| Species | ||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Lachnoclostridium; | |||||||||||
| CAZyme ID | MGYG000003769_01528 | |||||||||||
| CAZy Family | PL1 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 54803; End: 56461 Strand: - | |||||||||||
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| PL1 | 150 | 405 | 1.1e-32 | 0.8118811881188119 |
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| smart00656 | Amb_all | 2.51e-13 | 155 | 366 | 19 | 167 | Amb_all domain. |
| COG3866 | PelB | 1.47e-10 | 174 | 365 | 123 | 251 | Pectate lyase [Carbohydrate transport and metabolism]. |
| pfam00544 | Pec_lyase_C | 0.001 | 175 | 364 | 59 | 190 | Pectate lyase. This enzyme forms a right handed beta helix structure. Pectate lyase is an enzyme involved in the maceration and soft rotting of plant tissue. |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QNF29855.1 | 3.75e-309 | 1 | 551 | 1 | 551 |
| QGH35942.1 | 2.77e-297 | 1 | 549 | 1 | 549 |
| QYR22341.1 | 9.13e-273 | 17 | 550 | 17 | 552 |
| ADL50775.1 | 1.69e-263 | 1 | 551 | 1 | 553 |
| BAV13078.1 | 1.88e-263 | 1 | 551 | 4 | 556 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 5GT5_A | 5.26e-39 | 70 | 363 | 27 | 293 | Structuralbasis of the specific activity and thermostability of pectate lyase (pelN) from Paenibacillus sp. 0602 [Paenibacillus sp. 0602],5GT5_B Structural basis of the specific activity and thermostability of pectate lyase (pelN) from Paenibacillus sp. 0602 [Paenibacillus sp. 0602] |
| 5AMV_A | 1.81e-11 | 55 | 408 | 15 | 343 | Structuralinsights into the loss of catalytic competence in pectate lyase at low pH [Bacillus subtilis],5X2I_A Polygalacturonate Lyase by Fusing with a Self-assembling Amphipathic Peptide [Bacillus subtilis subsp. subtilis str. 168] |
| 1BN8_A | 1.98e-11 | 55 | 408 | 36 | 364 | BacillusSubtilis Pectate Lyase [Bacillus subtilis] |
| 3KRG_A | 4.26e-11 | 55 | 408 | 15 | 343 | ChainA, Pectate lyase [Bacillus subtilis] |
| 2BSP_A | 4.63e-11 | 55 | 408 | 36 | 364 | ChainA, PROTEIN (PECTATE LYASE) [Bacillus subtilis] |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| D3JTC2 | 2.86e-39 | 70 | 379 | 56 | 339 | Pectate lyase B OS=Paenibacillus amylolyticus OX=1451 GN=pelB PE=1 SV=1 |
| P39116 | 1.08e-10 | 55 | 408 | 36 | 364 | Pectate lyase OS=Bacillus subtilis (strain 168) OX=224308 GN=pel PE=1 SV=1 |
| Q9WYR4 | 2.50e-07 | 151 | 377 | 79 | 255 | 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 | 1.02e-06 | 151 | 377 | 77 | 253 | Pectate trisaccharide-lyase OS=Thermotoga sp. (strain RQ2) OX=126740 GN=pelA PE=3 SV=1 |
| A1CYB8 | 1.50e-06 | 301 | 415 | 178 | 269 | Probable pectate lyase A OS=Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) OX=331117 GN=plyA PE=3 SV=1 |
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 0.001293 | 0.971430 | 0.026517 | 0.000288 | 0.000225 | 0.000210 |
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