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Conserved domains on  [gi|18409953|ref|NP_565029|]
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Proteinase inhibitor, propeptide [Arabidopsis thaliana]

Protein Classification

Inhibitor_I9 domain-containing protein( domain architecture ID 10531338)

Inhibitor_I9 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Inhibitor_I9 pfam05922
Peptidase inhibitor I9; This family includes the proteinase B inhibitor from Saccharomyces ...
 49-125 1.80e-17

Peptidase inhibitor I9; This family includes the proteinase B inhibitor from Saccharomyces cerevisiae and the activation peptides from peptidases of the subtilisin family. The subtilisin propeptides are known to function as molecular chaperones, assisting in the folding of the mature peptidase, but have also been shown to act as 'temporary inhibitors'.


:

Pssm-ID: 428674  Cd Length: 82  Bit Score: 71.56  E-value: 1.80e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409953    49 VHIIYTEKPTDEEPKTY-----HLRTLSSALGSEEAAKDALIYSYKEAASGFSAKLTPEQVAEISKQPGVIQVVPSQTYQ 123
Cdd:pfam05922   1 TYIVYLKEGAAAADSFSshtewHSSLLRSVLSEESSAEAGILYSYKIGFNGFAAKLTEEEAEKLRKHPEVVSVEPDQVVK 80


                  ..
gi 18409953   124 LH 125
Cdd:pfam05922  81 LH 82
 
Name Accession Description Interval E-value
Inhibitor_I9 pfam05922
Peptidase inhibitor I9; This family includes the proteinase B inhibitor from Saccharomyces ...
 49-125 1.80e-17

Peptidase inhibitor I9; This family includes the proteinase B inhibitor from Saccharomyces cerevisiae and the activation peptides from peptidases of the subtilisin family. The subtilisin propeptides are known to function as molecular chaperones, assisting in the folding of the mature peptidase, but have also been shown to act as 'temporary inhibitors'.


Pssm-ID: 428674  Cd Length: 82  Bit Score: 71.56  E-value: 1.80e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409953    49 VHIIYTEKPTDEEPKTY-----HLRTLSSALGSEEAAKDALIYSYKEAASGFSAKLTPEQVAEISKQPGVIQVVPSQTYQ 123
Cdd:pfam05922   1 TYIVYLKEGAAAADSFSshtewHSSLLRSVLSEESSAEAGILYSYKIGFNGFAAKLTEEEAEKLRKHPEVVSVEPDQVVK 80


                  ..
gi 18409953   124 LH 125
Cdd:pfam05922  81 LH 82
 
Name Accession Description Interval E-value
Inhibitor_I9 pfam05922
Peptidase inhibitor I9; This family includes the proteinase B inhibitor from Saccharomyces ...
 49-125 1.80e-17

Peptidase inhibitor I9; This family includes the proteinase B inhibitor from Saccharomyces cerevisiae and the activation peptides from peptidases of the subtilisin family. The subtilisin propeptides are known to function as molecular chaperones, assisting in the folding of the mature peptidase, but have also been shown to act as 'temporary inhibitors'.


Pssm-ID: 428674  Cd Length: 82  Bit Score: 71.56  E-value: 1.80e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18409953    49 VHIIYTEKPTDEEPKTY-----HLRTLSSALGSEEAAKDALIYSYKEAASGFSAKLTPEQVAEISKQPGVIQVVPSQTYQ 123
Cdd:pfam05922   1 TYIVYLKEGAAAADSFSshtewHSSLLRSVLSEESSAEAGILYSYKIGFNGFAAKLTEEEAEKLRKHPEVVSVEPDQVVK 80


                  ..
gi 18409953   124 LH 125
Cdd:pfam05922  81 LH 82
 
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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