Species | Parabacteroides sp000436495 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae; Parabacteroides; Parabacteroides sp000436495 | |||||||||||
CAZyme ID | MGYG000002218_00720 | |||||||||||
CAZy Family | GH95 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location | Start: 5555; End: 8008 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH95 | 32 | 782 | 2.1e-284 | 0.9889196675900277 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam14498 | Glyco_hyd_65N_2 | 7.56e-68 | 39 | 285 | 3 | 231 | 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 | 155 | 276 | 90 | 219 | 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 |
---|---|---|---|---|---|
BBK92411.1 | 0.0 | 16 | 817 | 9 | 811 |
QUR47708.1 | 0.0 | 16 | 817 | 7 | 809 |
QIX67531.1 | 0.0 | 16 | 817 | 7 | 809 |
QUT50631.1 | 0.0 | 15 | 817 | 10 | 809 |
QJE29167.1 | 0.0 | 13 | 817 | 7 | 812 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
4UFC_A | 1.36e-181 | 15 | 776 | 10 | 742 | Crystalstructure of the GH95 enzyme BACOVA_03438 [Bacteroides ovatus],4UFC_B Crystal structure of the GH95 enzyme BACOVA_03438 [Bacteroides ovatus] |
7KMQ_A | 8.83e-179 | 29 | 775 | 35 | 757 | 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] |
2RDY_A | 6.59e-160 | 39 | 768 | 7 | 745 | ChainA, BH0842 protein [Halalkalibacterium halodurans C-125],2RDY_B Chain B, BH0842 protein [Halalkalibacterium halodurans C-125] |
2EAB_A | 6.12e-98 | 31 | 812 | 32 | 886 | 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 | 4.41e-97 | 31 | 812 | 32 | 886 | 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 | 5.85e-155 | 39 | 758 | 56 | 795 | Alpha-L-fucosidase 2 OS=Arabidopsis thaliana OX=3702 GN=FUC95A PE=1 SV=1 |
A2R797 | 2.34e-103 | 50 | 760 | 39 | 761 | Probable alpha-fucosidase A OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=afcA PE=3 SV=1 |
Q5AU81 | 1.05e-85 | 52 | 786 | 46 | 807 | 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 | 6.46e-66 | 43 | 761 | 23 | 701 | 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 |
---|---|---|---|---|---|
0.000372 | 0.107087 | 0.892359 | 0.000046 | 0.000068 | 0.000061 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.