S8 family serine peptidase [Streptococcus pseudopneumoniae]
Protein Classification
S8/S53 family peptidase( domain architecture ID 10165472)
S8/S53 family peptidase has an Asp/His/Ser catalytic triad, and may be a member of the peptidases S8 (subtilisin and kexin) or S53 (sedolisin) families; contains a fibronectin type III (FN3)-like domain
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||||
| Peptidases_S8_C5a_Peptidase | cd07475 | Peptidase S8 family domain in Streptococcal C5a peptidases; Streptococcal C5a peptidase (SCP), ... |
158-639 | 2.18e-136 | ||||||||
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: 425.14 E-value: 2.18e-136
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| PA_C5a_like | cd02133 | PA_C5a_like: Protease-associated domain containing proteins like Streptococcus pyogenes C5a ... |
407-536 | 1.12e-35 | ||||||||
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: 132.80 E-value: 1.12e-35
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| fn3_6 super family | cl05663 | Fibronectin type-III domain; This FN3 like domain is found at the C-terminus of cucumisin ... |
653-763 | 5.38e-16 | ||||||||
Fibronectin type-III domain; This FN3 like domain is found at the C-terminus of cucumisin proteins. The actual alignment was detected with superfamily member pfam06280: Pssm-ID: 471288 Cd Length: 112 Bit Score: 75.48 E-value: 5.38e-16
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| PRK03918 super family | cl35229 | DNA double-strand break repair ATPase Rad50; |
1270-1460 | 3.65e-03 | ||||||||
DNA double-strand break repair ATPase Rad50; The actual alignment was detected with superfamily member PRK03918: Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 3.65e-03
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| Name | Accession | Description | Interval | E-value | ||||||||
| Peptidases_S8_C5a_Peptidase | cd07475 | Peptidase S8 family domain in Streptococcal C5a peptidases; Streptococcal C5a peptidase (SCP), ... |
158-639 | 2.18e-136 | ||||||||
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: 425.14 E-value: 2.18e-136
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| AprE | COG1404 | Serine protease, subtilisin family [Posttranslational modification, protein turnover, ... |
159-668 | 1.30e-56 | ||||||||
Serine protease, subtilisin family [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 441014 [Multi-domain] Cd Length: 456 Bit Score: 204.18 E-value: 1.30e-56
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| Peptidase_S8 | pfam00082 | Subtilase family; Subtilases are a family of serine proteases. They appear to have ... |
166-630 | 4.76e-44 | ||||||||
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: 162.24 E-value: 4.76e-44
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| PA_C5a_like | cd02133 | PA_C5a_like: Protease-associated domain containing proteins like Streptococcus pyogenes C5a ... |
407-536 | 1.12e-35 | ||||||||
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: 132.80 E-value: 1.12e-35
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| T7SS_mycosin | TIGR03921 | type VII secretion-associated serine protease mycosin; Members of this family are ... |
165-642 | 1.87e-23 | ||||||||
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: 103.94 E-value: 1.87e-23
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| fn3_5 | pfam06280 | Fn3-like domain; Fn3_5 is an fn3-like domain which is frequently found as the first of three ... |
653-763 | 5.38e-16 | ||||||||
Fn3-like domain; Fn3_5 is an fn3-like domain which is frequently found as the first of three on streptococcal C5a peptidase (SCP), a highly specific protease and adhesin/invasin. The family is found in conjunction with pfam00082, pfam02225 and pfam00746. Pssm-ID: 428863 Cd Length: 112 Bit Score: 75.48 E-value: 5.38e-16
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| PA | pfam02225 | PA domain; The PA (Protease associated) domain is found as an insert domain in diverse ... |
421-504 | 6.74e-14 | ||||||||
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: 68.69 E-value: 6.74e-14
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| germ_prot_CspBA | NF040809 | bifunctional germination protease/germinant receptor pseudoprotease CspBA; CspBA, as found in ... |
166-585 | 2.95e-11 | ||||||||
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: 68.65 E-value: 2.95e-11
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| T9SSA_dep_M36 | NF038113 | T9SS-dependent M36 family metallopeptidase; Members of this family have an M36 family ... |
442-506 | 7.43e-11 | ||||||||
T9SS-dependent M36 family metallopeptidase; Members of this family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal T9SS type A sorting domain (see TIGR04131). Pssm-ID: 468356 [Multi-domain] Cd Length: 868 Bit Score: 67.37 E-value: 7.43e-11
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| germ_prot_CspBA | NF040809 | bifunctional germination protease/germinant receptor pseudoprotease CspBA; CspBA, as found in ... |
