Peptidase M36 family, also known as fungalysin family; The M36 peptidase family, also known as ...
336-499
5.20e-20
Peptidase M36 family, also known as fungalysin family; The M36 peptidase family, also known as fungalysin (elastinolytic metalloproteinase) family, includes endopeptidases from pathogenic fungi. Fungalysin can hydrolyze extracellular matrix proteins such as elastin and keratin, with a preference for cleavage on the amino side of hydrophobic residues with bulky side-chains. This family is similar to the M4 (thermolysin) family due to the presence of the HEXXH motif in the active site residues, as well as its fold prediction. Some of these enzymes also contain a protease-associated (PA) domain insert. The eukaryotic M36 and bacterial M4 families of metalloproteases also share a conserved domain in their propeptides called FTP (fungalysin/thermolysin propeptide). Aspergillus fumigatus causes the pulmonary disease aspergillosis by invading the lungs of immuno-compromised animals; it secretes fungalysin that possibly breaks down proteinaceous structural barriers. A solid lesion known as an aspergilloma can grow in a lung cavity, particularly following recovery from tuberculosis. Fungalysins are also found as multiple copies in the human and animal pathogenic fungi such as Microsporum canis, Trichophyton rubrum and T. mentagrophytes, which cause cutaneous infections.
Pssm-ID: 341059 [Multi-domain] Cd Length: 317 Bit Score: 90.80 E-value: 5.20e-20
T9SS-dependent M36 family metallopeptidase; Members of this family have an M36 family ...
340-503
1.96e-06
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: 50.42 E-value: 1.96e-06
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ...
21-112
1.14e-04
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: 45.03 E-value: 1.14e-04
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ...
336-376
2.09e-04
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: 44.26 E-value: 2.09e-04
Peptidase M36 family, also known as fungalysin family; The M36 peptidase family, also known as ...
336-499
5.20e-20
Peptidase M36 family, also known as fungalysin family; The M36 peptidase family, also known as fungalysin (elastinolytic metalloproteinase) family, includes endopeptidases from pathogenic fungi. Fungalysin can hydrolyze extracellular matrix proteins such as elastin and keratin, with a preference for cleavage on the amino side of hydrophobic residues with bulky side-chains. This family is similar to the M4 (thermolysin) family due to the presence of the HEXXH motif in the active site residues, as well as its fold prediction. Some of these enzymes also contain a protease-associated (PA) domain insert. The eukaryotic M36 and bacterial M4 families of metalloproteases also share a conserved domain in their propeptides called FTP (fungalysin/thermolysin propeptide). Aspergillus fumigatus causes the pulmonary disease aspergillosis by invading the lungs of immuno-compromised animals; it secretes fungalysin that possibly breaks down proteinaceous structural barriers. A solid lesion known as an aspergilloma can grow in a lung cavity, particularly following recovery from tuberculosis. Fungalysins are also found as multiple copies in the human and animal pathogenic fungi such as Microsporum canis, Trichophyton rubrum and T. mentagrophytes, which cause cutaneous infections.
Pssm-ID: 341059 [Multi-domain] Cd Length: 317 Bit Score: 90.80 E-value: 5.20e-20
Peptidase M4 family (includes thermolysin, aureolysin, neutral protease and bacillolysin) and ...
274-499
3.38e-19
Peptidase M4 family (includes thermolysin, aureolysin, neutral protease and bacillolysin) and Peptidase M36 family (also known as fungalysin); This family includes the peptidases M4 as well as M36, both belonging to the Gluzincin family. The M4 peptidase family includes numerous zinc-dependent metallopeptidases that hydrolyze peptide bonds, such as thermolysin (EC 3.4.24.27), pseudolysin (the extracellullar elastase of Pseudomonas aeruginosa), aureolysin (the extracellular metalloproteinase from Staphylococcus aureus), neutral protease from Bacillus cereus, as well as bacillolysin (EC 3.4.24.28). The M36 family also known as fungalysin (elastinolytic metalloproteinase) family, includes endopeptidases from pathogenic fungi. Both M4 and M36 families have similar folds and contain the Zn-binding site and the active site HEXXH motif. The eukaryotic M36 and bacterial M4 families of metalloproteases also share a conserved domain in their propeptides called FTP (fungalysin/thermolysin propeptide).
Pssm-ID: 341048 [Multi-domain] Cd Length: 313 Bit Score: 88.12 E-value: 3.38e-19
Peptidase M4 family containing mostly uncharacterized proteins; This family of uncharacterized ...
