Species | Prevotella sp900553155 | |||||||||||
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Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900553155 | |||||||||||
CAZyme ID | MGYG000004758_00819 | |||||||||||
CAZy Family | GH128 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 28964; End: 31756 Strand: + |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam11790 | Glyco_hydro_cc | 2.27e-20 | 221 | 431 | 19 | 235 | Glycosyl hydrolase catalytic core. This family is probably a glycosyl hydrolase, and is conserved in fungi and some Proteobacteria. The pombe member is annotated as being from IPR013781. |
pfam09458 | H_lectin | 0.002 | 673 | 736 | 5 | 67 | H-type lectin domain. The H-type lectin domain is a unit of six beta chains, combined into a homo-hexamer. It is involved in self/non-self recognition of cells, through binding with carbohydrates. It is sometimes found in association with the F5_F8_type_C domain pfam00754. |
cd00063 | FN3 | 0.008 | 455 | 532 | 3 | 77 | Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AGB28806.1 | 4.04e-152 | 1 | 557 | 12 | 572 |
QIM09904.1 | 3.48e-114 | 16 | 564 | 17 | 559 |
ASB49856.1 | 3.91e-108 | 30 | 850 | 62 | 849 |
QOG04727.1 | 3.00e-72 | 28 | 448 | 561 | 1007 |
AWK06263.1 | 9.89e-72 | 28 | 448 | 561 | 1007 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6UAQ_A | 5.71e-14 | 263 | 435 | 91 | 252 | Crystalstructure of a GH128 (subgroup I) endo-beta-1,3-glucanase from Amycolatopsis mediterranei (AmGH128_I) [Amycolatopsis mediterranei],6UAR_A Crystal structure of a GH128 (subgroup I) endo-beta-1,3-glucanase from Amycolatopsis mediterranei (AmGH128_I) in complex with laminaritriose [Amycolatopsis mediterranei] |
6UAT_A | 1.40e-13 | 277 | 435 | 102 | 252 | Crystalstructure of a GH128 (subgroup I) endo-beta-1,3-glucanase (E102A mutant) from Amycolatopsis mediterranei (AmGH128_I) in complex with laminaripentaose [Amycolatopsis mediterranei],6UAU_A Crystal structure of a GH128 (subgroup I) endo-beta-1,3-glucanase (E102A mutant) from Amycolatopsis mediterranei (AmGH128_I) in complex with laminaritriose and laminaribiose [Amycolatopsis mediterranei] |
6UFL_A | 1.40e-13 | 263 | 435 | 91 | 252 | Crystalstructure of a GH128 (subgroup I) endo-beta-1,3-glucanase (E199Q mutant) from Amycolatopsis mediterranei (AmGH128_I) in the complex with laminarihexaose [Amycolatopsis mediterranei],6UFZ_A Crystal structure of a GH128 (subgroup I) endo-beta-1,3-glucanase (E199Q mutant) from Amycolatopsis mediterranei (AmGH128_I) [Amycolatopsis mediterranei] |
6UAS_A | 3.43e-13 | 263 | 435 | 91 | 252 | Crystalstructure of a GH128 (subgroup I) endo-beta-1,3-glucanase (E199A mutant) from Amycolatopsis mediterranei (AmGH128_I) in complex with laminaripentaose [Amycolatopsis mediterranei] |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.590026 | 0.408672 | 0.000604 | 0.000305 | 0.000186 | 0.000209 |
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