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CAZyme Information: MGYG000003208_03014

You are here: Home > Sequence: MGYG000003208_03014

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Pseudomonas_E extremaustralis
Lineage Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae; Pseudomonas_E; Pseudomonas_E extremaustralis
CAZyme ID MGYG000003208_03014
CAZy Family CBM73
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
856 91438.86 6.8152
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003208 6254364 MAG United States North America
Gene Location Start: 66355;  End: 68925  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003208_03014.

CDD Domains      download full data without filtering help

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.

CAZyme Hits      help

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

PDB Hits      download full data without filtering help

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]

Swiss-Prot Hits      download full data without filtering help

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

SignalP and Lipop Annotations help

This protein is predicted as SP

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

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003208_03014.