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Conserved domains on  [gi|2065779077|gb|KAG7547557|]
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Papain-like cysteine peptidase superfamily [Arabidopsis suecica]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SCRL pfam06876
Plant self-incompatibility response (SCRL) protein; This family consists of several Plant ...
 15-88 5.26e-21

Plant self-incompatibility response (SCRL) protein; This family consists of several Plant self-incompatibility response (SCRL) proteins. The male component of the self-incompatibility response in Brassica has been shown to be encoded by the S locus cysteine-rich gene (SCR). SCR is related, at the sequence level, to the pollen coat protein (PCP) gene family whose members encode small, cysteine-rich proteins located in the proteo-lipidic surface layer (tryphine) of Brassica pollen grains.


:

Pssm-ID: 369118  Cd Length: 67  Bit Score: 83.60  E-value: 5.26e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2065779077  15 FLILSHVEESEAGAPPvDCWSEILFPGKCGFHGKKKCYKEMESKLKQRVLKCSCEDvkpdpkTPKDQHYCGCQR 88
Cdd:pfam06876   1 FIVSSHVQEVEANLMK-RCTRKQTFPGKCGNDGNKTCEKDFKKKVKKKPFSCTCTP------SHKGKRLCTCKR 67
Peptidase_C1 super family cl23744
C1 Peptidase family (MEROPS database nomenclature), also referred to as the papain family; ...
 90-196 3.87e-04

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: 40.58  E-value: 3.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065779077  90 NPYEYYWRQVCKRSPAMYNYsRSPGFYAEREVSIKSMKKELQRLEIWPSDAALSEDLMF----MLYPRRLLMRGQGNRA- 164
Cdd:cd02619    93 GAESDGEEPKSEAALNAAKV-KLKDYRRVLKNNIEDIKEALAKGGPVVAGFDVYSGFDRlkegIIYEEIVYLLYEDGDLg 171

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2065779077 165 --------------EGRLFWIIQNSWGKGWGE----TMDMHTFTAKLYED 196
Cdd:cd02619   172 ghavvivgyddnyvEGKGAFIVKNSWGTDWGDngygRISYEDVYEMTFGA 221
 
Name Accession Description Interval E-value
SCRL pfam06876
Plant self-incompatibility response (SCRL) protein; This family consists of several Plant ...
 15-88 5.26e-21

Plant self-incompatibility response (SCRL) protein; This family consists of several Plant self-incompatibility response (SCRL) proteins. The male component of the self-incompatibility response in Brassica has been shown to be encoded by the S locus cysteine-rich gene (SCR). SCR is related, at the sequence level, to the pollen coat protein (PCP) gene family whose members encode small, cysteine-rich proteins located in the proteo-lipidic surface layer (tryphine) of Brassica pollen grains.


Pssm-ID: 369118  Cd Length: 67  Bit Score: 83.60  E-value: 5.26e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2065779077  15 FLILSHVEESEAGAPPvDCWSEILFPGKCGFHGKKKCYKEMESKLKQRVLKCSCEDvkpdpkTPKDQHYCGCQR 88
Cdd:pfam06876   1 FIVSSHVQEVEANLMK-RCTRKQTFPGKCGNDGNKTCEKDFKKKVKKKPFSCTCTP------SHKGKRLCTCKR 67
Peptidase_C1 cd02619
C1 Peptidase family (MEROPS database nomenclature), also referred to as the papain family; ...
 90-196 3.87e-04

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: 40.58  E-value: 3.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065779077  90 NPYEYYWRQVCKRSPAMYNYsRSPGFYAEREVSIKSMKKELQRLEIWPSDAALSEDLMF----MLYPRRLLMRGQGNRA- 164
Cdd:cd02619    93 GAESDGEEPKSEAALNAAKV-KLKDYRRVLKNNIEDIKEALAKGGPVVAGFDVYSGFDRlkegIIYEEIVYLLYEDGDLg 171

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2065779077 165 --------------EGRLFWIIQNSWGKGWGE----TMDMHTFTAKLYED 196
Cdd:cd02619   172 ghavvivgyddnyvEGKGAFIVKNSWGTDWGDngygRISYEDVYEMTFGA 221
COG4870 COG4870
Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones];
170-182 1.65e-03

Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443898 [Multi-domain]  Cd Length: 426  Bit Score: 39.35  E-value: 1.65e-03
                          10
                  ....*....|...
gi 2065779077 170 WIIQNSWGKGWGE 182
Cdd:COG4870   193 FIIKNSWGTGWGD 205
Pept_C1 smart00645
Papain family cysteine protease;
165-182 2.05e-03

Papain family cysteine protease;


Pssm-ID: 214761 [Multi-domain]  Cd Length: 175  Bit Score: 37.95  E-value: 2.05e-03
                           10
                   ....*....|....*...
gi 2065779077  165 EGRLFWIIQNSWGKGWGE 182
Cdd:smart00645 134 NGKDYWIVKNSWGTDWGE 151
Peptidase_C1 pfam00112
Papain family cysteine protease;
169-182 4.48e-03

Papain family cysteine protease;


Pssm-ID: 425470 [Multi-domain]  Cd Length: 214  Bit Score: 37.52  E-value: 4.48e-03
                          10
                  ....*....|....
gi 2065779077 169 FWIIQNSWGKGWGE 182
Cdd:pfam00112 177 YWIVKNSWGTDWGE 190
 
Name Accession Description Interval E-value
SCRL pfam06876
Plant self-incompatibility response (SCRL) protein; This family consists of several Plant ...
 15-88 5.26e-21

Plant self-incompatibility response (SCRL) protein; This family consists of several Plant self-incompatibility response (SCRL) proteins. The male component of the self-incompatibility response in Brassica has been shown to be encoded by the S locus cysteine-rich gene (SCR). SCR is related, at the sequence level, to the pollen coat protein (PCP) gene family whose members encode small, cysteine-rich proteins located in the proteo-lipidic surface layer (tryphine) of Brassica pollen grains.


Pssm-ID: 369118  Cd Length: 67  Bit Score: 83.60  E-value: 5.26e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2065779077  15 FLILSHVEESEAGAPPvDCWSEILFPGKCGFHGKKKCYKEMESKLKQRVLKCSCEDvkpdpkTPKDQHYCGCQR 88
Cdd:pfam06876   1 FIVSSHVQEVEANLMK-RCTRKQTFPGKCGNDGNKTCEKDFKKKVKKKPFSCTCTP------SHKGKRLCTCKR 67
Peptidase_C1 cd02619
C1 Peptidase family (MEROPS database nomenclature), also referred to as the papain family; ...
 90-196 3.87e-04

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: 40.58  E-value: 3.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065779077  90 NPYEYYWRQVCKRSPAMYNYsRSPGFYAEREVSIKSMKKELQRLEIWPSDAALSEDLMF----MLYPRRLLMRGQGNRA- 164
Cdd:cd02619    93 GAESDGEEPKSEAALNAAKV-KLKDYRRVLKNNIEDIKEALAKGGPVVAGFDVYSGFDRlkegIIYEEIVYLLYEDGDLg 171

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2065779077 165 --------------EGRLFWIIQNSWGKGWGE----TMDMHTFTAKLYED 196
Cdd:cd02619   172 ghavvivgyddnyvEGKGAFIVKNSWGTDWGDngygRISYEDVYEMTFGA 221
Peptidase_C1A cd02248
Peptidase C1A subfamily (MEROPS database nomenclature); composed of cysteine peptidases (CPs) ...
 169-182 6.04e-04

Peptidase C1A subfamily (MEROPS database nomenclature); composed of cysteine peptidases (CPs) similar to papain, including the mammalian CPs (cathepsins B, C, F, H, L, K, O, S, V, X and W). Papain is an endopeptidase with specific substrate preferences, primarily for bulky hydrophobic or aromatic residues at the S2 subsite, a hydrophobic pocket in papain that accommodates the P2 sidechain of the substrate (the second residue away from the scissile bond). Most members of the papain subfamily are endopeptidases. Some exceptions to this rule can be explained by specific details of the catalytic domains like the occluding loop in cathepsin B which confers an additional carboxydipeptidyl activity and the mini-chain of cathepsin H resulting in an N-terminal exopeptidase activity. Papain-like CPs have different functions in various organisms. Plant CPs are used to mobilize storage proteins in seeds. Parasitic CPs act extracellularly to help invade tissues and cells, to hatch or to evade the host immune system. Mammalian CPs are primarily lysosomal enzymes with the exception of cathepsin W, which is retained in the endoplasmic reticulum. They are 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. In addition to its inhibitory role, the propeptide is required for proper folding of the newly synthesized enzyme and its stabilization in denaturing pH conditions. Residues within the propeptide region also play a role in the transport of the proenzyme to lysosomes or acidified vesicles. Also included in this subfamily are proteins classified as non-peptidase homologs, which lack peptidase activity or have missing active site residues.


