| Species | Robinsoniella sp900539655 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Robinsoniella; Robinsoniella sp900539655 | |||||||||||
| CAZyme ID | MGYG000000287_03926 | |||||||||||
| CAZy Family | GH29 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 1755; End: 3086 Strand: + | |||||||||||
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH29 | 4 | 353 | 1.9e-113 | 0.9219653179190751 |
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| smart00812 | Alpha_L_fucos | 4.60e-132 | 5 | 396 | 7 | 384 | Alpha-L-fucosidase. O-Glycosyl hydrolases (EC 3.2.1.-) are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families. This classification is available on the CAZy (CArbohydrate-Active EnZymes) web site. Because the fold of proteins is better conserved than their sequences, some of the families can be grouped in 'clans'. Family 29 encompasses alpha-L-fucosidases, which is a lysosomal enzyme responsible for hydrolyzing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins. Deficiency of alpha-L-fucosidase results in the lysosomal storage disease fucosidosis. |
| pfam01120 | Alpha_L_fucos | 7.74e-123 | 5 | 349 | 6 | 333 | Alpha-L-fucosidase. |
| COG3669 | AfuC | 2.11e-82 | 31 | 384 | 1 | 352 | Alpha-L-fucosidase [Carbohydrate transport and metabolism]. |
| pfam14871 | GHL6 | 0.001 | 105 | 216 | 2 | 128 | Hypothetical glycosyl hydrolase 6. GHL6 is a family of hypothetical glycoside hydrolases. |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QCU01968.1 | 2.82e-213 | 3 | 436 | 4 | 436 |
| CBL20743.1 | 6.59e-212 | 5 | 436 | 6 | 436 |
| QLB22199.1 | 2.10e-206 | 2 | 442 | 3 | 441 |
| QSX10742.1 | 3.32e-206 | 2 | 442 | 6 | 444 |
| QSX14984.1 | 6.69e-206 | 2 | 442 | 6 | 444 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 1ODU_A | 1.03e-148 | 1 | 398 | 4 | 403 | CrystalStructure Of Thermotoga Maritima Alpha-Fucosidase In Complex With Fucose [Thermotoga maritima MSB8],1ODU_B Crystal Structure Of Thermotoga Maritima Alpha-Fucosidase In Complex With Fucose [Thermotoga maritima MSB8] |
| 2ZWY_A | 1.26e-148 | 1 | 398 | 4 | 403 | alpha-L-fucosidase[Thermotoga maritima],2ZWY_B alpha-L-fucosidase [Thermotoga maritima],2ZWZ_A alpha-L-fucosidase complexed with inhibitor, Core1 [Thermotoga maritima],2ZWZ_B alpha-L-fucosidase complexed with inhibitor, Core1 [Thermotoga maritima],2ZX5_A alpha-L-fucosidase complexed with inhibitor, F10 [Thermotoga maritima],2ZX5_B alpha-L-fucosidase complexed with inhibitor, F10 [Thermotoga maritima],2ZX6_A alpha-L-fucosidase complexed with inhibitor, F10-1C [Thermotoga maritima],2ZX6_B alpha-L-fucosidase complexed with inhibitor, F10-1C [Thermotoga maritima],2ZX7_A alpha-L-fucosidase complexed with inhibitor, F10-2C [Thermotoga maritima],2ZX7_B alpha-L-fucosidase complexed with inhibitor, F10-2C [Thermotoga maritima],2ZX8_A alpha-L-fucosidase complexed with inhibitor, F10-2C-O [Thermotoga maritima],2ZX8_B alpha-L-fucosidase complexed with inhibitor, F10-2C-O [Thermotoga maritima],2ZX9_A alpha-L-fucosidase complexed with inhibitor, B4 [Thermotoga maritima],2ZX9_B alpha-L-fucosidase complexed with inhibitor, B4 [Thermotoga maritima],2ZXA_A alpha-L-fucosidase complexed with inhibitor, FNJ-acetyl [Thermotoga maritima],2ZXA_B alpha-L-fucosidase complexed with inhibitor, FNJ-acetyl [Thermotoga maritima],2ZXB_A alpha-L-fucosidase complexed with inhibitor, ph-6FNJ [Thermotoga maritima],2ZXB_B alpha-L-fucosidase complexed with inhibitor, ph-6FNJ [Thermotoga maritima],2ZXD_A alpha-L-fucosidase complexed with inhibitor, iso-6FNJ [Thermotoga maritima],2ZXD_B alpha-L-fucosidase complexed with inhibitor, iso-6FNJ [Thermotoga maritima] |
| 1HL8_A | 2.06e-148 | 1 | 398 | 4 | 403 | CrystalStructure Of Thermotoga Maritima Alpha-Fucosidase [Thermotoga maritima MSB8],1HL8_B Crystal Structure Of Thermotoga Maritima Alpha-Fucosidase [Thermotoga maritima MSB8],1HL9_A Crystal Structure Of Thermotoga Maritima Alpha-Fucosidase In Complex With A Mechanism Based Inhibitor [Thermotoga maritima MSB8],1HL9_B Crystal Structure Of Thermotoga Maritima Alpha-Fucosidase In Complex With A Mechanism Based Inhibitor [Thermotoga maritima MSB8] |
| 2WSP_A | 1.18e-147 | 1 | 398 | 4 | 403 | Thermotogamaritima alpha-L-fucosynthase, TmD224G, in complex with alpha-L-Fuc-(1-2)-beta-L-Fuc-N3 [Thermotoga maritima MSB8],2WSP_B Thermotoga maritima alpha-L-fucosynthase, TmD224G, in complex with alpha-L-Fuc-(1-2)-beta-L-Fuc-N3 [Thermotoga maritima MSB8] |
| 7LJJ_A | 7.03e-60 | 13 | 395 | 52 | 447 | ChainA, Exo-alpha-L-galactosidase [Phocaeicola plebeius DSM 17135],7LK7_A Chain A, Exo-alpha-L-galactosidase [Phocaeicola plebeius DSM 17135] |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P10901 | 2.22e-70 | 5 | 354 | 21 | 363 | Alpha-L-fucosidase OS=Dictyostelium discoideum OX=44689 GN=alfA PE=3 SV=1 |
| Q5RFI5 | 2.19e-67 | 5 | 378 | 32 | 390 | Plasma alpha-L-fucosidase OS=Pongo abelii OX=9601 GN=FUCA2 PE=2 SV=1 |
| C3YWU0 | 1.12e-66 | 5 | 396 | 18 | 396 | Alpha-L-fucosidase OS=Branchiostoma floridae OX=7739 GN=BRAFLDRAFT_56888 PE=3 SV=2 |
| Q9BTY2 | 9.55e-66 | 5 | 378 | 34 | 392 | Plasma alpha-L-fucosidase OS=Homo sapiens OX=9606 GN=FUCA2 PE=1 SV=2 |
| P17164 | 9.65e-64 | 5 | 389 | 33 | 401 | Tissue alpha-L-fucosidase OS=Rattus norvegicus OX=10116 GN=Fuca1 PE=1 SV=1 |
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 1.000022 | 0.000026 | 0.000001 | 0.000000 | 0.000000 | 0.000000 |
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