Species | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; UBA1394; | |||||||||||
CAZyme ID | MGYG000004304_00238 | |||||||||||
CAZy Family | CBM4 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location | Start: 2649; End: 4988 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH9 | 287 | 714 | 3e-108 | 0.9904306220095693 |
CBM4 | 35 | 160 | 1.2e-30 | 0.9920634920634921 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam00759 | Glyco_hydro_9 | 3.54e-93 | 290 | 715 | 2 | 374 | Glycosyl hydrolase family 9. |
397189 | pfam02927 | 2.40e-25 | 196 | 275 | 1 | 82 | CelD_N Cellulase N-terminal ig-like domain. |
cd02850 | E_set_Cellulase_N | 1.38e-24 | 198 | 282 | 2 | 86 | N-terminal Early set domain associated with the catalytic domain of cellulase. E or "early" set domains are associated with the catalytic domain of cellulases at the N-terminal end. Cellulases are O-glycosyl hydrolases (GHs) that hydrolyze beta 1-4 glucosidic bonds in cellulose. They are usually categorized into either exoglucanases, which sequentially release terminal sugar units from the cellulose chain, or endoglucanases, which also attack the chain internally. The N-terminal domain of cellulase may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family include members of the alpha amylase family, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase, among others. |
cd14256 | Dockerin_I | 7.51e-15 | 726 | 779 | 2 | 57 | 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. |
PLN03009 | PLN03009 | 1.91e-14 | 326 | 711 | 65 | 481 | cellulase |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
CBL16782.1 | 0.0 | 35 | 748 | 36 | 788 |
AQR94654.1 | 1.77e-220 | 13 | 719 | 15 | 725 |
AGF55906.1 | 4.04e-219 | 13 | 719 | 15 | 725 |
QEH68101.1 | 2.30e-218 | 31 | 716 | 32 | 722 |
ADZ82408.1 | 3.15e-218 | 31 | 716 | 32 | 722 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
4CJ0_A | 6.63e-107 | 194 | 747 | 26 | 581 | ChainA, ENDOGLUCANASE D [Acetivibrio thermocellus],4CJ1_A Chain A, ENDOGLUCANASE D [Acetivibrio thermocellus] |
1CLC_A | 9.67e-107 | 194 | 747 | 40 | 595 | ChainA, ENDOGLUCANASE CELD; EC: 3.2.1.4 [Acetivibrio thermocellus] |
3EZ8_A | 3.46e-94 | 198 | 714 | 9 | 527 | CrystalStructure of endoglucanase Cel9A from the thermoacidophilic Alicyclobacillus acidocaldarius [Alicyclobacillus acidocaldarius subsp. acidocaldarius],3GZK_A Structure of A. Acidocaldarius Cellulase CelA [Alicyclobacillus acidocaldarius subsp. acidocaldarius],3H2W_A Structure of A. acidocaldarius cellulase CelA in complex with cellobiose [Alicyclobacillus acidocaldarius subsp. acidocaldarius],3H3K_A Structure of A. acidocaldarius cellulase CelA in complex with cellotetraose [Alicyclobacillus acidocaldarius subsp. acidocaldarius],3RX5_A structure of AaCel9A in complex with cellotriose-like isofagomine [Alicyclobacillus acidocaldarius subsp. acidocaldarius],3RX7_A Structure of AaCel9A in complex with cellotetraose-like isofagomine [Alicyclobacillus acidocaldarius subsp. acidocaldarius],3RX8_A structure of AaCel9A in complex with cellobiose-like isofagomine [Alicyclobacillus acidocaldarius subsp. acidocaldarius] |
5E2J_A | 1.19e-93 | 198 | 714 | 32 | 550 | Crystalstructure of single mutant thermostable endoglucanase (D468A) from Alicyclobacillus acidocaldarius [Alicyclobacillus acidocaldarius subsp. acidocaldarius],5E2J_B Crystal structure of single mutant thermostable endoglucanase (D468A) from Alicyclobacillus acidocaldarius [Alicyclobacillus acidocaldarius subsp. acidocaldarius] |
3X17_A | 2.71e-79 | 198 | 714 | 18 | 552 | Crystalstructure of metagenome-derived glycoside hydrolase family 9 endoglucanase [uncultured bacterium],3X17_B Crystal structure of metagenome-derived glycoside hydrolase family 9 endoglucanase [uncultured bacterium] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P0C2S4 | 3.63e-106 | 194 | 747 | 26 | 581 | Endoglucanase D (Fragment) OS=Acetivibrio thermocellus OX=1515 GN=celD PE=1 SV=1 |
A3DDN1 | 6.92e-106 | 194 | 747 | 50 | 605 | Endoglucanase D OS=Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) OX=203119 GN=celD PE=1 SV=1 |
P23658 | 6.17e-95 | 198 | 718 | 4 | 545 | Cellodextrinase OS=Butyrivibrio fibrisolvens OX=831 GN=ced1 PE=1 SV=1 |
P10476 | 2.32e-78 | 201 | 726 | 40 | 606 | Endoglucanase A OS=Cellvibrio japonicus (strain Ueda107) OX=498211 GN=celA PE=3 SV=2 |
A7LXT3 | 1.54e-75 | 201 | 720 | 35 | 580 | Xyloglucan-specific endo-beta-1,4-glucanase BoGH9A OS=Bacteroides ovatus (strain ATCC 8483 / DSM 1896 / JCM 5824 / BCRC 10623 / CCUG 4943 / NCTC 11153) OX=411476 GN=BACOVA_02649 PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.003234 | 0.940442 | 0.055140 | 0.000619 | 0.000281 | 0.000223 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.