Species | Longibaculum sp900538465 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes; Bacilli; Erysipelotrichales; Erysipelatoclostridiaceae; Longibaculum; Longibaculum sp900538465 | |||||||||||
CAZyme ID | MGYG000001635_02366 | |||||||||||
CAZy Family | GH73 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 1131; End: 2960 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH73 | 312 | 429 | 4.5e-19 | 0.9765625 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd14256 | Dockerin_I | 2.66e-16 | 548 | 602 | 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 | 1.13e-15 | 548 | 603 | 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 | 2.67e-12 | 257 | 429 | 50 | 229 | Beta- N-acetylglucosaminidase [Carbohydrate transport and metabolism]. |
pfam01832 | Glucosaminidase | 1.03e-10 | 312 | 384 | 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 | 7.98e-10 | 300 | 434 | 1 | 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 | 8.83e-248 | 4 | 578 | 3 | 588 |
QNM11023.1 | 3.49e-134 | 2 | 579 | 4 | 606 |
BCT44532.1 | 6.76e-93 | 153 | 582 | 170 | 610 |
QSI26463.1 | 2.42e-87 | 120 | 582 | 88 | 562 |
QEK17141.1 | 9.77e-87 | 137 | 539 | 96 | 495 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
4Q2W_A | 1.24e-19 | 187 | 424 | 74 | 278 | CrystalStructure of pneumococcal peptidoglycan hydrolase LytB [Streptococcus pneumoniae TIGR4] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P59205 | 2.11e-18 | 187 | 424 | 442 | 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 | 2.27e-18 | 187 | 424 | 486 | 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 |
---|---|---|---|---|---|
0.000340 | 0.998944 | 0.000215 | 0.000180 | 0.000157 | 0.000138 |
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