proprotein convertase subtilisin/kexin type 9 [Homo sapiens]
Protein Classification
Peptidases_S8_PCSK9_ProteinaseK_like and PCSK9_C-CRD domain-containing protein( domain architecture ID 12067444)
protein containing domains Inhibitor_I9, Peptidases_S8_PCSK9_ProteinaseK_like, and PCSK9_C-CRD
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| PCSK9_C-CRD | cd16839 | proprotein convertase subtilisin/kexin type 9, C-terminal cysteine-rich domain (CRD); PCSK9 ... |
453-684 | 1.05e-137 | |||||
proprotein convertase subtilisin/kexin type 9, C-terminal cysteine-rich domain (CRD); PCSK9 post-translationally regulates hepatic low-density lipoprotein receptors (LDLRs) by binding to LDLRs on the cell surface, leading to their degradation. Other known PSCK9 targets include very-low-density lipoprotein receptor (VLDLR), apoE receptor2, lipoprotein receptor-related protein 1, etc. This PCSK9 C-terminal CRD may play an analogous role to the P (processing) domains of Furin and Kex2 (i.e. be required for the correct functioning/folding of the protein). Structural similarity has been noted between PCSK9 C-terminal CRD and the resistin homotrimer. This alignment model represents a three-fold repeat. : Pssm-ID: 319350 [Multi-domain] Cd Length: 225 Bit Score: 403.04 E-value: 1.05e-137
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| Peptidases_S8_PCSK9_ProteinaseK_like | cd04077 | Peptidase S8 family domain in ProteinaseK-like proteins; The peptidase S8 or Subtilase clan of ... |
157-422 | 5.09e-90 | |||||
Peptidase S8 family domain in ProteinaseK-like proteins; The peptidase S8 or Subtilase clan of proteases have a Asp/His/Ser catalytic triad that is not homologous to trypsin. This CD contains several members of this clan including: PCSK9 (Proprotein convertase subtilisin/kexin type 9), Proteinase_K, Proteinase_T, and other subtilisin-like serine proteases. PCSK9 posttranslationally regulates hepatic low-density lipoprotein receptors (LDLRs) by binding to LDLRs on the cell surface, leading to their degradation. The binding site of PCSK9 has been localized to the epidermal growth factor-like repeat A (EGF-A) domain of the LDLR. Characterized Proteinases K are secreted endopeptidases with a high degree of sequence conservation. Proteinases K are not substrate-specific and function in a wide variety of species in different pathways. It can hydrolyze keratin and other proteins with subtilisin-like specificity. The number of calcium-binding motifs found in these differ. Proteinase T is a novel proteinase from the fungus Tritirachium album Limber. The amino acid sequence of proteinase T as deduced from the nucleotide sequence is about 56% identical to that of proteinase K. : Pssm-ID: 173790 [Multi-domain] Cd Length: 255 Bit Score: 281.33 E-value: 5.09e-90
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| Inhibitor_I9 | pfam05922 | Peptidase inhibitor I9; This family includes the proteinase B inhibitor from Saccharomyces ... |
78-150 | 1.03e-09 | |||||
Peptidase inhibitor I9; This family includes the proteinase B inhibitor from Saccharomyces cerevisiae and the activation peptides from peptidases of the subtilisin family. The subtilisin propeptides are known to function as molecular chaperones, assisting in the folding of the mature peptidase, but have also been shown to act as 'temporary inhibitors'. : Pssm-ID: 428674 Cd Length: 82 Bit Score: 55.38 E-value: 1.03e-09
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| Name | Accession | Description | Interval | E-value | ||||||
| PCSK9_C-CRD | cd16839 | proprotein convertase subtilisin/kexin type 9, C-terminal cysteine-rich domain (CRD); PCSK9 ... |
453-684 | 1.05e-137 | ||||||
proprotein convertase subtilisin/kexin type 9, C-terminal cysteine-rich domain (CRD); PCSK9 post-translationally regulates hepatic low-density lipoprotein receptors (LDLRs) by binding to LDLRs on the cell surface, leading to their degradation. Other known PSCK9 targets include very-low-density lipoprotein receptor (VLDLR), apoE receptor2, lipoprotein receptor-related protein 1, etc. This PCSK9 C-terminal CRD may play an analogous role to the P (processing) domains of Furin and Kex2 (i.e. be required for the correct functioning/folding of the protein). Structural similarity has been noted between PCSK9 C-terminal CRD and the resistin homotrimer. This alignment model represents a three-fold repeat. Pssm-ID: 319350 [Multi-domain] Cd Length: 225 Bit Score: 403.04 E-value: 1.05e-137
