Species | Bacteroides oleiciplenus | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides oleiciplenus | |||||||||||
CAZyme ID | MGYG000001422_02350 | |||||||||||
CAZy Family | GH115 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 920869; End: 923439 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH115 | 36 | 837 | 1.2e-226 | 0.9971305595408895 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam15979 | Glyco_hydro_115 | 4.67e-176 | 179 | 523 | 1 | 334 | Glycosyl hydrolase family 115. Glyco_hydro_115 is a family of glycoside hydrolases likely to have the activity of xylan a-1,2-glucuronidase, EC:3.2.1.131, or a-(4-O-methyl)-glucuronidase EC:3.2.1.-. |
pfam17829 | GH115_C | 7.69e-15 | 716 | 851 | 32 | 170 | Gylcosyl hydrolase family 115 C-terminal domain. This domain is found at the C-terminus of glycosyl hydrolase family 115 proteins. This domain has a beta-sandwich fold. |
cd14587 | PTP-MTMR4 | 6.35e-04 | 659 | 701 | 3 | 47 | protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatase 4. Myotubularin related phosphoinositide phosphatase 4 (MTMR4), also known as FYVE domain-containing dual specificity protein phosphatase 2 (FYVE-DSP2) or zinc finger FYVE domain-containing protein 11 (ZFYVE11), is enzymatically active and contains a C-terminal FYVE domain and an N-terminal PH-GRAM domain. In general, myotubularins are a unique subgroup of protein tyrosine phosphatases that use inositol phospholipids, rather than phosphoproteins, as substrates. They dephosphorylate the D-3 position of phosphatidylinositol 3-phosphate [PI(3)P] and phosphatidylinositol 3,5-bisphosphate [PI(3,5)P2], generating phosphatidylinositol and phosphatidylinositol 5-phosphate [PI(5)P], respectively. MTMR4 localizes at the interface of early and recycling endosomes to regulate trafficking through this pathway. It plays a role in bacterial pathogenesis by stabilizing the integrity of bacteria-containing vacuoles. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
EEB22662.1 | 0.0 | 31 | 856 | 35 | 860 |
QJR78604.1 | 0.0 | 31 | 856 | 35 | 860 |
AII65956.1 | 0.0 | 31 | 856 | 35 | 860 |
QJR53583.1 | 0.0 | 31 | 856 | 35 | 860 |
QJR61620.1 | 0.0 | 31 | 856 | 35 | 860 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
5BY3_A | 1.99e-214 | 36 | 836 | 18 | 770 | Anovel family GH115 4-O-Methyl-alpha-glucuronidase, BtGH115A, with specificity for decorated arabinogalactans [Bacteroides thetaiotaomicron VPI-5482] |
4C90_A | 3.97e-88 | 35 | 663 | 41 | 640 | Evidencethat GH115 alpha-glucuronidase activity is dependent on conformational flexibility [Bacteroides ovatus],4C90_B Evidence that GH115 alpha-glucuronidase activity is dependent on conformational flexibility [Bacteroides ovatus],4C91_A Evidence that GH115 alpha-glucuronidase activity is dependent on conformational flexibility [Bacteroides ovatus],4C91_B Evidence that GH115 alpha-glucuronidase activity is dependent on conformational flexibility [Bacteroides ovatus] |
4ZMH_A | 2.73e-84 | 67 | 840 | 43 | 919 | Crystalstructure of a five-domain GH115 alpha-Glucuronidase from the Marine Bacterium Saccharophagus degradans 2-40T [Saccharophagus degradans 2-40],4ZMH_B Crystal structure of a five-domain GH115 alpha-Glucuronidase from the Marine Bacterium Saccharophagus degradans 2-40T [Saccharophagus degradans 2-40] |
7PUG_A | 1.20e-80 | 30 | 841 | 9 | 821 | ChainA, xylan alpha-1,2-glucuronidase [uncultured bacterium] |
7PXQ_A | 5.88e-80 | 30 | 841 | 8 | 820 | ChainA, xylan alpha-1,2-glucuronidase [uncultured bacterium] |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000586 | 0.998761 | 0.000184 | 0.000150 | 0.000132 | 0.000132 |
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