316-491
3.72e-13
Peptidase M4 family containing mostly uncharacterized proteins; This family of uncharacterized bacterial proteins are homologs of the M4 peptidase family that is also known as the thermolysin-like peptidase (TLP) family. Typically, the M4 peptidases consist of a presequence (signal sequence), a propeptide sequence and a peptidase unit. The presequence is cleaved off during export while the propeptide has inhibitory and chaperone functions and facilitates folding. The propeptide remains attached until the peptidase is secreted and can be safely activated. All peptidases in this family bind a single catalytic zinc ion which is tetrahedrally co-ordinated by three amino acid ligands and a water molecule that forms the nucleophile on activation during catalysis. TLPs are secreted eubacterial endopeptidases from Gram-positive or Gram-negative sources that degrade extracellular proteins and peptides for bacterial nutrition. They contain the HEXXH motif as part of their active site and belong to the Gluzincins family and are selectively inhibited by Steptomyces metalloproteinase inhibitor (SMPI) as well as by phosphoramidon from Streptomyces tanashiensis. A large number of these enzymes are implicated as key factors in the pathogenesis of various diseases, including gastritis, peptic ulcer, gastric carcinoma, cholera and several types of bacterial infections, and are therefore important drug targets. Some enzymes of the family can function at extremes of temperatures, while some function in organic solvents, thus rendering them novel targets for biotechnological applications.
Pssm-ID: 341061 Cd Length: 263 Bit Score: 69.65 E-value: 3.72e-13
Peptidase M4 family including thermolysin, protealysin, aureolysin, and neutral protease; This ...
293-500
6.13e-12
Peptidase M4 family including thermolysin, protealysin, aureolysin, and neutral protease; This peptidase M4 family includes several endopeptidases such as thermolysin (EC 3.4.24.27), aureolysin (the extracellular metalloproteinase from Staphylococcus aureus), neutral protease from Bacillus cereus, protealysin, and bacillolysin (EC 3.4.24.28). Typically, the M4 peptidases consist of a presequence (signal sequence), a propeptide sequence, and a peptidase unit. The presequence is cleaved off during export while the propeptide has inhibitory and chaperone functions and facilitates folding. The propeptide remains attached until the peptidase is secreted and can be safely activated. All peptidases in this family bind a single catalytic zinc ion which is tetrahedrally co-ordinated by three amino acid ligands and a water molecule that forms the nucleophile on activation during catalysis. The active site is found between two sub-domains; the N-terminal domain contains the HEXXH zinc-binding motif while the helical C-terminal domain, which is unique for the family, carries the third zinc ligand. These peptidases are secreted eubacterial endopeptidases from Gram-positive or Gram-negative sources that degrade extracellular proteins and peptides for bacterial nutrition. They are selectively inhibited by Steptomyces metalloproteinase inhibitor (SMPI) as well as by phosphoramidon from Streptomyces tanashiensis. A large number of these enzymes are implicated as key factors in the pathogenesis of various diseases, including gastritis, peptic ulcer, gastric carcinoma, cholera and several types of bacterial infections, and are therefore important drug targets. Some enzymes of the family can function at extremes of temperatures, while some function in organic solvents, thus rendering them novel targets for biotechnological applications. Thermolysin is widely used as a nonspecific protease to obtain fragments for peptide sequencing. It has also been used in production of the artificial sweetener aspartame.
Pssm-ID: 341060 [Multi-domain] Cd Length: 278 Bit Score: 66.10 E-value: 6.13e-12
T9SS-dependent M36 family metallopeptidase; Members of this family have an M36 family ...
340-503
1.96e-06
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: 50.42 E-value: 1.96e-06
Peptidase propeptide and YPEB domain; This region is likely to have an protease inhibitory ...
122-192
6.60e-05
Peptidase propeptide and YPEB domain; This region is likely to have an protease inhibitory function (personal obs:C Yeats). This model is likely to miss some members of this family as the separation from signal to noise is not clear. The name is derived from Peptidase _ Bacillus subtilis YPEB.
Pssm-ID: 427284 [Multi-domain] Cd Length: 59 Bit Score: 40.74 E-value: 6.60e-05
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ...
21-112
1.14e-04
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: 45.03 E-value: 1.14e-04
Fungalysin/Thermolysin Propeptide Motif; This motif is found in both the bacterial M4 ...
75-108
2.01e-04
Fungalysin/Thermolysin Propeptide Motif; This motif is found in both the bacterial M4 peptidase propeptide and the fungal M36 propeptide. Its exact function is not clear, but it is likely to either inhibit the peptidase, so as to prevent its premature activation, or has a chaperone activity. Both of these roles have been ascribed to the M4 and M36 propeptides.
Pssm-ID: 429499 [Multi-domain] Cd Length: 50 Bit Score: 39.00 E-value: 2.01e-04
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ...
336-376
2.09e-04
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: 44.26 E-value: 2.09e-04
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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