S53 family serine peptidase similar to Bacillus kumamolisin, an extracellular proteinase that belongs to the sedolisin family of endopeptidases characterized by a subtilisin-like fold and a Ser-Glu-Asp catalytic triad
Peptidase domain in the S53 family; Members of the peptidases S53 (sedolisin) family include ...
208-560
1.65e-130
Peptidase domain in the S53 family; Members of the peptidases S53 (sedolisin) family include endopeptidases and exopeptidases sedolisin, kumamolysin, and (PSCP) Pepstatin-insensitive Carboxyl Proteinase. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of Asn in subtilisin. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values. Characterized sedolisins include Kumamolisin, an extracellular calcium-dependent thermostable endopeptidase from Bacillus. The enzyme is synthesized with a 188 amino acid N-terminal preprotein region which is cleaved after the extraction into the extracellular space with low pH. One kumamolysin paralog, kumamolisin-As, is believed to be a collagenase. TPP1 is a serine protease that functions as a tripeptidyl exopeptidase as well as an endopeptidase. Less is known about PSCP from Pseudomonas which is thought to be an aspartic proteinase.
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Pssm-ID: 173788 [Multi-domain] Cd Length: 361 Bit Score: 385.52 E-value: 1.65e-130
Activation domain of S53 peptidases; Members of this family are found in various subtilase ...
36-173
1.42e-47
Activation domain of S53 peptidases; Members of this family are found in various subtilase propeptides, such as pro-kumamolysin and tripeptidyl peptidase I, and adopt a ferredoxin-like fold, with an alpha+beta sandwich. Cleavage of the domain results in activation of the peptidase.
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Pssm-ID: 206778 Cd Length: 139 Bit Score: 162.42 E-value: 1.42e-47
Peptidase domain in the S53 family; Members of the peptidases S53 (sedolisin) family include ...
208-560
1.65e-130
Peptidase domain in the S53 family; Members of the peptidases S53 (sedolisin) family include endopeptidases and exopeptidases sedolisin, kumamolysin, and (PSCP) Pepstatin-insensitive Carboxyl Proteinase. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of Asn in subtilisin. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values. Characterized sedolisins include Kumamolisin, an extracellular calcium-dependent thermostable endopeptidase from Bacillus. The enzyme is synthesized with a 188 amino acid N-terminal preprotein region which is cleaved after the extraction into the extracellular space with low pH. One kumamolysin paralog, kumamolisin-As, is believed to be a collagenase. TPP1 is a serine protease that functions as a tripeptidyl exopeptidase as well as an endopeptidase. Less is known about PSCP from Pseudomonas which is thought to be an aspartic proteinase.
Pssm-ID: 173788 [Multi-domain] Cd Length: 361 Bit Score: 385.52 E-value: 1.65e-130
Activation domain of S53 peptidases; Members of this family are found in various subtilase ...
36-173
1.42e-47
Activation domain of S53 peptidases; Members of this family are found in various subtilase propeptides, such as pro-kumamolysin and tripeptidyl peptidase I, and adopt a ferredoxin-like fold, with an alpha+beta sandwich. Cleavage of the domain results in activation of the peptidase.
Pssm-ID: 206778 Cd Length: 139 Bit Score: 162.42 E-value: 1.42e-47
Pro-kumamolisin, activation domain; Members of this family are found in various subtilase ...
36-176
7.63e-47
Pro-kumamolisin, activation domain; Members of this family are found in various subtilase propeptides, and adopt a ferredoxin-like fold, with an alpha+beta sandwich. Cleavage of the domain results in activation of the peptide.
Pssm-ID: 401284 Cd Length: 142 Bit Score: 160.46 E-value: 7.63e-47
Pro-kumamolisin, activation domain; This domain is found at the N-terminus of peptidases ...
38-173
7.28e-35
Pro-kumamolisin, activation domain; This domain is found at the N-terminus of peptidases belonging to MEROPS peptidase family S53 (sedolisin, clan SB). The domain adopts a ferredoxin-like fold, with an alpha+beta sandwich. Cleavage of the domain results in activation of the peptidase.
Pssm-ID: 214928 Cd Length: 136 Bit Score: 128.14 E-value: 7.28e-35
Subtilase family; Subtilases are a family of serine proteases. They appear to have ...
290-497
2.77e-05
Subtilase family; Subtilases are a family of serine proteases. They appear to have independently and convergently evolved an Asp/Ser/His catalytic triad, like that found in the trypsin serine proteases (see pfam00089). Structure is an alpha/beta fold containing a 7-stranded parallel beta sheet, order 2314567.
Pssm-ID: 395035 [Multi-domain] Cd Length: 287 Bit Score: 46.30 E-value: 2.77e-05
Peptidase domain in the S53 family; Members of the peptidases S53 (sedolisin) family include ...
208-560
1.65e-130
Peptidase domain in the S53 family; Members of the peptidases S53 (sedolisin) family include endopeptidases and exopeptidases sedolisin, kumamolysin, and (PSCP) Pepstatin-insensitive Carboxyl Proteinase. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of Asn in subtilisin. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values. Characterized sedolisins include Kumamolisin, an extracellular calcium-dependent thermostable endopeptidase from Bacillus. The enzyme is synthesized with a 188 amino acid N-terminal preprotein region which is cleaved after the extraction into the extracellular space with low pH. One kumamolysin paralog, kumamolisin-As, is believed to be a collagenase. TPP1 is a serine protease that functions as a tripeptidyl exopeptidase as well as an endopeptidase. Less is known about PSCP from Pseudomonas which is thought to be an aspartic proteinase.
