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CAZyme Information: MGYG000001032_00295
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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 | ||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Eubacterium_G; | |||||||||||
| CAZyme ID | MGYG000001032_00295 | |||||||||||
| CAZy Family | GH55 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 8566; End: 11631 Strand: - | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH55 | 466 | 705 | 2.6e-60 | 0.3837837837837838 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| pfam13306 | LRR_5 | 1.92e-08 | 915 | 979 | 9 | 63 | Leucine rich repeats (6 copies). This family includes a number of leucine rich repeats. This family contains a large number of BSPA-like surface antigens from Trichomonas vaginalis. |
| sd00036 | LRR_3 | 2.85e-08 | 917 | 979 | 14 | 67 | leucine-rich repeats. A leucine-rich repeat (LRR) is a structural protein motif of 20-30 amino acids that is unusually rich in the hydrophobic amino acid leucine. The conserved eleven-residue sequence motif (LxxLxLxxN/CxL) within the LRRs corresponds to the beta-strand and adjacent loop regions, whereas the remaining parts of the repeats are variable. LRRs fold together to form a solenoid protein domain, termed leucine-rich repeat domain. Leucine-rich repeats are usually involved in protein-protein interactions. |
| sd00036 | LRR_3 | 5.69e-08 | 917 | 979 | 83 | 136 | leucine-rich repeats. A leucine-rich repeat (LRR) is a structural protein motif of 20-30 amino acids that is unusually rich in the hydrophobic amino acid leucine. The conserved eleven-residue sequence motif (LxxLxLxxN/CxL) within the LRRs corresponds to the beta-strand and adjacent loop regions, whereas the remaining parts of the repeats are variable. LRRs fold together to form a solenoid protein domain, termed leucine-rich repeat domain. Leucine-rich repeats are usually involved in protein-protein interactions. |
| sd00036 | LRR_3 | 1.99e-07 | 917 | 979 | 60 | 113 | leucine-rich repeats. A leucine-rich repeat (LRR) is a structural protein motif of 20-30 amino acids that is unusually rich in the hydrophobic amino acid leucine. The conserved eleven-residue sequence motif (LxxLxLxxN/CxL) within the LRRs corresponds to the beta-strand and adjacent loop regions, whereas the remaining parts of the repeats are variable. LRRs fold together to form a solenoid protein domain, termed leucine-rich repeat domain. Leucine-rich repeats are usually involved in protein-protein interactions. |
| sd00036 | LRR_3 | 2.46e-06 | 917 | 979 | 37 | 90 | leucine-rich repeats. A leucine-rich repeat (LRR) is a structural protein motif of 20-30 amino acids that is unusually rich in the hydrophobic amino acid leucine. The conserved eleven-residue sequence motif (LxxLxLxxN/CxL) within the LRRs corresponds to the beta-strand and adjacent loop regions, whereas the remaining parts of the repeats are variable. LRRs fold together to form a solenoid protein domain, termed leucine-rich repeat domain. Leucine-rich repeats are usually involved in protein-protein interactions. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QLY78981.1 | 8.59e-202 | 140 | 776 | 463 | 1121 |
| QLY78983.1 | 1.72e-191 | 96 | 807 | 412 | 1138 |
| QMW75525.1 | 2.54e-175 | 146 | 776 | 489 | 1159 |
| QQV06003.1 | 2.54e-175 | 146 | 776 | 489 | 1159 |
| QPS14140.1 | 2.54e-175 | 146 | 776 | 489 | 1159 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 4PEW_A | 5.93e-136 | 180 | 747 | 21 | 542 | Structureof sacteLam55A from Streptomyces sp. SirexAA-E [Streptomyces sp. SirexAA-E],4PEW_B Structure of sacteLam55A from Streptomyces sp. SirexAA-E [Streptomyces sp. SirexAA-E] |
| 4TZ1_A | 8.01e-136 | 180 | 747 | 9 | 530 | Ensemblerefinement of the E502A variant of sacteLam55A from Streptomyces sp. SirexAA-E in complex with laminaritriose [Streptomyces sp. SirexAA-E],4TZ3_A Ensemble refinement of the E502A variant of sacteLam55A from Streptomyces sp. SirexAA-E in complex with laminaritetraose [Streptomyces sp. SirexAA-E],4TZ5_A Ensemble refinement of the E502A variant of sacteLam55A from Streptomyces sp. SirexAA-E in complex with laminarihexaose [Streptomyces sp. SirexAA-E],4TZ5_B Ensemble refinement of the E502A variant of sacteLam55A from Streptomyces sp. SirexAA-E in complex with laminarihexaose [Streptomyces sp. SirexAA-E] |
| 4TYV_A | 8.53e-136 | 180 | 747 | 11 | 532 | Ensemblerefinement of the E502A variant of sacteLam55A from Streptomyces sp. SirexAA-E in complex with glucose [Streptomyces sp. SirexAA-E],4TYV_B Ensemble refinement of the E502A variant of sacteLam55A from Streptomyces sp. SirexAA-E in complex with glucose [Streptomyces sp. SirexAA-E] |
| 4PEX_A | 1.17e-135 | 180 | 747 | 21 | 542 | Structureof the E502A variant of sacteLam55A from Streptomyces sp. SirexAA-E in complex with glucose [Streptomyces sp. SirexAA-E],4PEX_B Structure of the E502A variant of sacteLam55A from Streptomyces sp. SirexAA-E in complex with glucose [Streptomyces sp. SirexAA-E],4PEY_A Structure of the E502A variant of sacteLam55A from Streptomyces sp. SirexAA-E in complex with laminaritriose [Streptomyces sp. SirexAA-E],4PEZ_A Structure of the E502A variant of sacteLam55A from Streptomyces sp. SirexAA-E in complex with laminaritetraose [Streptomyces sp. SirexAA-E],4PF0_A Structure of the E502A variant of sacteLam55A from Streptomyces sp. SirexAA-E in complex with laminarihexaose [Streptomyces sp. SirexAA-E],4PF0_B Structure of the E502A variant of sacteLam55A from Streptomyces sp. SirexAA-E in complex with laminarihexaose [Streptomyces sp. SirexAA-E] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| G2NFJ9 | 3.27e-135 | 180 | 747 | 65 | 586 | Exo-beta-1,3-glucanase OS=Streptomyces sp. (strain SirexAA-E / ActE) OX=862751 GN=SACTE_4363 PE=1 SV=1 |
SignalP and Lipop Annotations help
This protein is predicted as LIPO
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 0.000001 | 0.000353 | 0.999684 | 0.000000 | 0.000000 | 0.000000 |