Species | ||||||||||||
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Lineage | Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; Borkfalkiaceae; UBA10281; | |||||||||||
CAZyme ID | MGYG000004310_01725 | |||||||||||
CAZy Family | GH95 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 706; End: 3234 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH95 | 39 | 687 | 2.9e-170 | 0.8545706371191135 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam14498 | Glyco_hyd_65N_2 | 1.97e-13 | 2 | 183 | 15 | 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. |
pfam03633 | Glyco_hydro_65C | 0.002 | 638 | 690 | 1 | 48 | Glycosyl hydrolase family 65, C-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. The C-terminal domain forms a two layered jelly roll motif. This domain is situated at the base of the catalytic domain, however its function remains unknown. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QDO70897.1 | 6.57e-183 | 1 | 721 | 60 | 788 |
QNL40018.1 | 1.91e-182 | 1 | 724 | 59 | 792 |
QDO95459.1 | 3.63e-180 | 2 | 723 | 77 | 805 |
QGH69931.1 | 1.34e-179 | 1 | 773 | 90 | 887 |
ANW96103.1 | 5.24e-157 | 1 | 815 | 61 | 880 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
7KMQ_A | 5.60e-93 | 42 | 690 | 138 | 763 | 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 | 8.34e-86 | 1 | 724 | 52 | 895 | 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 | 8.34e-86 | 1 | 724 | 52 | 895 | ChainA, Alpha-fucosidase [Bifidobacterium bifidum],2EAD_B Chain B, Alpha-fucosidase [Bifidobacterium bifidum] |
2EAE_A | 1.09e-84 | 1 | 724 | 51 | 894 | ChainA, Alpha-fucosidase [Bifidobacterium bifidum] |
2RDY_A | 3.61e-83 | 1 | 719 | 18 | 796 | ChainA, BH0842 protein [Halalkalibacterium halodurans C-125],2RDY_B Chain B, BH0842 protein [Halalkalibacterium halodurans C-125] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q8L7W8 | 1.02e-64 | 198 | 667 | 320 | 795 | Alpha-L-fucosidase 2 OS=Arabidopsis thaliana OX=3702 GN=FUC95A PE=1 SV=1 |
A2R797 | 2.50e-57 | 54 | 683 | 137 | 777 | Probable alpha-fucosidase A OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=afcA PE=3 SV=1 |
Q5AU81 | 1.86e-47 | 214 | 675 | 313 | 787 | 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 | 5.62e-35 | 41 | 679 | 118 | 719 | 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 |
---|---|---|---|---|---|
1.000028 | 0.000020 | 0.000001 | 0.000000 | 0.000000 | 0.000000 |
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