| Species | Cellulomonas timonensis | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Cellulomonadaceae; Cellulomonas; Cellulomonas timonensis | |||||||||||
| CAZyme ID | MGYG000001537_02665 | |||||||||||
| CAZy Family | PL1 | |||||||||||
| CAZyme Description | Pectate lyase | |||||||||||
| CAZyme Property |
|
|||||||||||
| Genome Property |
|
|||||||||||
| Gene Location | Start: 1003350; End: 1004795 Strand: - | |||||||||||
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| PL1 | 178 | 385 | 5.3e-90 | 0.9812206572769953 |
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| COG3866 | PelB | 1.26e-57 | 63 | 466 | 35 | 345 | Pectate lyase [Carbohydrate transport and metabolism]. |
| smart00656 | Amb_all | 4.12e-51 | 187 | 385 | 13 | 185 | Amb_all domain. |
| pfam00544 | Pec_lyase_C | 1.34e-38 | 188 | 385 | 32 | 210 | 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 |
|---|---|---|---|---|---|
| QJW36767.1 | 3.16e-171 | 48 | 465 | 38 | 451 |
| QGQ18988.1 | 3.46e-171 | 15 | 477 | 23 | 502 |
| ARU53175.1 | 1.21e-169 | 48 | 465 | 43 | 456 |
| QCB93221.1 | 9.85e-165 | 47 | 477 | 56 | 511 |
| QVI64659.1 | 2.51e-162 | 53 | 472 | 31 | 465 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 1VBL_A | 3.53e-105 | 52 | 465 | 1 | 415 | Structureof the thermostable pectate lyase PL 47 [Bacillus sp. TS-47] |
| 1BN8_A | 6.35e-104 | 48 | 465 | 18 | 419 | BacillusSubtilis Pectate Lyase [Bacillus subtilis] |
| 5AMV_A | 1.31e-103 | 53 | 465 | 2 | 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] |
| 2BSP_A | 1.79e-103 | 48 | 465 | 18 | 419 | ChainA, PROTEIN (PECTATE LYASE) [Bacillus subtilis] |
| 2NZM_A | 1.04e-102 | 53 | 465 | 2 | 398 | 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 | 3.48e-103 | 48 | 465 | 18 | 419 | Pectate lyase OS=Bacillus subtilis (strain 168) OX=224308 GN=pel PE=1 SV=1 |
| Q60140 | 5.01e-57 | 64 | 466 | 39 | 380 | Pectate lyase OS=Pseudomonas viridiflava OX=33069 GN=pel PE=3 SV=1 |
| Q59671 | 2.70e-56 | 64 | 465 | 40 | 380 | Pectate lyase OS=Pseudomonas fluorescens OX=294 GN=pel PE=3 SV=1 |
| P72242 | 7.58e-55 | 64 | 465 | 39 | 379 | Pectate lyase OS=Pseudomonas amygdali pv. lachrymans OX=53707 GN=pelP PE=3 SV=1 |
| Q56806 | 2.76e-54 | 64 | 465 | 36 | 377 | Pectate lyase OS=Xanthomonas campestris pv. malvacearum OX=86040 PE=3 SV=1 |
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 0.000337 | 0.998911 | 0.000179 | 0.000228 | 0.000167 | 0.000143 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.