Species | HGM04593 sp900770655 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; HGM04593; HGM04593 sp900770655 | |||||||||||
CAZyme ID | MGYG000003607_00277 | |||||||||||
CAZy Family | GH35 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 22147; End: 24438 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH35 | 26 | 336 | 1.3e-115 | 0.993485342019544 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam01301 | Glyco_hydro_35 | 1.27e-131 | 26 | 335 | 2 | 315 | Glycosyl hydrolases family 35. |
PLN03059 | PLN03059 | 1.41e-59 | 26 | 589 | 37 | 731 | beta-galactosidase; Provisional |
COG1874 | GanA | 2.11e-45 | 23 | 577 | 4 | 589 | Beta-galactosidase GanA [Carbohydrate transport and metabolism]. |
pfam02449 | Glyco_hydro_42 | 6.65e-12 | 42 | 175 | 3 | 139 | Beta-galactosidase. This group of beta-galactosidase enzymes belong to the glycosyl hydrolase 42 family. The enzyme catalyzes the hydrolysis of terminal, non-reducing terminal beta-D-galactosidase residues. |
pfam00754 | F5_F8_type_C | 3.38e-06 | 685 | 755 | 4 | 70 | F5/8 type C domain. This domain is also known as the discoidin (DS) domain family. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
EDO09322.1 | 0.0 | 3 | 763 | 16 | 777 |
QRQ59141.1 | 0.0 | 3 | 763 | 14 | 775 |
ALJ49196.1 | 0.0 | 3 | 763 | 14 | 775 |
SCV08614.1 | 0.0 | 3 | 763 | 16 | 777 |
QRP57237.1 | 0.0 | 3 | 763 | 14 | 775 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6EON_A | 3.66e-185 | 1 | 760 | 9 | 777 | GalactanaseBT0290 [Bacteroides thetaiotaomicron VPI-5482] |
4MAD_A | 6.72e-148 | 23 | 597 | 21 | 596 | ChainA, Beta-galactosidase [Niallia circulans],4MAD_B Chain B, Beta-galactosidase [Niallia circulans] |
3D3A_A | 1.95e-147 | 16 | 596 | 5 | 591 | Crystalstructure of a beta-galactosidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482] |
7KDV_A | 2.34e-122 | 16 | 595 | 13 | 630 | ChainA, Beta-galactosidase [Mus musculus],7KDV_C Chain C, Beta-galactosidase [Mus musculus],7KDV_E Chain E, Beta-galactosidase [Mus musculus],7KDV_G Chain G, Beta-galactosidase [Mus musculus],7KDV_I Chain I, Beta-galactosidase [Mus musculus],7KDV_K Chain K, Beta-galactosidase [Mus musculus] |
3THC_A | 1.56e-114 | 19 | 633 | 9 | 650 | Crystalstructure of human beta-galactosidase in complex with galactose [Homo sapiens],3THC_B Crystal structure of human beta-galactosidase in complex with galactose [Homo sapiens],3THC_C Crystal structure of human beta-galactosidase in complex with galactose [Homo sapiens],3THC_D Crystal structure of human beta-galactosidase in complex with galactose [Homo sapiens],3THD_A Crystal structure of human beta-galactosidase in complex with 1-deoxygalactonojirimycin [Homo sapiens],3THD_B Crystal structure of human beta-galactosidase in complex with 1-deoxygalactonojirimycin [Homo sapiens],3THD_C Crystal structure of human beta-galactosidase in complex with 1-deoxygalactonojirimycin [Homo sapiens],3THD_D Crystal structure of human beta-galactosidase in complex with 1-deoxygalactonojirimycin [Homo sapiens] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P48982 | 1.12e-138 | 1 | 561 | 9 | 573 | Beta-galactosidase OS=Xanthomonas manihotis OX=43353 GN=bga PE=1 SV=1 |
P23780 | 2.92e-121 | 2 | 595 | 12 | 647 | Beta-galactosidase OS=Mus musculus OX=10090 GN=Glb1 PE=1 SV=1 |
O19015 | 2.29e-119 | 2 | 595 | 12 | 647 | Beta-galactosidase OS=Felis catus OX=9685 GN=GLB1 PE=2 SV=1 |
Q58D55 | 1.58e-118 | 2 | 603 | 10 | 652 | Beta-galactosidase OS=Bos taurus OX=9913 GN=GLB1 PE=2 SV=1 |
Q9TRY9 | 3.37e-118 | 1 | 594 | 17 | 645 | Beta-galactosidase OS=Canis lupus familiaris OX=9615 GN=GLB1 PE=1 SV=3 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000000 | 0.000002 | 1.000051 | 0.000000 | 0.000000 | 0.000000 |
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