Species | Paenibacillus amylolyticus | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus; Paenibacillus amylolyticus | |||||||||||
CAZyme ID | MGYG000003072_01851 | |||||||||||
CAZy Family | GH29 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 103572; End: 105032 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH29 | 8 | 375 | 3.6e-113 | 0.9508670520231214 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
smart00812 | Alpha_L_fucos | 1.10e-144 | 14 | 434 | 2 | 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 | 2.54e-122 | 16 | 371 | 3 | 333 | Alpha-L-fucosidase. |
COG3669 | AfuC | 1.23e-107 | 45 | 427 | 1 | 373 | Alpha-L-fucosidase [Carbohydrate transport and metabolism]. |
pfam16757 | Fucosidase_C | 1.95e-05 | 402 | 469 | 4 | 70 | Alpha-L-fucosidase C-terminal domain. The C-terminal domain of Structure 1hl8 is constructed of eight anti-parallel-strands packed into two-sheets of five and three strands, respectively, forming a two-layer-sandwich containing a Greek key motif. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
APO45663.1 | 0.0 | 1 | 486 | 1 | 486 |
QZN74049.1 | 0.0 | 1 | 486 | 1 | 485 |
QLG42953.1 | 0.0 | 1 | 486 | 1 | 485 |
QOS78812.1 | 0.0 | 1 | 486 | 1 | 485 |
QKS54997.1 | 0.0 | 1 | 486 | 1 | 485 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
7LJJ_A | 2.06e-132 | 6 | 485 | 27 | 510 | ChainA, Exo-alpha-L-galactosidase [Phocaeicola plebeius DSM 17135],7LK7_A Chain A, Exo-alpha-L-galactosidase [Phocaeicola plebeius DSM 17135] |
7LNP_A | 1.16e-131 | 6 | 485 | 27 | 510 | ChainA, Exo-alpha-L-galactosidase [Phocaeicola plebeius DSM 17135],7LNP_C Chain C, Exo-alpha-L-galactosidase [Phocaeicola plebeius DSM 17135],7LNP_D Chain D, Exo-alpha-L-galactosidase [Phocaeicola plebeius DSM 17135],7LNP_E Chain E, Exo-alpha-L-galactosidase [Phocaeicola plebeius DSM 17135] |
4NI3_A | 1.11e-87 | 17 | 469 | 5 | 474 | ChainA, Alpha-fucosidase GH29 [Fusarium graminearum],4NI3_B Chain B, Alpha-fucosidase GH29 [Fusarium graminearum],4PSP_A Chain A, Alpha-fucosidase GH29 [Fusarium graminearum],4PSP_B Chain B, Alpha-fucosidase GH29 [Fusarium graminearum],4PSR_A Chain A, Alpha-fucosidase GH29 [Fusarium graminearum],4PSR_B Chain B, Alpha-fucosidase GH29 [Fusarium graminearum] |
1ODU_A | 1.57e-68 | 18 | 434 | 7 | 401 | 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 | 1.83e-68 | 18 | 434 | 7 | 401 | 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] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P17164 | 1.32e-59 | 19 | 484 | 33 | 451 | Tissue alpha-L-fucosidase OS=Rattus norvegicus OX=10116 GN=Fuca1 PE=1 SV=1 |
Q99LJ1 | 1.60e-57 | 18 | 484 | 22 | 441 | Tissue alpha-L-fucosidase OS=Mus musculus OX=10090 GN=Fuca1 PE=1 SV=1 |
P48300 | 1.14e-56 | 18 | 468 | 36 | 441 | Tissue alpha-L-fucosidase OS=Canis lupus familiaris OX=9615 GN=FUCA1 PE=2 SV=1 |
P04066 | 4.80e-53 | 18 | 464 | 36 | 437 | Tissue alpha-L-fucosidase OS=Homo sapiens OX=9606 GN=FUCA1 PE=1 SV=4 |
Q60HF8 | 1.89e-52 | 18 | 433 | 38 | 414 | Tissue alpha-L-fucosidase OS=Macaca fascicularis OX=9541 GN=FUCA1 PE=2 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.999997 | 0.000027 | 0.000003 | 0.000000 | 0.000000 | 0.000000 |
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