| Species | ||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; | |||||||||||
| CAZyme ID | MGYG000002063_01545 | |||||||||||
| CAZy Family | PL1 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 1730; End: 4153 Strand: + | |||||||||||
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| PL1 | 481 | 652 | 1.3e-40 | 0.8366336633663366 |
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| COG3866 | PelB | 2.15e-50 | 352 | 768 | 8 | 345 | Pectate lyase [Carbohydrate transport and metabolism]. |
| smart00656 | Amb_all | 1.10e-27 | 488 | 650 | 17 | 186 | Amb_all domain. |
| pfam00544 | Pec_lyase_C | 1.36e-15 | 486 | 650 | 33 | 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 |
|---|---|---|---|---|---|
| QCD40816.1 | 1.16e-311 | 228 | 807 | 10 | 589 |
| QCP73706.1 | 1.16e-311 | 228 | 807 | 10 | 589 |
| QUT73893.1 | 1.66e-226 | 284 | 806 | 20 | 542 |
| QOR18408.1 | 1.08e-212 | 271 | 801 | 63 | 583 |
| QUB83317.1 | 6.29e-212 | 274 | 801 | 28 | 544 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 3VMV_A | 9.30e-27 | 438 | 650 | 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] |
| 1AIR_A | 6.39e-19 | 489 | 766 | 91 | 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] |
| 2EWE_A | 1.55e-18 | 489 | 766 | 91 | 342 | ChainA, Pectate lyase C [Dickeya chrysanthemi] |
| 1VBL_A | 2.25e-17 | 488 | 650 | 133 | 330 | Structureof the thermostable pectate lyase PL 47 [Bacillus sp. TS-47] |
| 3ZSC_A | 4.75e-16 | 490 | 639 | 71 | 225 | Catalyticfunction and substrate recognition of the pectate lyase from Thermotoga maritima [Thermotoga maritima] |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| Q8GCB2 | 4.93e-23 | 435 | 658 | 67 | 280 | Pectate trisaccharide-lyase OS=Bacillus licheniformis OX=1402 GN=pelA PE=1 SV=1 |
| B1B6T1 | 4.93e-23 | 435 | 658 | 67 | 280 | Pectate trisaccharide-lyase OS=Bacillus sp. OX=1409 GN=pel PE=1 SV=1 |
| Q65DC2 | 4.93e-23 | 435 | 658 | 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 | 4.46e-18 | 488 | 663 | 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 |
| P11073 | 4.54e-18 | 489 | 766 | 113 | 364 | Pectate lyase C OS=Dickeya chrysanthemi OX=556 GN=pelC PE=1 SV=1 |
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 0.000476 | 0.998754 | 0.000193 | 0.000224 | 0.000174 | 0.000159 |
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