163-585 | 1.17e-09 | ||||||||
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: 63.26 E-value: 1.17e-09
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| myxo_dep_M36 | NF038112 | myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ... |
340-506 | 1.24e-09 | ||||||||
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: 63.52 E-value: 1.24e-09
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| PTZ00262 | PTZ00262 | subtilisin-like protease; Provisional |
548-609 | 3.07e-09 | ||||||||
subtilisin-like protease; Provisional Pssm-ID: 240338 [Multi-domain] Cd Length: 639 Bit Score: 61.52 E-value: 3.07e-09
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| PRK03918 | PRK03918 | DNA double-strand break repair ATPase Rad50; |
1270-1460 | 3.65e-03 | ||||||||
DNA double-strand break repair ATPase Rad50; Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 3.65e-03
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| FIVAR | pfam07554 | FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell ... |
1246-1309 | 6.13e-03 | ||||||||
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Swiss:O82833, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures. Pssm-ID: 400096 [Multi-domain] Cd Length: 69 Bit Score: 36.91 E-value: 6.13e-03
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| Name | Accession | Description | Interval | E-value | ||||||||
| Peptidases_S8_C5a_Peptidase | cd07475 | Peptidase S8 family domain in Streptococcal C5a peptidases; Streptococcal C5a peptidase (SCP), ... |
158-639 | 2.18e-136 | ||||||||
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: 425.14 E-value: 2.18e-136
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| AprE | COG1404 | Serine protease, subtilisin family [Posttranslational modification, protein turnover, ... |
159-668 | 1.30e-56 | ||||||||
Serine protease, subtilisin family [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 441014 [Multi-domain] Cd Length: 456 Bit Score: 204.18 E-value: 1.30e-56
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| Peptidases_S8_subtilisin_Vpr-like | cd07474 | Peptidase S8 family domain in Vpr-like proteins; The maturation of the peptide antibiotic ... |
166-637 | 1.40e-50 | ||||||||
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: 181.37 E-value: 1.40e-50
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| Peptidases_S8_5 | cd07489 | Peptidase S8 family domain, uncharacterized subfamily 5; gap in seq This family is a member of ... |
156-645 | 2.23e-46 | ||||||||
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: 169.71 E-value: 2.23e-46
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| Peptidase_S8 | pfam00082 | Subtilase family; Subtilases are a family of serine proteases. They appear to have ... |
166-630 | 4.76e-44 | ||||||||
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: 162.24 E-value: 4.76e-44
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| Peptidases_S8_Subtilisin_like | cd07473 | Peptidase S8 family domain in Subtilisin-like proteins; This family is a member of the ... |
167-611 | 4.56e-37 | ||||||||
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: 141.18 E-value: 4.56e-37
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| Peptidases_S8_1 | cd07487 | Peptidase S8 family domain, uncharacterized subfamily 1; This family is a member of the ... |
166-610 | 5.24e-37 | ||||||||
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: 141.18 E-value: 5.24e-37
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| PA_C5a_like | cd02133 | PA_C5a_like: Protease-associated domain containing proteins like Streptococcus pyogenes C5a ... |
407-536 | 1.12e-35 | ||||||||
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: 132.80 E-value: 1.12e-35
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| Peptidases_S8_Thermitase_like | cd07484 | Peptidase S8 family domain in Thermitase-like proteins; Thermitase is a non-specific, ... |
152-612 | 6.43e-35 | ||||||||
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: 134.70 E-value: 6.43e-35
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| Peptidases_S8_Subtilisin_subset | cd07477 | Peptidase S8 family domain in Subtilisin proteins; This group is composed of many different ... |
168-604 | 4.45e-33 | ||||||||
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: 128.42 E-value: 4.45e-33
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| Peptidases_S8_CspA-like | cd07478 | Peptidase S8 family domain in CspA-like proteins; GSP (germination-specific protease) converts ... |
166-619 | 3.53e-31 | ||||||||
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: 128.89 E-value: 3.53e-31
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| Peptidases_S8_S53 | cd00306 | Peptidase domain in the S8 and S53 families; Members of the peptidases S8 (subtilisin and ... |
169-609 | 1.22e-30 | ||||||||
