2C0Y,1CJL,3F75


Conserved Protein Domain Family
Inhibitor_I29

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smart00848: Inhibitor_I29 
Cathepsin propeptide inhibitor domain (I29)
This domain is found at the N-terminus of some C1 peptidases such as Cathepsin L where it acts as a propeptide. There are also a number of proteins that are composed solely of multiple copies of this domain such as the peptidase inhibitor salarin. This family is classified as I29 by MEROPS. Peptide proteinase inhibitors can be found as single domain proteins or as single or multiple domains within proteins; these are referred to as either simple or compound inhibitors, respectively. In many cases they are synthesised as part of a larger precursor protein, either as a prepropeptide or as an N-terminal domain associated with an inactive peptidase or zymogen. This domain prevents access of the substrate to the active site. Removal of the N-terminal inhibitor domain either by interaction with a second peptidase or by autocatalytic cleavage activates the zymogen. Other inhibitors interact direct with proteinases using a simple noncovalent lock and key mechanism; while yet others use a conformational change-based trapping mechanism that depends on their structural and thermodynamic properties.
Statistics
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PSSM-Id: 214853
Aligned: 578 rows
Threshold Bit Score: 32.6006
Threshold Setting Gi: 67476440
Created: 13-Jul-2011
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
PubMed ReferencesClick to see Conserved Features Help

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
2C0Y_A        12 WHLWKKTYGKqYKEKNEEAVRR-LIWEKNLKFVMLHNLEHsmgmhSYDLGMNH-LGDMTSEE 71  human
XP_952571    129 FNDFNKHHDRkHNNYRHKKASY-NNFRNNLNDINEHNSKPn---mSYTKSMNH-FGDVSPKD 185 Theileria annulata strain Ankara
XP_764666    180 FKSFISRYEKkYKDEDEYKTRY-LNFRDNRIFIETHNSNHn---kIFTMGYTS-STDSSDEE 236 Theileria parva strain Muguga
XP_952610    180 FKSFLKRYLKtYKDLNEYKARY-LNFRVNRIFIETHNSNLn---kLYTMGYTT-AADNSDQE 236 Theileria annulata strain Ankara
XP_001016704  41 lnifssygyvanpsseRF-----KIFKQRLIDIIKHNLNph---kTYTQKINK-FSFYTQEE 93  Tetrahymena thermophila
XP_001015137  41 lklfgsygfypnqnseRF-----QLFKKRVAKIAEHNLNpn---kKYTQKISK-FTFYTNEE 93  Tetrahymena thermophila
XP_001027491  36 HDDYVLSLARlYRPHLNVEHLEfQHFKESVRRVREHNKKvn---aTYTLSIDSpFAFMSDEQ 94  Tetrahymena thermophila
XP_764668    150 HRDFLRKYFKvYRTKKAFMESY-TNFRLNRKRIEDHNnkp---drLYNMTLTN-FAD-TDGD 205 Theileria parva strain Muguga
XP_001021616  56 hqqtkqtllgdseysETYRL---TNFKENLLKISEHNKKfidghySFTMKLNQ-FAHLSSEE 113 Tetrahymena thermophila
XP_763301    120 FDSFVEKHKRvHKTFDQRLERF-LIFRKNFYIVRAHKVSe-----pYSLELNK-FADLSEEE 174 Theileria parva strain Muguga
XP_952571    129 FNDFNKHHDRkHNNYRHKKASY-NNFRNNLNDINEHNSKPn---mSYTKSMNH-FGDVSPKD 185 Theileria annulata strain Ankara
XP_764666    180 FKSFISRYEKkYKDEDEYKTRY-LNFRDNRIFIETHNSNHn---kIFTMGYTS-STDSSDEE 236 Theileria parva strain Muguga
XP_952610    180 FKSFLKRYLKtYKDLNEYKARY-LNFRVNRIFIETHNSNLn---kLYTMGYTT-AADNSDQE 236 Theileria annulata strain Ankara
XP_001016704  41 lnifssygyvanpsseRF-----KIFKQRLIDIIKHNLNph---kTYTQKINK-FSFYTQEE 93  Tetrahymena thermophila
XP_001015137  41 lklfgsygfypnqnseRF-----QLFKKRVAKIAEHNLNpn---kKYTQKISK-FTFYTNEE 93  Tetrahymena thermophila
XP_001027491  36 HDDYVLSLARlYRPHLNVEHLEfQHFKESVRRVREHNKKvn---aTYTLSIDSpFAFMSDEQ 94  Tetrahymena thermophila
XP_764668    150 HRDFLRKYFKvYRTKKAFMESY-TNFRLNRKRIEDHNnkp---drLYNMTLTN-FAD-TDGD 205 Theileria parva strain Muguga
XP_001021616  56 hqqtkqtllgdseysETYRL---TNFKENLLKISEHNKKfidghySFTMKLNQ-FAHLSSEE 113 Tetrahymena thermophila
XP_763301    120 FDSFVEKHKRvHKTFDQRLERF-LIFRKNFYIVRAHKVSe-----pYSLELNK-FADLSEEE 174 Theileria parva strain Muguga
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