subtilisin-like protease SBT1.6 [Arabidopsis lyrata subsp. lyrata]
Protein Classification
S8 family peptidase( domain architecture ID 15916511)
S8 family peptidase is a subtilisin-like serine protease containing an Asp/His/Ser catalytic triad that is not homologous to trypsin; similar to Arabidopsis thaliana subtilisin-like proteases
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||||
| Peptidases_S8_3 | cd04852 | Peptidase S8 family domain, uncharacterized subfamily 3; This family is a member of the ... |
97-570 | 9.20e-142 | |||||||
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: 418.93 E-value: 9.20e-142
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| PA_subtilisin_like | cd02120 | PA_subtilisin_like: Protease-associated domain containing subtilisin-like proteases. This ... |
343-467 | 5.42e-38 | |||||||
PA_subtilisin_like: Protease-associated domain containing subtilisin-like proteases. This group contains various PA domain-containing subtilisin-like proteases including melon cucumisin, Arabidopsis thaliana Ara12, a nodule specific serine protease from Alnus glutinosa ag12, members of the tomato P69 family, and tomato LeSBT2. These proteins belong to the peptidase S8 family. Cucumisin from the juice of melon fruits is a thermostable serine peptidase, with a broad substrate specificity for oligopeptides and proteins. A. thaliana Ara12 is a thermostable, extracellular serine protease, found chiefly in silique tissue and stem tissue. Ara12 is stimulated by Ca2+ ions. A. glutinosa ag12 is expressed at high levels in the nodules, and at low levels in the shoot tips; it is implicated in both symbiotic and non-symbiotic processes in plant development. The tomato P69 protease family is comprised of various protein isoforms of approximately 69KDa. These isoforms accumulate extracellularly. Some of the P69 genes are tightly regulated in a tissue specific fashion, and by environmental and developmental signals. For example: infection with avirulent bacteria activates transcription of the genes for the P69 B and C isoforms, the P69 E transcript was detected only in roots, and the P69F transcript only in hydathodes. The Tomato LeSBT2 subtilase transcript was not detected in flowers and roots, but was present in cotyledons and leaves. The significance of the PA domain to these proteins has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate. : Pssm-ID: 239035 [Multi-domain] Cd Length: 126 Bit Score: 137.55 E-value: 5.42e-38
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| fn3_6 | pfam17766 | Fibronectin type-III domain; This FN3 like domain is found at the C-terminus of cucumisin ... |
653-758 | 1.09e-34 | |||||||
Fibronectin type-III domain; This FN3 like domain is found at the C-terminus of cucumisin proteins. : Pssm-ID: 465493 Cd Length: 98 Bit Score: 127.32 E-value: 1.09e-34
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| Inhibitor_I9 | pfam05922 | Peptidase inhibitor I9; This family includes the proteinase B inhibitor from Saccharomyces ... |
33-99 | 4.48e-15 | |||||||
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: 70.79 E-value: 4.48e-15
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| Name | Accession | Description | Interval | E-value | ||||||||
| Peptidases_S8_3 | cd04852 | Peptidase S8 family domain, uncharacterized subfamily 3; This family is a member of the ... |
97-570 | 9.20e-142 | ||||||||
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: 418.93 E-value: 9.20e-142
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| PA_subtilisin_like | cd02120 | PA_subtilisin_like: Protease-associated domain containing subtilisin-like proteases. This ... |
343-467 | 5.42e-38 | ||||||||