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| Peptidases_S8_PCSK9_ProteinaseK_like | cd04077 | Peptidase S8 family domain in ProteinaseK-like proteins; The peptidase S8 or Subtilase clan of ... |
157-422 | 5.09e-90 | ||||||
Peptidase S8 family domain in ProteinaseK-like proteins; The peptidase S8 or Subtilase clan of proteases have a Asp/His/Ser catalytic triad that is not homologous to trypsin. This CD contains several members of this clan including: PCSK9 (Proprotein convertase subtilisin/kexin type 9), Proteinase_K, Proteinase_T, and other subtilisin-like serine proteases. PCSK9 posttranslationally regulates hepatic low-density lipoprotein receptors (LDLRs) by binding to LDLRs on the cell surface, leading to their degradation. The binding site of PCSK9 has been localized to the epidermal growth factor-like repeat A (EGF-A) domain of the LDLR. Characterized Proteinases K are secreted endopeptidases with a high degree of sequence conservation. Proteinases K are not substrate-specific and function in a wide variety of species in different pathways. It can hydrolyze keratin and other proteins with subtilisin-like specificity. The number of calcium-binding motifs found in these differ. Proteinase T is a novel proteinase from the fungus Tritirachium album Limber. The amino acid sequence of proteinase T as deduced from the nucleotide sequence is about 56% identical to that of proteinase K. Pssm-ID: 173790 [Multi-domain] Cd Length: 255 Bit Score: 281.33 E-value: 5.09e-90
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| PCSK9_C1 | pfam18459 | Proprotein convertase subtilisin-like/kexin type 9 C-terminal domain; This entry represents a ... |
450-532 | 7.15e-52 | ||||||
Proprotein convertase subtilisin-like/kexin type 9 C-terminal domain; This entry represents a subdomain found in the C-terminal cysteine/histidine-rich domain (CRD) of PCSK9 (also known as neural apoptosis-regulated convertase, NARC-1). PCSK9 has been shown to regulate circulating LDL-R levels by controlling LDL-R degradation. Furthermore, numerous mutations in the PCSK9 gene have been identified and associated with hypercholesterolemia (gain of function) or hypocholesterolemia (loss of function). The fully folded CRD, shows structural similarity to the resistin homotrimer, a small cytokine associated with obesity and diabetes. The C-terminal domain from PCSK9 consists of three, three-stranded beta-subdomains arranged in a pseudothreefold, and each of the subdomains in the CRD of PCSK9 consists of three structurally conserved disulfide bonds. Pssm-ID: 408252 Cd Length: 83 Bit Score: 173.77 E-value: 7.15e-52
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| AprE | COG1404 | Serine protease, subtilisin family [Posttranslational modification, protein turnover, ... |
89-424 | 1.16e-42 | ||||||
Serine protease, subtilisin family [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 441014 [Multi-domain] Cd Length: 456 Bit Score: 160.65 E-value: 1.16e-42
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| Peptidase_S8 | pfam00082 | Subtilase family; Subtilases are a family of serine proteases. They appear to have ... |
178-429 | 2.06e-19 | ||||||
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: 89.06 E-value: 2.06e-19
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| Inhibitor_I9 | pfam05922 | Peptidase inhibitor I9; This family includes the proteinase B inhibitor from Saccharomyces ... |
78-150 | 1.03e-09 | ||||||
Peptidase inhibitor I9; This family includes the proteinase B inhibitor from Saccharomyces cerevisiae and the activation peptides from peptidases of the subtilisin family. The subtilisin propeptides are known to function as molecular chaperones, assisting in the folding of the mature peptidase, but have also been shown to act as 'temporary inhibitors'. Pssm-ID: 428674 Cd Length: 82 Bit Score: 55.38 E-value: 1.03e-09
