Species | Bacteroides congonensis | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides congonensis | |||||||||||
CAZyme ID | MGYG000000675_03654 | |||||||||||
CAZy Family | GH33 | |||||||||||
CAZyme Description | Sialidase | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location | Start: 10389; End: 11552 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH33 | 39 | 355 | 7.3e-78 | 0.9385964912280702 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd15482 | Sialidase_non-viral | 9.02e-90 | 38 | 354 | 2 | 327 | 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 | 1.54e-25 | 61 | 329 | 1 | 259 | BNR repeat-like domain. This family of proteins contains BNR-like repeats suggesting these proteins may act as sialidases. |
pfam13859 | BNR_3 | 2.10e-10 | 52 | 219 | 1 | 165 | BNR repeat-like domain. This family of proteins contains BNR-like repeats suggesting these proteins may act as sialidases. |
COG4409 | NanH | 2.92e-09 | 30 | 374 | 253 | 669 | Neuraminidase (sialidase) [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis]. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QUR43338.1 | 1.39e-278 | 1 | 387 | 1 | 387 |
QIU95628.1 | 1.58e-236 | 3 | 387 | 3 | 387 |
SEH77633.1 | 3.51e-100 | 38 | 380 | 69 | 402 |
QUR43337.1 | 1.57e-74 | 35 | 382 | 59 | 422 |
QIU95629.1 | 4.60e-73 | 35 | 382 | 57 | 420 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
7MHU_A | 1.36e-77 | 35 | 382 | 35 | 398 | ChainA, Exo-alpha-sialidase [Bacteroides acidifaciens],7MHU_B Chain B, Exo-alpha-sialidase [Bacteroides acidifaciens] |
6MNJ_A | 7.24e-31 | 37 | 352 | 187 | 523 | Hadzamicrobial sialidase Hz136 [Alistipes],6MNJ_B Hadza microbial sialidase Hz136 [Alistipes] |
1EUR_A | 9.50e-29 | 43 | 350 | 18 | 344 | Sialidase[Micromonospora viridifaciens],1EUS_A Sialidase Complexed With 2-Deoxy-2,3-Dehydro-N- Acetylneuraminic Acid [Micromonospora viridifaciens] |
1EUT_A | 8.26e-28 | 43 | 350 | 18 | 344 | Sialidase,Large 68kd Form, Complexed With Galactose [Micromonospora viridifaciens],1EUU_A Sialidase Or Neuraminidase, Large 68kd Form [Micromonospora viridifaciens] |
1W8N_A | 1.10e-27 | 43 | 350 | 14 | 340 | Contributionof the Active Site Aspartic Acid to Catalysis in the Bacterial Neuraminidase from Micromonospora viridifaciens. [Micromonospora viridifaciens],1W8O_A Contribution of the Active Site Aspartic Acid to Catalysis in the Bacterial Neuraminidase from Micromonospora viridifaciens [Micromonospora viridifaciens] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q02834 | 5.12e-27 | 43 | 350 | 60 | 386 | Sialidase OS=Micromonospora viridifaciens OX=1881 GN=nedA PE=1 SV=1 |
P31206 | 6.30e-27 | 42 | 352 | 195 | 528 | Sialidase OS=Bacteroides fragilis (strain YCH46) OX=295405 GN=nanH PE=3 SV=2 |
P29767 | 1.11e-24 | 39 | 387 | 384 | 839 | Sialidase OS=Clostridium septicum OX=1504 PE=3 SV=1 |
P15698 | 5.48e-23 | 29 | 350 | 31 | 380 | Sialidase OS=Paeniclostridium sordellii OX=1505 PE=1 SV=1 |
A6BMK7 | 2.86e-22 | 46 | 340 | 73 | 376 | Sialidase-1 OS=Bos taurus OX=9913 GN=NEU1 PE=2 SV=2 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.001017 | 0.383390 | 0.614806 | 0.000371 | 0.000221 | 0.000191 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.