| Species | Bacillus_A luti | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae_G; Bacillus_A; Bacillus_A luti | |||||||||||
| CAZyme ID | MGYG000002288_05945 | |||||||||||
| CAZy Family | PL1 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 171; End: 611 Strand: - | |||||||||||
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| PL1 | 5 | 95 | 4e-28 | 0.4504950495049505 |
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| COG3866 | PelB | 4.46e-26 | 5 | 99 | 180 | 280 | Pectate lyase [Carbohydrate transport and metabolism]. |
| smart00656 | Amb_all | 5.82e-20 | 5 | 96 | 96 | 190 | Amb_all domain. |
| pfam00544 | Pec_lyase_C | 1.32e-13 | 5 | 92 | 119 | 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 |
|---|---|---|---|---|---|
| AMP47052.1 | 1.33e-84 | 5 | 132 | 48 | 175 |
| QNT67442.1 | 1.20e-79 | 5 | 132 | 370 | 497 |
| QUB83317.1 | 2.97e-57 | 5 | 132 | 306 | 433 |
| QCD40816.1 | 4.64e-57 | 5 | 132 | 345 | 472 |
| QCP73706.1 | 4.64e-57 | 5 | 132 | 345 | 472 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 3VMV_A | 1.24e-16 | 5 | 131 | 157 | 286 | 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 | 1.43e-12 | 5 | 105 | 170 | 270 | 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] |
| 1VBL_A | 2.18e-12 | 5 | 92 | 233 | 330 | Structureof the thermostable pectate lyase PL 47 [Bacillus sp. TS-47] |
| 2EWE_A | 3.65e-12 | 5 | 105 | 170 | 270 | ChainA, Pectate lyase C [Dickeya chrysanthemi] |
| 3ZSC_A | 7.09e-10 | 5 | 69 | 143 | 213 | 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 |
|---|---|---|---|---|---|---|
| B1B6T1 | 1.84e-14 | 5 | 101 | 184 | 281 | Pectate trisaccharide-lyase OS=Bacillus sp. OX=1409 GN=pel PE=1 SV=1 |
| Q65DC2 | 1.84e-14 | 5 | 101 | 184 | 281 | 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 |
| Q8GCB2 | 1.84e-14 | 5 | 101 | 184 | 281 | Pectate trisaccharide-lyase OS=Bacillus licheniformis OX=1402 GN=pelA PE=1 SV=1 |
| P11073 | 8.24e-12 | 5 | 105 | 192 | 292 | Pectate lyase C OS=Dickeya chrysanthemi OX=556 GN=pelC PE=1 SV=1 |
| P0C1C3 | 1.84e-10 | 5 | 107 | 191 | 293 | 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 |
|---|---|---|---|---|---|
| 1.000046 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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