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Conserved domains on  [gi|999627|pdb|1EPT|B]
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Chain B, PORCINE E-TRYPSIN

Protein Classification

serine protease family protein( domain architecture ID 229414)

trypsin-like serine protease family protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Tryp_SPc super family cl21584
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
1-82 1.40e-33

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


The actual alignment was detected with superfamily member cd00190:

Pssm-ID: 451320 [Multi-domain]  Cd Length: 232  Bit Score: 114.68  E-value: 1.40e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EPT_B        1 SRIQVRLGEHNIDVLEGNEQFINAAKIITHPNFNGNTLDNDIMLIKLSSPATLNSRVATVSLPRS--CAAAGTECLISGW 78
Cdd:cd00190  50 SNYTVRLGSHDLSSNEGGGQVIKVKKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSgyNLPAGTTCTVSGW 129

                ....
1EPT_B       79 GNTK 82
Cdd:cd00190 130 GRTS 133
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
1-82 1.40e-33

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 114.68  E-value: 1.40e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EPT_B        1 SRIQVRLGEHNIDVLEGNEQFINAAKIITHPNFNGNTLDNDIMLIKLSSPATLNSRVATVSLPRS--CAAAGTECLISGW 78
Cdd:cd00190  50 SNYTVRLGSHDLSSNEGGGQVIKVKKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSgyNLPAGTTCTVSGW 129

                ....
1EPT_B       79 GNTK 82
Cdd:cd00190 130 GRTS 133
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
1-82 3.66e-31

Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.


Pssm-ID: 214473 [Multi-domain]  Cd Length: 229  Bit Score: 108.53  E-value: 3.66e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EPT_B           1 SRIQVRLGEHNIDVlEGNEQFINAAKIITHPNFNGNTLDNDIMLIKLSSPATLNSRVATVSLPRS--CAAAGTECLISGW 78
Cdd:smart00020  51 SNIRVRLGSHDLSS-GEEGQVIKVSKVIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSnyNVPAGTTCTVSGW 129

                   ....
1EPT_B          79 GNTK 82
Cdd:smart00020 130 GRTS 133
Trypsin pfam00089
Trypsin;
1-82 6.49e-29

Trypsin;


Pssm-ID: 395042 [Multi-domain]  Cd Length: 219  Bit Score: 102.52  E-value: 6.49e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EPT_B          1 SRIQVRLGEHNIDVLEGNEQFINAAKIITHPNFNGNTLDNDIMLIKLSSPATLNSRVATVSLPRSCA--AAGTECLISGW 78
Cdd:pfam00089  48 SDVKVVLGAHNIVLREGGEQKFDVEKIIVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSdlPVGTTCTVSGW 127

                  ....
1EPT_B         79 GNTK 82
Cdd:pfam00089 128 GNTK 131
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
1-82 1.40e-33

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 114.68  E-value: 1.40e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EPT_B        1 SRIQVRLGEHNIDVLEGNEQFINAAKIITHPNFNGNTLDNDIMLIKLSSPATLNSRVATVSLPRS--CAAAGTECLISGW 78
Cdd:cd00190  50 SNYTVRLGSHDLSSNEGGGQVIKVKKVIVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSgyNLPAGTTCTVSGW 129

                ....
1EPT_B       79 GNTK 82
Cdd:cd00190 130 GRTS 133
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
1-82 3.66e-31

Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.


Pssm-ID: 214473 [Multi-domain]  Cd Length: 229  Bit Score: 108.53  E-value: 3.66e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EPT_B           1 SRIQVRLGEHNIDVlEGNEQFINAAKIITHPNFNGNTLDNDIMLIKLSSPATLNSRVATVSLPRS--CAAAGTECLISGW 78
Cdd:smart00020  51 SNIRVRLGSHDLSS-GEEGQVIKVSKVIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSnyNVPAGTTCTVSGW 129

                   ....
1EPT_B          79 GNTK 82
Cdd:smart00020 130 GRTS 133
Trypsin pfam00089
Trypsin;
1-82 6.49e-29

Trypsin;


Pssm-ID: 395042 [Multi-domain]  Cd Length: 219  Bit Score: 102.52  E-value: 6.49e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1EPT_B          1 SRIQVRLGEHNIDVLEGNEQFINAAKIITHPNFNGNTLDNDIMLIKLSSPATLNSRVATVSLPRSCA--AAGTECLISGW 78
Cdd:pfam00089  48 SDVKVVLGAHNIVLREGGEQKFDVEKIIVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSdlPVGTTCTVSGW 127

                  ....
1EPT_B         79 GNTK 82
Cdd:pfam00089 128 GNTK 131
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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