Species | Pseudomonas_E extremaustralis | |||||||||||
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Lineage | Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae; Pseudomonas_E; Pseudomonas_E extremaustralis | |||||||||||
CAZyme ID | MGYG000003208_03014 | |||||||||||
CAZy Family | CBM73 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 66355; End: 68925 Strand: - |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd04843 | Peptidases_S8_11 | 1.79e-69 | 167 | 433 | 1 | 277 | 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. |
cd07484 | Peptidases_S8_Thermitase_like | 1.16e-15 | 168 | 431 | 16 | 255 | 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. |
cd00306 | Peptidases_S8_S53 | 4.64e-15 | 186 | 431 | 5 | 241 | 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. |
cd07498 | Peptidases_S8_15 | 1.02e-13 | 217 | 431 | 42 | 242 | 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. |
cd04077 | Peptidases_S8_PCSK9_ProteinaseK_like | 1.51e-11 | 217 | 432 | 65 | 253 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QDH65771.1 | 0.0 | 1 | 855 | 1 | 855 |
QDG55268.1 | 0.0 | 1 | 855 | 1 | 855 |
VVM14985.1 | 1.28e-272 | 23 | 604 | 22 | 605 |
QXH59624.1 | 1.72e-242 | 1 | 604 | 1 | 606 |
QXI30404.1 | 5.46e-165 | 62 | 700 | 55 | 740 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3F7M_A | 5.09e-06 | 148 | 410 | 2 | 241 | Crystalstructure of apo Cuticle-Degrading Protease (ver112) from Verticillium psalliotae [Lecanicillium psalliotae] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P32823 | 6.47e-07 | 697 | 804 | 585 | 689 | Chitinase A OS=Pseudoalteromonas piscicida OX=43662 GN=chiA PE=1 SV=1 |
P9WEW5 | 1.94e-06 | 109 | 430 | 117 | 416 | Subtilisin-like serine protease Pen ch 18 OS=Penicillium rubens OX=1108849 PE=1 SV=1 |
P9WEW6 | 1.94e-06 | 109 | 430 | 117 | 416 | Subtilisin-like serine protease EN45_078720 OS=Penicillium chrysogenum OX=5076 GN=EN45_078720 PE=3 SV=1 |
Q9P8G3 | 1.94e-06 | 109 | 430 | 117 | 416 | Subtilisin-like serine protease Pen ch 18.0101 OS=Penicillium rubens OX=1108849 PE=1 SV=1 |
Q68GV9 | 3.49e-06 | 136 | 410 | 93 | 344 | Alkaline serine protease ver112 OS=Lecanicillium psalliotae OX=73499 PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000259 | 0.998999 | 0.000200 | 0.000184 | 0.000172 | 0.000154 |
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