PA_subtilisin_like: Protease-associated domain containing subtilisin-like proteases. This group contains various PA domain-containing subtilisin-like proteases including melon cucumisin, Arabidopsis thaliana Ara12, a nodule specific serine protease from Alnus glutinosa ag12, members of the tomato P69 family, and tomato LeSBT2. These proteins belong to the peptidase S8 family. Cucumisin from the juice of melon fruits is a thermostable serine peptidase, with a broad substrate specificity for oligopeptides and proteins. A. thaliana Ara12 is a thermostable, extracellular serine protease, found chiefly in silique tissue and stem tissue. Ara12 is stimulated by Ca2+ ions. A. glutinosa ag12 is expressed at high levels in the nodules, and at low levels in the shoot tips; it is implicated in both symbiotic and non-symbiotic processes in plant development. The tomato P69 protease family is comprised of various protein isoforms of approximately 69KDa. These isoforms accumulate extracellularly. Some of the P69 genes are tightly regulated in a tissue specific fashion, and by environmental and developmental signals. For example: infection with avirulent bacteria activates transcription of the genes for the P69 B and C isoforms, the P69 E transcript was detected only in roots, and the P69F transcript only in hydathodes. The Tomato LeSBT2 subtilase transcript was not detected in flowers and roots, but was present in cotyledons and leaves. The significance of the PA domain to these proteins has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate. Pssm-ID: 239035 [Multi-domain] Cd Length: 126 Bit Score: 137.55 E-value: 5.42e-38
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| fn3_6 | pfam17766 | Fibronectin type-III domain; This FN3 like domain is found at the C-terminus of cucumisin ... |
653-758 | 1.09e-34 | ||||||||
Fibronectin type-III domain; This FN3 like domain is found at the C-terminus of cucumisin proteins. Pssm-ID: 465493 Cd Length: 98 Bit Score: 127.32 E-value: 1.09e-34
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| AprE | COG1404 | Serine protease, subtilisin family [Posttranslational modification, protein turnover, ... |
183-700 | 1.08e-32 | ||||||||
Serine protease, subtilisin family [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 441014 [Multi-domain] Cd Length: 456 Bit Score: 132.14 E-value: 1.08e-32
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| Peptidase_S8 | pfam00082 | Subtilase family; Subtilases are a family of serine proteases. They appear to have ... |
122-570 | 2.46e-26 | ||||||||
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: 109.47 E-value: 2.46e-26
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| Inhibitor_I9 | pfam05922 | Peptidase inhibitor I9; This family includes the proteinase B inhibitor from Saccharomyces ... |
33-99 | 4.48e-15 | ||||||||
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: 70.79 E-value: 4.48e-15
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| PA | pfam02225 | PA domain; The PA (Protease associated) domain is found as an insert domain in diverse ... |
367-453 | 8.35e-12 | ||||||||
PA domain; The PA (Protease associated) domain is found as an insert domain in diverse proteases. The PA domain is also found in a plant vacuolar sorting receptor Swiss:O22925 and members of the RZF family Swiss:O43567. It has been suggested that this domain forms a lid-like structure that covers the active site in active proteases, and is involved in protein recognition in vacuolar sorting receptors. Pssm-ID: 460499 [Multi-domain] Cd Length: 91 Bit Score: 61.76 E-value: 8.35e-12
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| T7SS_mycosin | TIGR03921 | type VII secretion-associated serine protease mycosin; Members of this family are ... |
483-587 | 1.10e-10 | ||||||||
type VII secretion-associated serine protease mycosin; Members of this family are subtilisin-related serine proteases, found strictly in the Actinobacteria and associated with type VII secretion operons. The designation mycosin is used for members from Mycobacterium. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair] Pssm-ID: 274856 [Multi-domain] Cd Length: 350 Bit Score: 63.88 E-value: 1.10e-10
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| germ_prot_CspBA | NF040809 | bifunctional germination protease/germinant receptor pseudoprotease CspBA; CspBA, as found in ... |
481-551 | 6.44e-07 | ||||||||
bifunctional germination protease/germinant receptor pseudoprotease CspBA; CspBA, as found in Clostridium difficile, is translated as a fusion protein, but cleaved into separate homologous CspB and CspA proteins during spore formation. CspB is a protease, required to active SleC by cleaving it in order to trigger germination. CspA, like the bile salt germinant receptor CspC (encoded by the adjacent gene), has lost the catalytic residues necessary for subtilisin-like serine protease activity. Pssm-ID: 468750 [Multi-domain] Cd Length: 1099 Bit Score: 53.24 E-value: 6.44e-07
