Species | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; ; | |||||||||||
CAZyme ID | MGYG000004229_01469 | |||||||||||
CAZy Family | GH28 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location | Start: 1884; End: 4184 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH28 | 150 | 446 | 1e-25 | 0.7292307692307692 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG5434 | Pgu1 | 4.96e-22 | 59 | 364 | 13 | 338 | Polygalacturonase [Carbohydrate transport and metabolism]. |
cd14256 | Dockerin_I | 3.69e-15 | 25 | 79 | 1 | 55 | Type I dockerin repeat domain. Bacterial cohesin domains bind to a complementary protein domain named dockerin, and this interaction is required for the formation of the cellulosome, a cellulose-degrading complex. The cellulosome consists of scaffoldin, a noncatalytic scaffolding polypeptide, that comprises repeating cohesion modules and a single carbohydrate-binding module (CBM). Specific calcium-dependent interactions between cohesins and dockerins appear to be essential for cellulosome assembly. This subfamily represents type I dockerins, which are responsible for anchoring a variety of enzymatic domains to the complex. |
pfam13313 | DUF4082 | 8.66e-14 | 610 | 757 | 1 | 142 | Domain of unknown function (DUF4082). This family appears to be a parallel beta-helix repeated region that sits between successive Cadherin domains, pfam00028. |
pfam00404 | Dockerin_1 | 9.85e-09 | 26 | 79 | 1 | 54 | Dockerin type I repeat. The dockerin repeat is the binding partner of the cohesin domain pfam00963. The cohesin-dockerin interaction is the crucial interaction for complex formation in the cellulosome. The dockerin repeats, each bearing homology to the EF-hand calcium-binding loop bind calcium. |
cd14253 | Dockerin | 6.18e-07 | 26 | 79 | 1 | 54 | Dockerin repeat domain. Dockerins are modules in the cellulosome complex that often anchor catalytic subunits by binding to cohesin domains of scaffolding proteins. Three types of dockerins and their corresponding cohesin have been described in the literature. This alignment models two consecutive dockerin repeats, the functional unit. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QGQ94767.1 | 7.17e-107 | 118 | 762 | 37 | 705 |
ADB48561.1 | 3.30e-77 | 118 | 589 | 28 | 502 |
ADB48560.1 | 1.70e-66 | 118 | 658 | 28 | 580 |
ADB49825.1 | 1.64e-59 | 118 | 658 | 27 | 580 |
QYH35737.1 | 2.19e-54 | 117 | 622 | 125 | 654 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
5OLP_A | 2.26e-12 | 118 | 399 | 45 | 324 | Galacturonidase[Bacteroides thetaiotaomicron VPI-5482],5OLP_B Galacturonidase [Bacteroides thetaiotaomicron VPI-5482] |
2UVE_A | 1.16e-07 | 117 | 364 | 156 | 430 | Structureof Yersinia enterocolitica Family 28 Exopolygalacturonase [Yersinia enterocolitica],2UVE_B Structure of Yersinia enterocolitica Family 28 Exopolygalacturonase [Yersinia enterocolitica],2UVF_A Structure of Yersinia enterocolitica Family 28 Exopolygalacturonase in Complex with Digalaturonic Acid [Yersinia enterocolitica],2UVF_B Structure of Yersinia enterocolitica Family 28 Exopolygalacturonase in Complex with Digalaturonic Acid [Yersinia enterocolitica] |
5LW3_A | 2.27e-06 | 125 | 186 | 8 | 73 | Azotobactervinelandii Mannuronan C-5 epimerase AlgE6 A-module [Azotobacter vinelandii] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q9ZFG9 | 2.91e-06 | 125 | 175 | 8 | 65 | Alginate lyase 7 OS=Azotobacter vinelandii OX=354 GN=algE7 PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000508 | 0.998740 | 0.000182 | 0.000206 | 0.000173 | 0.000164 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.