Species | ||||||||||||
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Lineage | Bacteria; Firmicutes_A; Clostridia; UBA1212; ; ; | |||||||||||
CAZyme ID | MGYG000000728_01493 | |||||||||||
CAZy Family | GH140 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 4993; End: 7110 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH140 | 137 | 547 | 5.9e-42 | 0.9538834951456311 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam13204 | DUF4038 | 1.89e-43 | 145 | 471 | 3 | 318 | Protein of unknown function (DUF4038). A family of putative cellulases. |
pfam16586 | DUF5060 | 8.63e-22 | 37 | 107 | 1 | 70 | Domain of unknown function (DUF5060). This is the N-terminal domain of a putative glycoside hydrolase, DUF4038. It is found in a number of different bacterial orders. |
cd14256 | Dockerin_I | 2.58e-16 | 641 | 695 | 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. |
pfam00404 | Dockerin_1 | 3.93e-11 | 642 | 696 | 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 | 3.49e-06 | 642 | 697 | 1 | 56 | 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 |
---|---|---|---|---|---|
BCW44877.1 | 1.60e-130 | 54 | 573 | 98 | 593 |
BBI36498.1 | 6.06e-102 | 16 | 630 | 14 | 615 |
QJD82871.1 | 5.30e-94 | 39 | 572 | 41 | 569 |
QTH45264.1 | 1.47e-92 | 17 | 572 | 15 | 569 |
QNK56434.1 | 2.62e-92 | 30 | 617 | 29 | 613 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
4N0R_A | 8.27e-10 | 39 | 332 | 6 | 293 | ChainA, putative glycoside hydrolase [Phocaeicola vulgatus ATCC 8482],4N0R_B Chain B, putative glycoside hydrolase [Phocaeicola vulgatus ATCC 8482] |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.159164 | 0.720212 | 0.119008 | 0.000542 | 0.000401 | 0.000637 |
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