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| germ_prot_CspBA | NF040809 | bifunctional germination protease/germinant receptor pseudoprotease CspBA; CspBA, as found in ... |
486-550 | 8.39e-07 | ||||||||
bifunctional germination protease/germinant receptor pseudoprotease CspBA; CspBA, as found in Clostridium difficile, is translated as a fusion protein, but cleaved into separate homologous CspB and CspA proteins during spore formation. CspB is a protease, required to active SleC by cleaving it in order to trigger germination. CspA, like the bile salt germinant receptor CspC (encoded by the adjacent gene), has lost the catalytic residues necessary for subtilisin-like serine protease activity. Pssm-ID: 468750 [Multi-domain] Cd Length: 1099 Bit Score: 52.86 E-value: 8.39e-07
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| myxo_dep_M36 | NF038112 | myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ... |
392-455 | 1.26e-03 | ||||||||
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal MYXO-CTERM domain (see TIGR03901), suggesting processing and surface-anchoring by the still-unknown putative transpeptidase, myxosortase. Members of this family include MXAN_3564 (mepA), part of the effector cargo of outer membrane vesicles that the species produces in large numbers during predation on other microbes. Pssm-ID: 468355 [Multi-domain] Cd Length: 1597 Bit Score: 42.34 E-value: 1.26e-03
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| PTZ00262 | PTZ00262 | subtilisin-like protease; Provisional |
502-559 | 1.78e-03 | ||||||||
subtilisin-like protease; Provisional Pssm-ID: 240338 [Multi-domain] Cd Length: 639 Bit Score: 41.88 E-value: 1.78e-03
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| Name | Accession | Description | Interval | E-value | ||||||||
| Peptidases_S8_3 | cd04852 | Peptidase S8 family domain, uncharacterized subfamily 3; This family is a member of the ... |
97-570 | 9.20e-142 | ||||||||
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: 418.93 E-value: 9.20e-142
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| Peptidases_S8_subtilisin_Vpr-like | cd07474 | Peptidase S8 family domain in Vpr-like proteins; The maturation of the peptide antibiotic ... |
122-605 | 3.08e-39 | ||||||||
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: 147.09 E-value: 3.08e-39
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| PA_subtilisin_like | cd02120 | PA_subtilisin_like: Protease-associated domain containing subtilisin-like proteases. This ... |
343-467 | 5.42e-38 | ||||||||
PA_subtilisin_like: Protease-associated domain containing subtilisin-like proteases. This group contains various PA domain-containing subtilisin-like proteases including melon cucumisin, Arabidopsis thaliana Ara12, a nodule specific serine protease from Alnus glutinosa ag12, members of the tomato P69 family, and tomato LeSBT2. These proteins belong to the peptidase S8 family. Cucumisin from the juice of melon fruits is a thermostable serine peptidase, with a broad substrate specificity for oligopeptides and proteins. A. thaliana Ara12 is a thermostable, extracellular serine protease, found chiefly in silique tissue and stem tissue. Ara12 is stimulated by Ca2+ ions. A. glutinosa ag12 is expressed at high levels in the nodules, and at low levels in the shoot tips; it is implicated in both symbiotic and non-symbiotic processes in plant development. The tomato P69 protease family is comprised of various protein isoforms of approximately 69KDa. These isoforms accumulate extracellularly. Some of the P69 genes are tightly regulated in a tissue specific fashion, and by environmental and developmental signals. For example: infection with avirulent bacteria activates transcription of the genes for the P69 B and C isoforms, the P69 E transcript was detected only in roots, and the P69F transcript only in hydathodes. The Tomato LeSBT2 subtilase transcript was not detected in flowers and roots, but was present in cotyledons and leaves. The significance of the PA domain to these proteins has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate. Pssm-ID: 239035 [Multi-domain] Cd Length: 126 Bit Score: 137.55 E-value: 5.42e-38