Pssm-ID: 173788 [Multi-domain] Cd Length: 361 Bit Score: 385.52 E-value: 1.65e-130
Activation domain of S53 peptidases; Members of this family are found in various subtilase ...
36-173
1.42e-47
Activation domain of S53 peptidases; Members of this family are found in various subtilase propeptides, such as pro-kumamolysin and tripeptidyl peptidase I, and adopt a ferredoxin-like fold, with an alpha+beta sandwich. Cleavage of the domain results in activation of the peptidase.
Pssm-ID: 206778 Cd Length: 139 Bit Score: 162.42 E-value: 1.42e-47
Pro-kumamolisin, activation domain; Members of this family are found in various subtilase ...
36-176
7.63e-47
Pro-kumamolisin, activation domain; Members of this family are found in various subtilase propeptides, and adopt a ferredoxin-like fold, with an alpha+beta sandwich. Cleavage of the domain results in activation of the peptide.
Pssm-ID: 401284 Cd Length: 142 Bit Score: 160.46 E-value: 7.63e-47
Pro-kumamolisin, activation domain; This domain is found at the N-terminus of peptidases ...
38-173
7.28e-35
Pro-kumamolisin, activation domain; This domain is found at the N-terminus of peptidases belonging to MEROPS peptidase family S53 (sedolisin, clan SB). The domain adopts a ferredoxin-like fold, with an alpha+beta sandwich. Cleavage of the domain results in activation of the peptidase.
Pssm-ID: 214928 Cd Length: 136 Bit Score: 128.14 E-value: 7.28e-35
Peptidase domain in the S8 and S53 families; Members of the peptidases S8 (subtilisin and ...
284-497
2.74e-06
Peptidase domain in the S8 and S53 families; Members of the peptidases S8 (subtilisin and kexin) and S53 (sedolisin) family include endopeptidases and exopeptidases. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. Serine acts as a nucleophile, aspartate as an electrophile, and histidine as a base. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of subtilisin. The serine residue here is the nucleophilic equivalent of the serine residue in the S8 family, while glutamic acid has the same role here as the histidine base. However, the aspartic acid residue that acts as an electrophile is quite different. In S53, it follows glutamic acid, while in S8 it precedes histidine. The stability of these enzymes may be enhanced by calcium; some members have been shown to bind up to 4 ions via binding sites with different affinity. There is a great diversity in the characteristics of their members: some contain disulfide bonds, some are intracellular while others are extracellular, some function at extreme temperatures, and others at high or low pH values.
Pssm-ID: 173787 [Multi-domain] Cd Length: 241 Bit Score: 48.74 E-value: 2.74e-06
Subtilase family; Subtilases are a family of serine proteases. They appear to have ...
290-497
2.77e-05
Subtilase family; Subtilases are a family of serine proteases. They appear to have independently and convergently evolved an Asp/Ser/His catalytic triad, like that found in the trypsin serine proteases (see pfam00089). Structure is an alpha/beta fold containing a 7-stranded parallel beta sheet, order 2314567.
Pssm-ID: 395035 [Multi-domain] Cd Length: 287 Bit Score: 46.30 E-value: 2.77e-05
Peptidase S8 family domain in CspA-like proteins; GSP (germination-specific protease) converts ...
446-497
3.20e-05
Peptidase S8 family domain in CspA-like proteins; GSP (germination-specific protease) converts the spore peptidoglycan hydrolase (SleC) precursor to an active enzyme during germination of Clostridium perfringens S40 spores. Analysis of an enzyme fraction of GSP showed that it was composed of a gene cluster containing the processed forms of products of cspA, cspB, and cspC which are positioned in a tandem array just upstream of the 5' end of sleC. The amino acid sequences deduced from the nucleotide sequences of the csp genes showed significant similarity and showed a high degree of homology with those of the catalytic domain and the oxyanion binding region of subtilisin-like serine proteases. Members of the peptidases S8 and S35 clan include endopeptidases, exopeptidases and also a tripeptidyl-peptidase. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The S53 family contains a catalytic triad Glu/Asp/Ser. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.
Pssm-ID: 173804 [Multi-domain] Cd Length: 455 Bit Score: 46.46 E-value: 3.20e-05
Peptidase S8 family domain, uncharacterized subfamily 9; This family is a member of the ...
376-497
5.63e-05
Peptidase S8 family domain, uncharacterized subfamily 9; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.
Pssm-ID: 173818 [Multi-domain] Cd Length: 261 Bit Score: 44.99 E-value: 5.63e-05
Peptidase S8 family domain, uncharacterized subfamily 15; This family is a member of the ...
292-497
7.14e-04
Peptidase S8 family domain, uncharacterized subfamily 15; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.
Pssm-ID: 173822 [Multi-domain] Cd Length: 242 Bit Score: 41.56 E-value: 7.14e-04
Peptidase S8 family domain in Subtilisin-like proteins; This family is a member of the ...
289-497
9.42e-03
Peptidase S8 family domain in Subtilisin-like proteins; This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.
Pssm-ID: 173799 [Multi-domain] Cd Length: 259 Bit Score: 37.94 E-value: 9.42e-03
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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