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: 121.92 E-value: 1.22e-30
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| Peptidases_S8_Autotransporter_serine_protease_like | cd04848 | Peptidase S8 family domain in Autotransporter serine proteases; Autotransporter serine ... |
166-610 | 1.42e-28 | ||||||||
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: 116.65 E-value: 1.42e-28
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| Peptidases_S8_Kp43_protease | cd04842 | Peptidase S8 family domain in Kp43 proteases; Kp43 proteases are members of the peptidase S8 ... |
166-611 | 1.52e-28 | ||||||||
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: 117.43 E-value: 1.52e-28
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| Peptidases_S8_BacillopeptidaseF-like | cd07481 | Peptidase S8 family domain in BacillopeptidaseF-like proteins; Bacillus subtilis produces and ... |
166-604 | 1.63e-27 | ||||||||
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: 113.63 E-value: 1.63e-27
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| Peptidases_S8_3 | cd04852 | Peptidase S8 family domain, uncharacterized subfamily 3; This family is a member of the ... |
160-610 | 4.95e-25 | ||||||||
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: 107.30 E-value: 4.95e-25
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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 ... |
164-605 | 1.19e-24 | ||||||||
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: 104.91 E-value: 1.19e-24
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| T7SS_mycosin | TIGR03921 | type VII secretion-associated serine protease mycosin; Members of this family are ... |
165-642 | 1.87e-23 | ||||||||
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: 103.94 E-value: 1.87e-23
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| Peptidases_S8_6 | cd07490 | Peptidase S8 family domain, uncharacterized subfamily 6; This family is a member of the ... |
168-611 | 7.59e-23 | ||||||||
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: 99.54 E-value: 7.59e-23
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| Peptidases_S8_13 | cd07496 | Peptidase S8 family domain, uncharacterized subfamily 13; This family is a member of the ... |
168-604 | 2.94e-21 | ||||||||
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: 95.82 E-value: 2.94e-21
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| Peptidases_S8_Subtilisin_Novo-like | cd07483 | Peptidase S8 family domain in Subtilisin_Novo-like proteins; Subtilisins are a group of ... |
170-611 | 4.89e-20 | ||||||||
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: 92.43 E-value: 4.89e-20
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| Peptidases_S8_15 | cd07498 | Peptidase S8 family domain, uncharacterized subfamily 15; This family is a member of the ... |
169-381 | 7.95e-17 | ||||||||
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: 81.62 E-value: 7.95e-17
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| fn3_5 | pfam06280 | Fn3-like domain; Fn3_5 is an fn3-like domain which is frequently found as the first of three ... |
653-763 | 5.38e-16 | ||||||||
Fn3-like domain; Fn3_5 is an fn3-like domain which is frequently found as the first of three on streptococcal C5a peptidase (SCP), a highly specific protease and adhesin/invasin. The family is found in conjunction with pfam00082, pfam02225 and pfam00746. Pssm-ID: 428863 Cd Length: 112 Bit Score: 75.48 E-value: 5.38e-16
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| PA | cd00538 | PA: Protease-associated (PA) domain. The PA domain is an insert domain in a diverse fraction ... |
433-506 | 2.18e-15 | ||||||||
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: 74.09 E-value: 2.18e-15
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| Peptidases_S8_12 | cd07480 | Peptidase S8 family domain, uncharacterized subfamily 12; This family is a member of the ... |
166-588 | 2.62e-15 | ||||||||
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: 78.57 E-value: 2.62e-15
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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 ... |
160-381 | 1.45e-14 | ||||||||
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: 75.57 E-value: 1.45e-14
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| PA | pfam02225 | PA domain; The PA (Protease associated) domain is found as an insert domain in diverse ... |
421-504 | 6.74e-14 | ||||||||
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: 68.69 E-value: 6.74e-14
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| Peptidases_S8_9 | cd07493 | Peptidase S8 family domain, uncharacterized subfamily 9; This family is a member of the ... |
439-605 | 7.28e-14 | ||||||||
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: 73.49 E-value: 7.28e-14
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| PA_subtilisin_1 | cd04818 | PA_subtilisin_1: Protease-associated domain containing subtilisin-like proteases, subgroup 1. ... |