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| fn3_6 | pfam17766 | Fibronectin type-III domain; This FN3 like domain is found at the C-terminus of cucumisin ... |
653-758 | 1.09e-34 | ||||||||
Fibronectin type-III domain; This FN3 like domain is found at the C-terminus of cucumisin proteins. Pssm-ID: 465493 Cd Length: 98 Bit Score: 127.32 E-value: 1.09e-34
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| AprE | COG1404 | Serine protease, subtilisin family [Posttranslational modification, protein turnover, ... |
183-700 | 1.08e-32 | ||||||||
Serine protease, subtilisin family [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 441014 [Multi-domain] Cd Length: 456 Bit Score: 132.14 E-value: 1.08e-32
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| Peptidases_S8_1 | cd07487 | Peptidase S8 family domain, uncharacterized subfamily 1; This family is a member of the ... |
122-571 | 5.18e-31 | ||||||||
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: 122.31 E-value: 5.18e-31
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| Peptidases_S8_6 | cd07490 | Peptidase S8 family domain, uncharacterized subfamily 6; This family is a member of the ... |
199-571 | 3.74e-27 | ||||||||
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: 111.10 E-value: 3.74e-27
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| Peptidase_S8 | pfam00082 | Subtilase family; Subtilases are a family of serine proteases. They appear to have ... |
122-570 | 2.46e-26 | ||||||||
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: 109.47 E-value: 2.46e-26
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| Peptidases_S8_Subtilisin_subset | cd07477 | Peptidase S8 family domain in Subtilisin proteins; This group is composed of many different ... |
184-570 | 9.36e-24 | ||||||||
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: 100.30 E-value: 9.36e-24
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| Peptidases_S8_S53 | cd00306 | Peptidase domain in the S8 and S53 families; Members of the peptidases S8 (subtilisin and ... |
125-570 | 6.58e-22 | ||||||||
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: 95.34 E-value: 6.58e-22
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| Peptidases_S8_5 | cd07489 | Peptidase S8 family domain, uncharacterized subfamily 5; gap in seq This family is a member of ... |
199-605 | 6.62e-22 | ||||||||
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: 97.29 E-value: 6.62e-22
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| Peptidases_S8_C5a_Peptidase | cd07475 | Peptidase S8 family domain in Streptococcal C5a peptidases; Streptococcal C5a peptidase (SCP), ... |
201-607 | 5.64e-20 | ||||||||
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: 91.94 E-value: 5.64e-20
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| Peptidases_S8_Subtilisin_like | cd07473 | Peptidase S8 family domain in Subtilisin-like proteins; This family is a member of the ... |
123-571 | 4.15e-19 | ||||||||
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: 87.63 E-value: 4.15e-19
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| Peptidases_S8_CspA-like | cd07478 | Peptidase S8 family domain in CspA-like proteins; GSP (germination-specific protease) converts ... |
200-551 | 3.22e-18 | ||||||||
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: 88.06 E-value: 3.22e-18
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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 ... |
198-567 | 3.47e-16 | ||||||||
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: 79.10 E-value: 3.47e-16
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| Peptidases_S8_BacillopeptidaseF-like | cd07481 | Peptidase S8 family domain in BacillopeptidaseF-like proteins; Bacillus subtilis produces and ... |
198-556 | 1.57e-15 | ||||||||
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: 77.42 E-value: 1.57e-15
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| Inhibitor_I9 | pfam05922 | Peptidase inhibitor I9; This family includes the proteinase B inhibitor from Saccharomyces ... |
33-99 | 4.48e-15 | ||||||||
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: 70.79 E-value: 4.48e-15
