| Species | Paenibacillus lactis | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus; Paenibacillus lactis | |||||||||||
| CAZyme ID | MGYG000003402_01471 | |||||||||||
| CAZy Family | GH95 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 11354; End: 13834 Strand: - | |||||||||||
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH95 | 7 | 783 | 5.3e-179 | 0.9778393351800554 |
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| pfam14498 | Glyco_hyd_65N_2 | 4.17e-28 | 20 | 161 | 10 | 147 | 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 | 120 | 162 | 92 | 142 | 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 |
|---|---|---|---|---|---|
| ANY73534.1 | 0.0 | 1 | 826 | 1 | 826 |
| AYB47098.1 | 0.0 | 1 | 825 | 1 | 827 |
| ACX62422.1 | 0.0 | 19 | 825 | 1 | 808 |
| QZN78893.1 | 0.0 | 5 | 790 | 6 | 795 |
| QNK60566.1 | 0.0 | 19 | 820 | 1 | 819 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 2RDY_A | 9.98e-71 | 11 | 810 | 9 | 781 | ChainA, BH0842 protein [Halalkalibacterium halodurans C-125],2RDY_B Chain B, BH0842 protein [Halalkalibacterium halodurans C-125] |
| 4UFC_A | 2.02e-66 | 20 | 748 | 33 | 708 | Crystalstructure of the GH95 enzyme BACOVA_03438 [Bacteroides ovatus],4UFC_B Crystal structure of the GH95 enzyme BACOVA_03438 [Bacteroides ovatus] |
| 7KMQ_A | 2.40e-65 | 15 | 775 | 44 | 751 | ChainA, Glyco_hyd_65N_2 domain-containing protein [Xanthomonas citri pv. citri str. 306],7KMQ_B Chain B, Glyco_hyd_65N_2 domain-containing protein [Xanthomonas citri pv. citri str. 306] |
| 2EAB_A | 1.21e-39 | 18 | 748 | 45 | 816 | 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 | 6.66e-39 | 18 | 748 | 45 | 816 | ChainA, Alpha-fucosidase [Bifidobacterium bifidum],2EAD_B Chain B, Alpha-fucosidase [Bifidobacterium bifidum] |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| Q8L7W8 | 3.68e-79 | 20 | 760 | 63 | 792 | Alpha-L-fucosidase 2 OS=Arabidopsis thaliana OX=3702 GN=FUC95A PE=1 SV=1 |
| A2R797 | 3.36e-40 | 23 | 758 | 38 | 753 | Probable alpha-fucosidase A OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=afcA PE=3 SV=1 |
| Q5AU81 | 2.63e-37 | 27 | 761 | 47 | 776 | 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 | 2.60e-25 | 13 | 763 | 24 | 697 | 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 |
|---|---|---|---|---|---|
| 1.000053 | 0.000012 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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