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| PTZ00262 | PTZ00262 | subtilisin-like protease; Provisional |
168-416 | 1.98e-03 | ||||||
subtilisin-like protease; Provisional Pssm-ID: 240338 [Multi-domain] Cd Length: 639 Bit Score: 41.49 E-value: 1.98e-03
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| Name | Accession | Description | Interval | E-value | ||||||
| PCSK9_C-CRD | cd16839 | proprotein convertase subtilisin/kexin type 9, C-terminal cysteine-rich domain (CRD); PCSK9 ... |
453-684 | 1.05e-137 | ||||||
proprotein convertase subtilisin/kexin type 9, C-terminal cysteine-rich domain (CRD); PCSK9 post-translationally regulates hepatic low-density lipoprotein receptors (LDLRs) by binding to LDLRs on the cell surface, leading to their degradation. Other known PSCK9 targets include very-low-density lipoprotein receptor (VLDLR), apoE receptor2, lipoprotein receptor-related protein 1, etc. This PCSK9 C-terminal CRD may play an analogous role to the P (processing) domains of Furin and Kex2 (i.e. be required for the correct functioning/folding of the protein). Structural similarity has been noted between PCSK9 C-terminal CRD and the resistin homotrimer. This alignment model represents a three-fold repeat. Pssm-ID: 319350 [Multi-domain] Cd Length: 225 Bit Score: 403.04 E-value: 1.05e-137
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| Peptidases_S8_PCSK9_ProteinaseK_like | cd04077 | Peptidase S8 family domain in ProteinaseK-like proteins; The peptidase S8 or Subtilase clan of ... |
157-422 | 5.09e-90 | ||||||
Peptidase S8 family domain in ProteinaseK-like proteins; The peptidase S8 or Subtilase clan of proteases have a Asp/His/Ser catalytic triad that is not homologous to trypsin. This CD contains several members of this clan including: PCSK9 (Proprotein convertase subtilisin/kexin type 9), Proteinase_K, Proteinase_T, and other subtilisin-like serine proteases. PCSK9 posttranslationally regulates hepatic low-density lipoprotein receptors (LDLRs) by binding to LDLRs on the cell surface, leading to their degradation. The binding site of PCSK9 has been localized to the epidermal growth factor-like repeat A (EGF-A) domain of the LDLR. Characterized Proteinases K are secreted endopeptidases with a high degree of sequence conservation. Proteinases K are not substrate-specific and function in a wide variety of species in different pathways. It can hydrolyze keratin and other proteins with subtilisin-like specificity. The number of calcium-binding motifs found in these differ. Proteinase T is a novel proteinase from the fungus Tritirachium album Limber. The amino acid sequence of proteinase T as deduced from the nucleotide sequence is about 56% identical to that of proteinase K. Pssm-ID: 173790 [Multi-domain] Cd Length: 255 Bit Score: 281.33 E-value: 5.09e-90
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| PCSK9_C1 | pfam18459 | Proprotein convertase subtilisin-like/kexin type 9 C-terminal domain; This entry represents a ... |
450-532 | 7.15e-52 | ||||||
Proprotein convertase subtilisin-like/kexin type 9 C-terminal domain; This entry represents a subdomain found in the C-terminal cysteine/histidine-rich domain (CRD) of PCSK9 (also known as neural apoptosis-regulated convertase, NARC-1). PCSK9 has been shown to regulate circulating LDL-R levels by controlling LDL-R degradation. Furthermore, numerous mutations in the PCSK9 gene have been identified and associated with hypercholesterolemia (gain of function) or hypocholesterolemia (loss of function). The fully folded CRD, shows structural similarity to the resistin homotrimer, a small cytokine associated with obesity and diabetes. The C-terminal domain from PCSK9 consists of three, three-stranded beta-subdomains arranged in a pseudothreefold, and each of the subdomains in the CRD of PCSK9 consists of three structurally conserved disulfide bonds. Pssm-ID: 408252 Cd Length: 83 Bit Score: 173.77 E-value: 7.15e-52
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| AprE | COG1404 | Serine protease, subtilisin family [Posttranslational modification, protein turnover, ... |
