Species | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; | |||||||||||
CAZyme ID | MGYG000004009_01076 | |||||||||||
CAZy Family | PL1 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 6024; End: 7586 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
PL1 | 131 | 341 | 2e-42 | 0.8465346534653465 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG3866 | PelB | 9.50e-40 | 25 | 427 | 14 | 344 | Pectate lyase [Carbohydrate transport and metabolism]. |
smart00656 | Amb_all | 1.19e-34 | 134 | 342 | 12 | 190 | Amb_all domain. |
pfam00544 | Pec_lyase_C | 1.67e-21 | 169 | 338 | 41 | 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 |
---|---|---|---|---|---|
QUT75310.1 | 8.84e-120 | 42 | 462 | 23 | 423 |
QNH62939.1 | 3.83e-38 | 63 | 427 | 77 | 378 |
QHJ07062.1 | 5.26e-37 | 44 | 427 | 55 | 369 |
SCA88301.1 | 2.98e-33 | 42 | 427 | 36 | 334 |
QAT67521.1 | 2.98e-33 | 42 | 427 | 36 | 334 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3ZSC_A | 2.52e-22 | 47 | 427 | 8 | 331 | Catalyticfunction and substrate recognition of the pectate lyase from Thermotoga maritima [Thermotoga maritima] |
5AMV_A | 4.20e-21 | 167 | 319 | 150 | 298 | 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 | 5.10e-21 | 167 | 319 | 171 | 319 | BacillusSubtilis Pectate Lyase [Bacillus subtilis] |
3VMV_A | 7.78e-21 | 63 | 361 | 12 | 260 | 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] |
2BSP_A | 1.24e-20 | 167 | 319 | 171 | 319 | ChainA, PROTEIN (PECTATE LYASE) [Bacillus subtilis] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q8GCB2 | 9.10e-34 | 29 | 427 | 27 | 339 | Pectate trisaccharide-lyase OS=Bacillus licheniformis OX=1402 GN=pelA PE=1 SV=1 |
B1B6T1 | 9.10e-34 | 29 | 427 | 27 | 339 | Pectate trisaccharide-lyase OS=Bacillus sp. OX=1409 GN=pel PE=1 SV=1 |
Q65DC2 | 9.10e-34 | 29 | 427 | 27 | 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 |
B1L969 | 1.43e-21 | 47 | 427 | 33 | 356 | Pectate trisaccharide-lyase OS=Thermotoga sp. (strain RQ2) OX=126740 GN=pelA PE=3 SV=1 |
Q9WYR4 | 3.62e-21 | 47 | 427 | 35 | 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 |
---|---|---|---|---|---|
0.000407 | 0.998651 | 0.000308 | 0.000213 | 0.000204 | 0.000180 |
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