Pssm-ID: 239068 [Multi-domain]  Cd Length: 210  Bit Score: 39.91  E-value: 6.04e-04
                          10
                  ....*....|....
gi 2065779077 169 FWIIQNSWGKGWGE 182
Cdd:cd02248   175 YWIVKNSWGTSWGE 188
COG4870 COG4870
Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones];
170-182 1.65e-03

Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443898 [Multi-domain]  Cd Length: 426  Bit Score: 39.35  E-value: 1.65e-03
                          10
                  ....*....|...
gi 2065779077 170 WIIQNSWGKGWGE 182
Cdd:COG4870   193 FIIKNSWGTGWGD 205
Pept_C1 smart00645
Papain family cysteine protease;
165-182 2.05e-03

Papain family cysteine protease;


Pssm-ID: 214761 [Multi-domain]  Cd Length: 175  Bit Score: 37.95  E-value: 2.05e-03
                           10
                   ....*....|....*...
gi 2065779077  165 EGRLFWIIQNSWGKGWGE 182
Cdd:smart00645 134 NGKDYWIVKNSWGTDWGE 151
Peptidase_C1 pfam00112
Papain family cysteine protease;
169-182 4.48e-03

Papain family cysteine protease;


Pssm-ID: 425470 [Multi-domain]  Cd Length: 214  Bit Score: 37.52  E-value: 4.48e-03
                          10
                  ....*....|....
gi 2065779077 169 FWIIQNSWGKGWGE 182
Cdd:pfam00112 177 YWIVKNSWGTDWGE 190
Peptidase_C1A_CathepsinX cd02698
Cathepsin X; the only papain-like lysosomal cysteine peptidase exhibiting carboxymonopeptidase ...
 159-182 5.54e-03

Cathepsin X; the only papain-like lysosomal cysteine peptidase exhibiting carboxymonopeptidase activity. It can also act as a carboxydipeptidase, like cathepsin B, but has been shown to preferentially cleave substrates through a monopeptidyl carboxypeptidase pathway. The propeptide region of cathepsin X, the shortest among papain-like peptidases, is covalently attached to the active site cysteine in the inactive form of the enzyme. Little is known about the biological function of cathepsin X. Some studies point to a role in early tumorigenesis. A more recent study indicates that cathepsin X expression is restricted to immune cells suggesting a role in phagocytosis and the regulation of the immune response.


Pssm-ID: 239149  Cd Length: 239  Bit Score: 37.39  E-value: 5.54e-03
                          10        20
                  ....*....|....*....|....
gi 2065779077 159 GQGNRAEGRLFWIIQNSWGKGWGE 182
Cdd:cd02698   186 GWGVDENGVEYWIVRNSWGEPWGE 209
Peptidase_C1A_CathepsinB cd02620
Cathepsin B group; composed of cathepsin B and similar proteins, including tubulointerstitial ...
 169-182 7.25e-03

Cathepsin B group; composed of cathepsin B and similar proteins, including tubulointerstitial nephritis antigen (TIN-Ag). Cathepsin B is a lysosomal papain-like cysteine peptidase which is expressed in all tissues and functions primarily as an exopeptidase through its carboxydipeptidyl activity. Together with other cathepsins, it is involved in the degradation of proteins, proenzyme activation, Ag processing, metabolism and apoptosis. Cathepsin B has been implicated in a number of human diseases such as cancer, rheumatoid arthritis, osteoporosis and Alzheimer's disease. The unique carboxydipeptidyl activity of cathepsin B is attributed to the presence of an occluding loop in its active site which favors the binding of the C-termini of substrate proteins. Some members of this group do not possess the occluding loop. TIN-Ag is an extracellular matrix basement protein which was originally identified as a target Ag involved in anti-tubular basement membrane antibody-mediated interstitial nephritis. It plays a role in renal tubulogenesis and is defective in hereditary tubulointerstitial disorders. TIN-Ag is exclusively expressed in kidney tissues.


Pssm-ID: 239111 [Multi-domain]  Cd Length: 236  Bit Score: 36.86  E-value: 7.25e-03
                          10
                  ....*....|....
gi 2065779077 169 FWIIQNSWGKGWGE 182
Cdd:cd02620   201 YWLAANSWGTDWGE 214
 
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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