89-424 | 1.16e-42 | ||||||
Serine protease, subtilisin family [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 441014 [Multi-domain] Cd Length: 456 Bit Score: 160.65 E-value: 1.16e-42
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| PCSK9_C3 | pfam18463 | Proprotein convertase subtilisin-like/kexin type 9 C-terminal domain; This entry represents a ... |
603-683 | 5.27e-38 | ||||||
Proprotein convertase subtilisin-like/kexin type 9 C-terminal domain; This entry represents a subdomain found in the C-terminal cysteine/histidine-rich domain (CRD) of PCSK9 (also known as neural apoptosis-regulated convertase, NARC-1). PCSK9 has been shown to regulate circulating LDL-R levels by controlling LDL-R degradation. Furthermore, numerous mutations in the PCSK9 gene have been identified and associated with hypercholesterolemia (gain of function) or hypocholesterolemia (loss of function). The fully folded CRD, shows structural similarity to the resistin homotrimer, a small cytokine associated with obesity and diabetes. The C-terminal domain from PCSK9 consists of three, three-stranded beta-subdomains arranged in a pseudothreefold, and each of the subdomains in the CRD of PCSK9 consists of three structurally conserved disulfide bonds. Pssm-ID: 465777 Cd Length: 74 Bit Score: 135.54 E-value: 5.27e-38
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| PCSK9_C2 | pfam18464 | Proprotein convertase subtilisin-like/kexin type 9 C-terminal domain; This entry represents a ... |
536-601 | 9.12e-35 | ||||||
Proprotein convertase subtilisin-like/kexin type 9 C-terminal domain; This entry represents a subdomain found in the C-terminal cysteine/histidine-rich domain (CRD) of PCSK9 (also known as neural apoptosis-regulated convertase, NARC-1). PCSK9 has been shown to regulate circulating LDL-R levels by controlling LDL-R degradation. Furthermore, numerous mutations in the PCSK9 gene have been identified and associated with hypercholesterolemia (gain of function) or hypocholesterolemia (loss of function). The fully folded CRD, shows structural similarity to the resistin homotrimer, a small cytokine associated with obesity and diabetes. The C-terminal domain from PCSK9 consists of three, three-stranded beta-subdomains arranged in a pseudothreefold, and each of the subdomains in the CRD of PCSK9 consists of three structurally conserved disulfide bonds. Pssm-ID: 465778 Cd Length: 66 Bit Score: 126.06 E-value: 9.12e-35
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| Peptidases_S8_Subtilisin_subset | cd07477 | Peptidase S8 family domain in Subtilisin proteins; This group is composed of many different ... |
181-417 | 2.65e-31 | ||||||
Peptidase S8 family domain in Subtilisin proteins; This group is composed of many different subtilisins: Pro-TK-subtilisin, subtilisin Carlsberg, serine protease Pb92 subtilisin, and BPN subtilisins just to name a few. Pro-TK-subtilisin is a serine protease from the hyperthermophilic archaeon Thermococcus kodakaraensis and consists of a signal peptide, a propeptide, and a mature domain. TK-subtilisin is matured from pro-TK-subtilisin upon autoprocessing and degradation of the propeptide. Unlike other subtilisins though, the folding of the unprocessed form of pro-TK-subtilisin is induced by Ca2+ binding which is almost completed prior to autoprocessing. Ca2+ is required for activity unlike the bacterial subtilisins. The propeptide is not required for folding of the mature domain unlike the bacterial subtilases because of the stability produced from Ca2+ binding. Subtilisin Carlsberg is extremely similar in structure to subtilisin BPN'/Novo thought it has a 30% difference in amino acid sequence. The substrate binding regions are also similar and 2 possible Ca2+ binding sites have been identified recently. Subtilisin Carlsberg possesses the highest commercial importance as a proteolytic additive for detergents. Serine protease Pb92, the serine protease from the alkalophilic Bacillus strain PB92, also contains two calcium ions and the overall folding of the polypeptide chain closely resembles that of the subtilisins. 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: 173803 [Multi-domain] Cd Length: 229 Bit Score: 121.87 E-value: 2.65e-31
