Species | Prevotella sp900551055 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900551055 | |||||||||||
CAZyme ID | MGYG000004640_00991 | |||||||||||
CAZy Family | PL1 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 4911; End: 6473 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
PL1 | 131 | 340 | 7e-42 | 0.8415841584158416 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG3866 | PelB | 1.57e-46 | 23 | 427 | 12 | 344 | Pectate lyase [Carbohydrate transport and metabolism]. |
smart00656 | Amb_all | 8.39e-38 | 134 | 342 | 12 | 190 | Amb_all domain. |
pfam00544 | Pec_lyase_C | 7.11e-24 | 134 | 318 | 30 | 190 | 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 |
---|---|---|---|---|---|
QUT75310.1 | 5.42e-114 | 42 | 462 | 23 | 423 |
QNH62939.1 | 6.64e-36 | 63 | 427 | 77 | 378 |
QHJ07062.1 | 2.36e-34 | 44 | 427 | 55 | 369 |
SCA88301.1 | 2.60e-31 | 26 | 427 | 19 | 334 |
QAT67521.1 | 2.60e-31 | 26 | 427 | 19 | 334 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3ZSC_A | 3.06e-25 | 61 | 427 | 17 | 331 | Catalyticfunction and substrate recognition of the pectate lyase from Thermotoga maritima [Thermotoga maritima] |
3VMV_A | 2.43e-23 | 61 | 343 | 10 | 251 | 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] |
5AMV_A | 9.50e-22 | 222 | 427 | 191 | 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] |
1BN8_A | 1.16e-21 | 222 | 427 | 212 | 419 | BacillusSubtilis Pectate Lyase [Bacillus subtilis] |
2NZM_A | 1.72e-21 | 222 | 427 | 191 | 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 |
---|---|---|---|---|---|---|
Q65DC2 | 1.88e-30 | 42 | 427 | 41 | 339 | 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 |
B1B6T1 | 1.88e-30 | 42 | 427 | 41 | 339 | Pectate trisaccharide-lyase OS=Bacillus sp. OX=1409 GN=pel PE=1 SV=1 |
Q8GCB2 | 1.88e-30 | 42 | 427 | 41 | 339 | Pectate trisaccharide-lyase OS=Bacillus licheniformis OX=1402 GN=pelA PE=1 SV=1 |
B1L969 | 1.33e-24 | 17 | 427 | 5 | 356 | Pectate trisaccharide-lyase OS=Thermotoga sp. (strain RQ2) OX=126740 GN=pelA PE=3 SV=1 |
Q9WYR4 | 2.52e-24 | 17 | 427 | 7 | 358 | Pectate trisaccharide-lyase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=pelA PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000491 | 0.998478 | 0.000399 | 0.000215 | 0.000202 | 0.000188 |
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