| Species | Treponema_D berlinense | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Spirochaetota; Spirochaetia; Treponematales; Treponemataceae; Treponema_D; Treponema_D berlinense | |||||||||||
| CAZyme ID | MGYG000004570_01607 | |||||||||||
| CAZy Family | PL1 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 77535; End: 79829 Strand: + | |||||||||||
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| PL1 | 478 | 691 | 9.6e-74 | 0.9859154929577465 |
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| smart00656 | Amb_all | 9.68e-58 | 485 | 694 | 11 | 189 | Amb_all domain. |
| COG3866 | PelB | 4.48e-53 | 476 | 759 | 87 | 343 | Pectate lyase [Carbohydrate transport and metabolism]. |
| pfam00544 | Pec_lyase_C | 8.99e-43 | 462 | 691 | 9 | 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. |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| AEJ18226.1 | 1.26e-114 | 339 | 764 | 54 | 475 |
| AEE17959.1 | 1.38e-103 | 340 | 764 | 47 | 448 |
| QPH91275.1 | 7.60e-73 | 340 | 764 | 25 | 416 |
| QPH93180.1 | 7.77e-72 | 340 | 764 | 25 | 416 |
| QPH96000.1 | 5.68e-71 | 340 | 764 | 25 | 416 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 1VBL_A | 3.98e-49 | 467 | 691 | 109 | 330 | Structureof the thermostable pectate lyase PL 47 [Bacillus sp. TS-47] |
| 5AMV_A | 2.26e-47 | 347 | 758 | 12 | 396 | 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 | 3.62e-47 | 347 | 758 | 33 | 417 | BacillusSubtilis Pectate Lyase [Bacillus subtilis] |
| 2BSP_A | 9.29e-47 | 347 | 758 | 33 | 417 | ChainA, PROTEIN (PECTATE LYASE) [Bacillus subtilis] |
| 2NZM_A | 1.50e-46 | 347 | 758 | 12 | 396 | 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] |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P39116 | 1.98e-46 | 347 | 758 | 33 | 417 | Pectate lyase OS=Bacillus subtilis (strain 168) OX=224308 GN=pel PE=1 SV=1 |
| P18209 | 2.66e-43 | 481 | 758 | 107 | 389 | Pectate lyase D OS=Dickeya chrysanthemi OX=556 GN=pelD PE=3 SV=1 |
| P04960 | 8.13e-43 | 481 | 691 | 101 | 306 | Pectate lyase E OS=Dickeya chrysanthemi OX=556 GN=pelE PE=1 SV=1 |
| Q51915 | 1.36e-42 | 485 | 758 | 108 | 378 | Pectate lyase OS=Pseudomonas marginalis OX=298 GN=pel PE=1 SV=1 |
| P0C1A5 | 1.68e-42 | 481 | 691 | 119 | 324 | Pectate lyase E OS=Dickeya dadantii (strain 3937) OX=198628 GN=pelE PE=3 SV=2 |
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 0.000030 | 0.021524 | 0.978449 | 0.000009 | 0.000012 | 0.000009 |
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