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| Peptidases_S8_S53 | cd00306 | Peptidase domain in the S8 and S53 families; Members of the peptidases S8 (subtilisin and ... |
181-418 | 8.97e-31 | ||||||
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: 120.77 E-value: 8.97e-31
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| Peptidases_S8_1 | cd07487 | Peptidase S8 family domain, uncharacterized subfamily 1; This family is a member of the ... |
178-417 | 2.68e-30 | ||||||
Peptidase S8 family domain, uncharacterized subfamily 1; 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: 173812 [Multi-domain] Cd Length: 264 Bit Score: 120.38 E-value: 2.68e-30
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| Peptidases_S8_Subtilisin_like | cd07473 | Peptidase S8 family domain in Subtilisin-like proteins; This family is a member of the ... |
225-417 | 9.27e-29 | ||||||
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: 115.75 E-value: 9.27e-29
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| Peptidases_S8_Thermitase_like | cd07484 | Peptidase S8 family domain in Thermitase-like proteins; Thermitase is a non-specific, ... |
157-424 | 1.18e-25 | ||||||
Peptidase S8 family domain in Thermitase-like proteins; Thermitase is a non-specific, trypsin-related serine protease with a very high specific activity. It contains a subtilisin like domain. The tertiary structure of thermitase is similar to that of subtilisin BPN'. It contains a Asp/His/Ser catalytic triad. Members of the peptidases S8 (subtilisin and kexin) and S53 (sedolisin) clan 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 the 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: 173810 [Multi-domain] Cd Length: 260 Bit Score: 106.58 E-value: 1.18e-25
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| Peptidases_S8_subtilisin_Vpr-like | cd07474 | Peptidase S8 family domain in Vpr-like proteins; The maturation of the peptide antibiotic ... |
202-428 | 6.53e-23 | ||||||
Peptidase S8 family domain in Vpr-like proteins; The maturation of the peptide antibiotic (lantibiotic) subtilin in Bacillus subtilis ATCC 6633 includes posttranslational modifications of the propeptide and proteolytic cleavage of the leader peptide. Vpr was identified as one of the proteases, along with WprA, that are capable of processing subtilin. Asp, Ser, His triadPeptidases S8 or Subtilases are a 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: 173800 [Multi-domain] Cd Length: 295 Bit Score: 99.71 E-value: 6.53e-23
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| Peptidase_S8 | pfam00082 | Subtilase family; Subtilases are a family of serine proteases. They appear to have ... |
178-429 | 2.06e-19 | ||||||
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: 89.06 E-value: 2.06e-19
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| Peptidases_S8_13 | cd07496 | Peptidase S8 family domain, uncharacterized subfamily 13; This family is a member of the ... |
181-416 | 8.59e-18 | ||||||
Peptidase S8 family domain, uncharacterized subfamily 13; 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: 173820 [Multi-domain] Cd Length: 285 Bit Score: 84.27 E-value: 8.59e-18
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| Peptidases_S8_4 | cd05561 | Peptidase S8 family domain, uncharacterized subfamily 4; This family is a member of the ... |
181-423 | 6.07e-17 | ||||||
Peptidase S8 family domain, uncharacterized subfamily 4; 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: 173797 [Multi-domain] Cd Length: 239 Bit Score: 80.80 E-value: 6.07e-17
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| Peptidases_S8_15 | cd07498 | Peptidase S8 family domain, uncharacterized subfamily 15; This family is a member of the ... |
181-418 | 1.94e-16 | ||||||
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: 79.31 E-value: 1.94e-16
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| Peptidases_S8_5 | cd07489 | Peptidase S8 family domain, uncharacterized subfamily 5; gap in seq This family is a member of ... |