433-505 | 7.82e-14 | ||||||||
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: 69.28 E-value: 7.82e-14
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| Peptidases_S8_Lantibiotic_specific_protease | cd07482 | Peptidase S8 family domain in Lantiobiotic (lanthionine-containing antibiotics) specific ... |
169-382 | 3.87e-13 | ||||||||
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: 72.01 E-value: 3.87e-13
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| PA_SaNapH_like | cd04816 | PA_SaNapH_like: Protease-associated domain containing proteins like Streptomyces anulatus ... |
431-506 | 6.44e-13 | ||||||||
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: 66.97 E-value: 6.44e-13
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| Peptidases_S8_Protein_convertases_Kexins_Furin-lik | cd04059 | Peptidase S8 family domain in Protein convertases; Protein convertases, whose members include ... |
160-382 | 8.91e-13 | ||||||||
Peptidase S8 family domain in Protein convertases; Protein convertases, whose members include furins and kexins, are members of the peptidase S8 or Subtilase clan of proteases. They have an Asp/His/Ser catalytic triad that is not homologous to trypsin. Kexins are involved in the activation of peptide hormones, growth factors, and viral proteins. Furin cleaves cell surface vasoactive peptides and proteins involved in cardiovascular tissue remodeling in the TGN, at cell surface, or in endosomes but rarely in the ER. Furin also plays a key role in blood pressure regulation though the activation of transforming growth factor (TGF)-beta. High specificity is seen for cleavage after dibasic (Lys-Arg or Arg-Arg) or multiple basic residues in protein convertases. There is also strong sequence conservation. Pssm-ID: 173789 [Multi-domain] Cd Length: 297 Bit Score: 70.67 E-value: 8.91e-13
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| Peptidases_S8_Fervidolysin_like | cd07485 | Peptidase S8 family domain in Fervidolysin; Fervidolysin found in Fervidobacterium pennivorans ... |
158-346 | 5.29e-12 | ||||||||
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: 68.28 E-value: 5.29e-12
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| germ_prot_CspBA | NF040809 | bifunctional germination protease/germinant receptor pseudoprotease CspBA; CspBA, as found in ... |
166-585 | 2.95e-11 | ||||||||
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: 68.65 E-value: 2.95e-11
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| PA_C_RZF_like | cd02123 | PA_C-RZF_ like: Protease-associated (PA) domain C_RZF-like. This group includes various PA ... |
443-505 | 4.07e-11 | ||||||||
PA_C-RZF_ like: Protease-associated (PA) domain C_RZF-like. This group includes various PA domain-containing proteins similar to C-RZF (chicken embryo RING zinc finger) protein. These proteins contain a C3H2C3 RING finger. C-RZF is expressed in embryo cells and is restricted mainly to brain and heart, it is localized to both the nucleus and endosomes. Additional C3H2C3 RING finger proteins belonging to this group, include Arabidopsis ReMembR-H2 protein and mouse sperizin. ReMembR-H2 is likely to be an integral membrane protein, and to traffic through the endosomal pathway. Sperizin is expressed in haploid germ cells and localized in the cytoplasm, it may participate in spermatogenesis. 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: 239038 [Multi-domain] Cd Length: 153 Bit Score: 62.74 E-value: 4.07e-11
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| T9SSA_dep_M36 | NF038113 | T9SS-dependent M36 family metallopeptidase; Members of this family have an M36 family ... |
442-506 | 7.43e-11 | ||||||||
T9SS-dependent M36 family metallopeptidase; Members of this family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal T9SS type A sorting domain (see TIGR04131). Pssm-ID: 468356 [Multi-domain] Cd Length: 868 Bit Score: 67.37 E-value: 7.43e-11
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| Peptidases_S8_Tripeptidyl_Aminopeptidase_II | cd04857 | Peptidase S8 family domain in Tripeptidyl aminopeptidases_II; Tripeptidyl aminopeptidases II ... |
240-344 | 1.28e-10 | ||||||||
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: 65.38 E-value: 1.28e-10
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| PA_GCPII_like | cd02121 | PA_GCPII_like: Protease-associated domain containing protein, glutamate carboxypeptidase II ... |
423-472 | 3.20e-10 | ||||||||
