Species | Treponema_D sp900770075 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Spirochaetota; Spirochaetia; Treponematales; Treponemataceae; Treponema_D; Treponema_D sp900770075 | |||||||||||
CAZyme ID | MGYG000003575_01876 | |||||||||||
CAZy Family | PL1 | |||||||||||
CAZyme Description | Pectate lyase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 1370; End: 2680 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
PL1 | 166 | 369 | 3.3e-66 | 0.971830985915493 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
smart00656 | Amb_all | 1.77e-50 | 175 | 369 | 16 | 186 | Amb_all domain. |
COG3866 | PelB | 2.79e-47 | 33 | 432 | 35 | 344 | Pectate lyase [Carbohydrate transport and metabolism]. |
pfam00544 | Pec_lyase_C | 4.14e-36 | 175 | 369 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AEJ18226.1 | 3.45e-121 | 24 | 436 | 53 | 475 |
AEE17959.1 | 8.92e-85 | 21 | 434 | 42 | 446 |
QPH91275.1 | 1.97e-66 | 25 | 436 | 24 | 416 |
QPI07285.1 | 2.31e-64 | 6 | 436 | 3 | 416 |
QPH96000.1 | 1.77e-63 | 6 | 436 | 3 | 416 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1VBL_A | 5.30e-51 | 33 | 432 | 12 | 415 | Structureof the thermostable pectate lyase PL 47 [Bacillus sp. TS-47] |
5AMV_A | 7.57e-49 | 32 | 428 | 11 | 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 | 1.20e-48 | 32 | 428 | 32 | 417 | BacillusSubtilis Pectate Lyase [Bacillus subtilis] |
2BSP_A | 3.27e-48 | 32 | 428 | 32 | 417 | ChainA, PROTEIN (PECTATE LYASE) [Bacillus subtilis] |
2NZM_A | 5.60e-48 | 32 | 428 | 11 | 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 | 6.59e-48 | 32 | 428 | 32 | 417 | Pectate lyase OS=Bacillus subtilis (strain 168) OX=224308 GN=pel PE=1 SV=1 |
P04960 | 1.32e-41 | 171 | 432 | 106 | 385 | Pectate lyase E OS=Dickeya chrysanthemi OX=556 GN=pelE PE=1 SV=1 |
P18209 | 3.97e-38 | 171 | 432 | 112 | 391 | Pectate lyase D OS=Dickeya chrysanthemi OX=556 GN=pelD PE=3 SV=1 |
P0C1A4 | 7.05e-38 | 171 | 432 | 124 | 404 | Pectate lyase E OS=Dickeya chrysanthemi OX=556 GN=pelE PE=3 SV=1 |
P0C1A5 | 7.05e-38 | 171 | 432 | 124 | 404 | 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 |
---|---|---|---|---|---|
0.001294 | 0.997280 | 0.000375 | 0.000398 | 0.000340 | 0.000287 |
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