224-453 | 1.84e-14 | ||||||
Peptidase S8 family domain, uncharacterized subfamily 5; gap in seq 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: 173814 [Multi-domain] Cd Length: 312 Bit Score: 74.95 E-value: 1.84e-14
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| Peptidases_S8_6 | cd07490 | Peptidase S8 family domain, uncharacterized subfamily 6; This family is a member of the ... |
181-416 | 6.74e-14 | ||||||
Peptidase S8 family domain, uncharacterized subfamily 6; 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: 173815 [Multi-domain] Cd Length: 254 Bit Score: 72.20 E-value: 6.74e-14
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| Peptidases_S8_12 | cd07480 | Peptidase S8 family domain, uncharacterized subfamily 12; This family is a member of the ... |
174-390 | 1.30e-13 | ||||||
Peptidase S8 family domain, uncharacterized subfamily 12; 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: 173806 [Multi-domain] Cd Length: 297 Bit Score: 72.02 E-value: 1.30e-13
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| Peptidases_S8_Autotransporter_serine_protease_like | cd04848 | Peptidase S8 family domain in Autotransporter serine proteases; Autotransporter serine ... |
178-387 | 8.30e-11 | ||||||
Peptidase S8 family domain in Autotransporter serine proteases; Autotransporter serine proteases belong to Peptidase S8 or Subtilase family. Subtilases, or subtilisin-like serine proteases, have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure (an example of convergent evolution). Autotransporters are a superfamily of outer membrane/secreted proteins of gram-negative bacteria. The presence of these subtilisin-like domains in these autotransporters are may enable them to be auto-catalytic and may also serve to allow them to act as a maturation protease cleaving other outer membrane proteins at the cell surface. Pssm-ID: 173794 [Multi-domain] Cd Length: 267 Bit Score: 63.11 E-value: 8.30e-11
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| Inhibitor_I9 | pfam05922 | Peptidase inhibitor I9; This family includes the proteinase B inhibitor from Saccharomyces ... |
78-150 | 1.03e-09 | ||||||
Peptidase inhibitor I9; This family includes the proteinase B inhibitor from Saccharomyces cerevisiae and the activation peptides from peptidases of the subtilisin family. The subtilisin propeptides are known to function as molecular chaperones, assisting in the folding of the mature peptidase, but have also been shown to act as 'temporary inhibitors'. Pssm-ID: 428674 Cd Length: 82 Bit Score: 55.38 E-value: 1.03e-09
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| Peptidases_S8_Subtilisin_Novo-like | cd07483 | Peptidase S8 family domain in Subtilisin_Novo-like proteins; Subtilisins are a group of ... |
226-414 | 1.09e-09 | ||||||
Peptidase S8 family domain in Subtilisin_Novo-like proteins; Subtilisins are a group of alkaline proteinases originating from different strains of Bacillus subtilis. Novo is one of the strains that produced enzymes belonging to this group. The enzymes obtained from the Novo and BPN' strains are identical. The Carlsburg and Novo subtilisins are thought to have arisen from a common ancestral protein. They have similar peptidase and esterase activities, pH profiles, catalyze transesterification reactions, and are both inhibited by diispropyl fluorophosphate, though they differ in 85 positions in the amino acid sequence. 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 with an additional acidic residue Asp in the oxyanion hole, similar to that of 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. Pssm-ID: 173809 [Multi-domain] Cd Length: 291 Bit Score: 60.07 E-value: 1.09e-09
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| Peptidases_S8_BacillopeptidaseF-like | cd07481 | Peptidase S8 family domain in BacillopeptidaseF-like proteins; Bacillus subtilis produces and ... |
218-417 | 1.58e-09 | ||||||