PA_GCPII_like: Protease-associated domain containing protein, glutamate carboxypeptidase II (GCPII)-like. This group contains various PA domain-containing proteins similar to GCPII including, GCPIII (NAALADase2) and NAALADase L. These proteins belong to the peptidase M28 family. GCPII is also known N-acetylated-alpha-linked acidic dipeptidase (NAALDase1), folate hydrolase or prostate-specific membrane antigen (PSMA). GCPII is found in various human tissues including prostate, small intestine, and the central nervous system. In the brain, GCPII is known as NAALDase1, it functions as a NAALDase hydrolyzing the neuropeptide N-acetyl-L-aspartyl-L-glutamate (alpha-NAAG), to release free glutamate. In the small intestine, GCPII releases the terminal glutamate from poly-gamma-glutamated folates. GCPII (PSMA) is a useful cancer marker; its expression is markedly increased in prostate cancer and in tumor-associated neovasculature. GCPIII hydrolyzes alpha-NAAG with a lower efficiency than does GCPII; NAALADase L is not able to hydrolyze alpha-NAAG. The GCPII PA domain (referred to as the apical domain) participates in substrate binding and may act as a protein-protein interaction domain. Pssm-ID: 239036 Cd Length: 220 Bit Score: 61.92 E-value: 3.20e-10
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| PA_GRAIL_like | cd02122 | PA _GRAIL_like: Protease-associated (PA) domain GRAIL-like. This group includes PA domain ... |
444-504 | 3.94e-10 | ||||||||
PA _GRAIL_like: Protease-associated (PA) domain GRAIL-like. This group includes PA domain containing E3 (ubiquitin ligases) similar to human GRAIL (gene related to anergy in lymphocytes) protein. Proteins in this group contain a C3H2C3 RING finger. E3 ubiquitin ligase is part of an enzymic cascade, the end result of which is the ubiquitination of proteins. In this cascade, E1 activates the ubiquitin, the activated ubiquitin is carried by E2, and E3 recognizes the acceptor protein as well as catalyzes the transfer of the activated ubiquitin from E2 to this acceptor. GRAIL, a transmembrane protein localized in the endosomes, controls the development of T cell clonal anergy, and may ubiquitinate membrane-associated targets for T cell activation. GRAIL1 is associated with, and regulated by, two isoforms of otubain 1 (the ubiquitin-specific protease). Additional E3s belonging to this group include human (h)Goliath and Xenopus GREUL1 (Goliath Related E3 Ubiquitin Ligase 1). hGoliath and GRAIL both have the property of self-ubiquitination. hGoliath is expressed in leukocytes; its expression and localization is not modified in leukemia. GREUL1 may play a role in the generation of anterior ectoderm. 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: 239037 [Multi-domain] Cd Length: 138 Bit Score: 59.62 E-value: 3.94e-10
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| PA_ScAPY_like | cd02130 | PA_ScAPY_like: Protease-associated domain containing proteins like Saccharomyces cerevisiae ... |
432-506 | 4.61e-10 | ||||||||
PA_ScAPY_like: Protease-associated domain containing proteins like Saccharomyces cerevisiae aminopeptidase Y (ScAPY). This group contains various PA domain-containing proteins similar to the S. cerevisiae APY, including Trichophyton rubrum leucine aminopeptidase 1(LAP1). Proteins in this group belong to the peptidase M28 family. ScAPY hydrolyzes amino acid-4-methylcoumaryl-7-amides (MCAs). ScAPY more rapidly hydrolyzes dipeptidyl-MCAs. Hydrolysis of amino acid-MCAs or dipeptides is stimulated by Co2+ while the hydrolysis of dipeptidyl-MCAs, tripeptides, and longer peptides is inhibited by Co2+. ScAPY is vacuolar and is activated by proteolytic processing. LAP1 is a secreted leucine aminopeptidase. 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: 239045 [Multi-domain] Cd Length: 122 Bit Score: 58.81 E-value: 4.61e-10
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| PA_EDEM3_like | cd02126 | PA_EDEM3_like: protease associated domain (PA) domain-containing EDEM3-like proteins. This ... |
433-504 | 7.48e-10 | ||||||||
PA_EDEM3_like: protease associated domain (PA) domain-containing EDEM3-like proteins. This group contains various PA domain-containing proteins similar to mouse EDEM3 (ER-degradation-enhancing mannosidase-like 3 protein). EDEM3 contains a region, similar to Class I alpha-mannosidases (gylcosyl hydrolase family 47), N-terminal to the PA domain. EDEM3 accelerates glycoprotein ERAD (ER-associated degradation). In transfected mammalian cells, overexpression of EDEM3 enhances the mannose trimming from the N-glycans, of a model misfolded protein [alpha1-antitrypsin null (Hong Kong)] as well as, from total glycoproteins. Mannose trimming appears to be involved in the selection of ERAD substrates. EDEM3 has a different specificity of trimming than ER alpha-mannosidase 1. The significance of the PA domain to EDEM3 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: 239041 [Multi-domain] Cd Length: 126 Bit Score: 58.14 E-value: 7.48e-10
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| germ_prot_CspBA | NF040809 | bifunctional germination protease/germinant receptor pseudoprotease CspBA; CspBA, as found in ... |
163-585 | 1.17e-09 | ||||||||
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: 63.26 E-value: 1.17e-09
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| myxo_dep_M36 | NF038112 | myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ... |
