Species | Prevotella sp900550365 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900550365 | |||||||||||
CAZyme ID | MGYG000002877_00354 | |||||||||||
CAZy Family | PL1 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 11077; End: 12639 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
PL1 | 131 | 341 | 8.8e-42 | 0.8465346534653465 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG3866 | PelB | 2.29e-45 | 44 | 427 | 33 | 344 | Pectate lyase [Carbohydrate transport and metabolism]. |
smart00656 | Amb_all | 9.89e-37 | 134 | 342 | 12 | 190 | Amb_all domain. |
366158 | pfam00544 | 5.00e-24 | 134 | 338 | 30 | 211 | Pec_lyase_C 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 | 5.86e-117 | 24 | 430 | 5 | 386 |
QNH62939.1 | 1.40e-37 | 49 | 427 | 61 | 378 |
QHJ07062.1 | 1.91e-36 | 65 | 427 | 66 | 369 |
SCA88301.1 | 2.79e-32 | 29 | 428 | 23 | 335 |
QAT67521.1 | 2.79e-32 | 29 | 428 | 23 | 335 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1VBL_A | 1.12e-21 | 107 | 427 | 102 | 415 | Structureof the thermostable pectate lyase PL 47 [Bacillus sp. TS-47] |
3ZSC_A | 3.83e-21 | 47 | 322 | 8 | 220 | Catalyticfunction and substrate recognition of the pectate lyase from Thermotoga maritima [Thermotoga maritima] |
5AMV_A | 7.60e-21 | 166 | 428 | 149 | 399 | 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 | 9.21e-21 | 166 | 428 | 170 | 420 | BacillusSubtilis Pectate Lyase [Bacillus subtilis] |
2BSP_A | 2.23e-20 | 166 | 428 | 170 | 420 | ChainA, PROTEIN (PECTATE LYASE) [Bacillus subtilis] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
B1B6T1 | 5.99e-29 | 42 | 428 | 41 | 340 | Pectate trisaccharide-lyase OS=Bacillus sp. OX=1409 GN=pel PE=1 SV=1 |
Q65DC2 | 5.99e-29 | 42 | 428 | 41 | 340 | 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 | 5.99e-29 | 42 | 428 | 41 | 340 | Pectate trisaccharide-lyase OS=Bacillus licheniformis OX=1402 GN=pelA PE=1 SV=1 |
B8NBC2 | 9.40e-21 | 64 | 340 | 46 | 260 | Probable pectate lyase B OS=Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) OX=332952 GN=plyB PE=3 SV=1 |
Q2TZY0 | 9.40e-21 | 64 | 340 | 46 | 260 | Probable pectate lyase B OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=plyB PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000524 | 0.998610 | 0.000332 | 0.000174 | 0.000158 | 0.000141 |
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