Species | Ruminococcus_C sp900545285 | |||||||||||
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Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Ruminococcus_C; Ruminococcus_C sp900545285 | |||||||||||
CAZyme ID | MGYG000002573_01510 | |||||||||||
CAZy Family | GH8 | |||||||||||
CAZyme Description | Endoglucanase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 9684; End: 11123 Strand: - |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam01270 | Glyco_hydro_8 | 2.54e-21 | 46 | 410 | 8 | 321 | Glycosyl hydrolases family 8. |
COG3405 | BcsZ | 7.30e-17 | 38 | 410 | 18 | 346 | Endo-1,4-beta-D-glucanase Y [Carbohydrate transport and metabolism]. |
PRK11097 | PRK11097 | 9.98e-11 | 46 | 396 | 28 | 340 | cellulase. |
cd14256 | Dockerin_I | 3.43e-10 | 424 | 476 | 2 | 56 | 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. |
pfam00404 | Dockerin_1 | 9.60e-07 | 424 | 476 | 1 | 55 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
CBL17008.1 | 2.85e-165 | 1 | 474 | 1 | 468 |
BCK01002.1 | 4.02e-119 | 37 | 415 | 114 | 500 |
QNU66099.1 | 3.48e-112 | 42 | 415 | 522 | 905 |
AJS61487.1 | 2.89e-97 | 17 | 415 | 984 | 1383 |
QNK49086.1 | 3.76e-96 | 29 | 415 | 50 | 425 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
5XD0_A | 1.69e-84 | 29 | 412 | 49 | 406 | ApoStructure of Beta-1,3-1,4-glucanase from Paenibacillus sp.X4 [Paenibacillus sp. X4],5XD0_B Apo Structure of Beta-1,3-1,4-glucanase from Paenibacillus sp.X4 [Paenibacillus sp. X4] |
7CJU_A | 5.03e-57 | 29 | 416 | 24 | 393 | Crystalstructure of inactive form of chitosanase crystallized by ammonium sulfate [Bacillus sp. K17-2],7CJU_B Crystal structure of inactive form of chitosanase crystallized by ammonium sulfate [Bacillus sp. K17-2],7XGQ_A Chain A, chitosanase [Bacillus sp. K17-2],7XGQ_B Chain B, chitosanase [Bacillus sp. K17-2] |
1V5C_A | 5.47e-57 | 29 | 415 | 18 | 386 | Thecrystal structure of the inactive form chitosanase from Bacillus sp. K17 at pH3.7 [Bacillus sp. (in: Bacteria)],1V5D_A The crystal structure of the active form chitosanase from Bacillus sp. K17 at pH6.4 [Bacillus sp. (in: Bacteria)],1V5D_B The crystal structure of the active form chitosanase from Bacillus sp. K17 at pH6.4 [Bacillus sp. (in: Bacteria)] |
1KWF_A | 1.02e-33 | 36 | 415 | 21 | 359 | ChainA, Endoglucanase A [Acetivibrio thermocellus] |
1CEM_A | 1.94e-33 | 36 | 415 | 21 | 359 | ChainA, CELLULASE CELA (1,4-BETA-D-GLUCAN-GLUCANOHYDROLASE) [Acetivibrio thermocellus],1IS9_A Chain A, endoglucanase A [Acetivibrio thermocellus] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P19254 | 4.22e-85 | 29 | 412 | 49 | 406 | Beta-glucanase OS=Niallia circulans OX=1397 GN=bgc PE=3 SV=1 |
P29019 | 1.34e-55 | 29 | 427 | 74 | 452 | Endoglucanase OS=Bacillus sp. (strain KSM-330) OX=72575 PE=1 SV=1 |
A3DC29 | 7.64e-38 | 36 | 445 | 53 | 437 | Endoglucanase A OS=Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) OX=203119 GN=celA PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000001 | 0.000526 | 0.999550 | 0.000000 | 0.000000 | 0.000000 |
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