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| Peptidases_S8_Lantibiotic_specific_protease | cd07482 | Peptidase S8 family domain in Lantiobiotic (lanthionine-containing antibiotics) specific ... |
201-321 | 4.00e-14 | ||||||||
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: 73.55 E-value: 4.00e-14
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| Peptidases_S8_Thermitase_like | cd07484 | Peptidase S8 family domain in Thermitase-like proteins; Thermitase is a non-specific, ... |
122-337 | 1.63e-13 | ||||||||
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: 71.14 E-value: 1.63e-13
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| Peptidases_S8_12 | cd07480 | Peptidase S8 family domain, uncharacterized subfamily 12; This family is a member of the ... |
198-598 | 1.98e-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: 71.64 E-value: 1.98e-13
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| Peptidases_S8_Kp43_protease | cd04842 | Peptidase S8 family domain in Kp43 proteases; Kp43 proteases are members of the peptidase S8 ... |
122-571 | 1.62e-12 | ||||||||
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: 68.90 E-value: 1.62e-12
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| PA | pfam02225 | PA domain; The PA (Protease associated) domain is found as an insert domain in diverse ... |
367-453 | 8.35e-12 | ||||||||
PA domain; The PA (Protease associated) domain is found as an insert domain in diverse proteases. The PA domain is also found in a plant vacuolar sorting receptor Swiss:O22925 and members of the RZF family Swiss:O43567. It has been suggested that this domain forms a lid-like structure that covers the active site in active proteases, and is involved in protein recognition in vacuolar sorting receptors. Pssm-ID: 460499 [Multi-domain] Cd Length: 91 Bit Score: 61.76 E-value: 8.35e-12
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| T7SS_mycosin | TIGR03921 | type VII secretion-associated serine protease mycosin; Members of this family are ... |
483-587 | 1.10e-10 | ||||||||
type VII secretion-associated serine protease mycosin; Members of this family are subtilisin-related serine proteases, found strictly in the Actinobacteria and associated with type VII secretion operons. The designation mycosin is used for members from Mycobacterium. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair] Pssm-ID: 274856 [Multi-domain] Cd Length: 350 Bit Score: 63.88 E-value: 1.10e-10
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| Peptidases_S8_Autotransporter_serine_protease_like | cd04848 | Peptidase S8 family domain in Autotransporter serine proteases; Autotransporter serine ... |
122-572 | 3.59e-10 | ||||||||
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: 61.57 E-value: 3.59e-10
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| Peptidases_S8_9 | cd07493 | Peptidase S8 family domain, uncharacterized subfamily 9; This family is a member of the ... |
125-338 | 1.21e-09 | ||||||||
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: 59.63 E-value: 1.21e-09
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| Peptidases_S8_13 | cd07496 | Peptidase S8 family domain, uncharacterized subfamily 13; This family is a member of the ... |
444-570 | 1.48e-09 | ||||||||
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: 59.61 E-value: 1.48e-09
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| Peptidases_S8_15 | cd07498 | Peptidase S8 family domain, uncharacterized subfamily 15; This family is a member of the ... |
199-380 | 1.90e-09 | ||||||||
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: 58.89 E-value: 1.90e-09
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| Peptidases_S53_like | cd05562 | Peptidase domain in the S53 family; Members of the peptidase S53 (sedolisin) family include ... |
464-605 | 2.27e-09 | ||||||||
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: 59.23 E-value: 2.27e-09
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| Peptidases_S8_Fervidolysin_like | cd07485 | Peptidase S8 family domain in Fervidolysin; Fervidolysin found in Fervidobacterium pennivorans ... |
482-570 | 8.51e-08 | ||||||||
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: 54.41 E-value: 8.51e-08
