Species | CAG-510 sp900550475 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; CAG-510; CAG-510 sp900550475 | |||||||||||
CAZyme ID | MGYG000001965_00828 | |||||||||||
CAZy Family | GH53 | |||||||||||
CAZyme Description | Arabinogalactan endo-beta-1,4-galactanase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 8787; End: 9860 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH53 | 4 | 351 | 1.8e-126 | 0.9883040935672515 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG3867 | GanB | 6.01e-143 | 3 | 351 | 39 | 388 | Arabinogalactan endo-1,4-beta-galactosidase [Carbohydrate transport and metabolism]. |
pfam07745 | Glyco_hydro_53 | 1.73e-133 | 4 | 351 | 1 | 330 | Glycosyl hydrolase family 53. This domain belongs to family 53 of the glycosyl hydrolase classification. These enzymes are enzymes are endo-1,4- beta-galactanases (EC:3.2.1.89). The structure of this domain is known and has a TIM barrel fold. |
cd19008 | LGIC_ECD_GABAR_RDL-like | 0.008 | 65 | 112 | 2 | 46 | gamma-aminobutyric acid receptor subunit beta-like extracellular domain in protostomia, such as RDL (resistant to dieldrin). This family contains extracellular domain of beta-like subunits of type-A gamma-aminobutyric acid receptor (GABAAR) found in protostomia, similar to Drosophila melanogaster resistant to dieldrin (RDL) subunits. Drosophila melanogaster expresses three GABA-receptor subunit orthologs: (RDL, resistant to dieldrin; GRD, GABA/glycine-like receptor of Drosophila; LCCH3, ligand-gated chloride channel homolog 3), and may possibly form homo- and/or heteropentameric associations. GABAARs are known to be the molecular targets of a class of insecticides. The resulting pentameric receptors in this family have been shown to be activated by insect GABA-receptor agonists muscimol and CACA, and blocked by antagonists fipronil, dieldrin, and picrotoxin, but not bicuculline. GABAARs are abundant in the CNS, where their physiological role is to mediate fast inhibitory neurotransmission. In insects, this inhibitory transmission plays a crucial role in olfactory information processing. Bombyx mori includes three RDL (RD1, RD2, RD3), one LCCH3, and one GRD subunits. Its RDL1 gene has RNA-editing sites, and the RDL1 and RDL3 genes possess alternative splicing, enhancing the diversity of its GABA-receptor gene family. The three RDL subunits may have arisen from two duplication events. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QNM03636.1 | 1.76e-211 | 1 | 357 | 1 | 357 |
AEN97260.1 | 3.58e-204 | 1 | 357 | 1 | 357 |
QJS19157.1 | 9.84e-155 | 1 | 351 | 1 | 351 |
BBF43148.1 | 2.00e-139 | 1 | 348 | 1 | 348 |
AEN97298.1 | 1.29e-121 | 1 | 356 | 1 | 365 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
7OSK_A | 2.17e-90 | 1 | 351 | 48 | 388 | ChainA, Arabinogalactan endo-1,4-beta-galactosidase [Ignisphaera aggregans DSM 17230],7OSK_B Chain B, Arabinogalactan endo-1,4-beta-galactosidase [Ignisphaera aggregans DSM 17230] |
1R8L_A | 1.95e-83 | 3 | 351 | 24 | 385 | Thestructure of endo-beta-1,4-galactanase from Bacillus licheniformis [Bacillus licheniformis],1R8L_B The structure of endo-beta-1,4-galactanase from Bacillus licheniformis [Bacillus licheniformis],1UR0_A The structure of endo-beta-1,4-galactanase from Bacillus licheniformis in complex with two oligosaccharide products. [Bacillus licheniformis],1UR0_B The structure of endo-beta-1,4-galactanase from Bacillus licheniformis in complex with two oligosaccharide products. [Bacillus licheniformis],1UR4_A The structure of endo-beta-1,4-galactanase from Bacillus licheniformis in complex with two oligosaccharide products. [Bacillus licheniformis],1UR4_B The structure of endo-beta-1,4-galactanase from Bacillus licheniformis in complex with two oligosaccharide products. [Bacillus licheniformis],2CCR_A Structure of Beta-1,4-Galactanase [Bacillus licheniformis],2CCR_B Structure of Beta-1,4-Galactanase [Bacillus licheniformis],2J74_A Structure of Beta-1,4-Galactanase [Bacillus licheniformis],2J74_B Structure of Beta-1,4-Galactanase [Bacillus licheniformis] |
2GFT_A | 1.55e-82 | 3 | 351 | 24 | 385 | ChainA, Glycosyl Hydrolase Family 53 [Bacillus licheniformis],2GFT_B Chain B, Glycosyl Hydrolase Family 53 [Bacillus licheniformis] |
6GPA_A | 6.04e-52 | 3 | 306 | 7 | 286 | Beta-1,4-galactanasefrom Bacteroides thetaiotaomicron with galactose [Bacteroides thetaiotaomicron VPI-5482],6GPA_B Beta-1,4-galactanase from Bacteroides thetaiotaomicron with galactose [Bacteroides thetaiotaomicron VPI-5482] |
6GP5_A | 1.61e-51 | 3 | 306 | 43 | 322 | Beta-1,4-galactanasefrom Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482],6GP5_B Beta-1,4-galactanase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P48843 | 2.19e-88 | 3 | 310 | 6 | 314 | Uncharacterized protein in bgaB 5'region (Fragment) OS=Niallia circulans OX=1397 PE=3 SV=1 |
Q65CX5 | 2.20e-82 | 3 | 351 | 49 | 410 | Endo-beta-1,4-galactanase OS=Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46) OX=279010 GN=ganB PE=1 SV=1 |
O07013 | 6.80e-76 | 3 | 351 | 53 | 414 | Endo-beta-1,4-galactanase OS=Bacillus subtilis (strain 168) OX=224308 GN=ganB PE=1 SV=1 |
P48841 | 1.48e-51 | 3 | 352 | 27 | 363 | Arabinogalactan endo-beta-1,4-galactanase OS=Cellvibrio japonicus (strain Ueda107) OX=498211 GN=ganB PE=1 SV=1 |
Q0CTQ7 | 4.47e-50 | 5 | 308 | 19 | 316 | Probable arabinogalactan endo-beta-1,4-galactanase A OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=galA PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000057 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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