Peptidase S8 family domain in BacillopeptidaseF-like proteins; Bacillus subtilis produces and secretes proteases and other types of exoenzymes at the end of the exponential phase of growth. The ones that make up this group is known as bacillopeptidase F, encoded by bpr, a serine protease with high esterolytic activity which is inhibited by PMSF. Like other members of the peptidases S8 family these have a 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 these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Pssm-ID: 173807 [Multi-domain] Cd Length: 264 Bit Score: 59.31 E-value: 1.58e-09
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| Peptidases_S8_Fervidolysin_like | cd07485 | Peptidase S8 family domain in Fervidolysin; Fervidolysin found in Fervidobacterium pennivorans ... |
171-390 | 2.73e-09 | ||||||
Peptidase S8 family domain in Fervidolysin; Fervidolysin found in Fervidobacterium pennivorans is an extracellular subtilisin-like keratinase. It is contains a signal peptide, a propeptide, and a catalytic region. The tertiary structure of fervidolysin is similar to that of subtilisin. It contains a Asp/His/Ser catalytic triad and is a member of the peptidase S8 (subtilisin and kexin) family. The catalytic triad is similar to that found in trypsin-like proteases, but it does 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: 173811 [Multi-domain] Cd Length: 273 Bit Score: 58.65 E-value: 2.73e-09
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| Peptidases_S53_like | cd05562 | Peptidase domain in the S53 family; Members of the peptidase S53 (sedolisin) family include ... |
300-416 | 6.23e-08 | ||||||
Peptidase domain in the S53 family; Members of the peptidase S53 (sedolisin) family include endopeptidases and exopeptidases. 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: 173798 [Multi-domain] Cd Length: 275 Bit Score: 54.61 E-value: 6.23e-08
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| Peptidases_S8_thiazoline_oxidase_subtilisin-like_p | cd07476 | Peptidase S8 family domain in Thiazoline oxidase/subtilisin-like proteases; Thiazoline oxidase ... |
209-403 | 1.15e-07 | ||||||
Peptidase S8 family domain in Thiazoline oxidase/subtilisin-like proteases; Thiazoline oxidase/subtilisin-like protease is produced by the symbiotic bacteria Prochloron spp. that inhabit didemnid family ascidians. The cyclic peptides of the patellamide class found in didemnid extracts are now known to be synthesized by the Prochloron spp. The prepatellamide is heterocyclized to form thiazole and oxazoline rings and the peptide is cleaved to form the two cyclic patellamides A and C. Subtilases, or subtilisin-like serine proteases, have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure (an example of convergent evolution). Pssm-ID: 173802 [Multi-domain] Cd Length: 267 Bit Score: 53.49 E-value: 1.15e-07
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| Peptidases_S8_8 | cd07492 | Peptidase S8 family domain, uncharacterized subfamily 8; This family is a member of the ... |
181-422 | 1.20e-07 | ||||||
Peptidase S8 family domain, uncharacterized subfamily 8; 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: 173817 [Multi-domain] Cd Length: 222 Bit Score: 53.11 E-value: 1.20e-07
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| Peptidases_S8_C5a_Peptidase | cd07475 | Peptidase S8 family domain in Streptococcal C5a peptidases; Streptococcal C5a peptidase (SCP), ... |
225-390 | 2.53e-06 | ||||||
Peptidase S8 family domain in Streptococcal C5a peptidases; Streptococcal C5a peptidase (SCP), is a highly specific protease and adhesin/invasin. The subtilisin-like protease domain is located at the N-terminus and contains a protease-associated domain inserted into a loop. There are three fibronectin type III (Fn) domains at the C-terminus. SCP binds to integrins with the help of Arg-Gly-Asp motifs which are thought to stabilize conformational changes required for substrate binding. Peptidases S8 or Subtilases are a 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: 173801 [Multi-domain] Cd Length: 346 Bit Score: 49.96 E-value: 2.53e-06
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| Peptidases_S8_Kp43_protease | cd04842 | Peptidase S8 family domain in Kp43 proteases; Kp43 proteases are members of the peptidase S8 ... |
