NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|15240266|ref|NP_198568|]
View 

NEP-interacting protein, putative (DUF239) [Arabidopsis thaliana]

Protein Classification

neprosin family prolyl endopeptidase( domain architecture ID 10503710)

neprosin family prolyl endopeptidase is a peptidase of unknown catalytic type, unaffected by standard peptidase inhibitors. Activity may be directed towards prolyl bonds with no restriction on sequence length or position of the proline residue

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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. ...
12-196 4.57e-53

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: 168.96  E-value: 4.57e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240266    12 SPQFSSSRMHVQIGD---DFIQAGWT---------------------AGQNQCYNSLCPaGIILVRSDIPLGGLRGPPGV 67
Cdd:pfam03080   1 PDQFSLAQIWISSGPgglNSIEAGWQvnpslygdsrtrlftywtadgYQKTGCYNLLCP-GFVQVSSDIPLGGAISPVSV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240266    68 RGSTQiVYDTYGLLKDKANGNWWLEFGGIQ-IGFWPANIF---QQSLANSVEWGGEVYS--ASLPGPRMGNGYFPLLDPV 141
Cdd:pfam03080  80 YGGKQ-YEITLSIFKDPKTGNWWLYYGGDEvIGYWPASLFthlLAGSANLVEWGGEVYSptGSHTSPPMGSGHFPSEGFG 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 15240266   142 DDAHVCNITLVDENFkVDKMVKNIETFSDNNHSYKVYEDLDSGlPVGHIIYFGGP 196
Cdd:pfam03080 159 KAAYFRNIKIVDDSN-GLPPPQDLETLADSPKCYNVIIFGYSG-DWGSYFYYGGP 211
 
Name Accession Description Interval E-value
Neprosin pfam03080
Neprosin; Pitcher plants are insectivorous and secrete a digestive fluid into the pitcher. ...
12-196 4.57e-53

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: 168.96  E-value: 4.57e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240266    12 SPQFSSSRMHVQIGD---DFIQAGWT---------------------AGQNQCYNSLCPaGIILVRSDIPLGGLRGPPGV 67
Cdd:pfam03080   1 PDQFSLAQIWISSGPgglNSIEAGWQvnpslygdsrtrlftywtadgYQKTGCYNLLCP-GFVQVSSDIPLGGAISPVSV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240266    68 RGSTQiVYDTYGLLKDKANGNWWLEFGGIQ-IGFWPANIF---QQSLANSVEWGGEVYS--ASLPGPRMGNGYFPLLDPV 141
Cdd:pfam03080  80 YGGKQ-YEITLSIFKDPKTGNWWLYYGGDEvIGYWPASLFthlLAGSANLVEWGGEVYSptGSHTSPPMGSGHFPSEGFG 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 15240266   142 DDAHVCNITLVDENFkVDKMVKNIETFSDNNHSYKVYEDLDSGlPVGHIIYFGGP 196
Cdd:pfam03080 159 KAAYFRNIKIVDDSN-GLPPPQDLETLADSPKCYNVIIFGYSG-DWGSYFYYGGP 211
 
Name Accession Description Interval E-value
Neprosin pfam03080
Neprosin; Pitcher plants are insectivorous and secrete a digestive fluid into the pitcher. ...
12-196 4.57e-53

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: 168.96  E-value: 4.57e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240266    12 SPQFSSSRMHVQIGD---DFIQAGWT---------------------AGQNQCYNSLCPaGIILVRSDIPLGGLRGPPGV 67
Cdd:pfam03080   1 PDQFSLAQIWISSGPgglNSIEAGWQvnpslygdsrtrlftywtadgYQKTGCYNLLCP-GFVQVSSDIPLGGAISPVSV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240266    68 RGSTQiVYDTYGLLKDKANGNWWLEFGGIQ-IGFWPANIF---QQSLANSVEWGGEVYS--ASLPGPRMGNGYFPLLDPV 141
Cdd:pfam03080  80 YGGKQ-YEITLSIFKDPKTGNWWLYYGGDEvIGYWPASLFthlLAGSANLVEWGGEVYSptGSHTSPPMGSGHFPSEGFG 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 15240266   142 DDAHVCNITLVDENFkVDKMVKNIETFSDNNHSYKVYEDLDSGlPVGHIIYFGGP 196
Cdd:pfam03080 159 KAAYFRNIKIVDDSN-GLPPPQDLETLADSPKCYNVIIFGYSG-DWGSYFYYGGP 211
 
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