Species | Coprobacillus cateniformis | |||||||||||
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Lineage | Bacteria; Firmicutes; Bacilli; Erysipelotrichales; Erysipelatoclostridiaceae; Coprobacillus; Coprobacillus cateniformis | |||||||||||
CAZyme ID | MGYG000001402_03609 | |||||||||||
CAZy Family | GH73 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 389719; End: 391545 Strand: + |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd14256 | Dockerin_I | 6.97e-17 | 547 | 601 | 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 | 5.74e-16 | 547 | 602 | 1 | 56 | 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. |
COG4193 | LytD | 3.59e-14 | 265 | 423 | 59 | 224 | Beta- N-acetylglucosaminidase [Carbohydrate transport and metabolism]. |
pfam01832 | Glucosaminidase | 1.79e-10 | 311 | 383 | 1 | 84 | Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase. This family includes Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase EC:3.2.1.96. As well as the flageller protein J that has been shown to hydrolyze peptidoglycan. |
smart00047 | LYZ2 | 1.53e-09 | 308 | 433 | 10 | 146 | Lysozyme subfamily 2. Eubacterial enzymes distantly related to eukaryotic lysozymes. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QUN13370.1 | 7.85e-251 | 4 | 576 | 3 | 587 |
QNM11023.1 | 2.20e-144 | 6 | 578 | 11 | 606 |
BCT44532.1 | 6.73e-102 | 28 | 581 | 35 | 610 |
QSI26463.1 | 4.86e-96 | 120 | 581 | 88 | 562 |
QJA02388.1 | 3.25e-93 | 122 | 581 | 90 | 564 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
4Q2W_A | 3.99e-22 | 185 | 423 | 73 | 278 | CrystalStructure of pneumococcal peptidoglycan hydrolase LytB [Streptococcus pneumoniae TIGR4] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P59205 | 9.97e-21 | 185 | 423 | 441 | 646 | Putative endo-beta-N-acetylglucosaminidase OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=lytB PE=1 SV=1 |
P59206 | 1.09e-20 | 185 | 423 | 485 | 690 | Putative endo-beta-N-acetylglucosaminidase OS=Streptococcus pneumoniae (strain ATCC BAA-255 / R6) OX=171101 GN=lytB PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.121571 | 0.811144 | 0.066100 | 0.000456 | 0.000321 | 0.000373 |
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