Species | Victivallis vadensis | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Verrucomicrobiota; Lentisphaeria; Victivallales; Victivallaceae; Victivallis; Victivallis vadensis | |||||||||||
CAZyme ID | MGYG000002473_01630 | |||||||||||
CAZy Family | GH39 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 8804; End: 12736 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH39 | 653 | 927 | 2.8e-31 | 0.6890951276102089 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd09621 | CBM9_like_5 | 2.96e-66 | 1123 | 1309 | 1 | 188 | DOMON-like type 9 carbohydrate binding module. Family 9 carbohydrate-binding modules (CBM9) play a role in the microbial degradation of cellulose and hemicellulose (materials found in plants). The domain has previously been called cellulose-binding domain. The polysaccharide binding sites of CBMs with available 3D structure have been found to be either flat surfaces with interactions formed by predominantly aromatic residues (tryptophan and tyrosine), or extended shallow grooves. CBM9 domains found in this uncharacterized heterogeneous subfamily are often located at the C-terminus of longer proteins and may co-occur with various other functional domains such as glycosyl hydrolases. The CBM9 module in these architectures may be involved in binding to carbohydrates. |
COG3693 | XynA | 1.71e-07 | 647 | 797 | 69 | 212 | Endo-1,4-beta-xylanase, GH35 family [Carbohydrate transport and metabolism]. |
smart00633 | Glyco_10 | 1.86e-07 | 647 | 765 | 3 | 122 | Glycosyl hydrolase family 10. |
cd09619 | CBM9_like_4 | 3.40e-07 | 1147 | 1294 | 29 | 175 | DOMON-like type 9 carbohydrate binding module. Family 9 carbohydrate-binding modules (CBM9) play a role in the microbial degradation of cellulose and hemicellulose (materials found in plants). The domain has previously been called cellulose-binding domain. The polysaccharide binding sites of CBMs with available 3D structure have been found to be either flat surfaces with interactions formed by predominantly aromatic residues (tryptophan and tyrosine), or extended shallow grooves. CBM9 domains found in this uncharacterized heterogeneous subfamily are often located at the C-terminus of longer proteins and may co-occur with various other domains. |
pfam00331 | Glyco_hydro_10 | 3.47e-07 | 647 | 735 | 46 | 128 | Glycosyl hydrolase family 10. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AVM47149.1 | 0.0 | 1 | 1310 | 1 | 1307 |
AVM46276.1 | 0.0 | 198 | 1310 | 18 | 1137 |
AVM44759.1 | 2.16e-207 | 371 | 1310 | 40 | 965 |
AHF94342.1 | 6.51e-169 | 458 | 1310 | 177 | 1033 |
AHF90198.1 | 9.24e-167 | 206 | 1309 | 44 | 1005 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
5JVK_A | 3.53e-21 | 725 | 993 | 214 | 496 | Structuralinsights into a family 39 glycoside hydrolase from the gut symbiont Bacteroides cellulosilyticus WH2. [Bacteroides cellulosilyticus],5JVK_B Structural insights into a family 39 glycoside hydrolase from the gut symbiont Bacteroides cellulosilyticus WH2. [Bacteroides cellulosilyticus],5JVK_C Structural insights into a family 39 glycoside hydrolase from the gut symbiont Bacteroides cellulosilyticus WH2. [Bacteroides cellulosilyticus] |
4ZN2_A | 1.18e-06 | 637 | 902 | 46 | 322 | Glycosylhydrolase from Pseudomonas aeruginosa [Pseudomonas aeruginosa PAO1],4ZN2_B Glycosyl hydrolase from Pseudomonas aeruginosa [Pseudomonas aeruginosa PAO1],4ZN2_C Glycosyl hydrolase from Pseudomonas aeruginosa [Pseudomonas aeruginosa PAO1],4ZN2_D Glycosyl hydrolase from Pseudomonas aeruginosa [Pseudomonas aeruginosa PAO1] |
5BX9_A | 1.18e-06 | 637 | 902 | 46 | 322 | Structureof PslG from Pseudomonas aeruginosa [Pseudomonas aeruginosa PAO1],5BXA_A Structure of PslG from Pseudomonas aeruginosa in complex with mannose [Pseudomonas aeruginosa PAO1] |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.001345 | 0.997588 | 0.000247 | 0.000344 | 0.000234 | 0.000204 |
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