKDQQT----ITYGGP 317
Cdd:pfam03080 164 RNIKIVDDSNGLPPPQDLETLADSPK--CYNVIIFGYSGDwgsyFYYGGP 211
Neprosin_AP pfam14365
Neprosin activation peptide; Pitcher plants are insectivorous and secrete a digestive fluid ...
 29-82 1.28e-06

Neprosin activation peptide; Pitcher plants are insectivorous and secrete a digestive fluid into the pitcher. This fluid contains a mixture of enzymes including peptidases. One of these is neprosin, characterized from the pitcher plant Nepenthes ventrata. This peptidase is of unknown catalytic type and is unaffected by standard peptidase inhibitors. Unusually, activity is directed towards prolyl bonds, but unlike most peptidase that cleave after proline, there is no restriction on sequence length or position of the proline residue. The peptidase is secreted and is presumed to possess an N-terminal activation peptide. This domain corresponds to the presumed activation peptide.


Pssm-ID: 464153  Cd Length: 119  Bit Score: 46.54  E-value: 1.28e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 15236547    29 FECVDFYKQPSLQHPLLKHHKLQimsspRRSTICPRGMVPIQKFRNNANNLNAQ 82
Cdd:pfam14365  10 IDCVDIHKQPAFDHPLLKNHTIQ-----MKPPERPEGTLLESKNDGSSKEKTAW 58
 
Name Accession Description Interval E-value
Neprosin pfam03080
Neprosin; Pitcher plants are insectivorous and secrete a digestive fluid into the pitcher. ...
 120-317 1.04e-70

Neprosin; Pitcher plants are insectivorous and secrete a digestive fluid into the pitcher. This fluid contains a mixture of enzymes including peptidases. One of these is neprosin, characterized from the pitcher plant Nepenthes ventrata. This peptidase is of unknown catalytic type and is unaffected by standard peptidase inhibitors. Unusually, activity is directed towards prolyl bonds, but unlike most peptidase that cleave after proline, there is no restriction on sequence length or position of the proline residue. The peptidase is secreted and is presumed to possess an N-terminal activation peptide. The neprosin domain corresponds to the mature peptidase. It is not known if other proteins with this domain are peptidases.


Pssm-ID: 460797  Cd Length: 211  Bit Score: 218.27  E-value: 1.04e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236547   120 SNIWIEKGaPQGLNCIIFGWAIEPKFYGDNKTHFTTYWSNDGFYKTGCYNTVCKGFIQHFSDLYPGKPFDQVSTYGGRQV 199
Cdd:pfam03080   7 AQIWISSG-PGGLNSIEAGWQVNPSLYGDSRTRLFTYWTADGYQKTGCYNLLCPGFVQVSSDIPLGGAISPVSVYGGKQY 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236547   200 AANLSIIRDGPTGNWMLM-NSGALVGYWPKELFSHLGLG-ADTIRYGGLTVG------GAPMGNGKFPDKGNdlSKSSYF 271
Cdd:pfam03080  86 EITLSIFKDPKTGNWWLYyGGDEVIGYWPASLFTHLLAGsANLVEWGGEVYSptgshtSPPMGSGHFPSEGF--GKAAYF 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 15236547   272 KDMKYVDANFKNNPISELEMIVDTPKpyCFRLNYLKDQQT----ITYGGP 317
Cdd:pfam03080 164 RNIKIVDDSNGLPPPQDLETLADSPK--CYNVIIFGYSGDwgsyFYYGGP 211
Neprosin_AP pfam14365
Neprosin activation peptide; Pitcher plants are insectivorous and secrete a digestive fluid ...
 29-82 1.28e-06

Neprosin activation peptide; Pitcher plants are insectivorous and secrete a digestive fluid into the pitcher. This fluid contains a mixture of enzymes including peptidases. One of these is neprosin, characterized from the pitcher plant Nepenthes ventrata. This peptidase is of unknown catalytic type and is unaffected by standard peptidase inhibitors. Unusually, activity is directed towards prolyl bonds, but unlike most peptidase that cleave after proline, there is no restriction on sequence length or position of the proline residue. The peptidase is secreted and is presumed to possess an N-terminal activation peptide. This domain corresponds to the presumed activation peptide.


Pssm-ID: 464153  Cd Length: 119  Bit Score: 46.54  E-value: 1.28e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 15236547    29 FECVDFYKQPSLQHPLLKHHKLQimsspRRSTICPRGMVPIQKFRNNANNLNAQ 82
Cdd:pfam14365  10 IDCVDIHKQPAFDHPLLKNHTIQ-----MKPPERPEGTLLESKNDGSSKEKTAW 58
 
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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