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| Peptidases_S8_15 | cd07498 | Peptidase S8 family domain, uncharacterized subfamily 15; This family is a member of the ... |
483-570 | 9.97e-08 | ||||||||
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: 53.50 E-value: 9.97e-08
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| germ_prot_CspBA | NF040809 | bifunctional germination protease/germinant receptor pseudoprotease CspBA; CspBA, as found in ... |
481-551 | 6.44e-07 | ||||||||
bifunctional germination protease/germinant receptor pseudoprotease CspBA; CspBA, as found in Clostridium difficile, is translated as a fusion protein, but cleaved into separate homologous CspB and CspA proteins during spore formation. CspB is a protease, required to active SleC by cleaving it in order to trigger germination. CspA, like the bile salt germinant receptor CspC (encoded by the adjacent gene), has lost the catalytic residues necessary for subtilisin-like serine protease activity. Pssm-ID: 468750 [Multi-domain] Cd Length: 1099 Bit Score: 53.24 E-value: 6.44e-07
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| germ_prot_CspBA | NF040809 | bifunctional germination protease/germinant receptor pseudoprotease CspBA; CspBA, as found in ... |
486-550 | 8.39e-07 | ||||||||
bifunctional germination protease/germinant receptor pseudoprotease CspBA; CspBA, as found in Clostridium difficile, is translated as a fusion protein, but cleaved into separate homologous CspB and CspA proteins during spore formation. CspB is a protease, required to active SleC by cleaving it in order to trigger germination. CspA, like the bile salt germinant receptor CspC (encoded by the adjacent gene), has lost the catalytic residues necessary for subtilisin-like serine protease activity. Pssm-ID: 468750 [Multi-domain] Cd Length: 1099 Bit Score: 52.86 E-value: 8.39e-07
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| Peptidases_S8_Subtilisin_Novo-like | cd07483 | Peptidase S8 family domain in Subtilisin_Novo-like proteins; Subtilisins are a group of ... |
482-568 | 1.49e-06 | ||||||||
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: 50.82 E-value: 1.49e-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 ... |
201-335 | 1.62e-06 | ||||||||
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: 50.14 E-value: 1.62e-06
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| PA_C5a_like | cd02133 | PA_C5a_like: Protease-associated domain containing proteins like Streptococcus pyogenes C5a ... |
344-493 | 3.27e-06 | ||||||||
PA_C5a_like: Protease-associated domain containing proteins like Streptococcus pyogenes C5a peptidase. This group contains various PA domain-containing proteins similar to S. pyogenes C5a, including, i) Vpr, a minor extracellular serine protease from Bacillus subtilis, ii) a large molecular mass collagenolytic protease from Geobacillus collagenovorans MO-1, and iii) PrtS, a cell envelope protease from Streptococcus thermophilus CNRZ 385. Proteins in this group belong to the peptidase S8 family. C5a peptidase is a cell surface serine protease which specifically inactivates C5a [a chemotactic peptide, which attracts polymorphonuclear leukocytes (PMNs)], by cleaving it to release a 7-residue carboxy-terminal fragment which contains the PMN binding site. The significance of the PA domain to these proteins has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate. Pssm-ID: 239048 [Multi-domain] Cd Length: 143 Bit Score: 47.28 E-value: 3.27e-06
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| Peptidases_S8_14 | cd07497 | Peptidase S8 family domain, uncharacterized subfamily 14; This family is a member of the ... |
201-333 | 3.45e-06 | ||||||||
Peptidase S8 family domain, uncharacterized subfamily 14; 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: 173821 [Multi-domain] Cd Length: 311 Bit Score: 49.78 E-value: 3.45e-06
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| Peptidases_S8_13 | cd07496 | Peptidase S8 family domain, uncharacterized subfamily 13; This family is a member of the ... |
198-335 | 3.76e-06 | ||||||||
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: 49.21 E-value: 3.76e-06
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| PA | cd00538 | PA: Protease-associated (PA) domain. The PA domain is an insert domain in a diverse fraction ... |
