Cysteine proteinases superfamily protein [Arabidopsis thaliana]
Protein Classification
C1 family peptidase( domain architecture ID 581054)
C1 family peptidase (also called papain family protein) may be an endopeptidase or an exopeptidase, and may be involved in protein degradation
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| Peptidase_C1 super family | cl23744 | C1 Peptidase family (MEROPS database nomenclature), also referred to as the papain family; ... |
4-156 | 1.68e-12 | ||||
C1 Peptidase family (MEROPS database nomenclature), also referred to as the papain family; composed of two subfamilies of cysteine peptidases (CPs), C1A (papain) and C1B (bleomycin hydrolase). Papain-like enzymes are mostly endopeptidases with some exceptions like cathepsins B, C, H and X, which are exopeptidases. Papain-like CPs have different functions in various organisms. Plant CPs are used to mobilize storage proteins in seeds while mammalian CPs are primarily lysosomal enzymes responsible for protein degradation in the lysosome. Papain-like CPs are synthesized as inactive proenzymes with N-terminal propeptide regions, which are removed upon activation. Bleomycin hydrolase (BH) is a CP that detoxifies bleomycin by hydrolysis of an amide group. It acts as a carboxypeptidase on its C-terminus to convert itself into an aminopeptidase and peptide ligase. BH is found in all tissues in mammals as well as in many other eukaryotes. It forms a hexameric ring barrel structure with the active sites imbedded in the central channel. Some members of the C1 family are proteins classified as non-peptidase homologs which lack peptidase activity or have missing active site residues. The actual alignment was detected with superfamily member cd02619: Pssm-ID: 451520 [Multi-domain] Cd Length: 223 Bit Score: 66.00 E-value: 1.68e-12
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| Name | Accession | Description | Interval | E-value | ||||
| Peptidase_C1 | cd02619 | C1 Peptidase family (MEROPS database nomenclature), also referred to as the papain family; ... |
4-156 | 1.68e-12 | ||||
C1 Peptidase family (MEROPS database nomenclature), also referred to as the papain family; composed of two subfamilies of cysteine peptidases (CPs), C1A (papain) and C1B (bleomycin hydrolase). Papain-like enzymes are mostly endopeptidases with some exceptions like cathepsins B, C, H and X, which are exopeptidases. Papain-like CPs have different functions in various organisms. Plant CPs are used to mobilize storage proteins in seeds while mammalian CPs are primarily lysosomal enzymes responsible for protein degradation in the lysosome. Papain-like CPs are synthesized as inactive proenzymes with N-terminal propeptide regions, which are removed upon activation. Bleomycin hydrolase (BH) is a CP that detoxifies bleomycin by hydrolysis of an amide group. It acts as a carboxypeptidase on its C-terminus to convert itself into an aminopeptidase and peptide ligase. BH is found in all tissues in mammals as well as in many other eukaryotes. It forms a hexameric ring barrel structure with the active sites imbedded in the central channel. Some members of the C1 family are proteins classified as non-peptidase homologs which lack peptidase activity or have missing active site residues. Pssm-ID: 239110 [Multi-domain] Cd Length: 223 Bit Score: 66.00 E-value: 1.68e-12
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| Name | Accession | Description | Interval | E-value | ||||
| Peptidase_C1 | cd02619 | C1 Peptidase family (MEROPS database nomenclature), also referred to as the papain family; ... |
4-156 | 1.68e-12 | ||||
C1 Peptidase family (MEROPS database nomenclature), also referred to as the papain family; composed of two subfamilies of cysteine peptidases (CPs), C1A (papain) and C1B (bleomycin hydrolase). Papain-like enzymes are mostly endopeptidases with some exceptions like cathepsins B, C, H and X, which are exopeptidases. Papain-like CPs have different functions in various organisms. Plant CPs are used to mobilize storage proteins in seeds while mammalian CPs are primarily lysosomal enzymes responsible for protein degradation in the lysosome. Papain-like CPs are synthesized as inactive proenzymes with N-terminal propeptide regions, which are removed upon activation. Bleomycin hydrolase (BH) is a CP that detoxifies bleomycin by hydrolysis of an amide group. It acts as a carboxypeptidase on its C-terminus to convert itself into an aminopeptidase and peptide ligase. BH is found in all tissues in mammals as well as in many other eukaryotes. It forms a hexameric ring barrel structure with the active sites imbedded in the central channel. Some members of the C1 family are proteins classified as non-peptidase homologs which lack peptidase activity or have missing active site residues. Pssm-ID: 239110 [Multi-domain] Cd Length: 223 Bit Score: 66.00 E-value: 1.68e-12
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