340-506 | 1.24e-09 | ||||||||
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: 63.52 E-value: 1.24e-09
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| PTZ00262 | PTZ00262 | subtilisin-like protease; Provisional |
548-609 | 3.07e-09 | ||||||||
subtilisin-like protease; Provisional Pssm-ID: 240338 [Multi-domain] Cd Length: 639 Bit Score: 61.52 E-value: 3.07e-09
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| Peptidases_S8_thiazoline_oxidase_subtilisin-like_p | cd07476 | Peptidase S8 family domain in Thiazoline oxidase/subtilisin-like proteases; Thiazoline oxidase ... |
235-343 | 5.05e-09 | ||||||||
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: 59.26 E-value: 5.05e-09
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| Peptidases_S53_like | cd05562 | Peptidase domain in the S53 family; Members of the peptidase S53 (sedolisin) family include ... |
537-610 | 7.84e-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: 58.46 E-value: 7.84e-09
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| PA_2 | cd04819 | PA_2: Protease-associated (PA) domain subgroup 2. A subgroup of PA-domain containing proteins. ... |
421-498 | 5.24e-08 | ||||||||
PA_2: Protease-associated (PA) domain subgroup 2. A subgroup of PA-domain containing proteins. 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 in this group contain a C-terminal RING-finger domain. Proteins into which the PA domain is inserted include the following: i) various signal peptide peptidases: such as hSPPL2a and 2b, ii) various E3 ubiquitin ligases similar to human GRAIL (gene related to anergy in lymphocytes) protein, iii) various proteins containing a RING finger motif such as Arabidopsis ReMembR-H2 protein, iv) EDEM3 (ER-degradation-enhancing mannosidase-like 3 protein), v) various plant vacuolar sorting receptors such as Pisum sativum BP-80, vi) prostate-specific membrane antigen (PSMA), vii) yeast aminopeptidase Y viii) Vibrio metschnikovii VapT, a sodium dodecyl sulfate (SDS) resistant extracellular alkaline serine protease, ix) various subtilisin-like proteases such as Cucumisin from the juice of melon fruits, and x) human TfR (transferrin receptor) 1 and human TfR2. The proteins listed above belong to other subgroups; relatively little is known about proteins in this subgroup. Pssm-ID: 240123 [Multi-domain] Cd Length: 127 Bit Score: 53.17 E-value: 5.24e-08
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| Peptidases_S8_4 | cd05561 | Peptidase S8 family domain, uncharacterized subfamily 4; This family is a member of the ... |
171-343 | 8.27e-08 | ||||||||
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: 54.99 E-value: 8.27e-08
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| PA_1 | cd04813 | PA_1: Protease-associated (PA) domain subgroup 1. A subgroup of PA-domain containing proteins. ... |
421-506 | 7.90e-07 | ||||||||
PA_1: Protease-associated (PA) domain subgroup 1. A subgroup of PA-domain containing proteins. Proteins in this subgroup contain a RING-finger (Really Interesting New Gene) domain C-terminal to this 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 in this group contain a C-terminal RING-finger domain. Proteins into which the PA domain is inserted include the following: i) various signal peptide peptidases: such as hSPPL2a and 2b, ii) various E3 ubiquitin ligases similar to human GRAIL (gene related to anergy in lymphocytes) protein, iii) various proteins containing a RING finger motif such as Arabidopsis ReMembR-H2 protein, iv) EDEM3 (ER-degradation-enhancing mannosidase-like 3 protein), v) various plant vacuolar sorting receptors such as Pisum sativum BP-80, vi) prostate-specific membrane antigen (PSMA), vii) yeast aminopeptidase Y viii) Vibrio metschnikovii VapT, a sodium dodecyl sulfate (SDS) resistant extracellular alkaline serine protease, ix) various subtilisin-like proteases such as Cucumisin from the juice of melon fruits, and x) human TfR (transferrin receptor) 1 and human TfR2. The proteins listed above belong to other subgroups; relatively little is known about proteins in this subgroup. Pssm-ID: 240117 [Multi-domain] Cd Length: 117 Bit Score: 49.31 E-value: 7.90e-07
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| Peptidases_S8_8 | cd07492 | Peptidase S8 family domain, uncharacterized subfamily 8; This family is a member of the ... |
168-349 | 3.46e-06 | ||||||||
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: 50.03 E-value: 3.46e-06
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| PA_TfR | cd02128 | PA_TfR: Protease-associated domain containing proteins like transferrin receptor (TfR). This ... |
430-472 | 4.65e-06 | ||||||||
