| Species | Campylobacter_A concisus_K | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Campylobacterota; Campylobacteria; Campylobacterales; Campylobacteraceae; Campylobacter_A; Campylobacter_A concisus_K | |||||||||||
| CAZyme ID | MGYG000002425_00787 | |||||||||||
| CAZy Family | PL1 | |||||||||||
| CAZyme Description | Pectate lyase E | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 136535; End: 137338 Strand: - | |||||||||||
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| PL1 | 2 | 198 | 3.8e-67 | 0.9436619718309859 |
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| smart00656 | Amb_all | 1.84e-50 | 3 | 201 | 14 | 189 | Amb_all domain. |
| COG3866 | PelB | 7.65e-46 | 3 | 263 | 99 | 344 | Pectate lyase [Carbohydrate transport and metabolism]. |
| pfam00544 | Pec_lyase_C | 4.73e-35 | 3 | 198 | 32 | 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 |
|---|---|---|---|---|---|
| QPH93180.1 | 7.59e-180 | 1 | 267 | 150 | 416 |
| QPH85838.1 | 1.08e-179 | 1 | 267 | 150 | 416 |
| QPH91275.1 | 3.58e-178 | 1 | 267 | 150 | 416 |
| QPH96000.1 | 1.02e-177 | 1 | 267 | 150 | 416 |
| QPI07285.1 | 4.16e-177 | 1 | 267 | 150 | 416 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 1VBL_A | 1.16e-43 | 3 | 219 | 130 | 358 | Structureof the thermostable pectate lyase PL 47 [Bacillus sp. TS-47] |
| 1PCL_A | 9.36e-38 | 3 | 263 | 78 | 355 | ChainA, PECTATE LYASE E [Dickeya chrysanthemi] |
| 5AMV_A | 4.47e-34 | 3 | 263 | 125 | 398 | 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 | 6.17e-34 | 3 | 263 | 146 | 419 | BacillusSubtilis Pectate Lyase [Bacillus subtilis] |
| 2BSP_A | 1.66e-33 | 3 | 263 | 146 | 419 | ChainA, PROTEIN (PECTATE LYASE) [Bacillus subtilis] |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P04960 | 9.12e-37 | 3 | 263 | 108 | 385 | Pectate lyase E OS=Dickeya chrysanthemi OX=556 GN=pelE PE=1 SV=1 |
| P18209 | 1.05e-35 | 3 | 263 | 114 | 391 | Pectate lyase D OS=Dickeya chrysanthemi OX=556 GN=pelD PE=3 SV=1 |
| Q51915 | 1.28e-33 | 1 | 263 | 109 | 380 | Pectate lyase OS=Pseudomonas marginalis OX=298 GN=pel PE=1 SV=1 |
| P0C1A5 | 1.90e-33 | 3 | 263 | 126 | 404 | Pectate lyase E OS=Dickeya dadantii (strain 3937) OX=198628 GN=pelE PE=3 SV=2 |
| P39116 | 3.38e-33 | 3 | 263 | 146 | 419 | Pectate lyase OS=Bacillus subtilis (strain 168) OX=224308 GN=pel PE=1 SV=1 |
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 1.000042 | 0.000006 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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