| Species | Paenibacillus_A senegalimassiliensis | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_A; Paenibacillus_A senegalimassiliensis | |||||||||||
| CAZyme ID | MGYG000001526_02544 | |||||||||||
| CAZy Family | GH93 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
|
|||||||||||
| Genome Property |
|
|||||||||||
| Gene Location | Start: 581461; End: 583611 Strand: + | |||||||||||
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH93 | 60 | 356 | 1.5e-76 | 0.9869706840390879 |
| CBM66 | 387 | 542 | 1.9e-32 | 0.9870967741935484 |
| CBM66 | 560 | 713 | 2.4e-31 | 0.967741935483871 |
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd15482 | Sialidase_non-viral | 1.61e-12 | 63 | 261 | 148 | 323 | Non-viral sialidases. Sialidases or neuraminidases function to bind and hydrolyze terminal sialic acid residues from various glycoconjugates, they play vital roles in pathogenesis, bacterial nutrition and cellular interactions. They have a six-bladed, beta-propeller fold with the non-viral sialidases containing 2-5 Asp-box motifs (most commonly Ser/Thr-X-Asp-[X]-Gly-X-Thr- Trp/Phe). This CD includes eubacterial and eukaryotic sialidases. |
| cd15482 | Sialidase_non-viral | 1.46e-09 | 65 | 376 | 19 | 339 | Non-viral sialidases. Sialidases or neuraminidases function to bind and hydrolyze terminal sialic acid residues from various glycoconjugates, they play vital roles in pathogenesis, bacterial nutrition and cellular interactions. They have a six-bladed, beta-propeller fold with the non-viral sialidases containing 2-5 Asp-box motifs (most commonly Ser/Thr-X-Asp-[X]-Gly-X-Thr- Trp/Phe). This CD includes eubacterial and eukaryotic sialidases. |
| pfam13088 | BNR_2 | 1.15e-06 | 97 | 350 | 22 | 275 | BNR repeat-like domain. This family of proteins contains BNR-like repeats suggesting these proteins may act as sialidases. |
| pfam06439 | DUF1080 | 3.56e-06 | 553 | 714 | 6 | 180 | Domain of Unknown Function (DUF1080). This family has structural similarity to an endo-1,3-1,4-beta glucanase belonging to glycoside hydrolase family 16. However, the structure surrounding the active site differs from that of the endo-1,3-1,4-beta glucanase. |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| AYQ71526.1 | 0.0 | 3 | 716 | 2 | 717 |
| AIQ42231.1 | 6.34e-208 | 8 | 544 | 11 | 546 |
| AIQ30649.1 | 1.84e-199 | 8 | 544 | 11 | 546 |
| AIQ59359.1 | 2.61e-199 | 8 | 544 | 11 | 546 |
| AYQ75607.1 | 1.73e-144 | 34 | 384 | 33 | 381 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 3A71_A | 2.85e-11 | 62 | 277 | 25 | 244 | Highresolution structure of Penicillium chrysogenum alpha-L-arabinanase [Penicillium chrysogenum],3A72_A High resolution structure of Penicillium chrysogenum alpha-L-arabinanase complexed with arabinobiose [Penicillium chrysogenum] |
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 0.000295 | 0.998943 | 0.000199 | 0.000193 | 0.000187 | 0.000162 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.