PA_TfR: Protease-associated domain containing proteins like transferrin receptor (TfR). This group contains various PA domain-containing proteins similar to human TfR1 and TfR2. TfR1 and TfR2 are type II membrane proteins, belonging to the peptidase M28 family. TfR1 is homodimeric, widely expressed, and a key player in the uptake of iron-loaded transferrin (Tf) into cells. The TfR1 homodimer binds two molecules of Tf and this complex is internalized. In addition to its role in iron uptake, TfR1 may participate in cell growth and proliferation. TfR2 also binds Tf but with a significantly lower affinity than does TfR1. TfR2 is expressed chiefly in hepatocytes, hematopoietic cells, and duodenal crypt cells; its expression overlaps with that of hereditary hemochromatosis protein (HFE). TfR2 is involved in iron homeostasis. HFE and TfR2 interact in cells. By one model for serum iron sensing, at low or basal iron concentrations, HFE and TFR1 form a complex at the plasma membrane; at increased Tf, Tf competes with HFE for binding of TfR1, resulting in HFE disassociating from TfR1 and associating with TfR2 . The TfR1-TfR2 association might initiate a signal cascade leading to the induction of hepcidin (a small peptide hormone that controls systemic iron levels). Human mutations in TfR2 are associated with a form of hemochromatosis (HFE3). The significance of the PA domain to TfRs 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: 239043 [Multi-domain] Cd Length: 183 Bit Score: 48.94 E-value: 4.65e-06
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| Peptidases_S8_14 | cd07497 | Peptidase S8 family domain, uncharacterized subfamily 14; This family is a member of the ... |
526-610 | 5.38e-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: 50.16 E-value: 5.38e-06
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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 ... |
169-387 | 5.52e-06 | ||||||||
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: 49.99 E-value: 5.52e-06
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| Peptidases_S8_10 | cd07494 | Peptidase S8 family domain, uncharacterized subfamily 10; This family is a member of the ... |
544-625 | 1.60e-05 | ||||||||
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: 48.63 E-value: 1.60e-05
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| Peptidases_S8_thiazoline_oxidase_subtilisin-like_p | cd07476 | Peptidase S8 family domain in Thiazoline oxidase/subtilisin-like proteases; Thiazoline oxidase ... |
523-613 | 1.89e-05 | ||||||||
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: 48.09 E-value: 1.89e-05
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| PA_VSR | cd02125 | PA_VSR: Protease-associated (PA) domain-containing plant vacuolar sorting receptor (VSR). This ... |
446-507 | 2.44e-05 | ||||||||
PA_VSR: Protease-associated (PA) domain-containing plant vacuolar sorting receptor (VSR). This group includes various PA domain-containing VSRs such as garden pea BP-80, pumpkin PV72, and various Arabidopsis VSRs including AtVSR1. In contrast to most eukaryotes, which only have one or two VSRs, plants have several. This may in part be a reflection of having a more complex vacuolar system with both lytic vacuoles and storage vacuoles. The lytic vacuole is thought to be equivalent to the mammalian lysosome and the yeast vacuole. Pea BP-80 is a type 1 transmembrane protein, involved in the targeting of proteins to the lytic vacuole; it has been suggested that this protein also mediates targeting to the storage vacuole. PV72 and AtVSR1 may mediate transport of seed storage proteins to protein storage vacuoles. The significance of the PA domain to VSRs 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: 239040 [Multi-domain] Cd Length: 127 Bit Score: 45.55 E-value: 2.44e-05
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| Peptidases_S8_14 | cd07497 | Peptidase S8 family domain, uncharacterized subfamily 14; This family is a member of the ... |
166-381 | 5.23e-05 | ||||||||
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: 47.08 E-value: 5.23e-05
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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 ... |
527-606 | 5.27e-05 | ||||||||
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: 46.91 E-value: 5.27e-05
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| Peptidases_S8_11 | cd04843 | Peptidase S8 family domain, uncharacterized subfamily 11; This family is a member of the ... |
154-365 | 6.09e-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: 46.54 E-value: 6.09e-05
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| Peptidases_S8_11 | cd04843 | Peptidase S8 family domain, uncharacterized subfamily 11; This family is a member of the ... |
530-604 | 2.77e-04 | ||||||||
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: 44.61 E-value: 2.77e-04
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| PA_VapT_like | cd04817 | PA_VapT_like: Protease-associated domain containing proteins like VapT from Vibrio ... |
439-505 | 3.22e-04 | ||||||||