388-462 | 1.17e-05 | ||||||||
PA: Protease-associated (PA) domain. The PA domain is an insert domain in a diverse fraction of proteases. The significance of the PA domain to many of the proteins in which it is inserted is undetermined. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate. Proteins into which the PA domain is inserted include the following: i) various signal peptide peptidases including, hSPPL2a and 2b which catalyze the intramembrane proteolysis of tumor necrosis factor alpha, ii) various proteins containing a C3H2C3 RING finger including, Arabidopsis ReMembR-H2 protein and various E3 ubiquitin ligases such as human GRAIL (gene related to anergy in lymphocytes), iii) EDEM3 (ER-degradation-enhancing mannosidase-like 3 protein), iv) various plant vacuolar sorting receptors such as Pisum sativum BP-80, v) glutamate carboxypeptidase II (GCPII), vi) yeast aminopeptidase Y, vii) Vibrio metschnikovii VapT, a sodium dodecyl sulfate (SDS) resistant extracellular alkaline serine protease, viii) lactocepin (a cell envelope-associated protease from Lactobacillus paracasei subsp. paracasei NCDO 151), ix) various subtilisin-like proteases such as melon Cucumisin, and x) human TfR (transferrin receptor) 1 and 2. Pssm-ID: 238300 [Multi-domain] Cd Length: 126 Bit Score: 45.20 E-value: 1.17e-05
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| Peptidases_S53 | cd04056 | Peptidase domain in the S53 family; Members of the peptidases S53 (sedolisin) family include ... |
233-334 | 1.27e-05 | ||||||||
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: 48.08 E-value: 1.27e-05
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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 ... |
462-568 | 3.26e-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: 46.29 E-value: 3.26e-05
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| Peptidases_S8_Fervidolysin_like | cd07485 | Peptidase S8 family domain in Fervidolysin; Fervidolysin found in Fervidobacterium pennivorans ... |
203-337 | 3.62e-05 | ||||||||
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: 46.32 E-value: 3.62e-05
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| Peptidases_S8_8 | cd07492 | Peptidase S8 family domain, uncharacterized subfamily 8; This family is a member of the ... |
481-567 | 8.53e-05 | ||||||||
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: 44.64 E-value: 8.53e-05
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| Peptidases_S8_4 | cd05561 | Peptidase S8 family domain, uncharacterized subfamily 4; This family is a member of the ... |
501-573 | 1.36e-04 | ||||||||
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: 44.20 E-value: 1.36e-04
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| Peptidases_S8_Subtilisin_like_2 | cd04847 | Peptidase S8 family domain in Subtilisin-like proteins; This family is a member of the ... |
466-568 | 3.85e-04 | ||||||||
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: 173793 [Multi-domain] Cd Length: 291 Bit Score: 43.06 E-value: 3.85e-04
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| Peptidases_S8_thiazoline_oxidase_subtilisin-like_p | cd07476 | Peptidase S8 family domain in Thiazoline oxidase/subtilisin-like proteases; Thiazoline oxidase ... |
201-331 | 3.93e-04 | ||||||||
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: 43.09 E-value: 3.93e-04
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| Peptidases_S8_14 | cd07497 | Peptidase S8 family domain, uncharacterized subfamily 14; This family is a member of the ... |
482-570 | 4.42e-04 | ||||||||
Peptidase S8 family domain, uncharacterized subfamily 14; 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: 173821 [Multi-domain] Cd Length: 311 Bit Score: 43.23 E-value: 4.42e-04
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| Peptidases_S8_Tripeptidyl_Aminopeptidase_II | cd04857 | Peptidase S8 family domain in Tripeptidyl aminopeptidases_II; Tripeptidyl aminopeptidases II ... |
201-331 | 5.96e-04 | ||||||||
