Species | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; CAG-382; UMGS1387; | |||||||||||
CAZyme ID | MGYG000000481_01495 | |||||||||||
CAZy Family | GH95 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 5873; End: 8002 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH95 | 3 | 706 | 1.5e-235 | 0.9529085872576177 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam14498 | Glyco_hyd_65N_2 | 2.05e-54 | 4 | 245 | 1 | 233 | 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. |
COG1554 | ATH1 | 4.21e-07 | 106 | 300 | 100 | 313 | Trehalose and maltose hydrolase (possible phosphorylase) [Carbohydrate transport and metabolism]. |
pfam03636 | Glyco_hydro_65N | 0.001 | 98 | 169 | 76 | 144 | 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 |
---|---|---|---|---|---|
QYR21245.1 | 2.75e-198 | 3 | 708 | 8 | 726 |
AIQ20551.1 | 6.62e-191 | 3 | 707 | 11 | 745 |
AIQ65584.1 | 1.99e-190 | 3 | 707 | 11 | 743 |
QDH20664.1 | 5.30e-190 | 3 | 706 | 8 | 731 |
AEY65031.1 | 1.31e-188 | 4 | 707 | 5 | 726 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2RDY_A | 9.07e-151 | 3 | 708 | 4 | 739 | ChainA, BH0842 protein [Halalkalibacterium halodurans C-125],2RDY_B Chain B, BH0842 protein [Halalkalibacterium halodurans C-125] |
4UFC_A | 7.87e-144 | 3 | 703 | 23 | 723 | Crystalstructure of the GH95 enzyme BACOVA_03438 [Bacteroides ovatus],4UFC_B Crystal structure of the GH95 enzyme BACOVA_03438 [Bacteroides ovatus] |
7KMQ_A | 3.20e-131 | 3 | 706 | 42 | 742 | 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 | 2.89e-80 | 6 | 708 | 39 | 836 | 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 | 2.01e-79 | 6 | 708 | 39 | 836 | 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 | 3.70e-139 | 3 | 708 | 53 | 799 | Alpha-L-fucosidase 2 OS=Arabidopsis thaliana OX=3702 GN=FUC95A PE=1 SV=1 |
A2R797 | 1.36e-68 | 2 | 708 | 21 | 763 | Probable alpha-fucosidase A OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=afcA PE=3 SV=1 |
Q5AU81 | 1.36e-51 | 19 | 701 | 46 | 775 | 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 | 1.31e-43 | 4 | 709 | 18 | 702 | 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 |
---|---|---|---|---|---|
1.000058 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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