PA_VapT_like: Protease-associated domain containing proteins like VapT from Vibrio metschnikovii strain RH530. This group contains various PA domain-containing proteins similar to V. metschnikovii VapT, including the serine alkaline protease SapSh from the psychotroph Shewanella strain Ac10 and the Apa1 protease from the psychrotroph Pseudoalteromonas Sp. As-11. VapT is a sodium dodecyl sulfate (SDS) resistant extracellular alkaline serine protease showing high activity over a broad pH range and temperature. SapSh has a high level of protease activity at low temperatures. Apa1 is also cold-adapted. 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: 240121 Cd Length: 139 Bit Score: 42.47 E-value: 3.22e-04
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| Peptidases_S8_8 | cd07492 | Peptidase S8 family domain, uncharacterized subfamily 8; This family is a member of the ... |
521-599 | 3.65e-04 | ||||||||
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: 43.87 E-value: 3.65e-04
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| Peptidases_S8_4 | cd05561 | Peptidase S8 family domain, uncharacterized subfamily 4; This family is a member of the ... |
534-581 | 4.05e-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: 43.82 E-value: 4.05e-04
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| PA_M28_1_3 | cd04822 | PA_M28_1_3: Protease-associated (PA) domain, peptidase family M28, subfamily-1, subgroup 3. A ... |
421-476 | 4.58e-04 | ||||||||
PA_M28_1_3: Protease-associated (PA) domain, peptidase family M28, subfamily-1, subgroup 3. A subgroup of PA-domain containing proteins belonging to the peptidase family M28. Family M28 contains aminopeptidases and carboxypeptidases, and has co-catalytic zinc ions. 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 members of the peptidase family M28: i) prostate-specific membrane antigen (PSMA), ii) yeast aminopeptidase Y, and ii) human TfR (transferrin receptor)1 and human TfR2. The proteins listed above belong to other subgroups; relatively little is known about proteins in this subgroup. Pssm-ID: 240126 [Multi-domain] Cd Length: 151 Bit Score: 42.44 E-value: 4.58e-04
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| PA_hPAP21_like | cd02127 | PA_hPAP21_like: Protease-associated domain containing proteins like the human secreted ... |
433-496 | 5.00e-04 | ||||||||
PA_hPAP21_like: Protease-associated domain containing proteins like the human secreted glycoprotein hPAP21 (human protease-associated domain-containing protein, 21kDa). This group contains various PA domain-containing proteins similar to hPAP21. Complex N-glycosylation may be required for the secretion of hPAP21. The significance of the PA domain to hPAP21 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: 239042 [Multi-domain] Cd Length: 118 Bit Score: 41.59 E-value: 5.00e-04
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| PA_PoS1_like | cd02124 | PA_PoS1_like: Protease-associated (PA) domain PoS1-like. This group includes various PA ... |
439-478 | 1.17e-03 | ||||||||
PA_PoS1_like: Protease-associated (PA) domain PoS1-like. This group includes various PA domain-containing proteins similar to Pleurotus ostreatus (Po)S1. PoSl, the main extracellular protease in P. ostreatus is a subtilisin-like serine protease belonging to the peptidase S8 family. Ca2+ and Mn2+ both stimulate the protease activity of (Po)S1. Ca2+ protects PoS1 from autolysis. PoS1 is a monomeric glycoprotein, which may play a role in the regulation of laccases in lignin formation. (Po)S1 participates in the degradation of POXA1b, and in the activation of POXA3, (POXA1b and POXA3 are laccase isoenzymes), but its effect may be indirect. The significance of the PA domain to PoS1 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: 239039 Cd Length: 129 Bit Score: 40.78 E-value: 1.17e-03
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| PA_GO-like | cd02132 | PA_GO-like: Protease-associated domain containing proteins like Arabidopsis thaliana growth-on ... |
442-507 | 2.00e-03 | ||||||||
PA_GO-like: Protease-associated domain containing proteins like Arabidopsis thaliana growth-on protein GRO10. This group contains various PA domain-containing proteins similar to the functionally uncharacterized Arabidopsis GRO10. The PA domain 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: 239047 [Multi-domain] Cd Length: 139 Bit Score: 40.10 E-value: 2.00e-03
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| PRK03918 | PRK03918 | DNA double-strand break repair ATPase Rad50; |
1270-1460 | 3.65e-03 | ||||||||
DNA double-strand break repair ATPase Rad50; Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 3.65e-03
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| FIVAR | pfam07554 | FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell ... |
1246-1309 | 6.13e-03 | ||||||||
FIVAR domain; This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Swiss:O82833, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures. Pssm-ID: 400096 [Multi-domain] Cd Length: 69 Bit Score: 36.91 E-value: 6.13e-03
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