Species | Ruminococcus_C callidus | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Ruminococcus_C; Ruminococcus_C callidus | |||||||||||
CAZyme ID | MGYG000002295_01216 | |||||||||||
CAZy Family | PL1 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 57679; End: 60816 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
PL1 | 209 | 437 | 4.7e-34 | 0.9554455445544554 |
CBM13 | 563 | 709 | 9.5e-21 | 0.7021276595744681 |
CBM13 | 717 | 885 | 1.6e-19 | 0.8351063829787234 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG3866 | PelB | 6.81e-37 | 157 | 510 | 14 | 341 | Pectate lyase [Carbohydrate transport and metabolism]. |
smart00656 | Amb_all | 2.10e-20 | 239 | 438 | 17 | 190 | Amb_all domain. |
pfam14200 | RicinB_lectin_2 | 8.34e-18 | 557 | 642 | 8 | 89 | Ricin-type beta-trefoil lectin domain-like. |
pfam14200 | RicinB_lectin_2 | 3.31e-16 | 648 | 747 | 1 | 89 | Ricin-type beta-trefoil lectin domain-like. |
cd14256 | Dockerin_I | 7.99e-15 | 979 | 1035 | 1 | 57 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
CBL17651.1 | 3.33e-165 | 35 | 715 | 33 | 700 |
CDM70399.1 | 5.07e-155 | 6 | 707 | 2 | 696 |
AUO18238.1 | 1.00e-145 | 2 | 707 | 4 | 707 |
CBL16867.1 | 5.98e-97 | 34 | 855 | 33 | 847 |
ASR46637.1 | 6.23e-77 | 31 | 520 | 31 | 527 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3ZSC_A | 1.21e-15 | 190 | 406 | 20 | 214 | Catalyticfunction and substrate recognition of the pectate lyase from Thermotoga maritima [Thermotoga maritima] |
3VMV_A | 1.59e-11 | 172 | 415 | 2 | 233 | Crystalstructure of pectate lyase Bsp165PelA from Bacillus sp. N165 [Bacillus sp. N16-5],3VMW_A Crystal structure of pectate lyase Bsp165PelA from Bacillus sp. N165 in complex with trigalacturonate [Bacillus sp. N16-5] |
1VBL_A | 1.62e-11 | 291 | 405 | 192 | 301 | Structureof the thermostable pectate lyase PL 47 [Bacillus sp. TS-47] |
1PCL_A | 4.74e-11 | 187 | 470 | 14 | 318 | ChainA, PECTATE LYASE E [Dickeya chrysanthemi] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
O34819 | 3.35e-22 | 172 | 513 | 34 | 339 | Pectin lyase OS=Bacillus subtilis (strain 168) OX=224308 GN=pelB PE=3 SV=1 |
P94449 | 3.35e-22 | 172 | 513 | 34 | 339 | Pectin lyase OS=Bacillus subtilis OX=1423 GN=pelB PE=1 SV=1 |
Q9WYR4 | 1.49e-16 | 163 | 406 | 23 | 241 | Pectate trisaccharide-lyase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=pelA PE=1 SV=1 |
B1L969 | 4.69e-16 | 163 | 406 | 21 | 239 | Pectate trisaccharide-lyase OS=Thermotoga sp. (strain RQ2) OX=126740 GN=pelA PE=3 SV=1 |
Q65DC2 | 2.33e-11 | 174 | 406 | 44 | 250 | Pectate trisaccharide-lyase OS=Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46) OX=279010 GN=BLi04129 PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000237 | 0.999140 | 0.000173 | 0.000157 | 0.000147 | 0.000135 |
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