cathepsin M isoform X4 [Mus musculus]
Protein Classification
C1 family peptidase( domain architecture ID 10656546)
C1 family peptidase (also called papain family protein) is a papain-like cysteine peptidase that catalyzes the hydrolysis of peptide bonds in substrates using a catalytic dyad of Cys and His residues
List of domain hits
| Name | Accession | Description | Interval | E-value | |||
| Peptidase_C1A | cd02248 | Peptidase C1A subfamily (MEROPS database nomenclature); composed of cysteine peptidases (CPs) ... |
115-260 | 1.32e-64 | |||
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: 200.93 E-value: 1.32e-64
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| Inhibitor_I29 | smart00848 | Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 ... |
29-87 | 2.20e-19 | |||
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. : Pssm-ID: 214853 [Multi-domain] Cd Length: 57 Bit Score: 79.21 E-value: 2.20e-19
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| Name | Accession | Description | Interval | E-value | |||||
| Peptidase_C1A | cd02248 | Peptidase C1A subfamily (MEROPS database nomenclature); composed of cysteine peptidases (CPs) ... |
115-260 | 1.32e-64 | |||||
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: 200.93 E-value: 1.32e-64
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| Peptidase_C1 | pfam00112 | Papain family cysteine protease; |
114-260 | 4.28e-62 | |||||
Papain family cysteine protease; Pssm-ID: 425470 [Multi-domain] Cd Length: 214 Bit Score: 194.68 E-value: 4.28e-62
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| Pept_C1 | smart00645 | Papain family cysteine protease; |
114-205 | 2.84e-42 | |||||
Papain family cysteine protease; Pssm-ID: 214761 [Multi-domain] Cd Length: 175 Bit Score: 142.72 E-value: 2.84e-42
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| PTZ00021 | PTZ00021 | falcipain-2; Provisional |
36-260 | 2.11e-40 | |||||
falcipain-2; Provisional Pssm-ID: 240232 [Multi-domain] Cd Length: 489 Bit Score: 145.68 E-value: 2.11e-40
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| COG4870 | COG4870 | Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones]; |
114-260 | 2.32e-21 | |||||
Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 443898 [Multi-domain] Cd Length: 426 Bit Score: 92.50 E-value: 2.32e-21
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| Inhibitor_I29 | smart00848 | Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 ... |
29-87 | 2.20e-19 | |||||
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. Pssm-ID: 214853 [Multi-domain] Cd Length: 57 Bit Score: 79.21 E-value: 2.20e-19
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| Inhibitor_I29 | pfam08246 | Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 ... |
29-88 | 6.99e-17 | |||||
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 Swiss:Q70SU8. This family is classified as I29 by MEROPS. Pssm-ID: 462410 [Multi-domain] Cd Length: 58 Bit Score: 72.68 E-value: 6.99e-17
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| Name | Accession | Description | Interval | E-value | |||||
| Peptidase_C1A | cd02248 | Peptidase C1A subfamily (MEROPS database nomenclature); composed of cysteine peptidases (CPs) ... |
115-260 | 1.32e-64 | |||||
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: 200.93 E-value: 1.32e-64
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| Peptidase_C1 | pfam00112 | Papain family cysteine protease; |
114-260 | 4.28e-62 | |||||
Papain family cysteine protease; Pssm-ID: 425470 [Multi-domain] Cd Length: 214 Bit Score: 194.68 E-value: 4.28e-62
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| Pept_C1 | smart00645 | Papain family cysteine protease; |
114-205 | 2.84e-42 | |||||
Papain family cysteine protease; Pssm-ID: 214761 [Multi-domain] Cd Length: 175 Bit Score: 142.72 E-value: 2.84e-42
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| PTZ00021 | PTZ00021 | falcipain-2; Provisional |
36-260 | 2.11e-40 | |||||
falcipain-2; Provisional Pssm-ID: 240232 [Multi-domain] Cd Length: 489 Bit Score: 145.68 E-value: 2.11e-40
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| PTZ00203 | PTZ00203 | cathepsin L protease; Provisional |
29-259 | 7.76e-35 | |||||
cathepsin L protease; Provisional Pssm-ID: 185513 [Multi-domain] Cd Length: 348 Bit Score: 128.28 E-value: 7.76e-35
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| PTZ00200 | PTZ00200 | cysteine proteinase; Provisional |
27-267 | 4.26e-30 | |||||
cysteine proteinase; Provisional Pssm-ID: 240310 [Multi-domain] Cd Length: 448 Bit Score: 117.10 E-value: 4.26e-30
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| COG4870 | COG4870 | Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones]; |
114-260 | 2.32e-21 | |||||
Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 443898 [Multi-domain] Cd Length: 426 Bit Score: 92.50 E-value: 2.32e-21
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| Peptidase_C1 | cd02619 | C1 Peptidase family (MEROPS database nomenclature), also referred to as the papain family; ... |
119-269 | 9.74e-20 | |||||
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: 84.87 E-value: 9.74e-20
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| Inhibitor_I29 | smart00848 | Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 ... |
29-87 | 2.20e-19 | |||||
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. Pssm-ID: 214853 [Multi-domain] Cd Length: 57 Bit Score: 79.21 E-value: 2.20e-19
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| Inhibitor_I29 | pfam08246 | Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 ... |
29-88 | 6.99e-17 | |||||
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 Swiss:Q70SU8. This family is classified as I29 by MEROPS. Pssm-ID: 462410 [Multi-domain] Cd Length: 58 Bit Score: 72.68 E-value: 6.99e-17
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| Peptidase_C1A_CathepsinX | cd02698 | Cathepsin X; the only papain-like lysosomal cysteine peptidase exhibiting carboxymonopeptidase ... |
114-251 | 9.01e-15 | |||||
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: 71.68 E-value: 9.01e-15
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| Peptidase_C1A_CathepsinB | cd02620 | Cathepsin B group; composed of cathepsin B and similar proteins, including tubulointerstitial ... |
128-260 | 3.95e-12 | |||||
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: 64.21 E-value: 3.95e-12
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| PTZ00364 | PTZ00364 | dipeptidyl-peptidase I precursor; Provisional |
114-216 | 2.92e-03 | |||||
dipeptidyl-peptidase I precursor; Provisional Pssm-ID: 240381 [Multi-domain] Cd Length: 548 Bit Score: 38.72 E-value: 2.92e-03
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| Blast search parameters | ||||
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