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Conserved domains on  [gi|914333838|ref|NP_001298719|]
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dipeptidyl peptidase 1 isoform 2 precursor [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CathepsinC_exc super family cl07399
Cathepsin C exclusion domain; Cathepsin C (dipeptidyl peptidase I) is the physiological ...
 25-106 2.18e-42

Cathepsin C exclusion domain; Cathepsin C (dipeptidyl peptidase I) is the physiological activator of a group of serine proteases. This domain corresponds to the exclusion domain whose structure excludes the approach of a polypeptide apart from its termini. It forms an enclosed beta barrel structure composed from 8 anti-parallel beta strands. Based on a structural comparison and interaction data, it is suggested that the exclusion domain originates from a metallo-protease inhibitor.


The actual alignment was detected with superfamily member pfam08773:

Pssm-ID: 462598 [Multi-domain]  Cd Length: 118  Bit Score: 135.87  E-value: 2.18e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914333838   25 DTPANCTYPDLLGTWVFQVGPRSSRSDINCSVM----EATEEKVVVHLKKLDTAYDELGNSGHFTLIYNQGFEIVLNDYK 100
Cdd:pfam08773   1 DTPANCTYEDIVGTWVFQVGEGGNDKRVNCSHPgpdnFNTSKTVTVSLQKPDVAIDELGNTGFWTLIYNQGFEVVINGRK 80


                  ....*.
gi 914333838  101 WFAFFK 106
Cdd:pfam08773  81 YFAFFK 86
 
Name Accession Description Interval E-value
CathepsinC_exc pfam08773
Cathepsin C exclusion domain; Cathepsin C (dipeptidyl peptidase I) is the physiological ...
 25-106 2.18e-42

Cathepsin C exclusion domain; Cathepsin C (dipeptidyl peptidase I) is the physiological activator of a group of serine proteases. This domain corresponds to the exclusion domain whose structure excludes the approach of a polypeptide apart from its termini. It forms an enclosed beta barrel structure composed from 8 anti-parallel beta strands. Based on a structural comparison and interaction data, it is suggested that the exclusion domain originates from a metallo-protease inhibitor.


Pssm-ID: 462598 [Multi-domain]  Cd Length: 118  Bit Score: 135.87  E-value: 2.18e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914333838   25 DTPANCTYPDLLGTWVFQVGPRSSRSDINCSVM----EATEEKVVVHLKKLDTAYDELGNSGHFTLIYNQGFEIVLNDYK 100
Cdd:pfam08773   1 DTPANCTYEDIVGTWVFQVGEGGNDKRVNCSHPgpdnFNTSKTVTVSLQKPDVAIDELGNTGFWTLIYNQGFEVVINGRK 80


                  ....*.
gi 914333838  101 WFAFFK 106
Cdd:pfam08773  81 YFAFFK 86
PTZ00364 PTZ00364
dipeptidyl-peptidase I precursor; Provisional
 25-109 7.78e-08

dipeptidyl-peptidase I precursor; Provisional


Pssm-ID: 240381 [Multi-domain]  Cd Length: 548  Bit Score: 49.89  E-value: 7.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914333838  25 DTPANCTYPDLLGTWVFQV-GPRSSRSD--INC-SVMEATEEKVVVHLKKLDTAYDELGNSGHFTLIYNQGFEIVLNDYK 100
Cdd:PTZ00364  14 YTPARCLSDQYLGLWSFTItKFKYLKTNdrVECpASISSRVTKLIVTLMPNGAAQEQGGATGRWTPVYNHGFEIRIAGLV 93


                 ....*....
gi 914333838 101 WFAFFKDVT 109
Cdd:PTZ00364  94 YLFISAWAE 102
 
Name Accession Description Interval E-value
CathepsinC_exc pfam08773
Cathepsin C exclusion domain; Cathepsin C (dipeptidyl peptidase I) is the physiological ...
 25-106 2.18e-42

Cathepsin C exclusion domain; Cathepsin C (dipeptidyl peptidase I) is the physiological activator of a group of serine proteases. This domain corresponds to the exclusion domain whose structure excludes the approach of a polypeptide apart from its termini. It forms an enclosed beta barrel structure composed from 8 anti-parallel beta strands. Based on a structural comparison and interaction data, it is suggested that the exclusion domain originates from a metallo-protease inhibitor.


Pssm-ID: 462598 [Multi-domain]  Cd Length: 118  Bit Score: 135.87  E-value: 2.18e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914333838   25 DTPANCTYPDLLGTWVFQVGPRSSRSDINCSVM----EATEEKVVVHLKKLDTAYDELGNSGHFTLIYNQGFEIVLNDYK 100
Cdd:pfam08773   1 DTPANCTYEDIVGTWVFQVGEGGNDKRVNCSHPgpdnFNTSKTVTVSLQKPDVAIDELGNTGFWTLIYNQGFEVVINGRK 80


                  ....*.
gi 914333838  101 WFAFFK 106
Cdd:pfam08773  81 YFAFFK 86
PTZ00364 PTZ00364
dipeptidyl-peptidase I precursor; Provisional
 25-109 7.78e-08

dipeptidyl-peptidase I precursor; Provisional


Pssm-ID: 240381 [Multi-domain]  Cd Length: 548  Bit Score: 49.89  E-value: 7.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914333838  25 DTPANCTYPDLLGTWVFQV-GPRSSRSD--INC-SVMEATEEKVVVHLKKLDTAYDELGNSGHFTLIYNQGFEIVLNDYK 100
Cdd:PTZ00364  14 YTPARCLSDQYLGLWSFTItKFKYLKTNdrVECpASISSRVTKLIVTLMPNGAAQEQGGATGRWTPVYNHGFEIRIAGLV 93


                 ....*....
gi 914333838 101 WFAFFKDVT 109
Cdd:PTZ00364  94 YLFISAWAE 102
 
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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