| Species | Treponema_D sp900770075 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Spirochaetota; Spirochaetia; Treponematales; Treponemataceae; Treponema_D; Treponema_D sp900770075 | |||||||||||
| CAZyme ID | MGYG000003575_01223 | |||||||||||
| CAZy Family | PL1 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 2011; End: 6045 Strand: - | |||||||||||
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| PL1 | 1049 | 1258 | 2e-64 | 0.9671361502347418 |
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| smart00656 | Amb_all | 4.79e-44 | 1056 | 1261 | 15 | 189 | Amb_all domain. |
| COG3866 | PelB | 1.89e-43 | 1036 | 1340 | 80 | 344 | Pectate lyase [Carbohydrate transport and metabolism]. |
| pfam00544 | Pec_lyase_C | 2.22e-30 | 1057 | 1258 | 34 | 211 | 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. |
| pfam01095 | Pectinesterase | 1.14e-11 | 282 | 528 | 12 | 240 | Pectinesterase. |
| COG4677 | PemB | 2.75e-11 | 211 | 522 | 8 | 349 | Pectin methylesterase and related acyl-CoA thioesterases [Carbohydrate transport and metabolism, Lipid transport and metabolism]. |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| AEE17959.1 | 1.33e-102 | 925 | 1344 | 37 | 448 |
| QPI00741.1 | 2.35e-79 | 925 | 1344 | 19 | 416 |
| QPH98945.1 | 2.35e-79 | 925 | 1344 | 19 | 416 |
| QPH93180.1 | 1.87e-77 | 925 | 1344 | 19 | 416 |
| QPI07285.1 | 8.92e-77 | 925 | 1344 | 19 | 416 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 5AMV_A | 1.75e-37 | 1050 | 1341 | 120 | 399 | 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 | 2.67e-37 | 1050 | 1341 | 141 | 420 | BacillusSubtilis Pectate Lyase [Bacillus subtilis] |
| 2BSP_A | 6.58e-37 | 1050 | 1341 | 141 | 420 | ChainA, PROTEIN (PECTATE LYASE) [Bacillus subtilis] |
| 2NZM_A | 1.07e-36 | 1050 | 1341 | 120 | 399 | ChainA, Pectate lyase [Bacillus subtilis],2O04_A Chain A, Pectate lyase [Bacillus subtilis],2O0V_A Chain A, Pectate lyase [Bacillus subtilis],2O0W_A Chain A, Pectate lyase [Bacillus subtilis],2O17_A Chain A, Pectate lyase [Bacillus subtilis],2O1D_A Chain A, Pectate lyase [Bacillus subtilis] |
| 1VBL_A | 1.50e-36 | 1050 | 1340 | 125 | 415 | Structureof the thermostable pectate lyase PL 47 [Bacillus sp. TS-47] |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P39116 | 1.46e-36 | 1050 | 1341 | 141 | 420 | Pectate lyase OS=Bacillus subtilis (strain 168) OX=224308 GN=pel PE=1 SV=1 |
| P04960 | 2.03e-32 | 1057 | 1340 | 110 | 385 | Pectate lyase E OS=Dickeya chrysanthemi OX=556 GN=pelE PE=1 SV=1 |
| P0C1A5 | 2.91e-32 | 1057 | 1340 | 128 | 404 | Pectate lyase E OS=Dickeya dadantii (strain 3937) OX=198628 GN=pelE PE=3 SV=2 |
| P0C1A4 | 5.30e-32 | 1057 | 1258 | 128 | 324 | Pectate lyase E OS=Dickeya chrysanthemi OX=556 GN=pelE PE=3 SV=1 |
| P18209 | 4.58e-31 | 1057 | 1222 | 116 | 282 | Pectate lyase D OS=Dickeya chrysanthemi OX=556 GN=pelD PE=3 SV=1 |
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 0.011932 | 0.029316 | 0.956656 | 0.000526 | 0.001396 | 0.000166 |
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