| Species | NSJ-32 sp014384895 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; UBA1390; NSJ-32; NSJ-32 sp014384895 | |||||||||||
| CAZyme ID | MGYG000003214_03809 | |||||||||||
| CAZy Family | GH95 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 4651; End: 7026 Strand: - | |||||||||||
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH95 | 75 | 753 | 3.4e-201 | 0.8573407202216067 |
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| pfam14498 | Glyco_hyd_65N_2 | 1.36e-39 | 6 | 226 | 1 | 232 | Glycosyl hydrolase family 65, N-terminal domain. This domain represents a domain found to the N-terminus of the glycosyl hydrolase 65 family catalytic domain. |
| pfam03636 | Glyco_hydro_65N | 0.002 | 40 | 132 | 19 | 139 | Glycosyl hydrolase family 65, N-terminal domain. This family of glycosyl hydrolases contains vacuolar acid trehalase and maltose phosphorylase.Maltose phosphorylase (MP) is a dimeric enzyme that catalyzes the conversion of maltose and inorganic phosphate into beta-D-glucose-1-phosphate and glucose. This domain is believed to be essential for catalytic activity although its precise function remains unknown. |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QDO95459.1 | 7.23e-249 | 2 | 786 | 40 | 803 |
| QNL40018.1 | 1.67e-246 | 2 | 786 | 24 | 789 |
| QGH69931.1 | 1.14e-242 | 4 | 788 | 54 | 834 |
| QDO70897.1 | 2.73e-242 | 2 | 790 | 24 | 792 |
| QBN17887.1 | 2.08e-215 | 30 | 789 | 51 | 805 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 2RDY_A | 1.00e-113 | 37 | 786 | 17 | 787 | ChainA, BH0842 protein [Halalkalibacterium halodurans C-125],2RDY_B Chain B, BH0842 protein [Halalkalibacterium halodurans C-125] |
| 2EAB_A | 1.15e-104 | 6 | 788 | 20 | 894 | Crystalstructure of 1,2-a-L-fucosidase from Bifidobacterium bifidum (apo form) [Bifidobacterium bifidum],2EAB_B Crystal structure of 1,2-a-L-fucosidase from Bifidobacterium bifidum (apo form) [Bifidobacterium bifidum],2EAC_A Crystal structure of 1,2-a-L-fucosidase from Bifidobacterium bifidum in complex with deoxyfuconojirimycin [Bifidobacterium bifidum],2EAC_B Crystal structure of 1,2-a-L-fucosidase from Bifidobacterium bifidum in complex with deoxyfuconojirimycin [Bifidobacterium bifidum] |
| 2EAD_A | 8.42e-104 | 6 | 788 | 20 | 894 | ChainA, Alpha-fucosidase [Bifidobacterium bifidum],2EAD_B Chain B, Alpha-fucosidase [Bifidobacterium bifidum] |
| 2EAE_A | 1.60e-103 | 6 | 788 | 19 | 893 | ChainA, Alpha-fucosidase [Bifidobacterium bifidum] |
| 4UFC_A | 1.89e-102 | 34 | 762 | 31 | 759 | Crystalstructure of the GH95 enzyme BACOVA_03438 [Bacteroides ovatus],4UFC_B Crystal structure of the GH95 enzyme BACOVA_03438 [Bacteroides ovatus] |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| Q8L7W8 | 1.54e-83 | 37 | 753 | 66 | 816 | Alpha-L-fucosidase 2 OS=Arabidopsis thaliana OX=3702 GN=FUC95A PE=1 SV=1 |
| A2R797 | 3.77e-63 | 15 | 731 | 80 | 758 | Probable alpha-fucosidase A OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=afcA PE=3 SV=1 |
| Q5AU81 | 3.00e-55 | 40 | 751 | 46 | 798 | Alpha-fucosidase A OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=afcA PE=1 SV=1 |
| Q2USL3 | 8.79e-43 | 13 | 731 | 44 | 696 | Probable alpha-fucosidase A OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=afcA PE=3 SV=2 |
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 1.000059 | 0.000005 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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