Species | ||||||||||||
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Lineage | Bacteria; Firmicutes_A; Clostridia; TANB77; CAG-508; CAG-452; | |||||||||||
CAZyme ID | MGYG000000521_01000 | |||||||||||
CAZy Family | GT2 | |||||||||||
CAZyme Description | Tyrocidine synthase 3 | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 16200; End: 23621 Strand: - |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
PRK05691 | PRK05691 | 0.0 | 8 | 2055 | 682 | 2772 | peptide synthase; Validated |
PRK12316 | PRK12316 | 0.0 | 1052 | 2055 | 53 | 1081 | peptide synthase; Provisional |
PRK12316 | PRK12316 | 0.0 | 124 | 2055 | 1684 | 3619 | peptide synthase; Provisional |
PRK12467 | PRK12467 | 0.0 | 4 | 2055 | 52 | 2160 | peptide synthase; Provisional |
cd05930 | A_NRPS | 7.77e-171 | 467 | 943 | 1 | 444 | The adenylation domain of nonribosomal peptide synthetases (NRPS). The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QND46664.1 | 2.96e-218 | 127 | 2028 | 692 | 2631 |
BAY30132.1 | 2.17e-155 | 948 | 2055 | 2134 | 3291 |
BAZ00088.1 | 4.70e-154 | 954 | 2055 | 2137 | 3289 |
BAZ75991.1 | 4.70e-154 | 954 | 2055 | 2137 | 3289 |
BAY90071.1 | 7.64e-153 | 954 | 2055 | 2128 | 3280 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6MFZ_A | 1.27e-260 | 450 | 2055 | 202 | 1794 | Crystalstructure of dimodular LgrA in a condensation state [Brevibacillus parabrevis],6MFZ_B Crystal structure of dimodular LgrA in a condensation state [Brevibacillus parabrevis] |
6MFY_A | 1.99e-251 | 450 | 1975 | 202 | 1714 | Crystalstructure of a 5-domain construct of LgrA in the substrate donation state [Brevibacillus parabrevis],6MG0_A Crystal structure of a 5-domain construct of LgrA in the thiolation state [Brevibacillus parabrevis],6MG0_B Crystal structure of a 5-domain construct of LgrA in the thiolation state [Brevibacillus parabrevis] |
6MFW_A | 8.62e-163 | 450 | 1477 | 202 | 1205 | Crystalstructure of a 4-domain construct of LgrA in the substrate donation state [Brevibacillus parabrevis] |
6MFX_A | 2.98e-162 | 450 | 1477 | 202 | 1205 | Crystalstructure of a 4-domain construct of a mutant of LgrA in the substrate donation state [Brevibacillus parabrevis] |
5U89_A | 1.00e-157 | 433 | 1482 | 5 | 1071 | Crystalstructure of a cross-module fragment from the dimodular NRPS DhbF [Geobacillus sp. Y4.1MC1] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P27206 | 0.0 | 2 | 2071 | 6 | 2099 | Surfactin synthase subunit 1 OS=Bacillus subtilis (strain 168) OX=224308 GN=srfAA PE=1 SV=4 |
P0C063 | 0.0 | 2 | 2070 | 1062 | 3131 | Gramicidin S synthase 2 OS=Aneurinibacillus migulanus OX=47500 GN=grsB PE=3 SV=2 |
P0C064 | 0.0 | 2 | 2070 | 1062 | 3130 | Gramicidin S synthase 2 OS=Brevibacillus brevis OX=1393 GN=grsB PE=1 SV=2 |
O30409 | 0.0 | 2 | 2070 | 1056 | 3130 | Tyrocidine synthase 3 OS=Brevibacillus parabrevis OX=54914 GN=tycC PE=1 SV=1 |
P39845 | 0.0 | 2 | 2054 | 6 | 2073 | Plipastatin synthase subunit A OS=Bacillus subtilis (strain 168) OX=224308 GN=ppsA PE=1 SV=2 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000064 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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