Species | Ruminococcus_C sp000437175 | |||||||||||
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Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Ruminococcus_C; Ruminococcus_C sp000437175 | |||||||||||
CAZyme ID | MGYG000004275_00948 | |||||||||||
CAZy Family | GH5 | |||||||||||
CAZyme Description | Endoglucanase A | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 167; End: 1504 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH5 | 73 | 355 | 7.9e-91 | 0.9891304347826086 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam00150 | Cellulase | 2.87e-44 | 72 | 321 | 14 | 237 | Cellulase (glycosyl hydrolase family 5). |
COG2730 | BglC | 1.13e-25 | 39 | 321 | 45 | 322 | Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism]. |
cd14256 | Dockerin_I | 1.71e-15 | 391 | 445 | 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 | 9.27e-10 | 391 | 445 | 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. |
cd14253 | Dockerin | 2.47e-05 | 391 | 438 | 1 | 48 | 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 |
---|---|---|---|---|---|
CBK96759.1 | 1.01e-163 | 33 | 381 | 38 | 386 |
CBL35076.1 | 5.78e-163 | 31 | 381 | 26 | 376 |
ADL52801.1 | 1.79e-157 | 26 | 403 | 37 | 413 |
BAV13032.1 | 1.79e-157 | 26 | 403 | 37 | 413 |
ADL51185.1 | 1.94e-146 | 33 | 403 | 41 | 412 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6XRK_A | 1.98e-76 | 37 | 379 | 23 | 370 | GH5-4broad specificity endoglucanase from an uncultured bovine rumen ciliate [uncultured bovine rumen ciliate],6XRK_B GH5-4 broad specificity endoglucanase from an uncultured bovine rumen ciliate [uncultured bovine rumen ciliate] |
5OYC_A | 2.37e-61 | 24 | 354 | 31 | 361 | GH5endo-xyloglucanase from Cellvibrio japonicus [Cellvibrio japonicus Ueda107],5OYC_B GH5 endo-xyloglucanase from Cellvibrio japonicus [Cellvibrio japonicus Ueda107],5OYD_A GH5 endo-xyloglucanase from Cellvibrio japonicus [Cellvibrio japonicus Ueda107],5OYD_B GH5 endo-xyloglucanase from Cellvibrio japonicus [Cellvibrio japonicus Ueda107],5OYE_A GH5 endo-xyloglucanase from Cellvibrio japonicus [Cellvibrio japonicus Ueda107],5OYE_B GH5 endo-xyloglucanase from Cellvibrio japonicus [Cellvibrio japonicus Ueda107] |
6WQY_A | 9.72e-61 | 37 | 354 | 23 | 346 | ChainA, Cellulase [Phocaeicola salanitronis DSM 18170] |
6HA9_A | 1.81e-60 | 24 | 354 | 31 | 361 | Structureof an endo-Xyloglucanase from Cellvibrio japonicus complexed with XXXG(2F)-beta-DNP [Cellvibrio japonicus Ueda107],6HA9_B Structure of an endo-Xyloglucanase from Cellvibrio japonicus complexed with XXXG(2F)-beta-DNP [Cellvibrio japonicus Ueda107],6HAA_A Structure of a covalent complex of endo-Xyloglucanase from Cellvibrio japonicus after reacting with XXXG(2F)-beta-DNP [Cellvibrio japonicus Ueda107],6HAA_B Structure of a covalent complex of endo-Xyloglucanase from Cellvibrio japonicus after reacting with XXXG(2F)-beta-DNP [Cellvibrio japonicus Ueda107] |
6WQP_A | 1.78e-59 | 28 | 326 | 6 | 295 | GH5-4broad specificity endoglucanase from Ruminococcus champanellensis [Ruminococcus champanellensis],6WQP_B GH5-4 broad specificity endoglucanase from Ruminococcus champanellensis [Ruminococcus champanellensis],6WQV_A GH5-4 broad specificity endoglucanase from Ruminococcus champanellensis with bound cellotriose [Ruminococcus champanellensis],6WQV_B GH5-4 broad specificity endoglucanase from Ruminococcus champanellensis with bound cellotriose [Ruminococcus champanellensis],6WQV_C GH5-4 broad specificity endoglucanase from Ruminococcus champanellensis with bound cellotriose [Ruminococcus champanellensis],6WQV_D GH5-4 broad specificity endoglucanase from Ruminococcus champanellensis with bound cellotriose [Ruminococcus champanellensis] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P28621 | 4.13e-59 | 33 | 403 | 37 | 398 | Endoglucanase B OS=Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B) OX=573061 GN=engB PE=3 SV=1 |
O08342 | 7.16e-56 | 30 | 378 | 32 | 393 | Endoglucanase A OS=Paenibacillus barcinonensis OX=198119 GN=celA PE=1 SV=1 |
P54937 | 1.30e-55 | 30 | 381 | 33 | 372 | Endoglucanase A OS=Clostridium longisporum OX=1523 GN=celA PE=1 SV=1 |
P28623 | 2.55e-53 | 33 | 354 | 38 | 337 | Endoglucanase D OS=Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B) OX=573061 GN=engD PE=1 SV=2 |
A7LXT7 | 2.75e-53 | 33 | 370 | 145 | 491 | Xyloglucan-specific endo-beta-1,4-glucanase BoGH5A OS=Bacteroides ovatus (strain ATCC 8483 / DSM 1896 / JCM 5824 / BCRC 10623 / CCUG 4943 / NCTC 11153) OX=411476 GN=BACOVA_02653 PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000217 | 0.999164 | 0.000158 | 0.000163 | 0.000144 | 0.000137 |
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