| Species | Prevotella salivae | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella salivae | |||||||||||
| CAZyme ID | MGYG000001360_02031 | |||||||||||
| CAZy Family | PL1 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 2425599; End: 2427947 Strand: - | |||||||||||
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| PL1 | 463 | 634 | 1.3e-40 | 0.8415841584158416 |
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| COG3866 | PelB | 4.52e-56 | 379 | 749 | 20 | 345 | Pectate lyase [Carbohydrate transport and metabolism]. |
| smart00656 | Amb_all | 3.63e-29 | 470 | 635 | 17 | 190 | Amb_all domain. |
| pfam00544 | Pec_lyase_C | 5.92e-17 | 445 | 631 | 7 | 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 |
|---|---|---|---|---|---|
| QOR20273.1 | 2.94e-311 | 263 | 782 | 35 | 554 |
| CBW15186.1 | 5.15e-311 | 263 | 782 | 50 | 569 |
| QOR18408.1 | 6.11e-311 | 237 | 782 | 39 | 583 |
| ATA84997.1 | 2.87e-299 | 274 | 782 | 36 | 544 |
| QUB83317.1 | 5.77e-299 | 272 | 782 | 34 | 544 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 3VMV_A | 4.86e-27 | 420 | 631 | 33 | 246 | Crystalstructure of pectate lyase Bsp165PelA from Bacillus sp. N165 [Bacillus sp. N16-5],3VMW_A Crystal structure of pectate lyase Bsp165PelA from Bacillus sp. N165 in complex with trigalacturonate [Bacillus sp. N16-5] |
| 1VBL_A | 3.79e-18 | 470 | 642 | 133 | 343 | Structureof the thermostable pectate lyase PL 47 [Bacillus sp. TS-47] |
| 1AIR_A | 1.26e-15 | 457 | 747 | 81 | 342 | ChainA, PECTATE LYASE C [Dickeya chrysanthemi],1O88_A Chain A, Pectate Lyase C [Dickeya chrysanthemi],1O8D_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8E_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8F_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8G_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8H_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8I_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8J_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8K_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8L_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8M_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1PLU_A Chain A, Protein (pectate Lyase C) [Dickeya chrysanthemi],2PEC_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi] |
| 1PCL_A | 1.28e-15 | 463 | 631 | 70 | 276 | ChainA, PECTATE LYASE E [Dickeya chrysanthemi] |
| 2EWE_A | 3.02e-15 | 457 | 747 | 81 | 342 | ChainA, Pectate lyase C [Dickeya chrysanthemi] |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| B1B6T1 | 2.13e-25 | 417 | 639 | 67 | 280 | Pectate trisaccharide-lyase OS=Bacillus sp. OX=1409 GN=pel PE=1 SV=1 |
| Q8GCB2 | 2.13e-25 | 417 | 639 | 67 | 280 | Pectate trisaccharide-lyase OS=Bacillus licheniformis OX=1402 GN=pelA PE=1 SV=1 |
| Q65DC2 | 2.13e-25 | 417 | 639 | 67 | 280 | Pectate trisaccharide-lyase OS=Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46) OX=279010 GN=BLi04129 PE=3 SV=1 |
| Q5AVN4 | 3.64e-20 | 470 | 644 | 99 | 277 | Pectate lyase A OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=plyA PE=1 SV=1 |
| P0C1C3 | 5.97e-17 | 434 | 747 | 72 | 363 | Pectate lyase 3 OS=Pectobacterium carotovorum subsp. carotovorum OX=555 GN=pel3 PE=3 SV=1 |
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 0.001196 | 0.996703 | 0.001473 | 0.000225 | 0.000195 | 0.000180 |
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