225-390 | 2.60e-06 | ||||||
Peptidase S8 family domain in Kp43 proteases; Kp43 proteases are members of the peptidase S8 or Subtilase clan of proteases. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure (an example of convergent evolution). Kp43 is topologically similar to kexin and furin both of which are proprotein convertases, but differ in amino acids sequence and the position of its C-terminal barrel. Kp43 has 3 Ca2+ binding sites that differ from the corresponding sites in the other known subtilisin-like proteases. KP-43 protease is known to be an oxidation-resistant protease when compared with the other subtilisin-like proteases Pssm-ID: 173791 [Multi-domain] Cd Length: 293 Bit Score: 49.64 E-value: 2.60e-06
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| Peptidases_S8_Lantibiotic_specific_protease | cd07482 | Peptidase S8 family domain in Lantiobiotic (lanthionine-containing antibiotics) specific ... |
181-368 | 6.23e-06 | ||||||
Peptidase S8 family domain in Lantiobiotic (lanthionine-containing antibiotics) specific proteases; Lantiobiotic (lanthionine-containing antibiotics) specific proteases are very similar in structure to serine proteases. Lantibiotics are ribosomally synthesised antimicrobial agents derived from ribosomally synthesised peptides with antimicrobial activities against Gram-positive bacteria. The proteases that cleave the N-terminal leader peptides from lantiobiotics include: epiP, nsuP, mutP, and nisP. EpiP, from Staphylococcus, is thought to cleave matured epidermin. NsuP, a dehydratase from Streptococcus and NisP, a membrane-anchored subtilisin-like serine protease from Lactococcus cleave nisin. MutP is highly similar to epiP and nisP and is thought to process the prepeptide mutacin III of S. mutans. Members of the peptidases S8 (subtilisin and kexin) and S53 (sedolisin) clan 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 the 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: 173808 [Multi-domain] Cd Length: 294 Bit Score: 48.52 E-value: 6.23e-06
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| Peptidases_S8_SKI-1_like | cd07479 | Peptidase S8 family domain in SKI-1-like proteins; SKI-1 (type I membrane-bound ... |
178-422 | 5.40e-05 | ||||||
Peptidase S8 family domain in SKI-1-like proteins; SKI-1 (type I membrane-bound subtilisin-kexin-isoenzyme) proteins are secretory Ca2+-dependent serine proteinases cleave at nonbasic residues: Thr, Leu, and Lys. SKI-1s play a critical role in the regulation of the synthesis and metabolism of cholesterol and fatty acid metabolism. 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: 173805 [Multi-domain] Cd Length: 255 Bit Score: 45.52 E-value: 5.40e-05
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| Peptidases_S8_11 | cd04843 | Peptidase S8 family domain, uncharacterized subfamily 11; This family is a member of the ... |
226-375 | 9.28e-05 | ||||||
Peptidase S8 family domain, uncharacterized subfamily 11; 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: 173792 Cd Length: 277 Bit Score: 45.00 E-value: 9.28e-05
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| Peptidases_S8_9 | cd07493 | Peptidase S8 family domain, uncharacterized subfamily 9; This family is a member of the ... |
295-414 | 2.84e-04 | ||||||
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: 43.06 E-value: 2.84e-04
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| Peptidases_S8_3 | cd04852 | Peptidase S8 family domain, uncharacterized subfamily 3; This family is a member of the ... |
306-413 | 5.75e-04 | ||||||
Peptidase S8 family domain, uncharacterized subfamily 3; 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: 173795 [Multi-domain] Cd Length: 307 Bit Score: 42.59 E-value: 5.75e-04
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| PTZ00262 | PTZ00262 | subtilisin-like protease; Provisional |
168-416 | 1.98e-03 | ||||||
subtilisin-like protease; Provisional Pssm-ID: 240338 [Multi-domain] Cd Length: 639 Bit Score: 41.49 E-value: 1.98e-03
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