Peptidase S8 family domain in Tripeptidyl aminopeptidases_II; Tripeptidyl aminopeptidases II are member of the 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). Tripeptidyl aminopeptidase II removes tripeptides from the free N terminus of oligopeptides as well as having endoproteolytic activity. Some tripeptidyl aminopeptidases have been shown to cleave tripeptides and small peptides, e.g. angiotensin II and glucagon, while others are believed to be involved in MHC I processing. Pssm-ID: 173796 [Multi-domain] Cd Length: 412 Bit Score: 43.04 E-value: 5.96e-04
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| myxo_dep_M36 | NF038112 | myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ... |
392-455 | 1.26e-03 | ||||||||
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal MYXO-CTERM domain (see TIGR03901), suggesting processing and surface-anchoring by the still-unknown putative transpeptidase, myxosortase. Members of this family include MXAN_3564 (mepA), part of the effector cargo of outer membrane vesicles that the species produces in large numbers during predation on other microbes. Pssm-ID: 468355 [Multi-domain] Cd Length: 1597 Bit Score: 42.34 E-value: 1.26e-03
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| PA_subtilisin_1 | cd04818 | PA_subtilisin_1: Protease-associated domain containing subtilisin-like proteases, subgroup 1. ... |
392-467 | 1.47e-03 | ||||||||
PA_subtilisin_1: Protease-associated domain containing subtilisin-like proteases, subgroup 1. A subgroup of PA domain-containing subtilisin-like proteases. The significance of the PA domain to many of the proteins in which it is inserted is undetermined. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate. Proteins into which the PA domain is inserted include the following subtilisin-like proteases: i) melon cucumisin, ii) Arabidopsis thaliana Ara12, iii) Alnus glutinosa ag12, iv) members of the tomato P69 family, and v) tomato LeSBT2. However, these proteins belong to other subtilisin-like subgroups. Relatively little is known about proteins in this subgroup. Pssm-ID: 240122 [Multi-domain] Cd Length: 118 Bit Score: 39.23 E-value: 1.47e-03
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| PTZ00262 | PTZ00262 | subtilisin-like protease; Provisional |
502-559 | 1.78e-03 | ||||||||
subtilisin-like protease; Provisional Pssm-ID: 240338 [Multi-domain] Cd Length: 639 Bit Score: 41.88 E-value: 1.78e-03
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| PA_SaNapH_like | cd04816 | PA_SaNapH_like: Protease-associated domain containing proteins like Streptomyces anulatus ... |
392-432 | 1.87e-03 | ||||||||
PA_SaNapH_like: Protease-associated domain containing proteins like Streptomyces anulatus N-acetylpuromycin N-acetylhydrolase (SaNapH).This group contains various PA domain-containing proteins similar SaNapH. Proteins in this group belong to the peptidase M28 family. NapH is a terminal enzyme in the puromycin biosynthetic pathway; NapH hydrolyzes N-acetylpuromycin to the active antibiotic. The significance of the PA domain to these proteins has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate. Pssm-ID: 240120 [Multi-domain] Cd Length: 122 Bit Score: 38.85 E-value: 1.87e-03
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| Peptidases_S8_Tripeptidyl_Aminopeptidase_II | cd04857 | Peptidase S8 family domain in Tripeptidyl aminopeptidases_II; Tripeptidyl aminopeptidases II ... |
533-570 | 4.26e-03 | ||||||||
Peptidase S8 family domain in Tripeptidyl aminopeptidases_II; Tripeptidyl aminopeptidases II are member of the 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). Tripeptidyl aminopeptidase II removes tripeptides from the free N terminus of oligopeptides as well as having endoproteolytic activity. Some tripeptidyl aminopeptidases have been shown to cleave tripeptides and small peptides, e.g. angiotensin II and glucagon, while others are believed to be involved in MHC I processing. Pssm-ID: 173796 [Multi-domain] Cd Length: 412 Bit Score: 40.35 E-value: 4.26e-03
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| Peptidases_S8_10 | cd07494 | Peptidase S8 family domain, uncharacterized subfamily 10; This family is a member of the ... |
407-590 | 5.56e-03 | ||||||||
Peptidase S8 family domain, uncharacterized subfamily 10; 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: 173819 [Multi-domain] Cd Length: 298 Bit Score: 39.38 E-value: 5.56e-03
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